CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
CP031165	Euzebya sp. DY32-46 chromosome, complete genome	18 crisprs	csa3,DEDDh,WYL,cas3	1	3	3	0
CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	2 crisprs	cas3,cas8e,cse2gr11,cas7,cas5,cas6e,cas1,cas2,DinG,DEDDh	0	32	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: CP031165_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_2

131016-131112

Orphan

Consensus_repeat	Method
CCCGAACCCGACACGCGTCGGGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_2

>merge|CP031165|2|131016-131112|CRISPRCasFinder
CCCGAACCCGACACGCGTCGGGGGGTGAGGGGTGGACCGCCCAGCCGGTTGTCGGGTTATCCCCGCCGGCCGTCCCGAATCCGACACGCGTCGGGGG

>CP031165|2|2|131016-131112|CRISPRCasFinder
CCCGAACCCGACACGCGTCGGGGG	GTGAGGGGTGGACCGCCCAGCCGGTTGTCGGGTTATCCCCGCCGGCCGT
CCCGAATCCGACACGCGTCGGGGG

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV04827.1\|128511_128628_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV04838.1\|139849_140554_+\|putative-TRANSCRIPTIONAL-REGULATORY-PROTEIN	unknown	unknown	gnl\|CDD\|225222
CP031165.1\|AXV04826.1\|127339_128518_-\|Mobile-element-protein	unknown	unknown	gnl\|CDD\|225382
CP031165.1\|AXV04828.1\|128736_129129_+\|putative-carboxymuconolactone-decarboxylase-family-protein	unknown	unknown	gnl\|CDD\|223672
CP031165.1\|AXV04839.1\|140659_141667_+\|General-stress-protein-69	unknown	unknown	gnl\|CDD\|381312
CP031165.1\|AXV04836.1\|137177_137801_+\|GTP-cyclohydrolase-I-type-1	unknown	unknown	gnl\|CDD\|236472
CP031165.1\|AXV04835.1\|135948_137181_+\|Ferredoxin-reductase	unknown	unknown	gnl\|CDD\|369639
CP031165.1\|AXV04833.1\|134590_135346_-\|putative-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225222
CP031165.1\|AXV04832.1\|131981_134525_-\|Alkaline-phosphatase	unknown	unknown	gnl\|CDD\|367829
CP031165.1\|AXV04819.1\|117664_118015_+\|Menaquinone-via-futalosine-polyprenyltransferase	unknown	unknown	unknown
CP031165.1\|AXV04820.1\|118025_118955_-\|L-fuco-beta-pyranose-dehydrogenase	unknown	unknown	gnl\|CDD\|381324
CP031165.1\|AXV04825.1\|125579_126887_-\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|235777
CP031165.1\|AXV04837.1\|137891_139853_+\|Cytochrome-c-oxidase-polypeptide-I	unknown	unknown	gnl\|CDD\|238832
CP031165.1\|AXV04822.1\|120513_121992_+\|Acetoacetyl-CoA-synthetase	unknown	unknown	gnl\|CDD\|341259
CP031165.1\|AXV04831.1\|131416_131935_-\|Phosphoesterase	unknown	unknown	gnl\|CDD\|378975
CP031165.1\|AXV04821.1\|119058_120372_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379258
CP031165.1\|AXV04824.1\|123937_125356_+\|Phytoene-dehydrogenase	unknown	unknown	gnl\|CDD\|224154
CP031165.1\|AXV04834.1\|135445_135919_+\|putative-TRANSMEMBRANE-PROTEIN	unknown	unknown	unknown
CP031165.1\|AXV04823.1\|122112_123918_+\|CONSERVED-MEMBRANE-PROTEIN	unknown	unknown	gnl\|CDD\|371888
CP031165.1\|AXV04830.1\|131117_131420_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377607

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV04821.1\|119058_120372_+\|hypothetical-protein	gnl\|CDD\|379258	pfam13556, HTH_30, PucR C-terminal helix-turn-helix domain. This helix-turn-helix domain is often found at the C-terminus of PucR-like transcriptional regulators such as Bacillus subtilis pucR and is likely to be DNA-binding.	5.61077e-13
CP031165.1\|AXV04826.1\|127339_128518_-\|Mobile-element-protein	gnl\|CDD\|225382	COG2826, Tra8, Transposase and inactivated derivatives, IS30 family [DNA replication, recombination, and repair].	8.11897e-98
CP031165.1\|AXV04828.1\|128736_129129_+\|putative-carboxymuconolactone-decarboxylase-family-protein	gnl\|CDD\|223672	COG0599, COG0599, Uncharacterized homolog of gamma-carboxymuconolactone decarboxylase subunit [Function unknown].	1.96587e-16
CP031165.1\|AXV04839.1\|140659_141667_+\|General-stress-protein-69	gnl\|CDD\|381312	cd19086, AKR_AKR11C1, AKR11C family of aldo-keto reductase (AKR). Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.	2.79458e-86
CP031165.1\|AXV04823.1\|122112_123918_+\|CONSERVED-MEMBRANE-PROTEIN	gnl\|CDD\|371888	pfam12077, DUF3556, Transmembrane protein of unknown function (DUF3556). This family of transmembrane proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 576 to 592 amino acids in length.	0
CP031165.1\|AXV04838.1\|139849_140554_+\|putative-TRANSCRIPTIONAL-REGULATORY-PROTEIN	gnl\|CDD\|225222	COG2345, COG2345, Predicted transcriptional regulator [Transcription].	3.74625e-20
CP031165.1\|AXV04835.1\|135948_137181_+\|Ferredoxin-reductase	gnl\|CDD\|369639	pfam07992, Pyr_redox_2, Pyridine nucleotide-disulphide oxidoreductase. This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.	1.78058e-69
CP031165.1\|AXV04833.1\|134590_135346_-\|putative-transcriptional-regulator	gnl\|CDD\|225222	COG2345, COG2345, Predicted transcriptional regulator [Transcription].	1.00193e-16
CP031165.1\|AXV04831.1\|131416_131935_-\|Phosphoesterase	gnl\|CDD\|378975	pfam12850, Metallophos_2, Calcineurin-like phosphoesterase superfamily domain. Members of this family are part of the Calcineurin-like phosphoesterase superfamily.	5.44486e-40
CP031165.1\|AXV04820.1\|118025_118955_-\|L-fuco-beta-pyranose-dehydrogenase	gnl\|CDD\|381324	cd19098, AKR_unchar, uncharacterized aldo-keto reductase (AKR) superfamily protein. This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.	5.58732e-144
CP031165.1\|AXV04837.1\|137891_139853_+\|Cytochrome-c-oxidase-polypeptide-I	gnl\|CDD\|238832	cd01662, Ubiquinol_Oxidase_I, Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.	0
CP031165.1\|AXV04822.1\|120513_121992_+\|Acetoacetyl-CoA-synthetase	gnl\|CDD\|341259	cd05936, FC-FACS_FadD_like, Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD. This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.	2.3171e-173
CP031165.1\|AXV04832.1\|131981_134525_-\|Alkaline-phosphatase	gnl\|CDD\|367829	pfam04122, CW_binding_2, Putative cell wall binding repeat 2. This repeat is found in multiple tandem copies in proteins including amidase enhancers and adhesins.	6.03788e-10
CP031165.1\|AXV04824.1\|123937_125356_+\|Phytoene-dehydrogenase	gnl\|CDD\|224154	COG1233, COG1233, Phytoene dehydrogenase and related proteins [Secondary metabolites biosynthesis, transport, and catabolism].	1.76194e-73
CP031165.1\|AXV04836.1\|137177_137801_+\|GTP-cyclohydrolase-I-type-1	gnl\|CDD\|236472	PRK09347, folE, GTP cyclohydrolase I; Provisional.	7.72574e-82
CP031165.1\|AXV04825.1\|125579_126887_-\|serine/threonine-protein-kinase	gnl\|CDD\|235777	PRK06302, PRK06302, acetyl-CoA carboxylase biotin carboxyl carrier protein.	0.00027974
CP031165.1\|AXV04830.1\|131117_131420_-\|hypothetical-protein	gnl\|CDD\|377607	pfam06108, DUF952, Protein of unknown function (DUF952). This family consists of several hypothetical bacterial and plant proteins of unknown function.	3.17569e-27

>CP031165.1|AXV04828.1|128736_129129_+|putative-carboxymuconolactone-decarboxylase-family-protein
MTATSITDTSISDAHNAQVIDDLRAPTRAFRKAAPEAWAGFGALHQAAVADGVVPASMKELVALAIAVTQHCDGCVAYHAKAAVMKGATREQAVEVLEVALLMAGGPASVWAPRALAAFDEFADVRGTTT
>CP031165.1|AXV04827.1|128511_128628_-|hypothetical-protein
MRGSTQPPRRVSDSGPPVVAASRLRCNTTLRGGGGRSW
>CP031165.1|AXV04826.1|127339_128518_-|Mobile-element-protein
MVRSRAKGEKRWLRLPDEVRAEVIRRARAGQGRRQILEEVDISVGSFLNVLKPFGGVLRAELATDPSPHRLSLDDRVEIRLGIGRGETYQAIADRVGRHKSSVWREVDRNGGREAYRPMLAHKRAHEQARRAKPTKLASCAELAGLVEHGLRRLWSPQQIAADLKERFGDDESMTVSHETIYKSLYVQGRGELRRELTSCLRTGRAKRVPSGRSPRPRMHDMVMISERPAEVEDRAVPGHWEGDLIIGKDGKSAVGTLVERSTRYVMLMHLDGDRTAATVRDAMTTAITGLPEHLRRSITWDQGIEMAEHVQFTIDTDVPVYFCDPHSPWQRGSNENTNGLLRQYMPKGTDLSVHTPADLNDFAESLNTRPRQTLGWKTPAAQLAQLVAPTG
>CP031165.1|AXV04825.1|125579_126887_-|serine/threonine-protein-kinase
MAALAVLLVVVGGLVGLLLLRDSGETTTEAEAPPPAEVDVPEEPAAAIPPAPEEEPTTEALPPAPLDEGKPERGSEDATVAAAAAGVDFSWLALASASPYTTYEWVTDDSGQLTVEIPTAWADRDLRNDTSDGVAIPSIWAAPDLEGLIDRWDGAGAILELRTAATGTTDTVLADMGGAIAADTTCTEQRSYAYDDGWYVGTAVLYAGCGSTDSAMLQIAATDGTNGILAVQVQMVSTADVDAAVRIVQTFQAITTTTPAPVPVPAPAAPAPVPNAPVAPAPAPAPNPPVNSFGLPTGLFCRDLADMGYSYADAMDYWYADGAPDRMDADVDGIPCETVYPLWEIDAYWGFTTPAPPTDEWVEAMWVAENAMYACGYTPALDTFVDGPFPDGGYTVTMNVDVGWDLIWAQFEVFPWSGEIYGFDAVADDLLWCNY
>CP031165.1|AXV04824.1|123937_125356_+|Phytoene-dehydrogenase
MTDAVVVGSGPNGLAAAVTLATAGVTVRVLEAADTIGGGVRSSELTVPGLLHDECSGFHPLAVDTAFSRSVDLAAHGLTWRWPEVQYSHPLDGGRGAAAFRSVDDTADGLGVDGQAWRRLFGPLVDRFDRIAEDFLQPMLHVPSNPFALARFGLRAAPSVQLLASRMSTPEARALWAGAGAHAMRPFGQPLSAAIGAALATAAHRYGWPVAEGGSQAIATAMRSVIEAHGGTIETGVRVESLDELGTPDLTVLDVAPGAVVRMAGKRLPARVARAYRRYRHGPGAFKVEYAVVGGVPWSHEPTRRAGTVHVIGDFEETAAAEQAVHRGRMPERPFVLLGQQSLADPGRANGDVHPIYAYAHTPHGWTGDATEAITGQVERFAPGFRDRIVATHVRSTTDMSVHNPNYVGGDIVTGANTPWQLVFRPRVALDPYATGIPGVYLCSAATPPGAGAHGMCGFHAARSALDWLGRR
>CP031165.1|AXV04823.1|122112_123918_+|CONSERVED-MEMBRANE-PROTEIN
MGFKTADMPPVDPAEYDSMPFMDRMRMLATHWVEYGFGGPKQMHMLYVYKLLFYVIAGVVVVGVSTPGLSLADLGDWWGEPIVYEKFIVWTLLFEITGYASSSGPLAFKFAPFTGGWRYWTRRNTLRLPPWPSKVPLTAGDHRTLADVTIYGTILVLLVGLLLAPGTQDNAFPGTDAGLIHPMGLLAYVVLIGIMGLRDRVVFLAARSEQYVAILFFFAVLSTPVDMILAAKVAMVSIWMGAGVSKFGHHFTSVVPPMVSNTPWITSTAFKRKLYRDFPNDLRPSRLSWAFAHIGGTVVELCLPVVLLFSTNTTLTWLAIGGMILFHVFITSTFPLAVPLEWNVFFMFAVAWLFGGFPAGEGWGLGDVSSPLVLLAFAVAFLTMPILGNLRPDLVSFLPSMRQYAGNWASATWAFRGDAAEDKLNQHLVKYNANQIDQLAAAFGKEVAEIFMQKAVAWRTMHSQGRALISLMMRHLDRLENYRIREAEFTCTTLVGWQFGDAHLHNEQTITAVQKRCNFEPGECVIVWIESQPIHRKRLEYKVIDAALGVVERGHYHPADAVNEQPWLPNGPIPHTVTWRREGYVPIGEWAHPSVRATVGA
>CP031165.1|AXV04822.1|120513_121992_+|Acetoacetyl-CoA-synthetase
MSLDYLPWRCPADRRAAVAVRDDRTELTYRQLDDWTRAVAGQLAGSGLGRGDVVAIVLPNRVELLVVMLAAWRLGAVATPVNPVFTEHEARYQIEDADALIVVNEGLDESPRGGRMATGVDDLARPSGDRPPVGPEPADLDGSDLALLIYTSGSTGRPKGVMLDHDNAEAMTSQMVRHFGLTSEDHCMLVLPLFHVNAIMVSVLSVWRAGGQVSVVGQFSASRFFDDVERLRPTYFSAVPTIYAMLVALPEEVKPDTSSLRFVVCGAAPVSEELLVASNERYGFEMVEGYGLTEGTCASACNPVDGVRKLGTVGPALPGQQIRVVDEDGHPVPNGQRGEVLIAGPTVMRGYLGRPEATAETIVDGWLRTGDVGVLDDDGYLRIVDRVKDMIIRGGENLYPKEIESVLTTVDGVLEAAVVGQHDPLFGEVPVAFVSRYPGSDVDEETLLDHCRLHLTRVKVPVAINLVEELPRNPVGKIDKPGLRRSLQPQPT
>CP031165.1|AXV04821.1|119058_120372_+|hypothetical-protein
MTSRPLQGRLVREDEPGAEEILRLVGVVGDRLQARFPEINDTMNLAIEDAIDVLDDPEILDSMHASVEGNVVTILHLLRQGIPLEHAQPITAATDYARRTAQQGVPSAALRRAYHIGSDDLLNHMFEEIQQLDAEADVKLRLLHHLAGWMHQYVDWITAVVLEVHEEERRHVLQRRASVVSGLVQRVLDGRPVPPADFLNRTGYRLSQVHIAAVAWLAGANQGTDRTADLTEVGHRLAGLLDSHGAPLLVPVDRNAVRIWIGLGQRSDPVDMADLRRRLDVDADVRVALGTPLDGPDGFRRSLEQAEVVKVVPTVASTSVTRAVGWAEDGMTTVARLAHDLGGTRRWVREVLGPLAEDTEGAERLRETVRVHLRNGGSYVRTGEVLLLHRNTVKYRIQQVEAMRGRPLEDGRLDLELALHAWHLLGSVVLVGGGHTR
>CP031165.1|AXV04820.1|118025_118955_-|L-fuco-beta-pyranose-dehydrogenase
MTNTDRLPTTTLGRGGPTIGRIGLGLAALGRPGYINVGHADDVGEDRSVEGMRRRAHRVLDLAVALGITYVDAARSYGRAEAFLSDWSPSAPVTIGSKWGYTYTADWQVEADVHEVKDHSLATFERQRAETDALLGDRLGLYQVHSATLDSGILEDEAVLDALRAEPVTVGLSVSGPGQADTIRRALAIPGSPFRCVQATWNVLEPSAGPALAEAHDAGWGVIVKEALANGRLTARGDHALRGPASSDALAIAAVLAQPFVDVVLSGAATEAHLRSNVGAVEVDPDDLPTVTPEDPAAYWNRRSALDWT
>CP031165.1|AXV04819.1|117664_118015_+|Menaquinone-via-futalosine-polyprenyltransferase
MISWPRTVVVVSLVGVLLGGCGIGGGVQEVRLERLADEQDAWDGRDVRTRGIVRMAEQPLHYWIEDDVPNRVEIQPADAVEDHVGRQVIVEGTFRFRDDEGRRITVGTVEVVTPDS
>CP031165.1|AXV04830.1|131117_131420_-|hypothetical-protein
MTAGPVIVHVIGRDEWAAVADVLAPASLEVEGFVHCADPDQVAGVIERYYADRDDLLLLQIDVGRVEAPIVREDTTGRGEAFPHVYGPIPRAAVVDVTPA
>CP031165.1|AXV04831.1|131416_131935_-|Phosphoesterase
MSTPDPSMRVAVLADTHRRADRAGDLPDAVFDLVRDADVILHAGDIVEQEVLDVLARHAPVHAVLGNNDPSLAGVLPERLEVELAGVRIGMVHDSGQAKGRAERLHGMFPEADVVVFGHSHIPWNETGVDGQLLFNPGSPTQRRRQPVATMGRLTLRDGVVEEATILPVVAA
>CP031165.1|AXV04832.1|131981_134525_-|Alkaline-phosphatase
MSAVGLLALLLPLLVGSLAPAAAQPDPDPPGVSSVADDVTAVPWDGAAPAERMRAVAALAPTSRAIVTTTGAFPDALASGVLQDDAMLVGATDGRLDDATKALLTTAGVDEVIILGGVAAVPEDVRDDLPVGADVTRISGLDRTETAAEAAVQAATGDVSTVLLARARGPEDNPSAGFIDAIGAGAWAAATGYPVLLVDNNFVTDATRAAMADLDPDELVVIGGTAAVSEEAAEAVAAGRDIRRVAGPERFTTAARIAEETRPDGAETVVLLDGTDPEAWTTGFAAAHPAATGDAAILLSNGDELPTATLAALDDLSPSALICAAPAVACNAARDAAGFAPLVPLAVAPAPGSPLPVGTTVSFTGETEVTLDDDGGCLTGGTRSGDAARDCTVVVRVAGDDNRVGRTATVTWPALITSDTTVEAPTEYLSPLAGGRWDFDEAVDVRPAADINNSKGAQVDTGASVLRYGGEPGNVPVLWSGFGGAVPVPPDGLAVPVDTTRFTRFLARVYSPAAGPLGLEFRSCSTTPNVDCINPASMVAQGRAGTNLQPGWQTVAIDLAGDPAWTGNPIHTIYLYANGGTIVDDLRITDGSTASTITTTTAPGVAVRWDLDEDPSNNTDPTSALWGELPGGVLDPDVLPPGRYWLHTVAADGTAGSTAGPIDIVSPGLSEGPLVLDGEWARDVRGNAWDFAAGGLVAGTDDVIELTNAERIDGPGLTGRNTNHSGDPYVVLDVPAPIDTAVWTHVVVEFSVDGPFDLAFAPGGGTMGRVLYQQGDQAWRNGNDIVAYPNQRTYVVEMTSPHSLEPNTPLWQAAPVTGLRFDPNEDEAPGRTWRVESISLTRGWPTR
>CP031165.1|AXV04833.1|134590_135346_-|putative-transcriptional-regulator
MPSAPTPDPTESIADPIETVAALGDPNRRKLYDHVVEANGWVGRDAAAEASGLRRGITAHHLDKLAELGLLEVDYQRLSGRSGPGAGRPAKVYRRARRDVDVSLPPRDYALPGRLLADALVAASTTGEDPGRLLDEAARREGIALGAAIAAGADEGGPGAEAAMVALEARGFEPTQDQDGTILLRNCPFHELARSHTSLICGMNHCLLTAAMESAGVTLDASLEPHDDMCCVRLHRRPIGDRPGSQPGEES
>CP031165.1|AXV04834.1|135445_135919_+|putative-TRANSMEMBRANE-PROTEIN
MSASVPATRSRVDHLSVESTDRLPTPVVQAFWLLRIGFTAAPILFGLDKFANVLVDWDTYVAPLFTDSLGISAGTLMSLVGVVEILAGLLVFARPRIGGYVVAAWLGGIILDLLVLGDHYDVALRDFGLLLGALTLARLAAVVPRDARPFPSAAATS
>CP031165.1|AXV04835.1|135948_137181_+|Ferredoxin-reductase
MTASPTHVIVGAGLAGANAARALREEGFDGRIVLIGDEADLPYDRPPLSKQYLRGETSPDDIRVLDADGWSQLDVDLVLGAAVTSVDIDGRHVTFGNGTTVGWDRLLLATGAEPRALPVRGGDLPGVHLLRRLADADRLRAALQRADRIVVVGAGWLGSEVAASARQMGVQVSLVEMGSVPLARTLGERVGSIYRDLHASNGVALHMRASVTAILGDRRATGVQLHDGTVLPADLVVVGVGVRPRAQLASRVGLAVGNGNGIEVDAELQTSAPGIYAAGDVASAWHPVLNRRLRVEHWANAIHQGRVAAANMLGANRPYDRQPYFFSDQYDLGMELTGHPDPAMEVVFRGDPSDGAFMAFWLADGRVSAAMNANIWDVTDTLRELVESGRPIASERLADPSEPLDALVSS
>CP031165.1|AXV04836.1|137177_137801_+|GTP-cyclohydrolase-I-type-1
MTGPSPTMRDGVGAPTRVPPPASGGVDRPAAIAAVHRLLVALGQDTADPQLRDTPRRVVDALEEMLTPPPFATTTFPDEVGYEGAVVVRDIPVQSLCAHHLLPFVGVAHVAYLPGARLVGLSKLARTVEAHARRLQVQEHLTVQVADWVMAELAPEGVAVVLEAEHLCMAMRGVRSRGTSTITTAVRGRVRDDPHLRTEVLALLAVR
>CP031165.1|AXV04837.1|137891_139853_+|Cytochrome-c-oxidase-polypeptide-I
MTVVDDRRASRTRRSVFARPTATTGWRSWVTTVDHKRIGIMYGVASLAFFAVGGLEALLIRVQLAGPNGSLVTADQYNQIFTMHGLTMVFFVVMPLGAAFMNFLLPLQIGARDVAFPRLNALSWWVFLASGIFVYSAVLFDGLPNGSWVGYSPLAGTVGPDPAGLTFGADSAAIHQSRMLFYSLGLQIAGVASLASAVNFITTTLNMRAPGMTLMRMPTFAWMTFVTAAMLLFAMPILGIALWQMMFQVRWAAPFYDPTNGGDPVLWQHMFWLFGHPEVYIMILPAFGIVSEILPVFSRKPLFGYSAVVFSGIAIAFMGWGVWAHHMFATGLGPVADAAFGISSMVIAVPTGIKIFNWMGTMWGGQIRFTTPMLFSIGLVSMFTIGGLSGVTHALVPSDTQQHDTYYIVAHFHYVLFGGALFALFGAIYYWAPKAFGRMFDERIGKVHFVLMLIGFNLTFGPMHLLGLNGMPRRYYTYADGMGWNTWNLVSSSGAFVIALSFLVFLYGCWRLRRSEQDLPPDPWDARTIEWLTPCPAPAHNFDTIPFVSERDEVWYRKHRDGGLEPPDPVDPSTIHMPSPSWFPLVLSLGLPVAAYGVFTEGAAQVALFVVGGMLVTGGMLGWAVEPSSEPSAEPDPAGRSTDDPGPRAGERS
>CP031165.1|AXV04838.1|139849_140554_+|putative-TRANSCRIPTIONAL-REGULATORY-PROTEIN
MTAPPDVAVDAPTRDHADARMSDATKVHRAMGDDSRSHIVDVLRATPDPMGIRDIADAVGLHVSTVRGHLDVLQDAGLVTSEQVVTDARGRPPLAWTATAAATTSADGGYRLLAEILLSQLVDRPASPLESGRRWGAHLIEAPRPGTVVSDDEAVQRVLALLDQLGFAPSLDDDTVLLRRCPFADLARGHEDLICQTHLGIVRGALDALGSTTRAEAMAPFVEPSLCTVRLSTS
>CP031165.1|AXV04839.1|140659_141667_+|General-stress-protein-69
MRMRQLTPDIEVSEIGFGNWTVTTGWWGDYSRQEAVALHRAAFDAGVTFFDTASVYRDGYGEEVLAEALGEVREQIVIGTKFGYDLDVDTGSRGQQERPHRTDVVSVAAALDDSLRRFGTDVIDVWQLHNPRMAHLVDDELFAFLQQVKEEGKVRATAIALGPRIGWRDEGLHAMHTRDLDVVHMIHNMLEQDPGRDLVAAARETDTGLIVRVPHSSGLLEGHLHADTVFPANDHRRHRPRSWLLEGVQKVERLRFLERSDRTLGQAALRWVLDHDVAATALPNIYNVDQLQEFVGASDAAELTDEEHRMVAELYADGFGVVPEADQETRLRDVS

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Crispr_ID: CP031165_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_5

554905-555003

Orphan

Consensus_repeat	Method
CACGGCGGGCGGCCCAGAACCCGACA	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_5

>merge|CP031165|5|554905-555003|CRISPRCasFinder
CACGGCGGGCGGCCCAGAACCCGACACGCGTGGGGGTGGTCGGGCGGCGCCACCCGGCCGCCTGTCGGGTGATCACGGCGGGCGGCCGAGAACCCGACA

>CP031165|5|5|554905-555003|CRISPRCasFinder
CACGGCGGGCGGCCCAGAACCCGACA	CGCGTGGGGGTGGTCGGGCGGCGCCACCCGGCCGCCTGTCGGGTGAT
CACGGCGGGCGGCCGAGAACCCGACA

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV05161.1\|562528_564844_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377378
CP031165.1\|AXV05147.1\|543431_544826_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225156
CP031165.1\|AXV05162.1\|564860_565838_-\|UDP-glucose-4-epimerase	unknown	unknown	gnl\|CDD\|212494
CP031165.1\|AXV05146.1\|541618_543220_-\|putative-RNA-helicase	unknown	unknown	gnl\|CDD\|223989
CP031165.1\|AXV05154.1\|555007_556780_-\|ABC-transporter,-ATP-binding/permease-protein	unknown	unknown	gnl\|CDD\|224055
CP031165.1\|AXV05163.1\|565955_566435_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05145.1\|539858_541406_+\|putative-penicillin-acylase	unknown	unknown	gnl\|CDD\|380277
CP031165.1\|AXV05156.1\|557410_557896_-\|Transcriptional-regulator,-MarR-family	unknown	unknown	gnl\|CDD\|197670
CP031165.1\|AXV05153.1\|553672_554851_-\|Mobile-element-protein	unknown	unknown	gnl\|CDD\|225382
CP031165.1\|AXV05150.1\|546087_546708_+\|secreted-protein	unknown	unknown	gnl\|CDD\|378440
CP031165.1\|AXV05144.1\|539714_539858_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05157.1\|558015_558840_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05152.1\|548279_553643_+\|Glycerophosphoryl-diester-phosphodiesterase	unknown	unknown	gnl\|CDD\|380277
CP031165.1\|AXV05160.1\|561025_562483_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225176
CP031165.1\|AXV05158.1\|558851_560246_-\|Gamma-glutamyltranspeptidase	unknown	unknown	gnl\|CDD\|223482
CP031165.1\|AXV05151.1\|547075_548164_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05159.1\|560300_560876_+\|Transcriptional-regulator,-TetR-family	unknown	unknown	gnl\|CDD\|376024
CP031165.1\|AXV05155.1\|556853_557258_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05149.1\|545324_545972_-\|Transmembrane-protein	unknown	unknown	gnl\|CDD\|379389
CP031165.1\|AXV05148.1\|544868_545315_-\|DipZ-protein	unknown	unknown	gnl\|CDD\|239310

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV05161.1\|562528_564844_+\|hypothetical-protein	gnl\|CDD\|377378	pfam04536, TPM_phosphatase, TPM domain. This family was first named TPM domain after its founding proteins: TLP18.3, Psb32 and MOLO-1. In Arabidopsis, this domain is called the thylakoid acid phosphatase -TAP - domain and has a Rossmann-like fold. In plants, the family resides in the thylakoid lumen attached to the outer membrane of the chloroplast/plastid. It is active in the photosystem II.	4.75983e-11
CP031165.1\|AXV05147.1\|543431_544826_+\|hypothetical-protein	gnl\|CDD\|225156	COG2247, LytB, Putative cell wall-binding domain [Cell envelope biogenesis, outer membrane].	7.18524e-10
CP031165.1\|AXV05162.1\|564860_565838_-\|UDP-glucose-4-epimerase	gnl\|CDD\|212494	cd08946, SDR_e, extended (e) SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	5.85001e-42
CP031165.1\|AXV05146.1\|541618_543220_-\|putative-RNA-helicase	gnl\|CDD\|223989	COG1061, SSL2, DNA or RNA helicases of superfamily II [Transcription / DNA replication, recombination, and repair].	1.36615e-48
CP031165.1\|AXV05154.1\|555007_556780_-\|ABC-transporter,-ATP-binding/permease-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	4.39437e-174
CP031165.1\|AXV05145.1\|539858_541406_+\|putative-penicillin-acylase	gnl\|CDD\|380277	NF033435, S-layer_Clost, S-layer protein SlpA. In Clostridiodes difficile, the S-layer protein precursor, SlpA, is one member of a large paralogous family of protein that share several cell wall-binding repeats. SlpA is cleaved into a larger and smaller protein. The S-layer protein itself is important to adhesion, and portions of it are highly variable, and then N-terminal and C-terminal are well-conserved.	2.31708e-09
CP031165.1\|AXV05156.1\|557410_557896_-\|Transcriptional-regulator,-MarR-family	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	1.06937e-15
CP031165.1\|AXV05153.1\|553672_554851_-\|Mobile-element-protein	gnl\|CDD\|225382	COG2826, Tra8, Transposase and inactivated derivatives, IS30 family [DNA replication, recombination, and repair].	4.11178e-97
CP031165.1\|AXV05150.1\|546087_546708_+\|secreted-protein	gnl\|CDD\|378440	pfam10517, DM13, Electron transfer DM13. The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme.	4.9049e-16
CP031165.1\|AXV05152.1\|548279_553643_+\|Glycerophosphoryl-diester-phosphodiesterase	gnl\|CDD\|380277	NF033435, S-layer_Clost, S-layer protein SlpA. In Clostridiodes difficile, the S-layer protein precursor, SlpA, is one member of a large paralogous family of protein that share several cell wall-binding repeats. SlpA is cleaved into a larger and smaller protein. The S-layer protein itself is important to adhesion, and portions of it are highly variable, and then N-terminal and C-terminal are well-conserved.	9.97984e-14
CP031165.1\|AXV05158.1\|558851_560246_-\|Gamma-glutamyltranspeptidase	gnl\|CDD\|223482	COG0405, Ggt, Gamma-glutamyltransferase [Amino acid transport and metabolism].	2.11717e-39
CP031165.1\|AXV05159.1\|560300_560876_+\|Transcriptional-regulator,-TetR-family	gnl\|CDD\|376024	pfam18598, TetR_C_36, Tetracyclin repressor-like, C-terminal domain. This is a C-terminal TetR regulatory domain found in QsdR proteins (quorum-sensing degradation regulation).	1.03114e-23
CP031165.1\|AXV05160.1\|561025_562483_+\|hypothetical-protein	gnl\|CDD\|225176	COG2267, PldB, Lysophospholipase [Lipid metabolism].	0.000252203
CP031165.1\|AXV05149.1\|545324_545972_-\|Transmembrane-protein	gnl\|CDD\|379389	pfam13829, DUF4191, Domain of unknown function (DUF4191).	3.21145e-82
CP031165.1\|AXV05148.1\|544868_545315_-\|DipZ-protein	gnl\|CDD\|239310	cd03012, TlpA_like_DipZ_like, TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.	6.52769e-27

>CP031165.1|AXV05153.1|553672_554851_-|Mobile-element-protein
MVRSRAKGEKRWLRLPDEVRAEVIRRARAGQGRRQILEEVDISVGSFLNVLKPFGGVLRAELATDPSPHRLSLDDRVEIRLGIGRGETYQAIADRVGRHKSSVWREVDRNGGREAYRPMLAHKRAHEQARRAKPTKLASCAELAGLVEHGLRRLWSPQQIAADLKERFGDDESMTVSHETIYKSLYVQGRGELRRELTSCLRTGRAKRVPSGRSPRPRMHDMVMISERPAEVEDRAVPGHWEGDLIIGKDGKSAVGTLVERSTRYVMLMHLDGDRTAATVRDAMTTAITGLPEHLRRSITWDQGIEMAEHVQFTIDTDVPVYFCDPHSPWQRGSNENTNGLLRQYMPKGTDLSVHTPANLNDFAESLNTRPRQTLGWKTPAAQLAQLVAPTG
>CP031165.1|AXV05152.1|548279_553643_+|Glycerophosphoryl-diester-phosphodiesterase
MKSRIVVGARGRVRLVVLMLSMVAATLLAVPPAAVAQPTLPTDFVIENVMDVSDTVLAAGMAFLPGEPLLAVAGKRGLVDLYGEDGTRHGRILDISDKVNHNNDHGLTGIAFHPDFDRADPATRLLYLWYVWDPDGLADEGSGRRISRLTSVELAPVVRDLGAGVQVQSYEVVPGSEAVVLGGAGMADPWAPTPAELEAALGPDPDCATTGGLCFPGCLNDGDPSNDADCLPTAACTDGAGYLEDCVAADDTLHAVGTLRFGPDGALHAGHGDGASASVADPRAFRAGDPDSLNGKVLRIDPATGLGLPDNPWYSGDPTDNRSRVVAAGLRNPFRFAVHPERNDLLLGDVGFSTMEEVNAGRGGTHGWPCYEGGQGENLPTFQYSGEEACQDLYDDVANGAVDITPALHAYRHDSYIPPGADPPSGGSIIGGDWFRGTGWPLTYQEGWFFSDFEDRTLSYLPAARDSGGLATGNLADAELFATDIGFVVDVQLAPDGTLWLLDIVDGSINRVRYVGEDPNRAPVISPPADQASGLGGDVNLQLLASDPDGQPVTFSVDPAGPLPPGIVMSATGRITGQPTTPGTYDVIVVASDGDRTSSSTFQWTVDTTYAPQASITSPTVEDGYAIGDMVAMTGEATDAEDGQLTGTSLEWHVQIHHNNHVHPDEASGTGASLAPFWIPDHGSNWYLTGCLTATDSSGYTDVECIDLRMDEHEYTITTDPPGLPVLLGGAQITQPTSFTLYTNQRVTVSSPLQQGALTFVGWSSGRAHTHAIVGGVSTTDVVARYVDTAAPTNQALAGTARQSTTHTYTPCGPHAASKAIDGSVAGYEGDCSISHTSKGTNQWWEVDLGGMRLVEEVRVWNWLQHSLGRLSNGHVMVSPTPFGSRTLDQLLADPTITVTSFSATVGRPTTFVEGVRGRYVRILLEGPGRELVMSEVQVIAGPLRPPVGAVSVPTGIIQRGAPAPLAAESWVDPDASSLTYAWTLDGASSAGFDDPTSATPILDTTDLTSGVHTVTVTVTDGDGQTAQASADIEIESEPLPPVAAIADPGPAVDAGTPVPLDASSSSDPQGAALTFAWDLDDDGAFDDATGATTTLDTTGFPAGTHPVAVRVTNTFGLEDTASASVAVTEPVEPADPPVAALADPGPAVAVGTVVDMDASASTDPEGGPLAFAWDVDDDGAFDADEGTTAINPVDTALLGAGDHDITVRVTSGASGLQDTATRVLSVRTPPTATIDDPEGPYEVGQQVPLDASTSTDPHGGSLAFAWDLDEDGAFDDATGPETTLDTTGFAVGIHEVVVRVTSDATGLAGEAVARIAVTDPAPGGGGGSPGGGGSPGGGGGGVPIEPEPEHADISLDLTASPREVAVDEPVVITTRVHNDGPAEAPVLLALDLGDLDLVAAPEDCRAVDGSLTCEGVRLAAGQSHELEVELSASTVGSQTVEATATVADVIDPTPDDLTASTTFSTFDAQSGGEDAISPAALAIELSQRLYRDVDGTRGEGRRQAAAVVLSRDDAFADSLTGSALTGDSPLLFTDPAQLDPATAAEIRRMLPLEGEVLVLGGEAALSAAVADELADMGYLVRRLAGPSRVETSVAIAEEVARRHDVPRQVGIARADGPSDNPTAAWADSVTAGGWAARTRQPILLTPTAELHPAVEAWLAEHGNAVPIVMGGEAALSEDVARAVGPHLRHAGANRYETAAMIAERRWDDPAGYLVTAGDHELGWAYGLAAAGLSAATNQPLLLVEQDRLPEETATALCDSRQEARVEFVGGSDVVSSSVRDAVTALC
>CP031165.1|AXV05151.1|547075_548164_+|hypothetical-protein
MSPPGQLRIARQPVADGDEVGVTIGGNDRAWLLSVEGEDPAELVGITRVTDPAGEVRYAADLRAGLLLVDDLHPRVLADEGAVGLYVASTPDEPLAEGEWRVRVATNGTTATVATAVSHDDGNPAPRQLDVVVWATVDVDVEAVAGRWRADMDAVLSPHGLGVDELDVVVAGEAGASHRVLGVDGLAGDGHKACTAADDALGPGPNTAVVVLAERIGEGVLSAAADPPRTWSMAYRNPDGDIGGFAVAAPGTPVVGPPSHACVLVSVGDDPSARGTVALHELLHIAGLPVHTSEDDGRAHDTIEDTPECTSAADGDRDGSVRADECVGLGADNLMFWAEGGHDLTAAQAWRVRWHPLLQTEG
>CP031165.1|AXV05150.1|546087_546708_+|secreted-protein
MSKPVIRAGIAAAVVVVLAVAFWLISPYFVDEVVDEAFPGEDTAAETGADADSGAFPLSDGAVVPDDMTQEEVEAEMEAAAAEDVEEVEDMPDGEPTAIVRGSFVGADSVHQGSGSATVYELADGSRVLRLEDFEVTNGPDLHVYLAPVVDGTPQINADAVDLGSLKGNVGNQNYDVPDGLDLSQELAVVIWCQPFQVTFATAVLG
>CP031165.1|AXV05149.1|545324_545972_-|Transmembrane-protein
MNQIKQIIQTFNVTRQHDPSVVPAVALGAGGALVLCLVLGFVLGPLLLWIPLALFAMIATALIILGRKAQSASLAAIEGQAGAAAAVLQSMRGAWEITPAVAFNRREDMIHLAVGPPGVVLVAEGTSPARVKQLMAKERRRFDRAAGEVPVTEVLVGDGEDQVELKKLAFHMAKLPRAIKPKEVGPLNRKLSALKASAPPMPKGPQMRRAPKKYR
>CP031165.1|AXV05148.1|544868_545315_-|DipZ-protein
MRDRRAPSLSGLDGWLQSPPRSLSQHRGRIVLVWFFSLSAPGCVEMVPALRSLWEDHRGLVDVIGVHAPQFADDADPQRIALGVARAGMPWPVAMDHRRTVFTRWHGDRSRQGWPSTHVVDQQGRVVAIHDGAGVDPIRTTVEALLDR
>CP031165.1|AXV05147.1|543431_544826_+|hypothetical-protein
MKPVLRALSILLVLSVTILGPVGAASAQIGDVVGQIPIPDLPPELEDPLTDIVDQVEDGVVGAIGDIPLDNAVQLLGDDGVEAAINLSKATFPDGMSPVAMISRSTIFPDSLSSGGAQGVLQAPLLVTAEDELDPRVVDELARLGVTQVVVLGNTSAISDSVVAQLEGLDLRVDRLGGPTRIETAVEVAAGLMPDASRAIIARAYPGDGGDDAQAYVDSLSVGPWAAEDRIPILLTQTDVLTPTLRTYLEGADITTVTIIGGEEAIAPAVATELEGLGITVERVAGVNRFATAVAVAAARGYLSVSDFDRLLLAEVDGRDDVWVPGFAAAANGGLYNGPILLTDGLILPTETIAYLVQGLPDTLADLGGAPVICTSFVNLLACEAAALLLLGALTEVQDLLGMTPLPVGDIIDIITGGDEEEDPPADEDPPADEEDPPADGEDPPAEEECLFPAPFPCVPPPGA
>CP031165.1|AXV05146.1|541618_543220_-|putative-RNA-helicase
MLRPWQRRALDALADHPHPDFLAVATPGAGKTTFALVAMIRELSRQPGPAVVVAPTAHLKIQWADAAARLGLHLDPSWSAGQPFSPDMHGIVTTYQQVASAAVDLAQRVAHGVVVLDEVHHAGDDRAWGDSVATAFQFTRRRIALSGTPFRSDTQAIPFVRYDFDEAQPDIEYGYGDALADGVVRPVYFPRIDGEMEWVSADGSHHAASFGDALDRTLTAQRLRTALSLHGEWLPSVLVRANSALMKVRRTHPDAGGLVIAIDTEHASGIVRLLRERCGVRAVVATSDDPDASDRIANFSRSADPWIVAVRMVSEGVDIPRLRVGVWATTTATELFFRQAVGRLVRVTPDTRGARSMMFLPDDPRLRAHSMGISEARRHLLKRKEEQEEDLLADPLEAMMVEEGEQISLFQAVAATASDNGSSEEPEWFTADPFPAADQEGVPLTLFPPPTPGGKVPQVGEDGLPIQAMHVTKATLRKRNADLVRLLVRRANMDHKAVNLELNRLSGIKRISDATADQLEQRLEAGEKWLTRL
>CP031165.1|AXV05145.1|539858_541406_+|putative-penicillin-acylase
MKRFPFVAGVLGAALIAGPVSAQLPLVPEIPIVDPILDPVLDPLDPVLDPVLDPVDDLPLPDLPGLPTDPTDLIDDPTGILGDLTDILDGLGPILEPADPILDPVTDIIDQLDGIITDVLADVILSNLLALKGEDAVDASIAFSQATYDASDTAIIARDDVFADALTTGALQGIFDAPLLLTGSSDLDSRTARELVRLGVERLVILGADSAINPLVVQKLEIAGLDVTRVGGPSRVETATLAAAETAPNATTAVMTRAYSADGDDSQAYADLLAVSPWAAENDWPVLLTQTDTLTPSVASYLTDSSITDVVIIGGETAVSAATQQAVEALGVTTRRVSGSNRYATAVAVANERGFANSGDADRLILAEGTSSRTDVWAPGFASAAHGATHRAPVLLTSGDVIPAETMSFITEGLEANLADGGPATICASFVSPIACEAAGLLLLGDLLDATDLLGLDLTDLPLVGDLLDVIEQVTGVELPDLDGLLGDPLGGVDGGAGGLDPVTDVVGGVLGGGN
>CP031165.1|AXV05144.1|539714_539858_-|hypothetical-protein
MWAHLWRSGSDCGTRCRTTSTACDPMVFQPHVESYPPFRPSFGAQTD
>CP031165.1|AXV05154.1|555007_556780_-|ABC-transporter,-ATP-binding/permease-protein
MNPLLRLWHHATDHRRRIVFAVITSILNKLMDLAPPLLIGAAVDVVVRQDDSFLADAGIATVRGQVVTLAVLSAIVWILESIFEYLYAVAWRTLAQRVQHDLRVEAFAHVMSLDQSVFADASTGSLMAILNDDINQLERFLDRGANEILQVAVTVLVIGGGFFVVAPDMAWWAVAPIPFILVGSMRFQRLLEPRYARVRERVGDLNATLAGALGGVATIKAFTAEPREIARVEAESQAYVDANDEAIRPSSAFIPLIRMAILFSFTAILVLGGFRAIDGTLEVGVYSVMVFVTQRLLWPLTELGEVFDQYQRAMASTRRVLDLLYSAPEIVDGPLRLDGPVRGDVALHDVRFAYPDGGVVLDGVDLTVPAGEMHAVVGSTGAGKSTIARLLLRLYDVTGGAVTVDGIDVRELHVTDLREQFGLVSQDVFLFHGTVADNIAYGAPGASHEEIVRAAKLAEADEFVAALPQQYQTVVGERGQKLSGGQRQRIAIARAILSDPPVLLLDEATSAVDNETEAAIQRSLAHVSQGRTTIVIAHRLSTIVAADRIHVLDRGRVVESGTHDELVSTGGRYAKLWAVQTGQPAVDLTT
>CP031165.1|AXV05155.1|556853_557258_-|hypothetical-protein
MSTALLRPYMRGAVHTVQRTGDWPRSFVVTLTDDHGQRCRAEYTLHTEGSALFTLEATRDNAMVDPPVVGWVSWSDGEVVCAFRDAASGTHGGGFLPDCAPVEDGPFQTTSFDVGRWIVLAQELLRTVEDSRLT
>CP031165.1|AXV05156.1|557410_557896_-|Transcriptional-regulator,-MarR-family
MSNTTTEPRWLTADEQVSWRAFVTAMTMLSRQLNAEMLSAHDLSMDDYAILAMLSEAPEGRLRFGELADVLRVAKAHITYRFRRLEERGLVERQACATDARGAYAALTADGRSRIEAAAPTHVESVRQHLLDHLTPEQLRVMGEAMTAVVEAECAETPHRH
>CP031165.1|AXV05157.1|558015_558840_+|hypothetical-protein
MIGPAHVLRVPQLAFVLGGLLVLCGSILCTGTALASTIGDAADNLNDGVFVASGSGQDPDALRGVVAEYADEERVVIAVFAGGLPPTPVDRANDLLRVVAADTVLLFTPDDVAVASTLHTTEEVDAAFDRAGQAALDSDAAVASRALLDALDHRPTPIWVWLAVAAALVGLVVLIAQLLDRRREQAGAQRSFDAEQARLRSRLQTLADRILQAEAHVTIADDPALEATLTEATGIYQDVLWSLERVNTLERLATLHQPLEQAEALMDRIADRTG
>CP031165.1|AXV05158.1|558851_560246_-|Gamma-glutamyltranspeptidase
MPPPLARPTTSLSGGVGVAAHSPATAAAGMALLDAGGTAADAAVGMTLAACAVEPFVVSLLSGLHGIHVDVDGTTRAVDGFVDVPAVPTGGRRAETTIDFGGARMPYSIGGATFGTPGLVAGCWHLHRRFGRLPWAEVVAPAIEWAGTGFVLSDRDESLLHMLEPVMTLGVGREVFCIDDRMRVEGELVRIPDLADALRQIAEEGGPTLYEGAMSRELATFAEEVGALVTAEDLGACTAVEHTPPTVRLGGWQVRSRRGLSPLTDWVARLDASDGPHAARLALAQSPTPPKALGTTSLAATDADGRACAVTASLGLGTGDWFRGSQLNSMLGEVDLLVGGLRPRTRMGSMMAPTAVVSPTGQATVLGAAGGSRIPSALLRTIDGIVLGELDATAAVDLPRIHRVGELVHVEPHLEDRDEAALVAAGFTVQRWTSRHHFFGGVSVAGAAGTEGDPRRGGVGLAHR
>CP031165.1|AXV05159.1|560300_560876_+|Transcriptional-regulator,-TetR-family
MLMSRVISYSDAYIAARRQFMASGDVDMKALAEELIVGRATLYRVVGSRDRLLGRIVADLAAVTQSQAVEAAASEHPPSVERIVQAAYRMNRDVVAFRPLRQLVTNDPETAFRVLFTEIGGVHAASVASWSALMDATARDGGFALPRDTDRLAYMFVRIGESMIFADLLHSHEPDLELARDLHRALLTLPA
>CP031165.1|AXV05160.1|561025_562483_+|hypothetical-protein
MRRPPIRLFLCLVLVLLLAAPATAADDYTDPEYRTHEADNLTRGRGMQLYQLATPAYHRAFVAASADSLARAQGHQLADATHGRAYVGASQYMSTWGVGNAEDYFDVTPREIAFVSQTGAKLYGHIWGSELPGPRPGVVITTGSIQGSNQMYWWAARALTAAGYVVMTYDVQGQGQSETFGHEPGSIAPTTEGVPFQQSFNFVQGTIDAMRFFLSTPDDPYVPATWTADDVVSQQASSDGERMDWVNPAWAVLDGDNIGIAGHSLGASAVTVVQQCSDESDRYLEVPDCHGESYPIRAVVGWDQLGTTDYEPVVPGMNQAADGYFLSPTPSPTAPDPDETLAAHTAWTAAGIDTYTVVVRAGTHLEWSQVAYHGPATRYGEALAAYYTVAWMDRWVPEDPTRNAVAYRALVEGPRPDDEAAPSSAAYMSVRRRGAFSLTDPTALAQDPDTAQAMEVVDLRDWAGRSAVGDWAGANADTVGAVLPD
>CP031165.1|AXV05161.1|562528_564844_+|hypothetical-protein
MTRLASLLLLLGTLVLAAAPVALAASSCGGVVQDGDDLLTPAEEEEVLAAAERLAAAGVRPLVVVTSTLSGTDAEAALEAIVEGCPGLTDGSGEWGANVLAVLVAPEDRETAIYEGGGLPALDVTETDVDLDVMNPRFAEGDLAGGLIAGLDRMAAIQQAEVDEATTDDGSTGSGGWFAGGVGATVLAGGGAALAARARTARRRREEAHARAVEAQADVAQTILDMERDVEVAALDANALADRLALVEATPLRQQLTTIRGTVQSVVTRWYALTQQVDATPSGDAIAYDRVAGEITELAPTARHARELVAGFATDVAALVAVEEGIPGRLDALGSRHEAARSAIADAQHRGYRTDPAEADLSVSIAALGRARDAHGQRLVRGADEHLDLAEAAVTEAIEWVEGIEEMRAALADDLSSLRARRQVLEDRVGPAGTTMESLEARWATAAWEDVAGNGSEAEAELSRAADALQAAEHAQLMDVQDWDEAHDALDAAEDDLDDAAALLDAIHARDAALQEAADLAPSTIAGATAAVDEAAGFARQHSADVSDPIESRIAQLSSLVDQVEAAMAEDRPNPAAAVAAAGQVQAEVTELLATARQEVTAADMARRRADQTVASARQELQQLQRYATGHRRYVAAGSARALQDIGDRLARLDAVTDPVQRATQAAGLQRELIGLSDDIRRSVRRATAPRPSPYGPGRGGGYGGGLGGVFGTSGPRRSSGGFGGGFGGGSSSRGSSSRSRTGSSSRSRSGSSSRSRSSSGRSRSGRSSRW
>CP031165.1|AXV05162.1|564860_565838_-|UDP-glucose-4-epimerase
MAPFFVEAGHDVTGLDTGYFAESVMGDPLPPLPELRKDLRDVEPGDLEGFDAVVHLAALSNDPVGSLEPQTTYDINHHASIHLAECARAAGVGRYVYSSSCSIYGKSGGAGALDETAEFAPVTPYAESKVRVEAELFELATDDFVCTSMRNATAYGWSPMLRTDIVLNDLVGWAYLTKEIKVLSDGTPWRPIVHIEDISRAFLAAVEAPAAQVQREAFNVGRDDENYQVSEIAGFVKEVVPEATLSITGEAGNDPRSYQVDFSKIGRHLPAYQPAWTALKGAEQLYEAYQRLDLTMDTFQRLYKRLPILKQHREQGLLDDMLRWT
>CP031165.1|AXV05163.1|565955_566435_-|hypothetical-protein
MADLAKKILKHAAETLEPGEQVLETAIVTPRGAMARQAVAGGVGGVVGLGVAAAMDKKRRDIAPEAPEGTWADQFPKRKVFLSVTDRRLVVHAFGEMMGRPKELLGWVPREVVHAVQMEKAKLAHKGTLWFSDGSAYEIDVARAGGEPDRLGRALGLHP

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Crispr_ID: CP031165_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_6

766565-766758

Orphan

Consensus_repeat	Method
CCCCAACGTGTGTCGGCCAATCACGACGGGTGGCCGCTTTTCCGACAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_6

>merge|CP031165|6|766565-766758|CRISPRCasFinder
CCCCAACGTGTGTCGGCCAATCACGACGGGTGGCCGCTTTTCCGACACGCGTCGGTGGGGGTGGCCGGCCCGACCCCAACGTGTGTCGGCCAATCACGACGGGTGGCCGCTTTTTCGACACACGTCGGTGGGGGTGCCCGGCCCGACCCCAACGTGTGTCGGCCAATCACGACGGGTGGCCGCTTTCTCGACAC

>CP031165|6|6|766565-766758|CRISPRCasFinder
CCCCAACGTGTGTCGGCCAATCACGACGGGTGGCCGCTTTTCCGACAC	GCGTCGGTGGGGGTGGCCGGCCCGACCCCAACGTGTGTCGGCCAATCACGACGGGTGGCCGCTTTTTCGACACACGTCGGTGGGGGTGCCCGGCCCGA
CCCCAACGTGTGTCGGCCAATCACGACGGGTGGCCGCTTTCTCGACAC

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV05327.1\|759682_760918_+\|Ribosomal-protein-S6-glutaminyl-transferase	unknown	unknown	gnl\|CDD\|182468
CP031165.1\|AXV05340.1\|777986_778784_-\|Glyoxalase/bleomycin-resistance-protein/dioxygenase	unknown	unknown	gnl\|CDD\|319911
CP031165.1\|AXV05332.1\|766095_766509_+\|NADH-dehydrogenase	unknown	unknown	gnl\|CDD\|237999
CP031165.1\|AXV05329.1\|761429_763268_+\|Long-chain-fatty-acid--CoA-ligase	unknown	unknown	gnl\|CDD\|223953
CP031165.1\|AXV05334.1\|768322_769282_-\|putative-beta-lactamase	unknown	unknown	gnl\|CDD\|293840
CP031165.1\|AXV05333.1\|766761_768306_-\|Salicylate-hydroxylase	unknown	unknown	gnl\|CDD\|236158
CP031165.1\|AXV05339.1\|774080_777809_+\|putative-penicillin-acylase	unknown	unknown	gnl\|CDD\|376618
CP031165.1\|AXV05325.1\|757022_758060_+\|putative-phosphotransferase	unknown	unknown	gnl\|CDD\|270703
CP031165.1\|AXV05338.1\|772733_773960_+\|Acetyl-CoA-acetyltransferase	unknown	unknown	gnl\|CDD\|235741
CP031165.1\|AXV05326.1\|758100_759609_+\|Serine-hydroxymethyltransferase	unknown	unknown	gnl\|CDD\|234571
CP031165.1\|AXV05337.1\|770574_772509_+\|Metalloprotease-MEP2	unknown	unknown	gnl\|CDD\|366930
CP031165.1\|AXV05328.1\|760980_761229_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05341.1\|779016_779520_+\|general-stress-protein	unknown	unknown	gnl\|CDD\|379804
CP031165.1\|AXV05330.1\|763383_763971_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|99749
CP031165.1\|AXV05342.1\|779516_780473_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274645
CP031165.1\|AXV05323.1\|755530_756220_-\|Methyltransferase-SCO0408	unknown	unknown	gnl\|CDD\|379312
CP031165.1\|AXV05324.1\|756227_756965_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|213772
CP031165.1\|AXV05336.1\|769764_770502_+\|3-oxoacyl-[acyl-carrier-protein]-reductase	unknown	unknown	gnl\|CDD\|235546
CP031165.1\|AXV05335.1\|769281_769614_-\|AclJ	unknown	unknown	gnl\|CDD\|281995
CP031165.1\|AXV05331.1\|764052_765891_-\|Intracellular-serine-protease	unknown	unknown	gnl\|CDD\|173810

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV05327.1\|759682_760918_+\|Ribosomal-protein-S6-glutaminyl-transferase	gnl\|CDD\|182468	PRK10446, PRK10446, 30S ribosomal protein S6--L-glutamate ligase.	9.54116e-100
CP031165.1\|AXV05340.1\|777986_778784_-\|Glyoxalase/bleomycin-resistance-protein/dioxygenase	gnl\|CDD\|319911	cd07247, SgaA_N_like, N-terminal domain of Streptomyces griseus SgaA and similar domains. SgaA suppresses the growth disturbances caused by high osmolarity and a high concentration of A-factor, a microbial hormone, during the early growth phase in Streptomyces griseus. A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) controls morphological differentiation and secondary metabolism in Streptomyces griseus. It is a chemical signaling molecule that at a very low concentration acts as a switch for yellow pigment production, aerial mycelium formation, streptomycin production, and streptomycin resistance. The structure and amino acid sequence of SgaA are closely related to a group of antibiotics resistance proteins, including bleomycin resistance protein, mitomycin resistance protein, and fosfomycin resistance proteins. SgaA might also function as a streptomycin resistance protein.	9.7593e-35
CP031165.1\|AXV05332.1\|766095_766509_+\|NADH-dehydrogenase	gnl\|CDD\|237999	cd00038, CAP_ED, effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels.	6.35712e-17
CP031165.1\|AXV05329.1\|761429_763268_+\|Long-chain-fatty-acid--CoA-ligase	gnl\|CDD\|223953	COG1022, FAA1, Long-chain acyl-CoA synthetases (AMP-forming) [Lipid metabolism].	5.31591e-169
CP031165.1\|AXV05334.1\|768322_769282_-\|putative-beta-lactamase	gnl\|CDD\|293840	cd16282, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	3.52394e-59
CP031165.1\|AXV05339.1\|774080_777809_+\|putative-penicillin-acylase	gnl\|CDD\|376618	pfam01804, Penicil_amidase, Penicillin amidase. Penicillin amidase or penicillin acylase EC:3.5.1.11 catalyzes the hydrolysis of benzylpenicillin to phenylacetic acid and 6-aminopenicillanic acid (6-APA) a key intermediate in the the synthesis of penicillins. Also in the family is cephalosporin acylase and aculeacin A acylase which are involved in the synthesis of related peptide antibiotics.	1.14304e-34
CP031165.1\|AXV05325.1\|757022_758060_+\|putative-phosphotransferase	gnl\|CDD\|270703	cd05154, ACAD10_11_N-like, N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins. This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).	1.61671e-90
CP031165.1\|AXV05338.1\|772733_773960_+\|Acetyl-CoA-acetyltransferase	gnl\|CDD\|235741	PRK06205, PRK06205, acetyl-CoA C-acetyltransferase.	0
CP031165.1\|AXV05326.1\|758100_759609_+\|Serine-hydroxymethyltransferase	gnl\|CDD\|234571	PRK00011, glyA, serine hydroxymethyltransferase; Reviewed.	2.91179e-75
CP031165.1\|AXV05337.1\|770574_772509_+\|Metalloprotease-MEP2	gnl\|CDD\|366930	pfam02128, Peptidase_M36, Fungalysin metallopeptidase (M36).	0
CP031165.1\|AXV05333.1\|766761_768306_-\|Salicylate-hydroxylase	gnl\|CDD\|236158	PRK08132, PRK08132, FAD-dependent oxidoreductase; Provisional.	3.80843e-176
CP031165.1\|AXV05341.1\|779016_779520_+\|general-stress-protein	gnl\|CDD\|379804	pfam16242, Pyrid_ox_like, Pyridoxamine 5'-phosphate oxidase like. This domain, approximately 140 residues in length, is mainly found in general stress proteins in various Xanthomonas species. It is composed of a six-stranded antiparallel beta-barrel flanked by five alpha-helices and can bind to FMN and FAD, suggesting that it may help the bacteria to react against the oxidative stress induced by the defense mechanisms of the plant.	2.25038e-48
CP031165.1\|AXV05330.1\|763383_763971_+\|hypothetical-protein	gnl\|CDD\|99749	cd06260, DUF820, Domain of unknown function (DUF820). This family consists of hypothetical proteins that are greatly expanded in cyanobacteria. The proteins are found sporadically in other bacteria. They have been predicted to belong to the PD-(D/E)xK superfamily of nucleases.	1.1122e-21
CP031165.1\|AXV05342.1\|779516_780473_+\|hypothetical-protein	gnl\|CDD\|274645	TIGR03557, F420_G6P_family, F420-dependent oxidoreductase, G6PDH family. Members of this protein family include F420-dependent glucose-6-phosphate dehydrogenases (TIGR03554) and related proteins. All members of this family come from species that synthesize coenzyme F420, with the exception of those that belong to TIGR03885, a clade within this family in which cofactor binding may instead be directed to FMN. [Unknown function, Enzymes of unknown specificity].	1.33759e-125
CP031165.1\|AXV05323.1\|755530_756220_-\|Methyltransferase-SCO0408	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	6.97049e-17
CP031165.1\|AXV05324.1\|756227_756965_-\|hypothetical-protein	gnl\|CDD\|213772	TIGR03081, Methylmalonyl-CoA_epimerase_mitochondrial, methylmalonyl-CoA epimerase. Members of this protein family are the enzyme methylmalonyl-CoA epimerase (EC 5.1.99.1), also called methylmalonyl-CoA racemase. This enzyme converts (2R)-methylmalonyl-CoA to (2S)-methylmalonyl-CoA, which is then a substrate for methylmalonyl-CoA mutase (TIGR00642). It is known in bacteria, archaea, and as a mitochondrial protein in animals. It is closely related to lactoylglutathione lyase (TIGR00068), which is also called glyoxylase I, and is also a homodimer.	4.10106e-09
CP031165.1\|AXV05336.1\|769764_770502_+\|3-oxoacyl-[acyl-carrier-protein]-reductase	gnl\|CDD\|235546	PRK05653, fabG, 3-oxoacyl-ACP reductase FabG.	4.36492e-102
CP031165.1\|AXV05335.1\|769281_769614_-\|AclJ	gnl\|CDD\|281995	pfam04075, F420H2_quin_red, F420H(2)-dependent quinone reductase. This family of proteins is found in the genera Mycobacterium and Streptomyces. Member protein Rv3547 has been characterized as a deazaflavin-dependent nitroreductase. Rv1558 is an F420H(2)-dependent quinone reductase involved in oxidative stress protection.	3.54998e-40
CP031165.1\|AXV05331.1\|764052_765891_-\|Intracellular-serine-protease	gnl\|CDD\|173810	cd07484, Peptidases_S8_Thermitase_like, Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.	1.74446e-76

>CP031165.1|AXV05332.1|766095_766509_+|NADH-dehydrogenase
MFRRRDPKTDVIRRLPAFADQSTRRVADASKVLDLVTVEAGHTLLTQGDLGHEFYLVVEGRARVERDGQVIAHISDGAVIGEMALVGAGRRNATVVAETEMVLATSTRPYFAGLVAEFPGFGRQVRQASEARTAVPA
>CP031165.1|AXV05331.1|764052_765891_-|Intracellular-serine-protease
MNRPFLPSFLACLLLLALVTPAAAEDAPADDQRGEEQPASLIIGVEGDLPAAVGALEAINGLEVVHVSPQGAFVAVEVDGLRALRLASTAVPGVAYVEEDETRYSQAIPNDARYGDQYGPEMMGAEEAWGAVGYGDTSISVAVLDTGTRHGHQDLTPTSRFSATQVYTGNSSDNCGHGTHVAGTVGATTNNGIGVAGMSQAQMMTYKVLDATGGIFNIQCSGSTSSIAQAVYDATDDGADIISMSLGGGGYSQSFENAIDYAWNNGVVVVAASGNDGASNGVSYPAAYDNAIAVGALDADKGKASYSNAGDELDVVAPGSSVLSTYNSSNSSYSSLSGTSMATPHVSGALALAWSCAPSGTTNADVRNAMESTAEDLGANGWDRSYGHGLVRVDLMVDVLCDGGTGGGPTNTAPTAAFTTTTDELTIDVDGTASSDADGDALTHSWDFGDGSTATGATASHTYAADGTYTVTLTVDDGTDTDTTSTTVTVEASDPGGDPDPSTPNLTSGQTVQVSLSGSGDEAFYKIAVPAGANSITVSIDGPSCGLFGCSFDADLYTRDAARPTDSAWDCRPYQGGSDETCTDTSPTAGYLYVRVDAYSGSGTVDLTATVS
>CP031165.1|AXV05330.1|763383_763971_+|hypothetical-protein
MDMETAGAELPDEVRRITRAEFNAMGDAGLFEDEQVELLEGVIVSMAAEGGPHVKAVMWLTNHFARMLSDDVMVGVSHPYAASDYSQPQPDLAVVDVDDVRRITDGVRGARLLVEVAVSSRRRDLVTKVRVYATAGIEEYWVADLVDEVVVVHRRPTEGAYVDVTRHGTGDVVRACGVDVPLADLFAFVDRGRDA
>CP031165.1|AXV05329.1|761429_763268_+|Long-chain-fatty-acid--CoA-ligase
MSLQISTLAQLLHARADASPNGVAIRTKGNGSWEDRTWAQVRDRADRIAAGLLTAMDLEDNDVVGLLGQTSEAWVTCDFAALSVGLQTVPIYASLHPEEVGYAHVDTGIKLVIVDDASQLEKIRTMRKGFTFFETDYSADQLVLQHVIVIDPTGIDPADDWESLADVEARGKEKLDELREEMTRRREAASPDQTATYTYTSGTTGPPKAVIQTHDNHLAMARAAEKSALLDDDMRAGGLFLFLPLAHSFGRLIQFSAPYMDLPLIISAVATLADDARETRPGFFPAAPRVYEKMKSKIETTVAGSPPARQKIFGWALGVGRQTVPFRTQGKELPLLLKLQYAVADKVVLSKLRALLGMDRTKALLSGSAPLDAEVHTFFLALGLDLIEAYGLTETCPGLTSNLPGDMKVGTVGKALPGVELKIANDREILAKGPNITQGYLNRPDATGDAFDDEGWFHTGDEGSIDADGFLKITGRKKELIKTSGGKYVAPAKIEGSLKLLPIIQEAVVIGDTKNYCTALISIDPEELEEWAKQQGIAPSQDAPEVAKAIEAHVAKVNGDLASFETIKYWSLVPEPLSVDNGFLTASLKVKRNVVHDAYADLIEDMYDGKKK
>CP031165.1|AXV05328.1|760980_761229_-|hypothetical-protein
MPQPLPDVPDADPDATVDPAWSDLRTNAALPSWYQPAAMPTQVAGWRRAAAWTVVVMLVSSASAGLCLTYGPDELWRFLGIG
>CP031165.1|AXV05327.1|759682_760918_+|Ribosomal-protein-S6-glutaminyl-transferase
MKLGILSRSPNAYSTQRLKIAALERGHEAKVLNTVRFGIDLTGGEPDLQFRGRHLSDYDAILPRIGASITFFGLAVVRQFEQMDVYTPNTAAGIANSRDKLRSIQILSRHSIGIPRTMFVRDRKDVPSAIKAVGGAPVVIKLLEGTQGIGVILAPDNKVAEAVVETLQSTKQNVLIQQFIAESRGKDVRALVVGDRVVAAMRRVAQGDEFRSNVHRGGRTELVDLDEEYERVAVQAAQIMGLRVAGVDMLESDHGPLVMEVNSSPGLEGIEGATGLDIAGAIVDYIASQVDFPELDVRQRLTVSTGYGVAELVVREGSPMVGKSITETDLRERDISVLTLNRGTKVIPNPRGNRVLEAEDRLLCFGRLDEMRDLVPARRRRRSQPKVQPLPDEPLHEVEDHSHDDNGNGDD
>CP031165.1|AXV05326.1|758100_759609_+|Serine-hydroxymethyltransferase
MEAATPFDAALLELTRAWKVRDDLRQQGNTDHAAIRAAWLELDRARLWIRKVTDPLMWRYEHAVDPRTWLPPSAADRVAAISADAHRLEVDGIARRLDALVQRDRDIHDHEAVNLDPAANTMNPAAEAMMARGLGSRPSLGYPGAKYETGLEAIEEIEVLATNLVREVFGATFAEVRVPSGAIANLYAFMATASPGDAVIVPPASIGGHVTHHEAGAAGLYGLEVHHAPIDPDTNSVDTAGLAALARRVRPSLITIGGSLNLAHHPVAEIRRIADEVDAKVLFDAAHLCGLIAGHAWPNPLQQGAHLMTMSTYKSLAGPPGGLVVTNDPALAERIEAIAHPGLTANFDAGKTAAMAITMLDWLVHGRQYAADMVTAAADLARGLEAQDLPVHRPAGQLTQVSHQLALDARALGGGTAAAQHLRRANLLTSAIGLPIPSIEGDANGLRMGTPEIVRWGISGAAIPQLAAFIGQAWRDDDPARLAPKVARFRSEFRRIRYIRDR
>CP031165.1|AXV05325.1|757022_758060_+|putative-phosphotransferase
MSDAHGVPLDVDALEGWLTDRVEVTPPLTASQISGGRSNLTYRVADADGRTFVVRRPPLGDLLPGAHDMSREARVMSALADSDVPVPEVIGYEGDESIIGGTFYVMRHVDGLILRTTEDGASIDEAARATATRSLASTMAELHRIDPYEIGLVKPGRGDNYLARQLHVWKRQMDAQKGRELPVADAVHDRLTAAIPEQPATAIVHGDYRVDNVILDPDGTVAAVLDWELWTAGDPLADLAITLVYWGDDSVPDALIGRPTGHPGYGTGADFVRAYVDAGGIDVPDDVLPYYMAFATWRLAAILEGVYQRNRAGAYGDADDGWRMFEEKVTDLFDMASGYADEAGI
>CP031165.1|AXV05324.1|756227_756965_-|hypothetical-protein
MTTVTYPRGMPLTEAVLDHVAIAVDDVDAAVSHWLGRGAVPVGGGEAPAFRSEQVRLGNGAKLELIGRTTGEPSFIDGYLERFGPGRVHHVTIKVGTSLAQAIEELDAEGIQTVDRNESYPHWHEAFVRPSVVGGMIVQIAWASGTDADFAERSGRPAPQSPDPAAPHLLALQMTHVDPPAARALWSAVGATVTDDGNGGFEAQWSASPMVVRVALGERSGPVGLVVPGLAPGERTDVAPVLLGV
>CP031165.1|AXV05323.1|755530_756220_-|Methyltransferase-SCO0408
MWPAEEFGEEWADVYDAVFADLDTDAKQAVAALTADLAPRTRVLELGVGTGRLAIPLAAAGLHVTGVDSSARMLARLGAKDGGDRVVGVLGDMADPPVAGPFDLVLIAFNTLFALPDQDRQVACLGAAGRLLVPGGRLIVEAAVPQPWRFADGDHDPVAQTVRSVRVVTDDATVRTLPLNMRYAWPSEIDLMARLAGLARVRRSCGWADEPFDDASTRHVTTYQKDQTT
>CP031165.1|AXV05333.1|766761_768306_-|Salicylate-hydroxylase
MVIAGGGPVGMTTALLLARHGVPSVVLEAEPLATRVGSKAICFQRDVLDVLDRVGVAQQAVAEGVTWRTGRTFYRDLELKVVELPSTGPEALPPFVNLSQSALEGYLMDRVDAEPLVDLRMGCRLVGLSSDDGGVAATVHTDEGSAQVEGAWLVGADGARSTVRQAIGASFEGETWDDQFLIADIEADLPFPAERRFHFDPEWNPGRQVLVHQQPRSIWRIDWQVPADFSLEEARSSGELDRRIRQIVGNAPYRIDWVSVYRFHQRIADPWRRDRVFLAGDAAHLMSPFGARGLNSGIQDAENLAWKLAFVERGWAGPDLLDSYAAERIPAARENLRVTGDTMRFIAPRAEEERRHRVDTLDRAVDDPSARASIDSGVLAEPFWYVDSPLTTPAGDLGGFPVDAGVPRPPVPGVLCPDGPVGGGRLRERFGDGIVLLAFGEDAEAVAARCGAEVGATGVGVTTLRFEPRSTVGRALEVVGDCVVVIRPDGHIAARLLLPCMGLVDAVRRCLGHP
>CP031165.1|AXV05334.1|768322_769282_-|putative-beta-lactamase
MAKPFASEADTAAKDEVLEVIGEGVYALTAGGDPTVGAIEGDDFLVCIEARATPHMADKWLAQLREHTDKPVRYLVLTHYHAVRTLGAAAFDADVIIAHDLTRALIAERGQQDWASEAGRMPRLFEGAETIPGLTWPDVTFSDTLTIPLGGARGSLELRYCGRGHTEGDLVAWLPAQRILFAGDLVESKAALYTGDAFHTDWSTTTLDAVADLGASTLVGGRGEVAHGEDAVAAAIEQTRDFLMVMRREVGAVHRDGGTLPQAFEAAHAALFEAYGHWPIFEHCMPFDVARLWDELDGIERPRIWTAERDREVWAELQG
>CP031165.1|AXV05335.1|769281_769614_-|AclJ
MPVIVLTTAGRTSGNLRKSPLMRVVHDGDYAAVASVGGAPEHPAWYHNLVAHPACTVQDGPTISDRVARELEGAEREEWWARCVEAFPDYAEYETRTDRIIPVMLLERDD
>CP031165.1|AXV05336.1|769764_770502_+|3-oxoacyl-[acyl-carrier-protein]-reductase
MGLLEGRVALITGGAQGIGLAIAQRFSDEGAQVVIADMREDAAVEAAGTLSGEATGVRANVTDPEDVTGMFEHAIEAFGRVDVLVNNAGITRDASLKNMTLEEFEQVIDVHLKGTWLGLKEGLARMKAQGEGGSMINMSSISGKVGNFGQSNYAAAKAGIVGMTKSVAREAARANIRVNAIQPGLIATEMTAAMPKEAYEAAEKAIPLGRAGQPDEIAKVALFLASDLSSYCTGITIEVAGGRHM
>CP031165.1|AXV05337.1|770574_772509_+|Metalloprotease-MEP2
MQEFLTVVSKGGAHPPSERTGDPLSKIRTLLAAGLVLAMAMMLSPAGAQDTGAADLTAQAALARTHLGGTDELSAADVAGSIVTDAYTDAHNGVTYVYLRQTVDGLPVLGAEATVNVLDGEVLLSGHHFVLDVADNATGEQALSAEEALAAGALAVDADPMQASGAELVYQALASDSARLAWNLDVETATSWWNLSIDAETGEVLAQYDRVAQDTVHEITARTVRQDDTAAAAAVIDPILPRDRADDGSSYNVFPMPMENPNDGPRVIVENPADARVSPFGWHDTDGQPGPEYTVTRGNNVNAYADTVPDNIPDPLSQPSGGDGLDFDHPLERYDLTPLAYRDAAVDNLFYWNNIMHDVTGVYGFTEEAGNFQVHNYTGKGAGNDAVEAQAQDGSGVNNANFGTPADGSAPRMQMYIWPDTGETRDGDLDAGIIAHEYGHGVSNRLVGGPSNVSCLGSHDERQGEGWSDYWSYVLTMRDGDDGATPRGVGTYVLHQENRSGAGIRITPYSTDMTVNPTTYDRVKTAAEPHGVGYVWATMLWDLYWNLVDEHGFNPNVYDGWETGGNNLAIQLTVDGMKMAVCQPGFVDARNAIIAADAALTGGENECLIWSTFARRGLGESADQANPASKTDGTEAFDVPAACE
>CP031165.1|AXV05338.1|772733_773960_+|Acetyl-CoA-acetyltransferase
MGELRDAVICEPLRTAVGGYGGMFRDVPVTDLASTVIRALVDRTGVDPAEVDEVILGQGYPNGEAPAIGRVAALDAGFPVEVPGLQLDRRCGSGLQAVVDAAMRVQTGVADLVVAGGAESMSQAEHYVLGARWGLKGRPAGFEDRLARGRVTAGGQYHPVEGGMIETAENLRRDFAVTREAQDELAVRSHDRAVAAQKAGRFDDEIVPVSVPQRKADDLVIDTDEHPRPGSTVEKLAGLRAIMGRQDPDATVTAGNASGQNDGAAVCLVTTRETADRLGLRPLVRLVSWAVAGVRPSHMGLGPVPATAKALDRAGLTLADMDLIELNEAFAAQVLAVTSEWGFTDADWDRTNVNGSGISLGHPIGATGARILATLTREMDRRQVRYGLETMCIGGGQGLAAVLERIEA
>CP031165.1|AXV05339.1|774080_777809_+|putative-penicillin-acylase
MLALPVVLAMALLASLLAPTADAQDDPPLDGRFQQNGDAGGFLNIMPPGADGVLNTLEILAAQAGQLPEHYNDQTAMYETLVYEGGLPVDGDHGEPLLGVTDGDLERFFKDGSFGADGDVVEIDVSACGDDVIAFRDTAFGVPHIYSSDRTQAQCANGYATAEDRLFLMDLLRHIGYARMSEFLGASEANKAMDRGQLLVAGYDEDDYIAQEAALCDSSDPERRQICADGTAYIEGVNHYVAAVRTNPMLLPGEYPALQILPEDFVLRDILSIASLVGGIFGKGGGNEAANSMFMADLIDQHGDAEGRAIFDDLKAANDPDASLTIQDSFPYNNPTALDETTTALLEPGSFVPAFEGGIGGVGVPGTVQARSGWPTSDTVNLGVVDGPFGPIDLRTPLGMSNAILATADVTDSGVPIAVFGPQTGYYTPQLLVETDIHAPGLDARGTAFAGTNIYVQLGRGGDYAWSATSASGDLVDEWAIELCDPDGGEATIDSTGYVWDGTCAEIPVLTHTQVAKPTAGGIPDPPVVDSIVFTLELGRIPELNDAAIVGRALATDGTPVAIAEQRSTFKDELGSAIGFMRINDPDFMTDGVESFNRAFDGIDFTFNWFYIDGEDIAYRHTCLCPIRQDDTDPDLLTWGGRGHQWTGAFLQPAGQPQDVNPEEGFYANWNNKQAQDFRSQDDTWKHHSTDRREHLAVRMEAAMASGQALTRGDMVNIAEDAGTVDFNPQEIYGLALEIMGTEPPAVLGGDADLASSMRSILQDWVDVGGHRRDLDRDSIYDHAVAVSIGDAWVRPMIEAVLGDEVPLETWPEGVEDHPRGGIGSAYNSGRMRFLQKDFWQVLDMPMREERSRTYCGTGTRADCSEVLWQSLADAIDVLSTTYEGEEEPPCGFPEAYHFGSTTPTEWVYPADCDNIVQGAAGVVAAPSMRWVNRPTFHQVVESGTITGRIAGADRIATSAAASRHAFPDGAETVVLAAAGTFADAVAGTPLAAANDAPLLLTDSGQLSPASEREIVRLGATTAIVLGGTAAITETVVSRLEVIGVSASRVAGDSRYETALAIAEELEVTDRFVLANAGSFADALAAGPFAAADDRAILLTDTDALPDDVADALDGADVVIAGGSAAVSATVAQQVTDSGATVARADGATRYATAAALTARAVEAGASAATAYVVTGEAFPDALSAGAVAARTGGVLVLLQPDSLDNAPAARDLLVDDAERIWFVGGTTPLPSALRQALESLT
>CP031165.1|AXV05340.1|777986_778784_-|Glyoxalase/bleomycin-resistance-protein/dioxygenase
MPERSSYDHGTPSWIDLMTPDTDGAKAFYGGLFGWTAEDMDGPDGEYIYTNLYKDEKLVCGMGPLNDDMADMPPAWTSYINVDDAEQVAKSVETAGGQVLMPVMQVMEEGTMALFTDPAGAAFGVWQPANHKGAGIVNEPDTYSWNELMSRDIDASKAFYTQVFGWEYDEMDMETMTYSVVKGGHEDEGRAGLMPMPAEIPEQVPSYWGVYFTVADADATVARAKELGGSVMFGPDDTPVGRLAAIVDPQGGNFSIMQPSEPSKG
>CP031165.1|AXV05341.1|779016_779520_+|general-stress-protein
MSTDTQQQTDRTALYEVLDDFDTAMLTTFTADGTPHGRPMHVAQRDGDTLWFVTGIDSGKVREIASGDPAVLTFQSSDTWVAATGEVEISHDRSKVDELWSPVMKAWFPEGPEDPGVVVVRVDLVSAEYWATTGTDKVSFAFGVARSILTGTPIDSDDEGEHGEVRL
>CP031165.1|AXV05342.1|779516_780473_+|hypothetical-protein
MTRFGLKLMSELRDARTLVGHAQLAEERGLEFVCISDHIHPWLPEHDHSPFAWTVLGAVAAATDMEMATGLTCPIGRYHPLVIAHAAATVASMSSKPFTLTIGAGERLNEHVTGDHFPAVDVRHDMLTEAGELMRRLWEGGFHTYRGRHFTAEDARIFDLPEIPIRLGVGVSGEQSLGVAKAVGADAIMAVDPDESLVSRWDDMGGDPTATWSEIPLAWAPTEEEGLRLAHERMRFAVPGWKVMAELPNPVNFDAATAHLSPEQVGEAIPHGPDPEPYAEMVRQFVDAGFTNLSLVPVGDDVEKTLDFFETEVRPLLD

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Crispr_ID: CP031165_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_7

1029820-1029919

Orphan

Consensus_repeat	Method
GCGAAGCGAGGCAAGCTCGTGACA	CRISPRCasFinder

1 spacers

DEDDh

The CRISPR arrays of CP031165_7

>merge|CP031165|7|1029820-1029919|CRISPRCasFinder
GCGAAGCGAGGCAAGCTCGTGACAGGCCGGGGGGCAGACTCGGCCCGACGGAGGAGTGGCGAGTCTGGGCTAGCTTGCGAAGCGAGGCAAGCTCGTGAAC

>CP031165|7|7|1029820-1029919|CRISPRCasFinder
GCGAAGCGAGGCAAGCTCGTGACA	GGCCGGGGGGCAGACTCGGCCCGACGGAGGAGTGGCGAGTCTGGGCTAGCTT
GCGAAGCGAGGCAAGCTCGTGAAC

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV05550.1\|1024612_1026097_-\|alkaline-serine-protease	unknown	unknown	gnl\|CDD\|173812
CP031165.1\|AXV05555.1\|1030488_1031067_-\|YceI-family-protein	unknown	unknown	gnl\|CDD\|377274
CP031165.1\|AXV05560.1\|1036058_1036406_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|283084
CP031165.1\|AXV05547.1\|1018053_1020522_-\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	unknown	unknown	gnl\|CDD\|238923
CP031165.1\|AXV05551.1\|1026209_1026977_-\|YbbM-seven-transmembrane-helix-protein	unknown	unknown	gnl\|CDD\|377092
CP031165.1\|AXV05543.1\|1010404_1011472_-\|Adenylate-cyclase	unknown	unknown	gnl\|CDD\|143636
CP031165.1\|AXV05556.1\|1031285_1032092_+\|Succinate-dehydrogenase-cytochrome-b-subunit	unknown	unknown	gnl\|CDD\|239578
CP031165.1\|AXV05561.1\|1036419_1036830_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224929
CP031165.1\|AXV05544.1\|1011931_1013887_+\|Acetyl-coenzyme-A-synthetase	unknown	unknown	gnl\|CDD\|234677
CP031165.1\|AXV05545.1\|1013852_1016432_-\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	unknown	unknown	gnl\|CDD\|238923
CP031165.1\|AXV05559.1\|1035396_1036056_-\|Putative-ATP/GTP-binding-protein	unknown	unknown	gnl\|CDD\|225138
CP031165.1\|AXV05554.1\|1029958_1030492_+\|3'-to-5'-oligoribonuclease-(orn)	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|235429
CP031165.1\|AXV05546.1\|1016457_1017963_-\|putative-LIPOPROTEIN	unknown	unknown	gnl\|CDD\|173812
CP031165.1\|AXV05548.1\|1020525_1021977_-\|alkaline-serine-protease	unknown	unknown	gnl\|CDD\|173812
CP031165.1\|AXV05557.1\|1032136_1034059_+\|Succinate-dehydrogenase-flavoprotein-subunit	unknown	unknown	gnl\|CDD\|236054
CP031165.1\|AXV05562.1\|1036826_1039394_-\|Putative-sensor-like-histidine-kinase	unknown	unknown	gnl\|CDD\|340391
CP031165.1\|AXV05552.1\|1027070_1028054_+\|Tryptophanyl-tRNA-synthetase	unknown	unknown	gnl\|CDD\|234866
CP031165.1\|AXV05563.1\|1039394_1039511_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05549.1\|1022177_1024658_-\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	unknown	unknown	gnl\|CDD\|238923
CP031165.1\|AXV05558.1\|1034070_1034811_+\|Succinate-dehydrogenase-iron-sulfur-protein	unknown	unknown	gnl\|CDD\|181038

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV05550.1\|1024612_1026097_-\|alkaline-serine-protease	gnl\|CDD\|173812	cd07487, Peptidases_S8_1, Peptidase S8 family domain, uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	3.04331e-67
CP031165.1\|AXV05555.1\|1030488_1031067_-\|YceI-family-protein	gnl\|CDD\|377274	pfam04264, YceI, YceI-like domain. E. coli YceI is a base-induced periplasmic protein. The recent structure of a member of this family shows that it binds to poly-isoprenoid. The structure consists of an extended, eight-stranded, antiparallel beta-barrel that resembles the lipocalin fold.	3.55954e-54
CP031165.1\|AXV05560.1\|1036058_1036406_-\|hypothetical-protein	gnl\|CDD\|283084	pfam05331, DUF742, Protein of unknown function (DUF742). This family consists of several uncharacterized Streptomyces proteins as well as one from Mycobacterium tuberculosis. The function of these proteins is unknown.	7.08819e-22
CP031165.1\|AXV05547.1\|1018053_1020522_-\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	gnl\|CDD\|238923	cd01948, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.	8.17645e-104
CP031165.1\|AXV05551.1\|1026209_1026977_-\|YbbM-seven-transmembrane-helix-protein	gnl\|CDD\|377092	pfam03649, UPF0014, Uncharacterized protein family (UPF0014).	6.8174e-61
CP031165.1\|AXV05543.1\|1010404_1011472_-\|Adenylate-cyclase	gnl\|CDD\|143636	cd07302, CHD, cyclase homology domain. Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.	6.36358e-22
CP031165.1\|AXV05556.1\|1031285_1032092_+\|Succinate-dehydrogenase-cytochrome-b-subunit	gnl\|CDD\|239578	cd03498, SQR_TypeB_2_TM, Succinate:quinone oxidoreductase (SQR)-like Type B subfamily 2, transmembrane subunit; composed of proteins with similarity to the SQRs of Geobacter metallireducens and Corynebacterium glutamicum. SQR catalyzes the oxidation of succinate to fumarate coupled to the reduction of quinone to quinol. C. glutamicum SQR reduces low potential quinones such as menaquinone. SQR is also called succinate dehydrogenase (Sdh) or Complex II and is part of the citric acid cycle and the aerobic respiratory chain. SQR is composed of a flavoprotein catalytic subunit, an iron-sulfur protein and one or two hydrophobic transmembrane subunits. Members of this subfamily are classified as Type B as they contain one transmembrane subunit and two heme groups. The heme and quinone binding sites reside in the transmembrane subunit. The transmembrane subunit of members of this subfamily is also called Sdh cytochrome b558 subunit based on the Bacillus subtilis protein. The structural arrangement allows efficient electron transfer between the catalytic subunit, through iron-sulfur centers, and the transmembrane subunit containing the electron acceptor (quinone). The reversible reduction of quinone is an essential feature of respiration, allowing transfer of electrons between respiratory complexes. Proteins in this subfamily from G. metallireducens and G. sulfurreducens are bifunctional enzymes with SQR and QFR activities.	5.40471e-59
CP031165.1\|AXV05561.1\|1036419_1036830_-\|hypothetical-protein	gnl\|CDD\|224929	COG2018, COG2018, Uncharacterized distant relative of homeotic protein bithoraxoid [General function prediction only].	1.5422e-20
CP031165.1\|AXV05544.1\|1011931_1013887_+\|Acetyl-coenzyme-A-synthetase	gnl\|CDD\|234677	PRK00174, PRK00174, acetyl-CoA synthetase; Provisional.	0
CP031165.1\|AXV05545.1\|1013852_1016432_-\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	gnl\|CDD\|238923	cd01948, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.	2.2648e-95
CP031165.1\|AXV05559.1\|1035396_1036056_-\|Putative-ATP/GTP-binding-protein	gnl\|CDD\|225138	COG2229, COG2229, Predicted GTPase [General function prediction only].	3.90354e-40
CP031165.1\|AXV05554.1\|1029958_1030492_+\|3'-to-5'-oligoribonuclease-(orn)	gnl\|CDD\|235429	PRK05359, PRK05359, oligoribonuclease; Provisional.	7.49081e-98
CP031165.1\|AXV05546.1\|1016457_1017963_-\|putative-LIPOPROTEIN	gnl\|CDD\|173812	cd07487, Peptidases_S8_1, Peptidase S8 family domain, uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	1.63264e-65
CP031165.1\|AXV05548.1\|1020525_1021977_-\|alkaline-serine-protease	gnl\|CDD\|173812	cd07487, Peptidases_S8_1, Peptidase S8 family domain, uncharacterized subfamily 1. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	1.82816e-69
CP031165.1\|AXV05557.1\|1032136_1034059_+\|Succinate-dehydrogenase-flavoprotein-subunit	gnl\|CDD\|236054	PRK07573, sdhA, fumarate reductase/succinate dehydrogenase flavoprotein subunit.	0
CP031165.1\|AXV05562.1\|1036826_1039394_-\|Putative-sensor-like-histidine-kinase	gnl\|CDD\|340391	cd00075, HATPase, Histidine kinase-like ATPase domain. This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.	6.20401e-19
CP031165.1\|AXV05552.1\|1027070_1028054_+\|Tryptophanyl-tRNA-synthetase	gnl\|CDD\|234866	PRK00927, PRK00927, tryptophanyl-tRNA synthetase; Reviewed.	0
CP031165.1\|AXV05549.1\|1022177_1024658_-\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	gnl\|CDD\|238923	cd01948, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.	4.78933e-94
CP031165.1\|AXV05558.1\|1034070_1034811_+\|Succinate-dehydrogenase-iron-sulfur-protein	gnl\|CDD\|181038	PRK07570, PRK07570, succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Validated.	5.89452e-177

>CP031165.1|AXV05552.1|1027070_1028054_+|Tryptophanyl-tRNA-synthetase
MPRVFSGIQPTGDVHLGNWIGAISRWAADQEDGHVFCIVDLHAITIPKDPEHLRTKTRDLAAWILAAGLDPEVATLFVQSHVREHSELAWVLSCSTQMGELNRMVQFKEKSAGKESVSAGLFTYPVLQAADILLYQADEVPVGEDQRQHIELTRDVAQRFNGRFGDTFTLPKATMPRAGARVMDLQQPANKMSKSAESDAGTIMLDETEKKTAKKVMRAVTDSGSEVRAGEDKPGVTNLLDLLSAVTGREIPDLEADFEGKMYGDFKKAVAEGVNEFLRPARERHAELSKDPAELDRLLAIGADRARNIAETTMDTVRDRVGFLPPA
>CP031165.1|AXV05551.1|1026209_1026977_-|YbbM-seven-transmembrane-helix-protein
MEGDVGPWGVVASLVLVAVAAAASWRFRLGLVRPLVESAVLACVQLLVVGAALLLVIRPEQPLWWSWLWVVAMIGYAAWTVRQRVPTAPAVLSAALVSFGVTALVALAVLFGLQVFPVEGRTVVPLAGMAVGNSMTAAVVAARMLVERFTDQRGQVEASLALGMSPSQAVLPLVRVVLREALSPQIERTRTVGLVFLPGAMVGLILAGVDPLDAVLVQVVVMYLVLGAVAASATTITIVLSRRLFTADWRPRVLS
>CP031165.1|AXV05550.1|1024612_1026097_-|alkaline-serine-protease
MSRLRILVVSVVTVAMLATSIGPAAAIGLGISISLPGVDLAVDLEGLDISLGLDLSAEELAWGGGGPTATMAHVAEAIGADDLHTDGITGAGVGIAIIDTGVADVAGLEDTLRGPDLSLDAPVEGHYGVDDYGHGTHLAGLIASDRPDARGIAPDASLLSLKVGAGNGAVDVSQTVAAIDWVVQHRDEHDIRVLVLAYGTDGTQDPQLDPLSHAVEVAWDHGIAVVVAVGNHGESSDPVVNPATNPNVIAVGAVDTRATTTTLDDRVPAFSAPGTAERRPDVFAPGVGIESLGAPGGYLDQTYPAARRDGQLFRGNGSSQAAAIVGGAAALLLQARPDLSPDDVKAVLARSATRLDNMLTGQGVIDLPRAVATPAVLTGQDHPASTGTGSLEAARGSTHLGEADDLLAGEVDVFGQPFDSSAWAQAAAAGTSWQDGVWNGTRWAGTDWADGHLVAVPWDGSTWNGWSWHGWSWHGWSWHGWSWHGWSWHAQGWE
>CP031165.1|AXV05549.1|1022177_1024658_-|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)
MELARLVVARPGLGMSMTAGAGRATTPRAAQRIWLGCAPVAAPLLAATALWGPRSASWTQLWQAAALAAVVAVCERWVSITVRTGTQSHSLTLSEAPLLIGLFLLPVPLLVGARIAGMVVANQVLRRQEGYKTALNVTQTWTETLIAAGLTAVVTGLALGVHVELLVAAAVVGLVVNIVGVVFMTVAVSSTAGHLVLGPARRAVWTGLVPAITSALVGAAAVALWAVSPVLVLAPAMLSVVLTVAYRSWLELVEANASHARLLTFTKAVAAAGDLDATIDTIVQETRTLLSPRHVAVRLPTSSDESAAWVGVDAATAAELDLLLEHEGNDGATVPPADEETLFVPLDTGWIAVSLERDSIRPHDRRTVGMLATHATVVVQNIRSADSLRDQAAEARHRANHDALTGLPNRQSLLTAIVEADLRGRAFGVLLLDLNDFKKVNDALGHHAGDQVLTELTRRVAPIAEDVRVFARLGGDEFAAVVEGDVSRCTLVAERLHLLIGRTTSVDGYDVATSASIGVALAPEHGSDPSTLLKHAELAMYGAKQRGCGTHVYGIESGGRALRDLKVSSGFRMALDRGEIDVVFQPIIDLESGRVAAVEALTRWSHPELGVIRPDEFIAAAEQNGMVTDLTRHVLHASLQWQRLWAAAGIDLQVAVNISARSLVDDQLADMVCSALSRHRVPANRLTLELTESSVVSDPSITIATLRRLRALGVRLAVDDFGTGYSSLAYLRELPVDEVKIDKSFVIPLVEELHTPPLLSGIINLCREMGFELVGEGIENATVQRKLTDMGCSRGQGFHIARPMDGADLLDWQARWRDDRHLSIVL
>CP031165.1|AXV05548.1|1020525_1021977_-|alkaline-serine-protease
MLLPAVLLLGTTPVAAEAPRHTSRSALPLDLGGLLGDTLALLDITAESVSWEQEGTNAELHHVGTAVGADNLHRRGLTGAGIGVALIDTGVADVRGLEDVVRGPDLSLDSQFEEAWARDLYGHGTHLAGILASDRPDVPGLASDATLVSVKVGATNGAVDVSQTIAAIDWVVQHRHEHNIRVLALAYGTDGTQDPIHDPLSHAIEVAWRHGIVVVVAAGNHGAVRDGVVNPALNPYVIAVGAVDTQGTSARLDDEVPEFSPTGTRQRRPDVFAPGVGIVSLQAPGGYLDTAYPQARQPDGRFRGNGTSQATMVVASAAALLLQDRPELSPDDVKQLLVRSSQGVSSLLSSTNMIDVEAARSLRPRRATQQFPHSRGDGSLELARGSMHIGVDGAWLDGERDIHGRPFDSARWAAAAEAGTSWSNGRWNGSRWTSSGRIDHAWPGQTWQGRSWSGWSWNGWSWNGWSWNGWSWNGWSWNAAEWR
>CP031165.1|AXV05547.1|1018053_1020522_-|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)
MTATPHVLTPIVDRPEQRVWIASALAAVLLALPISQMPLPPVGVTEMLLGLCLAATVAASERWASTTVRIGEQTHNLTLGEVPLVVGLMLVSPGVLLLARITGAFVGLKVFRRQAGHKTAFNIVHLTAETLVAIGLAAAVAPDGLHDGLRLTILGTSVAVAVATGGGLAMAAVMRITAGRPPPGTLVVSTVREGLFASLVASGAAVMGLALWGVSPLLLWGPLAVTTAIVAAHRSGLGLVQANAIQGGLLTFTRSVTGEEDVTATATHLVEATRSLLSAELVAIRLDGLDDGHDPSWIGVGSAEASKLDHDLALDGRHDEAGCCVGSARETVFAALPTGWLAVGMDRASIRPHDRSAVHMVGNHAAVVLANAERGTKLRRQAAEAHHQARHDSLTGLPNRLALRSAIQTAIEADQPFGVLLVDLNDFKQINDALGHAAGDEVLTELAKRLGPVTEGARLLSRLGGDEFAVVATGDQAACVALGQQLNGEIGREVHISSYDLLVGSSVGLALYPDHGTDVGELLKNADLAMYEAKALGGGVAVFGTDSSGRAMRQLEISSAFRHALQEQQLTVVFQPIIDVATSAVTGVEALTRWTHPELGAVSPDEFIAVAEQTGLITELTHFVLDTTLQWQRLWAAAGLDLQVAVNLSPRSLLDAALPRLVQRHLATHGLPANRLTLELTENSVITDPTRTLAALDRLSGLGVRLSVDDFGTGYSSLSYLRNLPIDCVKIDKSFVLPMDGDPRARGLVAGIIGLCDRLGFSVVAEGIETQDVLDALQDMGCASGQGYFISRPLDGAGILDWVRGRSPTEARDSLCVEANNS
>CP031165.1|AXV05546.1|1016457_1017963_-|putative-LIPOPROTEIN
MMTAASRPRLVRLLLVVLLTSVVGNIPLPAHADDLPARSSELPSPPSADEAVSWEAEGTTATLDHVAEAVRATRLHERGLTGRGIGIALIDTGVAPVVGLTDVVHGPDISLDSQAEQAQHYDVYGHGTHLAGIITSDRLDAPGLAPDATLLSVKVGAYNGAVDVSQVIAGIDWVVQHREEHNIRVLVLAYGTDSTQDPLVDPLSHAVETAWHNGITVVTAAGNDGQVRDSLVNPATNPWVIAVGAVDTQGTRRVSDDTVATFSPAGTPARGPDVLAPGVGMVSARVPGGYLDTTFPGAQRPGDLFRGNGTSQAAAVVGAGVALMLEDDPSLTPDDVKARIVDGSKVLRQDGTGEAPGMLNLTQARTSDVIGAQVHLLSSGTGTLEGARGSYHLLGDSPLTGEQDIFGQPFDSVVWAAEATALTSWDGGTWNNTEWTGWGWDGWGWDTAEWTGTTWDGWGWDGWGWDGWGWDGWGWDGWGWDGWGWDGWGWDGWGWDGTQWD
>CP031165.1|AXV05545.1|1013852_1016432_-|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)
MLRSLGGAPIHRGTGVTFFMDHTADMPQATTSNGPPPGAVRRVWMLTAAVAVISTVGTLVLPRSPITGGDVLRVLLLTALVAVTERWSLSARVGHVSHRLTLSEVPLVLGAFAVSPLLLVGARLVGGIVGLQVLRRQEPYKTAYNVGYLWIETLIVLNVLDLLGASSITGGPRASLAIVAIAVSVAVTGAVAKVGAISATQGRLVRGLALRGLRDGLGPSLATAAATTVGVVLYRTEPTLLWAPAVVLGVLMLAYRSHVQLVEAQDLQSSLIAITQGITGESTPEETAMLMATATRRILDAPAAAISLADPDTGRRTWYGADADSWTMLEEARLAAIRAAGPGARHAPGGTIAAPVDAATDSWLVVGYSRRSPTGEADRQTVGMLANHAAVALANAHRGAALRAQAEQATFEATHDPLTGLANRAALIIAIEAALVEDTTFAVLLIDLDNFKEINDALGHAAGDKVLGVIGQRLTPFVDEARLVCRLGGDEFAVIIDGGEVSARDVAGRIRDAIGAPVQLGSYTLQVGCSVGIATYPHLGRDADELMTHADLAMYEAKARGGGVAVFGAAAGGRAMRQLAISSGFRSALGNGDINLVFQPLVDLQTDRVVTMEALSRWTHPDLGPVSPEEFVRVAEQSGLITDLTHRVLDSALSWHRRWLDAGEDLPVSVNVSATSLLDTGLPRLVATTLDAHGVRADRLTLELTESSVIGDPQRTLEVLARLQRLGVRTAIDDFGTGYSSLAYLAQLPVDEVKIDKSFVLPMLDGTGSLPLVAGIIRLCTEMGFDIVAEGIETDEVQQTLRDMGCTRGQGFGIARPMGPEAVVEWVRRHHGHRTLHVVADPARRGTGVTGPWRPAAGR
>CP031165.1|AXV05544.1|1011931_1013887_+|Acetyl-coenzyme-A-synthetase
MSESSLENLYHEGRAFPPPDAFAAQANVSDDGVYEQAAKDPEAWWAQQAEHLRWTTPWEQVLEWNPPHAKWFVGGQLNIADNCLDRHLEAGRGDRVAYYWEGEPADERRTITYAELHEEVCRFANVLKARGVGKGDRVAIYLPMIPELPVAMLACARIGAIHSVVFAGFSSQALADRIDDADARLVITADGANRRGNTIGLKEAVDAGIERAESDRVSTVIVVNRTGTDVDMVDGRDVWWHDVMDGASADCPAEPMDAEDVLYILYTSGTTGKPKGIVHTTGGYLTQTTATHRLTFDLKPETDVYWCAADIGWVTGHSYIVYAPLANGATSVMYEGTPDFPDKDRFWDIVDRYDVSILYTAPTAIRAFMKWGTEYPERHDLTSLRVLGTVGEPINPEAWMWYHRHIGGESAPIVDTWWQTETGGHMITPLPGITHARPGSAMTAFPGIDARVVDIEGKEVGNGEGGYLVIAKPWPSMLRTIWGDDQRYRDTYWSRFGPDTYFAGDGAKLDEDGNIWLLGRVDDVMNISGHRLSTTEVESALVDHPSVAEAAVVGRADDLTGQAISAFVTLRGTHEPSEDLEAELKAHVAEVIGKIARPAEIYFTPDLPKTRSGKIMRRLLKQISEGSDLGDATTLANPDIVNALQQAARGR
>CP031165.1|AXV05543.1|1010404_1011472_-|Adenylate-cyclase
MTSHADPDRARQIRRLFRLGMSVQAATDAVDADRVTMALVDHLIGGGRDFTREEAAGRAGLSLHVAETIDRVAGVGDDARYSESGIHHLALIARLLQVLPEEEVLEQIRADIPILRALALRTLDTARTVFIDAARRDHPDPVDAGVALSEVAKPLLDLSSELVGASYRRVILELMTSDIVVESLRSEGETVDVAVGFVDVVGYTSLSARVDPSGLDEVLTRFESDCQAVVEAHPAVSLVKFMGDAGMFVALDPVELATALFGLVSDRADDDEESIPTSAGIAHGPALLRGGDYFGPPVNEAARLTDLARRHSVLVSDQLKEPLSGDFDLRRLAPVSLHGIGRRRPYALRRAQDDG
>CP031165.1|AXV05554.1|1029958_1030492_+|3'-to-5'-oligoribonuclease-(orn)
MWVDLEMTGLDPEREVIVEIAVIVTDGQLEQVHEGPDLVLHTDDDTLARMHPRVKEMHKRSGLTAEIRASELTVPEAEQEVLRFIKHYVPASSSAPLAGNSVHADRAFLKKYMPSLEGHLHYRNVDVSTLKELARRWHPEIVEAAPAKDGGHRALADIRESIKELAHYRREMFVQEG
>CP031165.1|AXV05555.1|1030488_1031067_-|YceI-family-protein
MSTTTTTDALDRTVAGQPFPAAGVYTIDGSHSSVEAVARHLVVTKVRGHFNEFEGTITVGETPEDSAVQVTIKADSIETKDGKRDEHLRSPDFLDVENFPELTFRSTSVDKGWVVTGDLTIRGVTREVTLDTDYMGTFKNPWGQTVAAFSAKTTLDREDFDMTWNAPLEAGGVLVSKELKIELEIQAPLQEG
>CP031165.1|AXV05556.1|1031285_1032092_+|Succinate-dehydrogenase-cytochrome-b-subunit
MSTMTPRSDDGAIKPLEKAPVPHRQRPKMWVRDFYGTAMGKKYVMALTGIIGLGFIVMHAVGNLHVFEGAEKFTEYGEGLRDLGEPLVPRTFLLWLGRLGLLGALVGHVHAAYSLTLMNRKKRPVAYQAPREYIAADYASRTMIYTGTIVLAFILFHLADLTWGLANPDYVRGAITNNLVASLSRIPVAIFYLVAVLALGMHIFHGTWSLFQTMGWSSKRFNPWRRYLAIGLAVVVTSINLTYPLGTMFGVIDCGEECEAIAEEFSAE
>CP031165.1|AXV05557.1|1032136_1034059_+|Succinate-dehydrogenase-flavoprotein-subunit
MTVLDSRVPDGPLADKWTNHKFDMKLVNPANKRKYEIIVVGTGLAGGAAAATFGELGYNVKCFTFHDSPRRAHSIAAQGGINAAKNYHGDGDSVYRLFYDTIKGGDYRGREENTYRLAEVSNNIIDQAVAQGVPFAREYGGLLDNRSFGGAQVSRTFYARGQTGQQLLLGAYQALARQISLGTVDMHIRSEMLDVVVKDGQACGIVTRDLLTGEIASHSAHAVVLATGGYSNVYYLSTNAMASNVTAAWRAHRKGAFFANPCYTQIHPTCIPSSDEHQSKLTLMSESLRNDGRIWVPKNIDDTGKPAADIAESDRDYYLERKYPSFGNLVPRDVASRNAKAVVDAELGIGPLKNGVYLDFSDAINRLGEDTIAARYGNLFEMYERITGENPYQRPMRIFPAPHYTMGGLWVDYELQTTVPGLFAAGEANFSDHGANRLGASALMQGLSDGYFVLPYTIGNYLAPKLGEKVVPTDDPVFKQAEAEVTDGINKYLSVKGTRTVDYFHRELGKIMWDECGMARNANGLQKALSEIKALREEFETDVRVLGSADTMNMSIEKVNRVADFFELGELMCQDALMREESCGGHFREEHQTEEGEAKRDDENFQFVGAWEFTGDTGNANLHKEELVFENVTPTTRSYK
>CP031165.1|AXV05558.1|1034070_1034811_+|Succinate-dehydrogenase-iron-sulfur-protein
MKLTLKVWRQPSPDAAGSFETYQLNEVSEDSSFLEMLDQLNEQLVNDGKEPVHFDHDCREGICGSCGLMIDGQAHGPQRSTATCQLHMRQYTDGDTITVEPWRASGFPVIKDLAVNRSAFDRIIEAGGYITVPTGSASDANLTPVPKDIADDAFDAAACIGCGACVAACPNGAAQLFTSAKMSQLNMLPQGQAEKTDRTLNMVETMEAFFGSCTNIGECSVSCPKDISLDYIAQMNKDYLKAKFSG
>CP031165.1|AXV05559.1|1035396_1036056_-|Putative-ATP/GTP-binding-protein
MTATYSSQSPSHNQSSSHNEANSMHTSPPRPVRRGPTSVKIVIAGGFGVGKTTMVTAVTEITPFTTEVPMTEASLGVDDTSIVGERKTHTTVAMDFGRISLGNDLYLYLFGTPGQDRFSFMWDDLTQGAVGAIVLVDTRRLEECFPAINYFEQRGVPFVVAINCFDGQVLHSPEAVRDALQVGEDTPVMLTDARDKAQVKVAMASVVRHAMARARATLG
>CP031165.1|AXV05560.1|1036058_1036406_-|hypothetical-protein
MTGARRLRPYALVGGRTHAEANLSMESMVVASGVQPGDDIGPEQLELLEQCRTPQSLVDLSAGLDVPLGVIRVLLGDLLAYGLITHSGAVEAPAAVPAHRDITLLGELLDGIEAL
>CP031165.1|AXV05561.1|1036419_1036830_-|hypothetical-protein
MNAGTDLNWLLSGFSSRTPGVIESVVVSIDGLLIAASEGLDRATADRVAAVASSLASITRGASRVFDAGTLKQVMVAYDNGYIVLTSLRDGAVLAVLATAGSDIGLIGHEMRTLGDQVGTALSPQLIEDLRAQLPR
>CP031165.1|AXV05562.1|1036826_1039394_-|Putative-sensor-like-histidine-kinase
MRSSIRLRLMTLMLVPAVALLALSGIQLRASTEVLAQTQQFASLVDLADAQYSLVHDLQIERTRTLEAFHIGDDGGMDMSGEDLQAARSTTDTSLARLHELASPELTDGLSGPVADALQRALDAADDLVVRRGDIDAGSMLDAQVQQAYDVPVGALLGIDDILIPEVTNPVIHTRLLASAAYARLKATALDRGDTILLAVAGSIDSGTAGRRVSAQANQQALWLDSLRRLATDDEVALLEQTADIDPSSEVSRVAGGLQAGNLGAIDEIAADNRDTARTLRTVEQQMAATSLSAADDLQTEATRTTFVIGGLVVLALLFGAYLVYALSRSVVRPLNRLTTLASRIATALPSTVEAVGRGEEVDTSVLDDAVSTELLNRRDELGDLARALGAATDQATTVALEQARTRHGVAQTISDVARREQSLVERQLSLLESMEDREEDAEQLSQLFRLDHLATRMRRNAENLLLLSTGQLPGSGDASHQPLVDVIRTAAAETEQYARVDVRVGIPVDVKGYAATPLSHLLAELVENATNFSPPNTRVTVTTAREASGVTVTVTDRGLGMDAQDLEEAKARLMAPPLLEAAESRRLGLYVVGLLAQRLGVAIDIRPGEPAGLHVLVWLPDSLFVTPPQARTGPAGLASVVAQQAEPATPTGPVQPAALLSATPPVERAPEPAPAAGPARFAEDAAPDALSVMQRLLDASPSTPPPLPPDVQPVASTLPTRAPLLPQRQPSGDEPASGISLARASNGRTVDFDPAAVADLISGFDSDFASGPPPAPTPEVTTDRLPVATSQPGFQPQAPGPAGFPPAPSAPPAPAAPAAPVDDTPAAADPTPPTTPFGGTSSWSTPFPQRDSAK
>CP031165.1|AXV05563.1|1039394_1039511_+|hypothetical-protein
MCGSSVQWRRRTWGGVPFPTSSVEGPVTLRERSPRAGG

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Crispr_ID: CP031165_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_8

1155981-1156089

Orphan

Consensus_repeat	Method
GGGTGGGCTCGGGCGGCCGAGCGGATGCGTGTCGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_8

>merge|CP031165|8|1155981-1156089|CRISPRCasFinder
GGGTGGGCTCGGGCGGCCGAGCGGATGCGTGTCGGGTTCCTGCGACGGGCGGCCCAGAACCCGACAAGCGGAGGGGTGGGCTCGGGCGGCCGAGCGGATGCGTGTCGGG

>CP031165|8|8|1155981-1156089|CRISPRCasFinder
GGGTGGGCTCGGGCGGCCGAGCGGATGCGTGTCGGG	TTCCTGCGACGGGCGGCCCAGAACCCGACAAGCGGAG
GGGTGGGCTCGGGCGGCCGAGCGGATGCGTGTCGGG

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV05667.1\|1162159_1163128_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379751
CP031165.1\|AXV05664.1\|1156126_1158070_-\|Serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|367829
CP031165.1\|AXV05656.1\|1147392_1148478_-\|RNA-polymerase-sigma-54-factor-RpoN	unknown	unknown	gnl\|CDD\|224511
CP031165.1\|AXV05665.1\|1158186_1159836_+\|Serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
CP031165.1\|AXV05663.1\|1154903_1155905_+\|Nucleotidyl-transferase	unknown	unknown	gnl\|CDD\|224129
CP031165.1\|AXV05655.1\|1146402_1147380_+\|putative-glycosyl-transferase	unknown	unknown	gnl\|CDD\|133016
CP031165.1\|AXV05659.1\|1150192_1151368_-\|Glycosyltransferase	unknown	unknown	gnl\|CDD\|340818
CP031165.1\|AXV05662.1\|1153365_1154712_+\|ATPase,-AAA-family	unknown	unknown	gnl\|CDD\|237355
CP031165.1\|AXV05658.1\|1149698_1150196_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05660.1\|1151364_1152342_-\|dTDP-glucose-4,6-dehydratase	unknown	unknown	gnl\|CDD\|187541
CP031165.1\|AXV05668.1\|1163145_1164297_-\|putative-glycosyltransferase	unknown	unknown	gnl\|CDD\|340828
CP031165.1\|AXV05666.1\|1159835_1162112_+\|Copper-resistance-protein-CopC-/-Copper-resistance-protein-CopD	unknown	unknown	gnl\|CDD\|377255
CP031165.1\|AXV05657.1\|1148583_1149702_-\|glycosyltransferase-(biosynthesis-of-lipopolisaccharide-O-antigen)	unknown	unknown	gnl\|CDD\|340825
CP031165.1\|AXV05671.1\|1168013_1169498_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378217
CP031165.1\|AXV05669.1\|1164299_1165289_-\|Glycosyltransferase	unknown	unknown	gnl\|CDD\|133030
CP031165.1\|AXV05673.1\|1172113_1174915_+\|Alkaline-phosphatase	unknown	unknown	gnl\|CDD\|225156
CP031165.1\|AXV05672.1\|1170124_1171666_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|349398
CP031165.1\|AXV05661.1\|1152726_1153329_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379393
CP031165.1\|AXV05670.1\|1165482_1168017_+\|glycosyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|133029
CP031165.1\|AXV05654.1\|1144012_1146406_+\|N-acetylmuramoyl-L-alanine-amidase	unknown	unknown	gnl\|CDD\|274252

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV05667.1\|1162159_1163128_+\|hypothetical-protein	gnl\|CDD\|379751	pfam15887, Peptidase_Mx, Putative zinc-binding metallo-peptidase. This family has a highly conserved HHExxH motif with a highly conserved ED pairing downstream. HExxH is indicative of a zinc-binding metallo-peptidase.	8.69928e-127
CP031165.1\|AXV05664.1\|1156126_1158070_-\|Serine/threonine-protein-kinase	gnl\|CDD\|367829	pfam04122, CW_binding_2, Putative cell wall binding repeat 2. This repeat is found in multiple tandem copies in proteins including amidase enhancers and adhesins.	8.24055e-08
CP031165.1\|AXV05656.1\|1147392_1148478_-\|RNA-polymerase-sigma-54-factor-RpoN	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	5.86718e-28
CP031165.1\|AXV05661.1\|1152726_1153329_+\|hypothetical-protein	gnl\|CDD\|379393	pfam13845, Septum_form, Septum formation. This domain is found in a protein which is predicted to play a role in septum formation during cell division.	1.29164e-10
CP031165.1\|AXV05663.1\|1154903_1155905_+\|Nucleotidyl-transferase	gnl\|CDD\|224129	COG1208, GCD1, Nucleoside-diphosphate-sugar pyrophosphorylase involved in lipopolysaccharide biosynthesis/translation initiation factor 2B, gamma/epsilon subunits (eIF-2Bgamma/eIF-2Bepsilon) [Cell envelope biogenesis, outer membrane / Translation, ribosomal structure and biogenesis].	4.86693e-80
CP031165.1\|AXV05655.1\|1146402_1147380_+\|putative-glycosyl-transferase	gnl\|CDD\|133016	cd02525, Succinoglycan_BP_ExoA, ExoA is involved in the biosynthesis of succinoglycan. Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.	1.95333e-58
CP031165.1\|AXV05659.1\|1150192_1151368_-\|Glycosyltransferase	gnl\|CDD\|340818	cd03785, GT28_MurG, undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	6.71413e-07
CP031165.1\|AXV05662.1\|1153365_1154712_+\|ATPase,-AAA-family	gnl\|CDD\|237355	PRK13342, PRK13342, recombination factor protein RarA; Reviewed.	0
CP031165.1\|AXV05660.1\|1151364_1152342_-\|dTDP-glucose-4,6-dehydratase	gnl\|CDD\|187541	cd05230, UGD_SDR_e, UDP-glucuronate decarboxylase (UGD) and related proteins, extended (e) SDRs. UGD catalyzes the formation of UDP-xylose from UDP-glucuronate; it is an extended-SDR, and has the characteristic glycine-rich NAD-binding pattern, TGXXGXXG, and active site tetrad. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	6.37343e-177
CP031165.1\|AXV05668.1\|1163145_1164297_-\|putative-glycosyltransferase	gnl\|CDD\|340828	cd03798, GT4_WlbH-like, Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.	3.59432e-51
CP031165.1\|AXV05666.1\|1159835_1162112_+\|Copper-resistance-protein-CopC-/-Copper-resistance-protein-CopD	gnl\|CDD\|377255	pfam04234, CopC, CopC domain. CopC is a bacterial blue copper protein that binds 1 atom of copper per protein molecule. Along with CopA, CopC mediates copper resistance by sequestration of copper in the periplasm.	3.71418e-17
CP031165.1\|AXV05657.1\|1148583_1149702_-\|glycosyltransferase-(biosynthesis-of-lipopolisaccharide-O-antigen)	gnl\|CDD\|340825	cd03794, GT4_WbuB-like, Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.	4.93256e-25
CP031165.1\|AXV05671.1\|1168013_1169498_+\|hypothetical-protein	gnl\|CDD\|378217	pfam09594, GT87, Glycosyltransferase family 87. The enzymes in this family are glycosyltransferases. PimE is involved in phosphatidylinositol mannoside (PIM) synthesis, a major class of glycolipids in all mycobacteria. PimE is a polyprenol-phosphate-mannose-dependent mannosyltransferase that transfers the fifth mannose of PIM. The family also includes alpha(1-->3) arabinofuranosyltransferase, invloved in the synthesis of of mycobacterial arabinogalactan.	2.11531e-05
CP031165.1\|AXV05669.1\|1164299_1165289_-\|Glycosyltransferase	gnl\|CDD\|133030	cd04187, DPM1_like_bac, Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.	8.02818e-69
CP031165.1\|AXV05673.1\|1172113_1174915_+\|Alkaline-phosphatase	gnl\|CDD\|225156	COG2247, LytB, Putative cell wall-binding domain [Cell envelope biogenesis, outer membrane].	3.51412e-09
CP031165.1\|AXV05672.1\|1170124_1171666_+\|hypothetical-protein	gnl\|CDD\|349398	cd05379, CAP_bacterial, Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins. Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown.	5.71644e-21
CP031165.1\|AXV05665.1\|1158186_1159836_+\|Serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	5.17028e-79
CP031165.1\|AXV05670.1\|1165482_1168017_+\|glycosyltransferase-domain-containing-protein	gnl\|CDD\|133029	cd04186, GT_2_like_c, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	1.40556e-53
CP031165.1\|AXV05654.1\|1144012_1146406_+\|N-acetylmuramoyl-L-alanine-amidase	gnl\|CDD\|274252	TIGR02669, stage_II_sporulation_protein_D, SpoIID/LytB domain. This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General].	2.66305e-27

>CP031165.1|AXV05663.1|1154903_1155905_+|Nucleotidyl-transferase
MRALILAGGRGTRLRPLTHLIPKPLVPFMGDPYAHGLLRRLVDAGVTRATFLVGRDAAPFQPLVDAAPQLGLAIDVATEEMALDTAGAVRRALAGEADEPVLVCNGDVLTDVDLRRIIDGHVESGAVATLTLHEVTDTSAFGVVVRNGQGMVRRFVEKPQPGTVPDNTINAGTYVLQPRLFDHFPGDGPLSFERQVFPGLLDAGEKMFGINDDAYWQDLGTPARYLEGHRAVIDGECTWPLAEGMVVVEGQSAIHPSAVVDETAVVRFGSVVGPRCRVGAGAVLQGAVLHEEVEVHDAAVISDALVGALSEIGTGVVVPKGSVLGIRTYLGTR
>CP031165.1|AXV05662.1|1153365_1154712_+|ATPase,-AAA-family
MPEAQLFGGDDDRASEETPPATRRVMSGAGAGSATAPLAARLRPRTLDEVVGQRHLIGPEGPIRRTIASGRLSSMVLWGPPGTGKTTLAGVIAAEANAEMIVLSAVTAGVKDVRAAVVEGRERLRRTQRRTILFVDEIHRFNKSQQDALLPSVEAGDVVLIGATTENPSFEVNAALLSRSILYRLAPLEEDDLSVLLDRGLADPGLEGVTATDEARAALLHAADGDARVLLTGLDAAAALSVGTEDGRITPEMVQSALAQPHLRYDKAGDNHYDQVSAFIKSMRGSDPDAAMYWLTRMLAEGEDPRFLARRMVILASEDIGLAHPQALAVSVAAFQALDRVGLPEARFALSQACIHLALAPKSNAVTRAMARADAEVERLGNAPVPASLRDAHYKGAKRLGHGVGYAYPHDDERGWVDQQYGPDGLRRIYEPGDHGAEPTLNSWRDSR
>CP031165.1|AXV05661.1|1152726_1153329_+|hypothetical-protein
MIIGLVVLVLVLAGGGLAAFLLSSGDDELATTDTEATASELGEAVDDLNSDLADEGTEPEVLDDLPQDEATPSAVPGEDASVFELAVGDCYNSPSTSDEVQSVAVVPCDTPHDSEVFFLVDYPDDGTGFPGLEELNTFADDQCQGQAFTDYVGVVWAESRFFTSQLTPTEASWEQGDREVVCLLYDPTTQLNASVRGTGQ
>CP031165.1|AXV05660.1|1151364_1152342_-|dTDP-glucose-4,6-dehydratase
MIARVTYDLTVFDGATAVITGGAGFLGSHLSHRLLDLGARVVVMDNLSTGSASNIEDLLGHDRFSFLRYDVTEYIHVGGSVDFVLHWASPASPIDYLKLPIQTMKVGALGTHKALGLARAKDARFMLASTSEVYGDPEIHPQPESYWGNVNPIGPRGVYDEAKRFAEALTFAYHRSHGMEVRVPRIFNTFGPKMRMDDGRAVPTFIAQTLRGEPLSVFGDGQQTRSLCYVDDLVEGLLRLLASDYDATPVNIGNQHEMTILELAQRIQKLAGVSPGIVHEPMPVDDPKVRQPDTTIARRELDWKPEVDIDDGLLRTIEWVRTNRM
>CP031165.1|AXV05659.1|1150192_1151368_-|Glycosyltransferase
MISGDVIGRADGPRVLFVPSNGMGLGHMTRAAAIARRLGEAGAMPILCVLSPLIDPLRQLGFMVEHIPSYASTPLERWHWQRLLADQLRHLIEAYDVTAVVFDGVAPYRGVRQVMAEEGAPPFVWVRRGRWRADARPAATAAGFTMVIEPGEVDRDEPDVAIPQPAARAVNGVPVRQVGPVLLHDHHDLRDRGQALVDLALPADGRYGLISLGTGLAGPLAHTAGPLVAALRSRGLVPVVAASPLSPPPTVEGALVRQRYPLAPSLAAFDVVVLAAGYNSVVEAVACRVPAVLVPNPAAAVDDQLARAVGLDQQGLAVLWDSTVRAGAEGAAGSAPAGALDRALDRALDGHSELVERMAARSVPQGATRAAALIQELTQSRAHQPKPRSIR
>CP031165.1|AXV05658.1|1149698_1150196_-|hypothetical-protein
MTSPTVPAQLRSGLRAVYGVVLALLPTRLGDRLRDLVARTRARWPQLDGPSGGRVRVPGPLDHPVVLVVAVGCAPTRLRQAVDGMSGVPVRPVWLVDTPLPGDLADQVIEWLPPAADLDRFGLDTAAVRRSRLRAVEQRYRPKRVVVIGPEGPLPDPVLIVPSPS
>CP031165.1|AXV05657.1|1148583_1149702_-|glycosyltransferase-(biosynthesis-of-lipopolisaccharide-O-antigen)
MSTHASSRPRVLVVTTVHPPDDPRIRYKTAASLAEDFAVRLATRAPGPDDTRGLDSVVLDGSRPRRALRALRQMLRRDVDLVAVHDPELLPVALLARLLRRVPVVFDVHEDLPVRAGLSRRHPAAGERGSAVRARVGPWLARRMLHVVERLVVVTLAEEGYARDFRRAHPVLPNHLLVEVLPPPSANATGGGVVYLGDVTTARGVTVLLDAVSSGLPGRTLHLIGRCAPGLAEELRHRADELGVSLEVHGWMPLPVALRLVAVAEVAACPLTDHPAYRRSLPTKVLEYLAVGVPVVASDLPGTREVVEGLPGVVLVAPDRVDELARGLAVAADPALRAAAVQGVAAVRERFGWPDERIRQVYRDVVSSSAER
>CP031165.1|AXV05656.1|1147392_1148478_-|RNA-polymerase-sigma-54-factor-RpoN
MTALWPPPDTMSDGMLLRRAAGGDDDAFTLLFHRHRAMVRRICVAHGPHGLAEDLSSETFVRLLQHAERLWDRDRLAPWLATVARNTAISALRRPAVHRESPVADVPMRFADADHAESVTQRLDVETLLAHADDGDAAMLRAHYMEGRPLADIASDLGTTVGSIKVRMHRARGRVRRTAFAQALRGLVPLPVLRWRTQVTDLLRADVSHVAMVLAPVAVAAAIASGIVGSGTPQGSEAPRAAATATASQTAGGTGPVAPAAVSSAPVVHGAVAPSPPTGASQPLGRPGQVDTPSDNRRPPVDVPTIWLSREPPAPEPDSTVGIAGLEVETTSPPGVSDSTREDVCDVIALLPEPVSCHNER
>CP031165.1|AXV05655.1|1146402_1147380_+|putative-glycosyl-transferase
MTLGPDDVGVVVPARHAAGTLARAVSSALAEGVGAVVIAVDPTDQPTASAAARVAERDTRISVVDNPGGATPTGLNIAIAALPHQVVARLDAHAAFRPGYVRAALTALEGQGAAVVGGLQRSLATSPVGRATATAMGTWLGSGGASHRTGTVAGPSETAYLGVFRREWLDRVGGYDPSLARNQDYEICHRIRRAGGLVWFSPDMDATHEPRDTWTELAAQYHDFGRWKRHVMATAPGSIQPRQLAAPALVVGLVGSVLVARRRPRPAAVVPMAWLAAIGTAAATADAVDASPLTRADRVRIGGALGVMHLAWGTGFWRGGRGRGR
>CP031165.1|AXV05654.1|1144012_1146406_+|N-acetylmuramoyl-L-alanine-amidase
MRITATLPRVRRATLLVVLALACVFASVPTAMAGQGAPPTTDLTGYIDDTPPPAQFAQGGCTPAGGSAIADPDLPSGDFVLVGGGWGHGAGMSQYGAQGAGLLGCTATQILTTYFPGTSITTVPQPDLVVIGLGTAMPKATYTAEVGTIPYRLCHYQSGECTDLPTSQPQGSTWRVDVTPDATYRITDTGSGAVVWEGGDKEWNLRTVLSPDPSVNRRVHVAEVGHTYRWGTLQLDSVLTGASEAYLTLEFTDMDLYLRGLAEVPISWPDATLQAQVISGRSYALARIQALGIRTDCRCHLYSTPRDQNYEGWDLESADSQGKWVNAVNATSGQILTHNGSIAETFYSSSHGGHSESSRFVFGGELPYVQPVDDSRWDLASSNPLRRWTAAFTAAELGSRAGVGTATSMRLLDPRGAAGRIGSPSRGYGGVEVTGTGGTVVLSGDQLKSRLGLRSTLVDVRSQPGGPDPQPTATPAPTPTSEPPPAAAPDSIARVAASDRIGTAVQVSAFGWNAASDVVIAASDRFPDALAGVALAASLEAPLLLTSTAELSPATAEEIRRLGATTAWLLGGTSALSTAVRGDLADMGLTTRRLAGDNRSETAAAIAGAAVGTADEVTLVPASDWPDAVSASSLAALVNGPPTLLAGRDQLDDATIEALEDLGARTVTIIGGTAVIAPSVVSQLEGLGYEVRRLAGSNRFGTSTAVAEEALSQRTGDVTLVIASASGFADALPAGALAARRSGVLVLAPRDSMADAPDIASFVEARVGRVADGVVVGGTGAISTTVETQLEQALARR
>CP031165.1|AXV05664.1|1156126_1158070_-|Serine/threonine-protein-kinase
MSAPHRRTATLLVVMLTMGLLTALPAQGEEYASFGCFSDPAGDAGGVDVADIVGTCLQYPDTSSSPEFPQGEPIRLTTVFAAGNNPLQDASWTNDDTALQVALSTDGDPNPELVLRLFHNGTSLVRSIEDGAGGQVADCDAQVELDPSFQGIDFVLQPSCIPDSPDVRYSVQMAYEETDGAAVAMDRWPDTDASVRMPRGDENPFCDAPTETGSEVTVARVACFIGGTEPVSQAVAISQFVFNDLSTQEYEPYTGQWAVIVRDDNFADALAGSSLGFGQGPLLFTYSPTSGPTLGQDHTRLAPATKQELVRTVPRGFPVYVLGGTAAIDEGVMDHLRELGYDARRLSGPTRVDTAAAVALEVRQRTQDFAARNAGFPDTNMVLMANQDNWPDAVLAGQVGALWGFPVLLTGATGPAPAATLAALDQLRPQAIQFIGGSAVISSDTLRSIRDHANTNGYAFGGPGAALTDDTSNPWRQFCANTNPDGSQIPRWTCRWGGDSRIATGAAVSQFGREMIQRFGGEDTLIPDTEVYASGVPLGGGVDSDNYAYVLAASMMSGRFGGAVFLPTDNNTLTDTVIQSVCDIRRGKDTNGDGEPDTPFIEFVELVALMADTDRLSDGFGEEIRSLITDGCPATFAGAAPDLVTAD
>CP031165.1|AXV05665.1|1158186_1159836_+|Serine/threonine-protein-kinase
MTDIPYSPDEPDPDWVRFAMPDDFVDAVRVGRGGFGYVFRARELSLSRVVAIKVLNQPSSTEKADQKFTRELQAMGTLAGHPHIITVYTWGKTSGGYPYIVMAYMPGGSLKDLVDNQGVMAWPDAFAAGIKVAGALETAHRAGILHRDIKPENILLNGFGEPSLGDFGIARITGGTETATGSITGSLSHVAPEVLEGNRPTASADVYSMASTLYALVQGRPAFASEGDETLTPMLARILLNPMPPVTAQEVPPDVVALIDQGLAKKPEDRYPSVEAFGNAMADVLSAHGMSAPGMLIRGDADDEVSASGAKTGEFTAPGVRVGDLPTVDRQPPVQASGSTTGEGLVVGAAAAAAGAPPTHRVSESILPPTAPPVPPADDSSRRGLFIGIAAVLAAAVIGIVGVVAFGGDDSVATDDPTPTESVSASETEPSEEDATPSESETDTVKEGTNGLVIPTESETPTETASPSETATATEIPVEETVEPAPVPQAPPPAPAPPPPAPAPPPPAPAPPPPPPPPPPPPPPPPPPPPPPPPPPPPPPPPPPTSSAD
>CP031165.1|AXV05666.1|1159835_1162112_+|Copper-resistance-protein-CopC-/-Copper-resistance-protein-CopD
MVRSPESTGRVGRFVLALVMAALGLALLAGPASAHTSLVASSPASGERLAYSPDEIVLTFATAVDPRTVTAELRSADGEVVAVEPLSGETGDTTVVAFAVPRLPHAVYGLAWQSVGDDGHRVLGEVLFGVGTEVGGTTSVAGGATPMARALDSAGLALRIAWYVVLALLAGVAVVGRAGVAGDVARRRIGGLLLLGAVVALGRGGVALAILLEAGAGDLAWTSRGTVGFAAVGVLLGLLAVAASRRTAGPEARSTPTPALVGLLVAVIGGTLAGHALSREDPVLAVTFGILHLGAAAAWTGPLLVVLLVARTPAWRGLDAEERTAQLRASLRRMVPVAGWSLAVVGATGLLLAARAWSGIQGGVLAVLVVKALVVLAVAVPLGIWHHRTREGWVDVPRTARVEALGLVVALVLGAVLVGWDPGWSQGTGGLDPAVAAVLDGTADDPTLCMDLEVGRAACYRSTLSTVLATQGPQAAIDAAVAAQAVDSYVAENCHQVVHDIGNDAAEQIDDMADALAVDGSACWSGYFHGFIEARLAEIDDDALSDRLPTFCDGAADPQYSFTHYNCLHGLGHGLMLRVDADLFEALPLCRDLEEFWLVRSCASGAFMENVMAAQQGLQTPGVPTDDLRYPCTDVDADLSEDCWMMQTSMIIWRLGGDLPGAFEWCDSVDGLDRTACYRSMGRDISSIAALDPDGVIQRCSMGSADAAHWCIDGAASNAVYETSARESADALCAAVQEDWTAACEVSRDQALSTVALG
>CP031165.1|AXV05667.1|1162159_1163128_+|hypothetical-protein
MITFSCDRCAQLVFFDNTSCTRCGAELVLDPATWSIRSATADDVRCANREHGCSWVTHNGDQYCRSCRLTRTRPSLEDPEIVEKWRRAEAAKRRLVFQLERIGLDVQGATFDLLSSRDEDVITGHADGVITLDLAEADDVERMRIREQMDEPYRTVLGHFRHEIGHWLWTRYVDGSDVIEDFRRVFGDERADYTEALQVHYDAEPPEGWADSYVSTYATAHPWEDFAETVAHWLHITDVLETAGAFGVTVDGPHEVLTSDPDEAEPDTDTMPELIQAWLPLTYALNAINRSMGHDDLYPFVLAPTVMTKLGWVHRRLTGVAA
>CP031165.1|AXV05668.1|1163145_1164297_-|putative-glycosyltransferase
MRAIALTHVFPRWDGDPSAAFLSTWTAALRADGHDVRVIAPHDAGLPEVDVVEDTPIRFVRYAPEDREVLAYRGEMHRIAMQPTGPPLVASMMTLMAGALRRAVRRWEPDVVHVHWWMPGAIITRMAGVDVPVVVHLHGTDIGIVEGRPKLRTLARWALDGADRLEVVSTSLARRTRSAVGRRVDGLNPMPLDIARFTGVEAQMSLDRPVVLGVGRLVPEKGFADLVDAVAGLEDRVVLRLVGDGPAARDLAIRAHERGVELQLPGRIDPADLPAEYAAAEVVVQPSHAEGLGLVAAEAVLMGRPIVATDSGGVRDVLDDRLLVRVGDIEAMTARIRESLHDPDLPAVARAGQRVRRTLSPGASAERTVDGWQQAIAAHRTRR
>CP031165.1|AXV05669.1|1164299_1165289_-|Glycosyltransferase
MRTPVTLSAVVPVYNEIESLPAFHAELVEALHALEVSSEIVYVDDGSSDGSTEELEKLHLGDPDTVRVVVLRRNFGKSAALAAGFDIARGDLLVTLDADGQDVPAEIGTLLATMDREDLDLVGGWRAARIDRRAKRWTSRGYNAATRTFTGLDLHDFNTGFKLLKREVVEEMPLYGEFHRFVPVLAHDLGFRVGEVAVTHRPRQAGTSKYLSLTRFPKTMLDLLTVLFLTRFADRPLYLFGGVGALLSAVGFVILAYLSVLKLATGAGIGQRPLLQFGILSLLVGVQLIGTGFIGDVLRHSASREQVPYRTRRTLAPGQDPTDPLDGDA
>CP031165.1|AXV05670.1|1165482_1168017_+|glycosyltransferase-domain-containing-protein
MSTPTHASLSTGLRQEQPTVSVVVVNLNGRDLLAPCLTSLVRQTHESDRLEIILIDNASTDGSVEMVRKDFPEVRILVNDSNVGFAPAVNQGAEVANGEYLALLNNDAEADPNWIASAVAYLTSHEEVGCLGSLILRDDRETIDYAGGRMAFNGMGYANKVEQSAWENPNYAERTLFASGGAMVVPTQLFLDVGGFDESFFAFFEDVDFGWRLWVLGHEVHFVPSSKVFHRHHGTIKRFGYARERYLLERNALATIFKNYGDDLLARTLPSAVLLTLMRGLTDLTERDGLPDFSIVEGAKNLDDEDFPVPAITAAHLAAMRDFGRNISNLTAKRNAIQDKRERPDSEILPLFKETLRPNVNGREYLEVWNAVEKAFDLHEHLVHRTHVLIITGDTLSERMAGPAIRCFEMATVLHDAGFEVTLASMSPPSVHSRGFHVTWTGAPGGINALLDVADIVIFQGFVMHAIPEIERFDGPVVVDIYDPFHLEGMSHRKHELEWQRYATHNSDTDVLNKQLQRGDFFVCASEKQRDFWLGQMSALKRINPATFDEDESLRSLIDIAPFGLPAGQPIKTEERVLRGVVDGIEEDDFLLLWGGGIYNWFDPLTLIKAVGRVAEDHPDVKLWFMGSAHPNPDVPKMQMASSSYNLAVELGLLGKNVFFNDGWIDYTQRQNYLLEADVGVSTHYEHLETRYSFRTRILDYIWCELPMVATEGDTLSLLAKERGLGITVPPEDVEACADAIRRLRNDKELYQECVDNLAAIKPEMTWERAVEPIVEFCRSPRRAADTSHKRHDYIASNFTLADVVPERSPYYYAKRFIGTATAQGPKTALIHAKNIIKHYTAGR
>CP031165.1|AXV05671.1|1168013_1169498_+|hypothetical-protein
MTDTRGGQTTQGLPRLLSWLPAPLHDPAQRPRLLGWFGVGMVVRLLIAPFTVSADMLAVYWRSHLIAYDGAVYSDYLVNMGAHYTHAMSLRILDPLLPSADVLWTDPWWWADGPALTPQVQRAFVDTDGIFGTLLALKLPYLAFDIAAGLLLLALVAHAAPKHISRAWAFWMLSPIGLYATYAFGRYEMFAVALVVAALWACERDHPWWGAVLLGLAITMRGYPIVLVPIFGLIVMRRPLPRIGWAALSLLPFALVMWTNTLLADTVGEFSRLRDYSTGSTFLAYTIPVDGVGPIYLFGLFAIGLYAVLIGRAYGWWGRGPVPIGELWIWLALFHFSMFALTTFSAHYFAWVTPFVALALARRPEWRGMLWLHLLQVGAVLALADLYGGPGTTWGLLQPLQPDVVDAVPNLREALLTSPGLVEQLAGALRTAFIALMALTCWPLVTSLRATSAPVAAGSAAVGTQAAHGKDESADQREQPEDREDRLGQQPAAR
>CP031165.1|AXV05672.1|1170124_1171666_+|hypothetical-protein
MAGWTMRQALVTPRQSHAAIDDGEHNVMHTHSARPALSPPAGHTSPPGPTRPAGIDRRLFLGGLLGGVATLALPASAARAATAVRAGTDPMAVMVQRINDYRVSNGRPPLPLDHQLSAVAQSWSEHQRNRSSMAHNGNRMAQYGWAVESDGEIVATASATGEDAAQLANRCVDGWIGSSGHRAIMLGDWTDMGLGWAVTSSGRLYATGNFVRTPLPSAGQEALTQSRELIGDGSAGRAVVVRGDLAADALAASGLIDGNTPLLMTRPDQPLPAWLLDELRRVLGGSGTVHLVGGALHGDIDGQIRSIGADPVRLRGSSRYETAAMVAHEVGSLRGTPWRVFLANGDGWADAVAAGAFAARFGTPVVLTPRGSLHGAARSVLDRWPEADRVVVGGELMIEKSVARAAGAWRLTGTDRADTGGRVMLDAWSTRAEPGSALVVSPGWTADGWATGLATTTFSARHSAPLLFAGSGMPGPVADAVRQAGFGPGAPAALRFVRNVPQAARDEFVAATT
>CP031165.1|AXV05673.1|1172113_1174915_+|Alkaline-phosphatase
MRALVALVVAALTAAALVAAPTPAEAASSYDNVTQVLVDNFVDAAVEVAAARTPLGTDTVVLATAANFPDGLTASAVAGDVDGPVLFVETDSLPDATAAEIDRLLDAGDTVYVMGGPSAISNAVTDELSDYTVQRVEGPTRLETAIAAADLVGVPSDGTVLLARAFGPDGAGTTSDRTTGWVDAISCGAYAAANEIPIYLTETDRLSDATAAAIEASSATDVIICGGTAAVNTTVSDALRALGLQVDRVEGPTRVETAIDAAQQLFGFTSAGGHEFTVINGYGENFGYGLAAAPLGDPILMVGTSEPTDCNDATQPSRETLCYLGTGTSTTPANLLVMGDETVIRDTVSNAVGEAAGGEETDDPSQFPALPAPDDVDAVDDIDDDGTRATVTWDEVADPNDILLGYNVYVDGEKQGTSTPTVAGDIETYMLSDLTAEEEVTVTVTTLDAAERESDPSAGATVTPTDEVPAALGAFDANAGNGEVTLSWERGPADTAEYVLSRSTNATCPGGTYAEVETITDERRTTYVDGDVTNAMTYCYQLVVVDEADQESDPANAGPVTPNVGTPQVSIQYPSSDDTVYYGPDLVVEYTVTDTDTDPEDLKATWQVSYDGGAGPYVDMVNGTNVAVDFVEADDDGKATFVARMCPVNDSTSTNCIRDAVDSNLRLRVNVTDGTTTERAFTPDLDLVRNPPPVEGLAVTDAAGQVNLEWERVPVPSTLVSGYRIERAEVRVQSDDEDAGVEVCDLAVQYDDVQGSPVPQPASGATVTFTDPTVDEEDGLSDFVYCYRVYTVRATPTLESPSRLGAGNPLETAGVGVTITDPANNGSLDTGTRETISYKLDIPDGQTVSSVSLYYCVDYGRANPLADPACQDSGGFTQITAANGLVGTPSTADGTNSVQWDVPASINQGDTEEGAIEVRTSGGNGRVIGILFV

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Crispr_ID: CP031165_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_9

1397774-1397886

Orphan

Consensus_repeat	Method
CGGGCGATCACGGCGGGCGGCCCGGAACCCGACACGCGTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_9

>merge|CP031165|9|1397774-1397886|CRISPRCasFinder
CGGGCGATCACGGCGGGCGGCCCGGAACCCGACACGCGTCGGGGGTGCGGGGGCGGTCGCCCCGGACGGTTGGCGGGCGATCACGACGGGCGGCCCGGAACCCGACACGCGTC

>CP031165|9|9|1397774-1397886|CRISPRCasFinder
CGGGCGATCACGGCGGGCGGCCCGGAACCCGACACGCGTC	GGGGGTGCGGGGGCGGTCGCCCCGGACGGTTGG
CGGGCGATCACGACGGGCGGCCCGGAACCCGACACGCGTC

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV05860.1\|1400990_1401476_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274610
CP031165.1\|AXV05850.1\|1394138_1394420_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|227179
CP031165.1\|AXV05851.1\|1394429_1394702_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05847.1\|1388407_1388698_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274862
CP031165.1\|AXV05866.1\|1406358_1406511_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV05854.1\|1396396_1397299_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379325
CP031165.1\|AXV05855.1\|1397332_1397689_+\|bleomycin-resistance-protein	unknown	unknown	gnl\|CDD\|319937
CP031165.1\|AXV05859.1\|1400081_1400960_-\|Flagellar-biosynthesis-protein-FliP	unknown	unknown	gnl\|CDD\|235566
CP031165.1\|AXV05862.1\|1402525_1403710_-\|Flagellar-motor-switch-protein-FliM	unknown	unknown	gnl\|CDD\|235849
CP031165.1\|AXV05864.1\|1404332_1404575_-\|Flagellar-protein-FlbD	unknown	unknown	gnl\|CDD\|377645
CP031165.1\|AXV05849.1\|1389572_1394084_+\|Cell-division-protein-FtsK	unknown	unknown	gnl\|CDD\|274860
CP031165.1\|AXV05861.1\|1401480_1402533_-\|Flagellar-motor-switch-protein-FliN	unknown	unknown	gnl\|CDD\|236154
CP031165.1\|AXV05863.1\|1403817_1404330_-\|Flagellar-biosynthesis-protein-FliL	unknown	unknown	gnl\|CDD\|377123
CP031165.1\|AXV05852.1\|1394706_1395378_+\|Putative-tellurium-resistance-protein	unknown	unknown	gnl\|CDD\|238741
CP031165.1\|AXV05865.1\|1404792_1406352_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380277
CP031165.1\|AXV05846.1\|1387127_1388327_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377587
CP031165.1\|AXV05853.1\|1395389_1396400_+\|Mn2+-dependent-serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
CP031165.1\|AXV05857.1\|1399037_1399799_-\|Flagellar-biosynthesis-protein-FliR	unknown	unknown	gnl\|CDD\|376520
CP031165.1\|AXV05858.1\|1399815_1400085_-\|Flagellar-biosynthesis-protein-FliQ	unknown	unknown	gnl\|CDD\|235567
CP031165.1\|AXV05848.1\|1388901_1389576_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274357

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV05860.1\|1400990_1401476_-\|hypothetical-protein	gnl\|CDD\|274610	TIGR03500, FliO_TIGR, flagellar biosynthetic protein FliO. This short protein found in flagellar biosynthesis operons contains a highly hydrophobic N-terminal sequence followed generally by two basic amino acids. This region is reminiscent of but distinct from the twin-arginine translocation signal sequence. Some instances of this gene have been names "FliZ" but phylogenetic tree building supports a single FliO family.	5.77909e-07
CP031165.1\|AXV05850.1\|1394138_1394420_+\|hypothetical-protein	gnl\|CDD\|227179	COG4842, COG4842, Uncharacterized protein conserved in bacteria [Function unknown].	1.20239e-09
CP031165.1\|AXV05858.1\|1399815_1400085_-\|Flagellar-biosynthesis-protein-FliQ	gnl\|CDD\|235567	PRK05700, fliQ, flagellar type III secretion system protein FliQ.	1.81641e-21
CP031165.1\|AXV05854.1\|1396396_1397299_+\|hypothetical-protein	gnl\|CDD\|379325	pfam13672, PP2C_2, Protein phosphatase 2C. Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.	1.0977e-13
CP031165.1\|AXV05855.1\|1397332_1397689_+\|bleomycin-resistance-protein	gnl\|CDD\|319937	cd08349, BLMA_like, Bleomycin binding protein (BLMA) and similar proteins. BLMA also called Bleomycin resistance protein, confers Bm resistance by directly binding to Bm. Bm is a glycopeptide antibiotic produced naturally by actinomycetes. It is a potent anti-cancer drug, which acts as a strong DNA-cutting agent, thereby causing cell death. BLMA is produced by actinomycetes to protect themselves against their own lethal compound. BLMA has two identically-folded subdomains, with the same alpha/beta fold; these two halves have no sequence similarity. BLMAs are dimers and each dimer binds to two Bm molecules at the Bm-binding pockets formed at the dimer interface; two Bm molecules are bound per dimer. BLMA belongs to a conserved domain superfamily that is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. As for the larger superfamily, this family contains members with or without domain swapping.	1.56239e-29
CP031165.1\|AXV05859.1\|1400081_1400960_-\|Flagellar-biosynthesis-protein-FliP	gnl\|CDD\|235566	PRK05699, fliP, flagellar biosynthesis protein FliP; Reviewed.	1.23313e-101
CP031165.1\|AXV05862.1\|1402525_1403710_-\|Flagellar-motor-switch-protein-FliM	gnl\|CDD\|235849	PRK06666, fliM, flagellar motor switch protein FliM; Validated.	8.73677e-80
CP031165.1\|AXV05864.1\|1404332_1404575_-\|Flagellar-protein-FlbD	gnl\|CDD\|377645	pfam06289, FlbD, Flagellar protein (FlbD). This family consists of several bacterial FlbD flagellar proteins. The exact function of this family is unknown.	1.30895e-18
CP031165.1\|AXV05849.1\|1389572_1394084_+\|Cell-division-protein-FtsK	gnl\|CDD\|274860	TIGR03928, T7_EssCb_Firm, type VII secretion protein EssC, C-terminal domain. This model describes the C-terminal domain, or longer subunit, of the Firmicutes type VII secretion protein EssC. This protein (homologous to EccC in Actinobacteria) and the WXG100 target proteins are the only homologous parts of type VII secretion between Firmicutes and Actinobacteria. [Protein fate, Protein and peptide secretion and trafficking].	3.97309e-133
CP031165.1\|AXV05861.1\|1401480_1402533_-\|Flagellar-motor-switch-protein-FliN	gnl\|CDD\|236154	PRK08119, PRK08119, flagellar motor switch protein; Validated.	7.46825e-38
CP031165.1\|AXV05863.1\|1403817_1404330_-\|Flagellar-biosynthesis-protein-FliL	gnl\|CDD\|377123	pfam03748, FliL, Flagellar basal body-associated protein FliL. This FliL protein controls the rotational direction of the flagella during chemotaxis. FliL is a cytoplasmic membrane protein associated with the basal body.	5.82906e-17
CP031165.1\|AXV05852.1\|1394706_1395378_+\|Putative-tellurium-resistance-protein	gnl\|CDD\|238741	cd01464, vWA_subfamily, VWA subfamily: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup have no assigned function. This subfamily is typified by the presence of a conserved MIDAS motif.	3.80131e-25
CP031165.1\|AXV05865.1\|1404792_1406352_-\|hypothetical-protein	gnl\|CDD\|380277	NF033435, S-layer_Clost, S-layer protein SlpA. In Clostridiodes difficile, the S-layer protein precursor, SlpA, is one member of a large paralogous family of protein that share several cell wall-binding repeats. SlpA is cleaved into a larger and smaller protein. The S-layer protein itself is important to adhesion, and portions of it are highly variable, and then N-terminal and C-terminal are well-conserved.	2.45181e-17
CP031165.1\|AXV05846.1\|1387127_1388327_-\|hypothetical-protein	gnl\|CDD\|377587	pfam06013, WXG100, Proteins of 100 residues with WXG. ESAT-6 is a small protein appears to be of fundamental importance in virulence and protective immunity in Mycobacterium tuberculosis. homologs have been detected in other Gram-positive bacterial species. It may represent a novel secretion system potentially driven by the pfam01580 domains in the YukA-like proteins.	0.00304643
CP031165.1\|AXV05853.1\|1395389_1396400_+\|Mn2+-dependent-serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.69911e-05
CP031165.1\|AXV05857.1\|1399037_1399799_-\|Flagellar-biosynthesis-protein-FliR	gnl\|CDD\|376520	pfam01311, Bac_export_1, Bacterial export proteins, family 1. This family includes the following members; FliR, MopE, SsaT, YopT, Hrp, HrcT and SpaR All of these members export proteins, that do not possess signal peptides, through the membrane. Although the proteins that these exporters move may be different, the exporters are thought to function in similar ways.	1.14835e-42
CP031165.1\|AXV05847.1\|1388407_1388698_-\|hypothetical-protein	gnl\|CDD\|274862	TIGR03930, WXG100_ESAT6, WXG100 family type VII secretion target. Members of this protein family include secretion targets for the two main variants of type VII secretion systems (T7SS), one found in the Actinobacteria, one found in the Firmicutes. This model was derived through iteration from pfam06013. The best characterized member of this family is ESAT-6 from Mycobacterium tuberculosis. Members of this family usually are ~100 amino acids in length but occasionally have a long C-terminal extension.	4.75144e-10
CP031165.1\|AXV05848.1\|1388901_1389576_+\|hypothetical-protein	gnl\|CDD\|274357	TIGR02937, RNA_polymerase_sigma_factor, RNA polymerase sigma factor, sigma-70 family. This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.	2.56064e-18

>CP031165.1|AXV05855.1|1397332_1397689_+|bleomycin-resistance-protein
MIGRSLGHIVPHMILPVADMAAAMAFYRGLGFDVEAHSDTYAWVRHRGHEILHLDLVPELDTATNPVTGYLHVRDADAWHREWADQPTLTPIVDQPWDMREFTLTDPSGNTLRVGHNR
>CP031165.1|AXV05854.1|1396396_1397299_+|hypothetical-protein
MTLVDRPGEPTTFGQPQRAAGVEAQLLRGDGVHAADTIIDHGCFGNLVVRAASVRGTYARYESGPREDDYTMGAAGDGRWLVVALADGVTSASASHLAATLAVRTAVQQVQRQLDEDGLGVDLHGVFQSAAYQLRRSAEPLLEADGLDCTADHIAALFATTLLVAIVPAAGADRRVRVARVGDSNAWTLGDGGWTPLLAPKAGGAPLASSAVRALPRLPEAVEVIEVDVAPGRTLVLASDGVTDPFGPTFDGDVARCLAREWHPELPAPLEFARQLSFRGQSWDDDRTAIAITGIGLPAT
>CP031165.1|AXV05853.1|1395389_1396400_+|Mn2+-dependent-serine/threonine-protein-kinase
MTSTTTPRTLRLRDLVLTDEIGDGGEGTVHDIQATRGVPAGAVLKRYQRNLSPARVDQLDALVALRAQLRLGMAPYAWPEATVLEDGLLVGVLMPRAPDPFWVEVTLRSGGRQQRLREVQYLLFPAEKLARLGIAFATLPERLELLAALAAAVGRLHDLGLVYGDLSARNVLYATDGPIGVFLLDCDGIVEEGARYVVDSPDWTDPAAPEVAMRATDVHKLGLLAARVLAVDPTTRTLPGGGGTPAVLRDVLSAALDPSPSARPDIFELQQALGRCAPGPADSGADLPRWALRPPAGELVLLSIPEPRRPEEDGGGRGSRSGRFGRRGVRSRRGRS
>CP031165.1|AXV05852.1|1394706_1395378_+|Putative-tellurium-resistance-protein
MTTSGQNLLPFYLVLDVSSSMVGEGMQAINTALPGLLDEISTNLIVADKTRFCLITFASEAQVALPLCDLSEVQAMPVLVPTGLTNYHKVFRLLRNTIAADVERLKAAGAAVYRPTVFFLTDGNPNSDDWVATYRDLVSDAFPYRPNIMAFGVGNVSTTILGQVATSKAFLAIDDPGAALTEFASTLTKSIVKSGEAADGRVQVPVEPGPGFREVDVIDIDQI
>CP031165.1|AXV05851.1|1394429_1394702_+|hypothetical-protein
MSETVVDPAHLRALAGRAEGLSGEVGGLGSLVEELAPAAAGDPGLAAAVGAFVQAWRARAVEMEAELTDAGGFLRTFADAAEQMDASLSE
>CP031165.1|AXV05850.1|1394138_1394420_+|hypothetical-protein
MTQFFVAPDELRGHAGQLDTYALSTQQGFDSLRSELADMEAYFTGLASTAFQGHMEEWQTSARALTTALASLGQFLNSEAASAEELDAQLAAG
>CP031165.1|AXV05849.1|1389572_1394084_+|Cell-division-protein-FtsK
MSAHDDEVVRQLVRGRDGRWTMADAPVTGSEDVERIPSNRSEPAPGRTSNSTLDTSPPGTSTPGTGPLDTGPMVRRLLVRAGGTDRHVVVLGDSGQSTDQLLEELQRIVPGTPLIDGAPLPRGTMVESLGLRDGQVVTVESDDPQVVTVEADDPQPAGPATGPVLRIVGGPDAGRTIPVRMGQMTIGRAAGNSIVLADPNASRSHCVVHRDADGIVVIDVGSANGTRVEGVPEPQARLQPGDLLRLGDSLLELGDADDVEAVVLEQGHDALGVHRRFRAGVDDPPNRIRYPQKRDPGEPQPLNLLMAILPAGGIAVMAFLFGRPEMLIFAAMSPMLAIGRNISAKRNHRDKVLQSEVDHREAVARFSTDFAVMRAAERRHRRHAVPDPARIVEAATRPTTELWNRRCTDADALTVRIGSAFAPSTIDVEGAPEQDADEPQPWLPVGVSLVEFGGLALVGDLPRVRALARSLVLQAAVLHAPSELRIVFLGGHDAAGDWSWLRWLPHVRRGPLEPSLLLGTDASSRAARVEELRRILTERREAAEDRRSVFAPRILLVCDDASARLGEGVAELVRDGGPLGIHALCLDTLQVPEGCDASVVLGERVDGARVERRGQPPVRGVITDALDADRCEEVSRALAPVRVIGEEDDDGLPTSCRLLSTLGLQPTATHVRARWRAMSPSSRATIGVGPERPIALDLTRDGPHALVAGTTGAGKSEFIKTFVASLALENHPDHLSFLFIDFKGGGDYRTLVRLPHAVALATNLDDPAAFDRTLALLEAEMGRRVGLLQAAGTTSIEGYMAVPGGPPTPMPRLVVVADEFAELKDKAPQQLDRLVSVARTGRSVGVHLLLATQRPGGVVTSQIDANVGLRVCFRVTDEQESKEVIGSPLAGRIAERHRGRAVFRSAATPLTEVQTARVAGARPGAVSAAPVRAVELDWERLGRPFPKGPETGEVPDADTDLHDVVEALRQAATDEGWTHSAIPWPPELPDQLPVSALPRDAAALADAIPVGLVDVPSTQRQEVQHIRLGGGHVVIAGSARTGRSTALRTFLTGVVQRFGPDDLRIAALDFGGGALLPVQQLPHCTGLSMEDLVEAEGIVASLERELARRRDLFAEHGWPDLPAQRAQSDTPLPWLLLAIEGWDNLAEEGMRQSLHTRVAQLLARGTPQGLQVVMTGDRGTTHSMIARHLTHRYSLRFNRSVDAELQGIMARDLPRHQPPGRAVEIRTTRLLQFAELDDPDRVGQAVAFQRALAEVVLAAGAGAEPRRGLGTEPTSTMPDAMDMAATGPPADTTFPLLLGMGEDPREPVWADLEDSGGLFFVVGPPGTGRSTTLRTMAVAAHHIGIDVAVAGPDTSPLATDPTVPGQRVSLADHETLVPRAGRRLLVLIDDLDLLEDSRALQQTLGSSLPGRGVVVTADITWMKARFSGLAAAVRRPRRGVILSPPSTANGVEMFAASLDPGLIAPPDPGRAVANLGGGHVLLRVPEPPGESSGAGEELGGVDR
>CP031165.1|AXV05848.1|1388901_1389576_+|hypothetical-protein
MQGARRGSAADGPPVDGHDGAPSDRVLVRSVRDGDEGAFADLYARYEPVARRSARRAARRHPQLDVEEVTNLAITRLWQVLDRFDDERDFAPWAAVVLAHAVRSAAERTRSATSRMNWGAMLAGSAGEDRDRIGELPAPSTPDADGLASVLLDEQERVVAGLLQDVLSPREAKVVRLRLAGWSYTEIADRLDLAPKAVDNALRRGMARLRDAFADGRVEAVMSP
>CP031165.1|AXV05847.1|1388407_1388698_-|hypothetical-protein
MSVIRANHEEITRMAGRVGQAAVVAQEEIASCRSQLSSLNDSFTGETAAAFQTRYEEWNTAAAELTTALDTLGRWLQERGDLIAEWDTRNAASVLS
>CP031165.1|AXV05846.1|1387127_1388327_-|hypothetical-protein
MNAPFHRPGISDGDSRWDLLGGCPTPGSPEAIDDAAASMRTRAEAAEDLYDQLQQLGLDLGDSGWGGPTAAAFAERFSALPARVLTARIALDAVSKALARWGEALHALRIDGLRALVDAEAAHAAWAAANDARTEAYQQGQLELHHDAAVGEAMRDLEAARARAAELRTDHAELAASATRIIHDQTPHAAGPDDDLLTAMLDHLGGPDLVAAVLGTGLDADSDGDGDTIDPAGEIAGIVADSWSEVVLGLQGALEDVMGAAVIGPARTDAYLHGEETAASTADILHLAVDIGEGVPLPPATLPPLEGLVDLVPTVPTGVSVPLDLVAGLQVTSVDIPRPLRYVDWFAAVAASPAALTPAWLDLMDLQAVAGPAVTRAGDTLALSGGVPVAGTFDAEAQR
>CP031165.1|AXV05857.1|1399037_1399799_-|Flagellar-biosynthesis-protein-FliR
MTLSIAPFLLTGFLLASVRAAAFLMVSPPFDSRLIPQRVKAGLAMSLGLVAGPHMAESQVPIEVGPLIAAGAFQIGLGVTLGFLVKLLFAAVQSAGEMIDVFGGIAVQPSFDPLSNSQASGFGRIYQVFATTLLFAIGGHVLLVRGFLESFEAVGVGGIEMATVQSLVVGNFLHFVVAAVEIAAPLLAVTFLLELGQGLVARAAPQMNVFLAVMPLKILMALVLIAIALPLLPGAVSSLVDNGVSDMVRLARS
>CP031165.1|AXV05858.1|1399815_1400085_-|Flagellar-biosynthesis-protein-FliQ
MNDVAVLEIGIQAMWVATKVAAPILVMALGIGLFVGLMQSVTQIQEVTLTFVPKFVGIAFVFAVGGNWMLNEIVTFTRVLFESIPSLLG
>CP031165.1|AXV05859.1|1400081_1400960_-|Flagellar-biosynthesis-protein-FliP
MHTLVNPRQSTLHTAVLLLLLVGTMLVLFAPAADAQGIDPSLVPDRIAPVSPAAGLAANVPTSPMLGDDTGVAFELDLGDTVQEPSQSLVVILLLTVLALAPSLLIMLTSFTRIVIVLSVTRNAIGLPSVPPTQVVVGLALFLSIFTMTPTFSEINETALQPLLNEEMETMEALELAQKPIRTFMMGQVGEEELAMFVDASGDVRPDTPEDIPMTTLIPAFILSELKAAFIIAFVIFVPFLIVDLITASTLMSMGMMMLPPVLVSLPFKLLLFVLVDGWTLVIRSLLESFAT
>CP031165.1|AXV05860.1|1400990_1401476_-|hypothetical-protein
MTDVSVISLLARLAVSMTVVIALMLLAARILRRTAGGMGIGGRGKERRTPIDVQTLQPLTKTAHVAVVRAAGRELVLGITDQQVTLLHSGIEPRDSLVDLDLDAADTTSETTTDDERISPLDVTSTRARIAPVPAEDATTPSALTAWTDALETLREKTVRR
>CP031165.1|AXV05861.1|1401480_1402533_-|Flagellar-motor-switch-protein-FliN
MSETLLEATVAAVVRRIGGRLPAAYTLDPQDLRIGGDADHTLPDGGTTVRWALGTDDGHLVVAITADAAEMLAAEGPLVDVMTARVEAAAIDLAIAFGGIPPMLGEGVEVDPSTAFEGPTGEPVSVLLDDAGVHRATIGLRLELTDALMGPVPEDLPEFDLGPFPGDDEPTVDAEDVPASSGDGVTPMTQPGQPQPGQPQPGQTQPASPHAQPQTGPGLVTAASRGQGRAPGRGPMDVPTGQAHPADFSSFDQLSALPGQGQSSMSLLGDVEMGVTAELGRTQLTVRDVLNLTPGSIVELDRAAGSPVDVVVNGTLIARGEVVVIDEEFGIRITEILGAVEQATPFPMAQ
>CP031165.1|AXV05862.1|1402525_1403710_-|Flagellar-motor-switch-protein-FliM
MSMPGTADVSTVIEVDRTGTPRERKVAPYDFRRPNKVSRDHVRALQLVHETFARQFSTILSSTLRTLAPIQVTSIEQRTYDEYISPMSNPTYLAILEVEPLPGQGIFHLPLAAAMEIVERLLGGPGGGEHPQRPLTEIEIGLLRGLLDRILRELTYAFESFMDVETRIASQESNPQFAQVVGLSDMVVVATYAVGIGEASWEATLCFPFQMLQPALEAFTESKKSAASDVAERQRHQSLLHDHLHDAPVDVAVHFNTVRLSGSEIVGLRTGDILPLRHRVDAPLTIAVGGVPCFSATPGKQGRRLAAMVLPPTEDLAAEQAAAGQPVGIEAAVGTALPSAFPASTFPAAAFEAPSGPTGPADTVSTHAVSTHAVPTHAVPTPAVPTHHEDQTHE
>CP031165.1|AXV05863.1|1403817_1404330_-|Flagellar-biosynthesis-protein-FliL
MARKKKADDAEAAGTDTAKTPDDDGAKKKGGMLPAIIVAVAVLAGGAMAGGVIGGGSGAAAAAGPAPEPTPTPMALGTVIEMDSITLNLVGEGMHFLKLGVAVELGPDTVEEPPSAPIYDVIIDLFGDYTYADLLAPDARDVTKEQLLAQLSAIYGESIVRVYYTEFVMQ
>CP031165.1|AXV05864.1|1404332_1404575_-|Flagellar-protein-FlbD
MNPDLMERIEATPDTVVSLVDGTKHVVIEDVDQVVALVRHFRASVVALAQHMEVQPASVGPDPGSAPAPGLRLVTRSGGE
>CP031165.1|AXV05865.1|1404792_1406352_-|hypothetical-protein
MPSPSIRLVSPALAVALLLALLTTMLVATPAAAESRCWADAAGDVDANNTADDEALDTVPEIDILAVCADLNADRLEMTFRVAAPHDPAGNADWDDTATSLGVEIDINGEDPENADRDYTVNMARFQDQPAGAFPEVRVYKGDSRTAYDPDGDGPQGACAMAGVFDGLRYKLTVPARCIDGATNIQLAMYAFHDAQLDDPTAGFYDEVPAFPEYNGPVTTTDDVETPVDRLAGPSRVETALAISQDDFEEGAAGAVVLARADASPDALAGAPLAVAVNGPLLLTARDSLPTSVEAEIQRILPDGGRVVLSGGTAAISEAVAEQLTAQGYEVVRAAGDTRYATSVEVARAAVADPSVIVVADGNGFADALVGGALAAEEDGVQVLSNGTQLDDTAAAYLAEHPDAEVIAIGQNAVQAVPDADVQLSGGSSFETAVIVARERYNDPSGVAIASGTNFPDGLAGGAHAGRAGIPLLLSWPDVLPDITSTYLGEVTPVDRVVMYGGVAATSYTVEATSASALG
>CP031165.1|AXV05866.1|1406358_1406511_+|hypothetical-protein
MLLVRRCRGPGLDCGCTHFSPARYSDVCRTRFIAADARPISQHMGNMGLG

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Crispr_ID: CP031165_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_10

1585806-1585903

Orphan

Consensus_repeat	Method
TGTCGCGCGATCACGACGGGCGGCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_10

>merge|CP031165|10|1585806-1585903|CRISPRCasFinder
TGTCGCGCGATCACGACGGGCGGCCGGTTTCCCGACACGCGTCGGGGTTGAGGGCTCGGGCAGGGGTGACGGGTGTCGGGCGATCACGACGGGCGGCC

>CP031165|10|10|1585806-1585903|CRISPRCasFinder
TGTCGCGCGATCACGACGGGCGGCC	GGTTTCCCGACACGCGTCGGGGTTGAGGGCTCGGGCAGGGGTGACGGG
TGTCGGGCGATCACGACGGGCGGCC

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV06018.1\|1575384_1576086_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06030.1\|1589171_1589807_-\|EpiH/GdmH-related-protein	unknown	unknown	gnl\|CDD\|99750
CP031165.1\|AXV06025.1\|1584418_1585150_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376806
CP031165.1\|AXV06028.1\|1586668_1587532_-\|lipase-class-3-family-protein	unknown	unknown	gnl\|CDD\|238287
CP031165.1\|AXV06031.1\|1589918_1590620_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226101
CP031165.1\|AXV06021.1\|1579284_1581405_-\|Gamma-glutamyltranspeptidase	unknown	unknown	gnl\|CDD\|367829
CP031165.1\|AXV06017.1\|1573965_1574961_+\|transporter-of-the-drug/metabolite-transporter-(DMT)-superfamily	unknown	unknown	gnl\|CDD\|273359
CP031165.1\|AXV06034.1\|1592012_1593431_-\|NADP-dependent-malic-enzyme	unknown	unknown	gnl\|CDD\|223358
CP031165.1\|AXV06020.1\|1577801_1579268_+\|Putative-amidase-amiC	unknown	unknown	gnl\|CDD\|181154
CP031165.1\|AXV06035.1\|1593457_1594123_-\|Iron-dependent-repressor-IdeR/DtxR	unknown	unknown	gnl\|CDD\|224240
CP031165.1\|AXV06036.1\|1594242_1594794_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06033.1\|1591444_1592011_-\|NTP-pyrophosphohydrolase-including-oxidative-damage-repair-enzymes	unknown	unknown	gnl\|CDD\|239646
CP031165.1\|AXV06026.1\|1585211_1585781_-\|putative-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
CP031165.1\|AXV06022.1\|1581443_1582082_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372667
CP031165.1\|AXV06019.1\|1576129_1577689_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|173787
CP031165.1\|AXV06024.1\|1583095_1584370_+\|putative-membrane-protein	unknown	unknown	gnl\|CDD\|341028
CP031165.1\|AXV06037.1\|1595011_1595953_+\|Peptide-chain-release-factor-2	unknown	unknown	gnl\|CDD\|234799
CP031165.1\|AXV06032.1\|1590703_1591375_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06029.1\|1587634_1589164_+\|Cyclohexanone-monooxygenase	unknown	unknown	gnl\|CDD\|224983
CP031165.1\|AXV06023.1\|1582209_1583058_+\|Acyl-CoA-thioesterase-II	unknown	unknown	gnl\|CDD\|224857

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV06030.1\|1589171_1589807_-\|EpiH/GdmH-related-protein	gnl\|CDD\|99750	cd06259, YdcF-like, YdcF-like. YdcF-like is a large family of mainly bacterial proteins, with a few members found in fungi, plants, and archaea. Escherichia coli YdcF has been shown to bind S-adenosyl-L-methionine (AdoMet), but a biochemical function has not been idenitified. The family also includes Escherichia coli sanA and Salmonella typhimurium sfiX, which are involved in vancomycin resistance; sfiX may also be involved in murein synthesis.	2.47919e-41
CP031165.1\|AXV06025.1\|1584418_1585150_+\|hypothetical-protein	gnl\|CDD\|376806	pfam02517, Abi, CAAX protease self-immunity. Members of this family are probably proteases (after a isoprenyl group is attached to the Cys residue in the C-terminal CAAX motif of a protein to attach it to the membrane, the AAX tripeptide being removed by one of the CAAX prenyl proteases). The family contains the CAAX prenyl protease. The proteins contain a highly conserved Glu-Glu motif at the amino end of the alignment. The alignment also contains two histidine residues that may be involved in zinc binding. While they are involved in membrane anchoring of proteins in eukaryotes, little is known about their function in prokaryotes. In some known bacteriocin loci, Abi genes have been found downstream of bacteriocin structural genes where they are probably involved in self-immunity. Investigation of the bacteriocin-like loci in the Gram positive bacteria locus from Lactobacillus sakei 23K confirmed that the bacteriocin-like genes (sak23Kalphabeta) exhibited antimicrobial activity when expressed in a heterologous host and that the associated Abi gene (sak23Ki) conferred immunity against the cognate bacteriocin. Interestingly, the immunity genes from three similar systems conferred a high degree of cross-immunity against each other's bacteriocins, suggesting the recognition of a common receptor. Site-directed mutagenesis demonstrated that the conserved motifs constituting the putative proteolytic active site of the Abi proteins are essential for the immunity function of Sak23Ki - thus a new concept in self-immunity.	3.59195e-06
CP031165.1\|AXV06028.1\|1586668_1587532_-\|lipase-class-3-family-protein	gnl\|CDD\|238287	cd00519, Lipase_3, Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site. .	3.24776e-32
CP031165.1\|AXV06031.1\|1589918_1590620_+\|hypothetical-protein	gnl\|CDD\|226101	COG3571, COG3571, Predicted hydrolase of the alpha/beta-hydrolase fold [General function prediction only].	3.75448e-38
CP031165.1\|AXV06021.1\|1579284_1581405_-\|Gamma-glutamyltranspeptidase	gnl\|CDD\|367829	pfam04122, CW_binding_2, Putative cell wall binding repeat 2. This repeat is found in multiple tandem copies in proteins including amidase enhancers and adhesins.	1.28554e-12
CP031165.1\|AXV06017.1\|1573965_1574961_+\|transporter-of-the-drug/metabolite-transporter-(DMT)-superfamily	gnl\|CDD\|273359	TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter. [Transport and binding proteins, Amino acids, peptides and amines].	6.2636e-13
CP031165.1\|AXV06034.1\|1592012_1593431_-\|NADP-dependent-malic-enzyme	gnl\|CDD\|223358	COG0281, SfcA, Malic enzyme [Energy production and conversion].	1.46569e-162
CP031165.1\|AXV06020.1\|1577801_1579268_+\|Putative-amidase-amiC	gnl\|CDD\|181154	PRK07869, PRK07869, amidase; Provisional.	0
CP031165.1\|AXV06035.1\|1593457_1594123_-\|Iron-dependent-repressor-IdeR/DtxR	gnl\|CDD\|224240	COG1321, TroR, Mn-dependent transcriptional regulator [Transcription].	4.9387e-46
CP031165.1\|AXV06033.1\|1591444_1592011_-\|NTP-pyrophosphohydrolase-including-oxidative-damage-repair-enzymes	gnl\|CDD\|239646	cd03674, Nudix_Hydrolase_1, Members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity. They also contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, U=I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of nudix hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.	7.54547e-30
CP031165.1\|AXV06026.1\|1585211_1585781_-\|putative-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	2.4276e-13
CP031165.1\|AXV06022.1\|1581443_1582082_+\|hypothetical-protein	gnl\|CDD\|372667	pfam13669, Glyoxalase_4, Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily.	5.89633e-05
CP031165.1\|AXV06019.1\|1576129_1577689_-\|hypothetical-protein	gnl\|CDD\|173787	cd00306, Peptidases_S8_S53, Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.	2.35658e-12
CP031165.1\|AXV06024.1\|1583095_1584370_+\|putative-membrane-protein	gnl\|CDD\|341028	cd17475, MFS_MT3072_like, Mycobacterium tuberculosis uncharacterized MFS-type transporter MT3072 and similar transporters of the Major Facilitator Superfamily. This family includes the Mycobacterium tuberculosis uncharacterized MFS-type transporter MT3072. It belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.76759e-25
CP031165.1\|AXV06037.1\|1595011_1595953_+\|Peptide-chain-release-factor-2	gnl\|CDD\|234799	PRK00578, prfB, peptide chain release factor 2; Validated.	4.95605e-180
CP031165.1\|AXV06029.1\|1587634_1589164_+\|Cyclohexanone-monooxygenase	gnl\|CDD\|224983	COG2072, TrkA, Predicted flavoprotein involved in K+ transport [Inorganic ion transport and metabolism].	4.10478e-94
CP031165.1\|AXV06023.1\|1582209_1583058_+\|Acyl-CoA-thioesterase-II	gnl\|CDD\|224857	COG1946, TesB, Acyl-CoA thioesterase [Lipid metabolism].	2.84251e-113

>CP031165.1|AXV06026.1|1585211_1585781_-|putative-acetyltransferase
MQPSTLVVRPVRPEEYVETGRIVLAAYDAAGRIEGPYRIRIEDTAARAEAGSEVWVAVDGDRVLGSVTFTDAGDPNLEDDTHGDCGFRMLGVAPAAQGLGVGRTLVQRCIDTATERGRRRLSIYSMIWMPAAHAMYERMGFTRRRDRDVLFPAGVGWAFQRNLVPDADAWFPPEGPPAEPPPWYLDVLG
>CP031165.1|AXV06025.1|1584418_1585150_+|hypothetical-protein
MSIERSQQLDPRADPELDRQVVRKLDRQGVRLAVAFVGLSVIWGLAFNLTGLPFFPVVVAGGVVTGLTGFWVRRANDEPEPSFALTWPVAGLAVVVALVHFAVGHLLFGLASRVLPAFTETALEVYQRTGTLPVWGQLLLGGVLTAGLEEVFWRGAFTTMVADRVRPHLPDGLGRKRQGFALVVVSTAGYALFHVATLKLALIAAAALGGLVWGSLLLVTRSVGATIIAHVLWTCLMILFPPT
>CP031165.1|AXV06024.1|1583095_1584370_+|putative-membrane-protein
MSQSDATSQFDAGAAAPTAAADPPGRWRALTVLSAAMILSMATWFSAAAVLPQLREDLGISAAQGSLLTIAVQLGFVVGAVATAATNLADLVRARRLVLLGTIGAAAANLGLLAAGSFGPALVLRFLVGASLSGVYGPSLKSMSTWFRQQRGTALGVMVGALTLGSALPHLVNSFGGIDWRLLIVVTSTLTVAGGLLAELGTDDGPFPFPSTPFDPSKLGLVFTDRKVRLASIGYFGHMYELYAMWAWFAVFFTDVLDGDTRGAALVTFVVIGMGAIGSWVGGVLGDRFSRTTSTSIAMGISGTMALVVGALVEAPWPIVLVAGLVWGFWVVADSAQFSALVTEHADQRYVGTAVTMQLAVGFTLTVVTIWLVPLVRDATSWWLAFAILVPGPVVGVVAMQRLARLVASESTASPGGGARTARA
>CP031165.1|AXV06023.1|1582209_1583058_+|Acyl-CoA-thioesterase-II
METPPSTLLQLLDIETLDVDLFRGTAPNTDVQRTFGGHVAAQSLVAAVRTVQEERSVHSLHAYFLRPGSPKHNIIYTVDRIRDGRSFSTRRVVATQQGKAIFHLSASFQVHEDGPEHAEAMPDVPSPDELENLPDQLKRYGVDWQPPHPEWASMDMRYVKLPNEAAAERSGRLQAWIRSLDTFPDEPHLHACVLTYMSDVSLLGASITPHGLFPGGPDRIRLASLDHAMWFHRPFRADEWMLYDMQSPSASGARGFSRGQVFTQDGRMVASVVQEGLTRPKA
>CP031165.1|AXV06022.1|1581443_1582082_+|hypothetical-protein
MQPTTLTAVHVADDPLAWQRAGFTVAAGVVHLGGLAVVLGAEGEAGVTGWSLDPVTDHVDGLPVLPPPASGDDLLAGQPAHANTATVLDHLVIGTPAPDRTTAALEGLGWSVSRSAAHPTLDRAMRFLVVPTPDGRTVLEVMAPSAPRPDDRPARFWGLAVTVADLDAAVALLGPDHIGRAKDAVQPGRRIATVRGERLGISVPLALMSPRP
>CP031165.1|AXV06021.1|1579284_1581405_-|Gamma-glutamyltranspeptidase
MRAASTLLSVLLVVLVVVTATPNEAVTAQEGATRVALADWTPLPAAGQAEVSAEAQALRAELLGPDALDPDTVTMHWFGVSGFVLTYRGHLLLLDAWEIIGATNDYAPIGREELAALEPEAILIGHGHFDHAADAGYVAGRTGAPIVGSEEICDNAEADATAEGNTITCVITGTADTPAPGTAQPLQLFADTEPITVLQHIHSAATPPGPDNQPNPQVPVFDPAPYIEHFADDPEELARFVASQSDQQGGTWMYHFVAGDFTLLWGNSSGPIFTDPAVGEALGAFPGCVDVMSNAILGFDQVVSGLQDPRLYVDAVQPKVYLPQHGDAWAPVISAGQAQYVPLWKVENTELGIGQPATRFLVDPDEYMIPVAFDIHDPLWADETPGSACATQRIDRRWGSERHATAVRLSQARFAPGADEVWLATGESYSDALAAVPAAALTASPVLTVRPDSIPAVVADELHRLRPSTVVIVGDETVIGTGVEEALATLGFAADDVQRIGSGDAYQRAAAVSAARFDAAETVVVTSGERFPDALAAGPLAAARQAPLLLTEAGTLPEATAAELQRLADGTGLPGGDPLQVVIVGGTAAVDDAVADAIAAITGGPVTRVAGPDRVATAAAVAALEDFDGAPTVYVARSDDFPDAVVAGAPASVDGAPVLLVGRDAVPEATRDALAVADGAAWAVVAGGDAVIGPAVRQQVSDALPD
>CP031165.1|AXV06020.1|1577801_1579268_+|Putative-amidase-amiC
MSDAVPTAVPDPVPDPDARPRVVADGPMADWDAVGTARRITGGDVTATEVLDAALARLAEVDTRIGGLFHLDGNRAHEVLARRQRTGDTDRPLHGVPTAVKDLDQLAGMPTSFGSRATAGHVSGRTDAPVRQFVDTGLIAVGKSAAPEFGMTATGEGLGFAPTRNPWDPQHTVGGSSSGAAALVAARALPIAHAVDGGGSIRIPAACAGLVGLKPTYGRLVEDEDMRGLPVKVVSHGVVTRSVRDTAAFLAAAERTFRNPTMPSIAGVDGPGLGSMRRVAMITESATGPVDGEVLEAVERTGAALETLGHRVEPVVLPFPSTLAEDFLLYWGALAQGVTVTGYAKVGRAFAPEQLDPWTRGLAGHFRSNLHRFPGAIRRLRAFRHDYATFTERYHVVLGPTLGTLPPELGWLSVELPFEDYRERVERFVPFTPAWNVSGAPAVSLPMALSRSGLPIGVHLGAAHGDDRTLLELAFALEASAGFNRPLG
>CP031165.1|AXV06019.1|1576129_1577689_-|hypothetical-protein
MRLPRLTAFAMTIAMASALPAVADPIPDPTATEADDAVVIAVVDSGFSPYHLDFRADLMPQHLDGDPSNDLPLDTDPADWLPGYADAVGVASTGAIDLTLTTDTSVPIEQLEDADNAHDQLPQSSAGDVHMRHIPGTKIVGALDFGGGTDGFFGANNSHGNGTSTVSAGTIHGTCPECLVVLIRYGGDDREAASNWAMNQPWIDVVTNSFGFSTLMRDRIYDGSNTDLQRQASERGQTIFFSAGNGQANAFVAPNTTYQSSQEGPDWIITVGATDTDGREYTGTGKAADISSIGTGYPAGYGGATINGSGNFSGTSNATPVAAGTYARALYDLRTAMAGPSRIQHDGVISVGDLSCGTAVADCAVADSEVDATEMRFGFLHAASQTDPGLRPGQVGVTTPAVDEVEYASEGHGTLFGRLPDNFRWLEEVAAVVEPLTGVRAPLDRPQAEHDWFVVDSWCRQEIHGGWDGGYWVEGETELPTVSGPLTTAMATACPTVFGALNALGTDDAADGPEQLDRG
>CP031165.1|AXV06018.1|1575384_1576086_-|hypothetical-protein
MANAPLVPPDLDEIRRLLRPQISSIPQILADWPRGEGPLADVPLLDPGMLSPRVFEELAGTVRVASATESLVTVAGLLEIPTGGLLVTAMVLCPADLSSPPDVEGSRRTLAEEGARSEQVLVEVAALLSPVEDGKGPAAGVGIVRPLVMADPAAFPHPEDPTAYGVELRETARTAVEEDVEVVSDLGGRPMDPLPVDLARIWSPIFSVARAATAGLAARGAGGTERDETGSGD
>CP031165.1|AXV06017.1|1573965_1574961_+|transporter-of-the-drug/metabolite-transporter-(DMT)-superfamily
MSNDRVAGFAQRFPLVLVASGVVLYSTGPIMLQASSLSGPAFSFWRLLIGAVLLTSLAAVGARRRHASVLPGREGRRWTVIAGVCFGVHQLLFMTAVKLTSVVDVSLMNALAPVATALGAWWLFRERPGPRFFAWSALAIGGGAWLAVQASGPTGNPLGMAMAIANVVCFAGFFLSSKRGREHVDVMPFLAGVMTVGVLLVGVFVALTGVDVGSATRADLLLAFGVAAGPGALGHFVMTWPLRWVPANIPPVMRLAQPALSGVLALLVLGEPLGWVHVAGGLVVVVGAAGAVLSRDGRALQRAAREGAGLPVGQTTAISLSTSRALRTPTG
>CP031165.1|AXV06028.1|1586668_1587532_-|lipase-class-3-family-protein
MASRPAPTADELHTRLDGRRLSELDDLTKALAMAELSMIAYLDGHDADEPAEVMGFADIEFIDRDGAQATVFLSEHDRVVACRGTEPHEWNDVKADANALTDLAETVGRVHRGFKREVDDLWPLVKDHLVADGRDVWFTGHSLGGAMAMICAGRCELEDIPIHPVQVITFGAPRVGTKRYVSHADLDILRWVNNNDVVARVPPMWMGYQHVGNLQYLDADGVLRKLSRKAIAQDRWRGFVEGLKRGRVDNLQDHLVLDYVAHIAANLERRDAGQRSSRRSAQDQSAK
>CP031165.1|AXV06029.1|1587634_1589164_+|Cyclohexanone-monooxygenase
MRPASSPTRSDPAAVDHQVVVVGAGFGGMGIAIQLRRDGIEDFVILDREDGVGGTWHVNRYPGLAVDIASVTYSYSFAPNPSWSRVFAPGEELRAYANRIADDHDLRRHLRLSINVTGVRWEEEGQRWHVDIDGQPGLTCRYLVMATGFLSHLKVPDIPGLHDFAGDVMHTARWDDDVEIDGRRVAIIGTGATSVQLVPELTARAAHLDVYQRTPIWCVPKVDGPIPRPLRTVFRHLPLVQRLARHANSGLLELLSLSVLFHRDAPALTAFAERLGRAHIRRQVRDPELRRKLTPTYEFGCKRPTFSNDYYPCFAEDHVDLVTDGIQRIDADGITTTDGVHHPADVLVLATGFRLMEEGNYPPFPVLGRDGRDLGTQWRTTRFTSYEGITVHGYPNLFYLPAPYTYSGLSYFFTVEAQMAHVSRVMGHLRRTGTQVFEATAEAEGRYVEGMRRSAARSLFTSGDCGRANSYYFNEQGEAAIARLSPTPMAGVRARTFDLDDYRWTAPPA
>CP031165.1|AXV06030.1|1589171_1589807_-|EpiH/GdmH-related-protein
MTRLSLPVRVLVWVLVTVLLYAALTFVQIAVTAVRDQSEPSDAILVLGAAQYQGRPSPVFAARLDHAADLYAEGLAPVVVVTGGRQPGDTLSEANAADAYLQARGVPDTALRLEVDGRTSYESLAASARFMRAEGITDVILVSDGWHLQRSAEIARSVGLDPHPSPAEESPYGTASALQQMVRETAGLAVGRLIGFRRLDNLATASIVPGI
>CP031165.1|AXV06031.1|1589918_1590620_+|hypothetical-protein
MPEPRTITVPLTPPQSVESTTAQVWDGSDPDAAAIVLAHGAGTDMTHRLMQRHAADLVGRGHAVALFNFAYTERGGRRPDPAPRLEQAWRDVIAALRPALGADRPLVIGGRSMGGRIASMVAVDAESLGVDGVACLAYPLHPPGKPEKLRVAHWPSLTRPILLLSGDRDSLAPLDSLRAQLEAAMPDGLATLHVVAGADHSYRVRKSDGRTEDEVCIEVADVISDWSQQLRTG
>CP031165.1|AXV06032.1|1590703_1591375_-|hypothetical-protein
MSSHERTRAEDDLHVTLDITTPASTTRPRDPLDDLTTPATARLARRADRLRRRDVSRFERLAQDHDVAPRRLRLLADAWAEAGRPGIDALGPAIPVDQGLMERAGDVIETWRRRHFPLDALRVDVWRNRLTVWWMRPTGDPTGVLESHPLMQLRRTDDGRWHLYRRAVQGEWWPVVVRGRRRRQSLSACLDAVRADPLHHFWGSQGPPDDLAVGDSMPDWPLG
>CP031165.1|AXV06033.1|1591444_1592011_-|NTP-pyrophosphohydrolase-including-oxidative-damage-repair-enzymes
MQGWTAEGLHAMRARLIADVSGLDPVDDREARSIEEVLHGLRTLPQPLDIDADPTHVTGSAIVLSARGVVLLKHKRLGIWLQPGGHVDPGEDPAAAAVREATEETGLVVDHPAGGPTLVHVDAHDGGRGHRHLDLRYLVQAAPDDPDPPPEESQDVAWFGWDAAIDRADEGLRGALLGLRSVQGPPNT
>CP031165.1|AXV06034.1|1592012_1593431_-|NADP-dependent-malic-enzyme
MTASFPPPSVSHTHEVRLTGAADGLDVVRACIDDHDGLVVDALAGDPTAADTDLVTFRAGSVEHAAAIVAAIGELPGIAVVDHVDVVLARHDGGKLRISSTSAVNDLTDLALVYTPGVARPCMDIFEEPAKAYDLTIKRNAVAVVSDGSAVLGLGDIGPLAAMPVMEGKAILMRDFAGVDAYPICLDERDPDRLVDMIVAMSTGFAGINLEDISAPRCFEVEGKLRQRLDIPVFHDDQHGTAVVVLAALINAVEVVGKTLGPDLRVVVQGIGAAGIAVANLLMAAGVSDVVGVDRDGIVTARRKDARDPIFRRFGKQTNPRDLRGGKAVALDGADVFIGLSAGNTLSVADVATMADDAIVFAMANPTPEIDPAVARQHAAVVATGRSDFPNQINNVLCFPGLFRGLLDVRASAVTDEVKLAAARAIAGIVDPAERGPDMIIPSPLDRRVVPVVAAAVAEAATRSGAAPVEDA
>CP031165.1|AXV06035.1|1593457_1594123_-|Iron-dependent-repressor-IdeR/DtxR
MTPLIDATEMYLRTVWELEEEGVPALRARLVERLGVSAPAVSETVNRLIDDGLLQLDEKRRVSLTEDGRHLAASVMRKHRLAERLLTDVIGLDWEQAHNEACRWEHVISDMVEARLIEVLGDPTTSPFGNPIPTGDDTQSWTNLITAREAAAGTMHGTVERISEKLQADVDVMRRLHAAGIAPGTDAALSARGGDIVLTVDSEEVVLSPDAASLVWINAAS
>CP031165.1|AXV06036.1|1594242_1594794_+|hypothetical-protein
MTHLIAVHLDLRDVQSARVWGWIRALGLQAEIEARPFSLDVAEPWDCEAPTFGLELLMLMEQARDHGPEAVARLIDTAYERIGVDAESAHAELAMWLQVGAAAGLPLAEYDEEMERLKAEVGYWMAEAREEHGILRPPTLVFDDGTTAYVQLDAPVEDPEDAQRFLALVLERLATIDGADRGA
>CP031165.1|AXV06037.1|1595011_1595953_+|Peptide-chain-release-factor-2
MKVHDSFAQRLDDLEVLEELAGEEDDADALAEVDEGLEGLAKDFVELETRVLLGGEYDGHDAVVTVHAGAGGTDSQDWAEMLYRMVRRWAEAHRFKVEVYDEQFGDEAGIRSATFSVAGARAYGWLRSEHGVHRLVRISPFDSQARRHTAFASIDVIPQMEEGDEEIEIADDDLRVDVYRSSGPGGQGVNTTDSAVRLTHIPTGLVTSCQNERSQLQNKATAMRLLKARLAVLEREKREAELAAVRGDQRSVEWGSQLRSYVLHPYQMVKDHRTGQETGNTQAVLDGALDDFMTAYLQWQARGGEPAGGDDVD

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Crispr_ID: CP031165_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_11

1821811-1821923

Orphan

Consensus_repeat	Method
CATCGTGGAGGACCTGCTCGCGTAGCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_11

>merge|CP031165|11|1821811-1821923|CRISPRCasFinder
CATCGTGGAGGACCTGCTCGCGTAGCCTGCGGAGCGAAGGTCCTCCACTGGGTTGGAGGCCGCGCGAAGGCGCCTGGCCGGGCTGACATCGTGGAGGACCTGCTCGCGTAGCC

>CP031165|11|11|1821811-1821923|CRISPRCasFinder
CATCGTGGAGGACCTGCTCGCGTAGCC	TGCGGAGCGAAGGTCCTCCACTGGGTTGGAGGCCGCGCGAAGGCGCCTGGCCGGGCTGA
CATCGTGGAGGACCTGCTCGCGTAGCC

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV06242.1\|1826806_1827847_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06240.1\|1825509_1826004_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06241.1\|1826003_1826831_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378238
CP031165.1\|AXV06236.1\|1818581_1819349_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274865
CP031165.1\|AXV06235.1\|1816648_1818598_+\|Fe-S-oxidoreductase	unknown	unknown	gnl\|CDD\|188475
CP031165.1\|AXV06227.1\|1807298_1808783_+\|Aldehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|143417
CP031165.1\|AXV06234.1\|1816513_1816702_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06228.1\|1808882_1810085_+\|3-ketoacyl-CoA-thiolase	unknown	unknown	gnl\|CDD\|236197
CP031165.1\|AXV06239.1\|1822939_1825513_+\|Cytochrome-c-oxidase-polypeptide-I	unknown	unknown	gnl\|CDD\|238832
CP031165.1\|AXV06230.1\|1812402_1813014_+\|putative-nudix-hydrolase-YeaB	unknown	unknown	gnl\|CDD\|239518
CP031165.1\|AXV06245.1\|1828860_1828974_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06232.1\|1814302_1815700_+\|Wax-ester-synthase/acyl-CoA:diacylglycerol-acyltransferase	unknown	unknown	gnl\|CDD\|274360
CP031165.1\|AXV06233.1\|1815787_1816096_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|227155
CP031165.1\|AXV06246.1\|1829073_1830165_-\|Adenylate-cyclase	unknown	unknown	gnl\|CDD\|143636
CP031165.1\|AXV06247.1\|1830249_1831146_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238017
CP031165.1\|AXV06238.1\|1822028_1822943_+\|Cytochrome-c-oxidase-polypeptide-II	unknown	unknown	gnl\|CDD\|274329
CP031165.1\|AXV06244.1\|1828456_1828816_-\|DNA-binding-protein	unknown	unknown	gnl\|CDD\|378988
CP031165.1\|AXV06229.1\|1810119_1812291_+\|Enoyl-CoA-hydratase	unknown	unknown	gnl\|CDD\|236864
CP031165.1\|AXV06231.1\|1813128_1814169_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|177614
CP031165.1\|AXV06243.1\|1827843_1828365_-\|putative-RNA-polymerase-ECF-subfamily-sigma-factor	unknown	unknown	gnl\|CDD\|224511

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV06241.1\|1826003_1826831_+\|hypothetical-protein	gnl\|CDD\|378238	pfam09678, Caa3_CtaG, Cytochrome c oxidase caa3 assembly factor (Caa3_CtaG). Members of this family are the CtaG protein required for assembly of active cytochrome c oxidase of the caa3 type, as found in Bacillus subtilis.	2.78402e-43
CP031165.1\|AXV06236.1\|1818581_1819349_+\|hypothetical-protein	gnl\|CDD\|274865	TIGR03936, radical_SAM-linked_protein, radical SAM-linked protein. This model describes an uncharacterized protein encoded adjacent to, or as a fusion protein with, an uncharacterized radical SAM protein.	7.38826e-54
CP031165.1\|AXV06235.1\|1816648_1818598_+\|Fe-S-oxidoreductase	gnl\|CDD\|188475	TIGR03960, radical_SAM_domain_protein, radical SAM family uncharacterized protein. This model describes a radical SAM protein, or protein region, regularly found paired with or fused to a region described by TIGR03936. PSI-BLAST analysis of TIGR03936 suggests a relationship to the tRNA pseudouridine synthase TruA, suggesting that this system may act in RNA modification. [Unknown function, Enzymes of unknown specificity].	0
CP031165.1\|AXV06227.1\|1807298_1808783_+\|Aldehyde-dehydrogenase	gnl\|CDD\|143417	cd07099, ALDH_DDALDH, Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like. The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.	0
CP031165.1\|AXV06246.1\|1829073_1830165_-\|Adenylate-cyclase	gnl\|CDD\|143636	cd07302, CHD, cyclase homology domain. Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide.	4.83268e-61
CP031165.1\|AXV06228.1\|1808882_1810085_+\|3-ketoacyl-CoA-thiolase	gnl\|CDD\|236197	PRK08242, PRK08242, acetyl-CoA C-acetyltransferase.	0
CP031165.1\|AXV06239.1\|1822939_1825513_+\|Cytochrome-c-oxidase-polypeptide-I	gnl\|CDD\|238832	cd01662, Ubiquinol_Oxidase_I, Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.	0
CP031165.1\|AXV06230.1\|1812402_1813014_+\|putative-nudix-hydrolase-YeaB	gnl\|CDD\|239518	cd03426, CoAse, Coenzyme A pyrophosphatase (CoAse), a member of the Nudix hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved Nudix fold and requires a single divalent cation for catalysis. In addition to a signature Nudix motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.	5.2205e-31
CP031165.1\|AXV06232.1\|1814302_1815700_+\|Wax-ester-synthase/acyl-CoA:diacylglycerol-acyltransferase	gnl\|CDD\|274360	TIGR02946, Putative_diacyglycerol_O-acyltransferase_Mb3115, acyltransferase, WS/DGAT/MGAT. This bacteria-specific protein family includes a characterized, homodimeric, broad specificity acyltransferase from Acinetobacter sp. strain ADP1, active as wax ester synthase, as acyl coenzyme A:diacylglycerol acyltransferase, and as acyl-CoA:monoacylglycerol acyltransferase. [Unknown function, Enzymes of unknown specificity].	7.15228e-135
CP031165.1\|AXV06233.1\|1815787_1816096_-\|hypothetical-protein	gnl\|CDD\|227155	COG4818, COG4818, Predicted membrane protein [Function unknown].	1.03767e-09
CP031165.1\|AXV06247.1\|1830249_1831146_+\|hypothetical-protein	gnl\|CDD\|238017	cd00060, FHA, Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).	1.48522e-06
CP031165.1\|AXV06238.1\|1822028_1822943_+\|Cytochrome-c-oxidase-polypeptide-II	gnl\|CDD\|274329	TIGR02866, Heme-copper_oxidase_subunit_2, cytochrome c oxidase, subunit II. Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport].	6.67428e-59
CP031165.1\|AXV06244.1\|1828456_1828816_-\|DNA-binding-protein	gnl\|CDD\|378988	pfam12900, Pyridox_ox_2, Pyridoxamine 5'-phosphate oxidase. Pyridoxamine 5'-phosphate oxidase is a FMN flavoprotein that catalyzes the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP). This entry contains several pyridoxamine 5'-phosphate oxidases, and related proteins.	7.55832e-16
CP031165.1\|AXV06229.1\|1810119_1812291_+\|Enoyl-CoA-hydratase	gnl\|CDD\|236864	PRK11154, fadJ, fatty acid oxidation complex subunit alpha FadJ.	1.18728e-157
CP031165.1\|AXV06231.1\|1813128_1814169_+\|hypothetical-protein	gnl\|CDD\|177614	PHA03377, PHA03377, EBNA-3C; Provisional.	0.00904815
CP031165.1\|AXV06243.1\|1827843_1828365_-\|putative-RNA-polymerase-ECF-subfamily-sigma-factor	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	3.04568e-26

>CP031165.1|AXV06236.1|1818581_1819349_+|hypothetical-protein
MRARVRFSKAGKLRYISAIDLGRVWERALRKADLPIAYSEGFSPHPKVSFGDALPLGFGSTAEFAELTFAGPIDLADMTTRINAAFPDGIDVLDAAEVEDGAPRLGKRLQASMWVLEYTTAAGVAEAVAAMPAEGPLEVERERKGRMVTADLRPPLVGIVADGATVRAIVRHPGFIPDDAGSGPAVRADDVHSVLGIEHRPTLITRAAQGLVSDDQSGIDDALRGTTTPLVPADGSPSGTATGPSVPSPAPEEPA
>CP031165.1|AXV06235.1|1816648_1818598_+|Fe-S-oxidoreductase
MSLTQQSQRSVWPDLEPHLLRVRKPARYVGGEDNIVVKQPRDGDTSWLVCYPDTYEVGQPNQGVQILYEVLNEVDGTRAERGFAPWPDMDEIMREEGIPFFSLENHLPAGSFDVVAFSLSAEVGYTNLLNCLDLAGIPLRAADRGPDDPIVMIGGHASFNPEPLAPFVDVACAGDGEEFVLEVDNVLKQVSNRAERLDHIADISGAYLPDRYRPDYLEPRDGEPHGRLRGIFPVEKGTANRVPKRTVTDLDEWPYPKKQIVPLTETVHERYAVEIFRGCTRGCRFCQAGMITRPVRERSSATVQKMVAEGLKNSGFEEVGLLSLSSADHAEIRGMCGDLADTYEGTATSLALPSTRVDAFNVELADELVRNGRRTGLTFAPEAGSERMRKVINKMVSEDDMLRTAETAFGNGWRHIKLYFMIGLPTETDDDVIAIADLGLKVLELGKSYGRKNKVTVSVGGFVPKPHTPFQWAAQDSPEETDRKLGLIKTRVARDRNLNLRYHDPYPGQIEGLLARGDRRVADVVERAWKLGARFDGWDELFDYNTWMQAADEVGVDVGWYCQRERASNEVFPWDQLDSGLEKDWLWQDYRDAVDPQGSSGPSEIDDCRWTPCYDCGVCPSLDLANQTAHAQPSQQHSRRLPILSARPG
>CP031165.1|AXV06234.1|1816513_1816702_-|hypothetical-protein
MRLQVGPHRALGLLGQGHLFDEEWGWRSTGGSPGRSWERLLGSVLATRWVSTVHRGDRCTSR
>CP031165.1|AXV06233.1|1815787_1816096_-|hypothetical-protein
MASLLAYLFGWIGGLIVYLTQKNPEARFHGAQSVLLSIAVFAVYVVLFVLTFVSNLFGIFLLLLWLAAFGVFIFMCVQGYQIKHTKLPIIGDIAEQWASKPT
>CP031165.1|AXV06232.1|1814302_1815700_+|Wax-ester-synthase/acyl-CoA:diacylglycerol-acyltransferase
MVLPITDGAWLMIESGEAPQHVGGLMVFDYPPDASPTWLHDTWQRLRTATDFAPPFSYRLRRPYGLAGLFDWEPDPDIDLDYHLRFSALPRPGRVRELLVLVSRLHSTLLDRHRPLWEVHLIEGLQPEHEGEPPRFAMYAKFHHSMFDGVGAMRVMRRMFSADPDLRGMAAPWEIASTAATTPSPVPEPLRSSPLEKPGLLDPVRSLGTIAGTLRDQARATRQGVEGEVMPFSAPRSLLNGRITGSRRFAADGFSFERMSGVAKALGVSINDVALAMSSHAMRTYLLDHMALPDKPLTGMIPVSVRTEDDGPQGNALSFLVVDLGTDIDDPIDRLERIRTSMQRGKDRLASMSRSERVGYAVAITSPYVIGPLLGIAGRGRPLANVVISNVPGPREPRYFDGARLQGMYPASLLQQGQALNITLTSYDTEMQFGLTACRKTLPQMQRMLDHLDSGLQELEKLTAA
>CP031165.1|AXV06231.1|1813128_1814169_+|hypothetical-protein
MLGGIGTAVGLATAITGDIVYGVVILLLVVGFVLLAERRLARAVRFRIRVWDNGSLEVHDGEPAWYPVAELTDVMVGVSATSDTNDRTLRLQHRGGEVTVALPGGIGYLFNGPSLTQVHTGQLVDALRHFAGLPARSAVGPPVAGPPVASPQVAGQPFAGQPSVGVPAVGAQPAGGAWSWRHPEAEVLARRRNRFVAISAVVVVTLMVVAGASQREEGLGAVLLSAAVAPGLLGLLLFGVAWFGYVRPSRFTLTTAGDGVLHRGGSSVSLVGAREVAVELLSSSTHTGTTTVRSRSWVLRIQPANGKPWSAALPGGSLGARLLTEQEAEHLAQQLRWFAGLPSWWS
>CP031165.1|AXV06230.1|1812402_1813014_+|putative-nudix-hydrolase-YeaB
MDLTANADLRDHVVRRLAAFDVIASPVEAHRQAAVALALVAAEDGSAGTVICRRGRVGSHRGQLGLPGGAVDHGESPEAAALRELEEEVGLQGEVLGRLDDYVTRSGFHISPFVVWCVGRVPRVTSPTEIVGFTVVPLGELLREDSPRWLDIPESDRPVLQLPLLHSSIHAPTAAYLYQFAEVVLRGRPTRVDTVEEPVFAWR
>CP031165.1|AXV06229.1|1810119_1812291_+|Enoyl-CoA-hydratase
MTNTINWDKGDDGIVTLTIDDPNQRVNTMNADFQSSLQATVQRLEDESDDITGVILTSGKETFFAGGDLRLMYAAGPDDAQQVYEEVAALGRAMRRMETLGKPVVAALNGTALGGGLELALACHHRIAVKGSRAKFGQPEVKLGLLPGGGGVVRITRMLGVVSAIMNVLAQGQEYRAEKAHELGLISELVDSTDDLIPAAKAFIAANPESSQPFDDPKYKVPGGVPTNPKLAQMLPGIPSNLRKQLKGAPMPAPLNILSAAVESLSVPIDRAWEIEHRYFVDLVVGQVSRNMTKAFFFDLQAINSGSLRPEGVPAWKATKVAVLGAGMMGAGIAYQCASVGIDVVLKDISVENAERGKNYSVKLVEKAKSRGKMSEEKAQALLDRITPTDSYDDLEGCDLIIEAVFEKTELKHAVFGDAEPKVLPDAVLGSNTSTIPITILAEGVTRPEDFIGLHFFSPVDKMPLVEIIAGEKTNDATIAKAIDLVQQIRKTPIVVNDSRGFFTSRVIGTFTGEAMMMLDEGVNLTRIDRAATMAGYPVGPLQMVDELTLTLPLKIIDEYENAARAAGEEVVSTPDVEVLRRMVAAGREGRSAGAGFFEYGEDGKRTQVWPGLTEMFPPAEEQLDVTEIQERMLFREAIETVKCFDEGVLRSVPEANIGSIFGIGFPAWTGGVIQYIDGYEGGVTGFVGRCKELADTYGERFTPPASLVAKAESGEPLSPAPF
>CP031165.1|AXV06228.1|1808882_1810085_+|3-ketoacyl-CoA-thiolase
MYIYDAIRTPRGRGKASGSLHTVKPVSLLTGLLDAVVERNPELDVSQIDDVITGVVSPVGDQGMDLARTAVIAAGWPQQVAGVQLNRFCASGLEAVNQAAARVRSGWEDLILAGGVESMSRVPMGSDGGPYAMDPETNYNGYFVPQGIGADLIATIEGFSREDVDAFALESQVRAGKAQANGYFDKSIVPVKDRNGLTILDRDEHVRPDTTMEGLAKLKASFEAQAAMGGFDQVALQRYPDVERINYVHHAGNSSGIVDGAALTLMGSKEAGERNGMTPRARVVAAAVTGSEPTIMLTGPTPASQKALSKAGMTAADIDLMEINEAFAAVALKTMRDLGIDHDRTNVNGGAIAMGHPLGATGAMILGTLVDELERRDKSTGLATLCIGGGMGIATIVERV
>CP031165.1|AXV06227.1|1807298_1808783_+|Aldehyde-dehydrogenase
MSDLDVIDPATGRVVGRVPSMTADDVTKAVDLARRAQPAWAALGVDGRHEVLRRVRREIVSRRAELRDVLVAESGKPWEDAQADLLLTLSMMAHWESNAAAACADESLSTRGVWGLGRRAAATYHPHGVVGAIGPWNFPVALTFGDAVAALHAGNTVVLKPSEVTPLSTRWVAEVFAEQARALDAPDHVLSCVTGDGATGAALVAEVDMVQFTGSVRTGRVIAHACIDRSIPCSLELGGKDPWIVLADADLDRVAAAATHYGLFNGGQVCMSAERIYVEDAVHDAFVERLAARVSTLRTVAGSGPGTTDVAPMIAPGQVDVVTAHIRDALDKGARAVTGGLPADVVHPAPTVLVDVDHTMACMTEETFGPTIPVMRVHDVDQAVALANDSAFGLTASVWTRDLARGRAIARRINAGTVSVNDAQLHVGIGHLPMGGVGASGTGARGGMDGIRKFQQRRVVVTNRSPLGRELSWLPYGRTVSAALDRAVGLLYGR
>CP031165.1|AXV06238.1|1822028_1822943_+|Cytochrome-c-oxidase-polypeptide-II
MWGSLDPRGPAARSIDDLWVLMLVLGIVAFAIFAVLLVVGIRRRATLDEERPSNRLIVWGGIVLPVVVVGAVLVATLDTMATTAAEAPEDALTVEVTGHQFWWEVRYPDADVVTANEVHIPAGEQVAIELTSSDVVHSFWIPQLTGKLDALPDGTHTLVIEADEPGEYRGTCAEFCGIQHANMGVLVIAHDPADFDAWLAAQAEPAVEPEDELAMQGRDLVAGASTCMECHTMNGSTNDGPPAPDLTHFASRRTIAARTLPNTPEALARWLDDPQHVKPGALMEAPNMTDAELEAVHAYLESLE
>CP031165.1|AXV06239.1|1822939_1825513_+|Cytochrome-c-oxidase-polypeptide-I
MTLSSSDEHVPGLERPAHASPTVAEAETDEQLERVWSDPPGLWGQLRAVQNDNIGLRLMLTGFFFVILGGSVDSVVMRTQLAFPEMGLVGPQLYNELFTNHGSVTMFLVILPIFEGFAILLLPLLLGSREMPFPRLGAFAYWTFLLGGLLYYSATLFQLVPDAGWFAYTPLSGPEFSPDLALDFWVLGLGVAEVGAIAAAVEIIVGVLKLRAPGMTLTRLPLFAWAMLVTAFMILFAFTPLIIGSLLLELDRGFGTQFFNPDAGGSSLLWQHLFWIFGHPEVYIQFLPAAGIVAMVLPVMVRHRTIGYTWIVASMVGIGVLSFGLWAHHMFTTGLPPLVLAFFAAASMVIAIPAGVQIFAWVSTIAAGRVRWTTPMLFVMGFLVIFVIGGITGVMVAAVPFDLQVHDSYFVVGHLHYVLIGGVAFPIFAGVHYWWPKITGKMMDERLGRIEFWLLFVGVNVAFFPMHIVGLQGMPRRIYTYPEEMGWQALNIVSTVGVYIVVAGIAVFVWNVVRSYRHGPPAGHNPWGGDTLEWAVPSPPKQHGWTVPPVVTSRHPLWDQDDIHSGDTEVEELVQGMARWPLRWRAVLVTGTANARPEEIYRVADPSIWPLVAACGTVLIFFSELIKLRPGALLGALIIAGSVIMWNRPTEAPMTVEEERAFEDAHGIPVHAGGSLVISRWGMGLSVLFVSIGFASLLLAYFYLRLDNAAWPPSGIAMPDLGALATGTALVVAAAAAVWVALRRVRDAGTTSFKGWLVAGSVIGIAAAVHLFLHINGLEFDSKTHAYGSIYHTLAGFLLLMVVIGAVMTTMMAVWAVQGHFTNHRHVPVTNTATWWAAISVIWVIGAATLGLGPVVT
>CP031165.1|AXV06240.1|1825509_1826004_+|hypothetical-protein
MTDGRPDPRTESAVEPVPRHDGTPPVRWLLFIGGPILFGVHFLVVYLTTEAACAVAPPADRLATSVTVVATGVAVLVGAAITWASYRWWREMEPQRDEGGRIRAARRRGVGPSAETEVPEGPDGSADPGPLRDSSLALTSTMLCALFTVSVLVVGLPALVLPAC
>CP031165.1|AXV06241.1|1826003_1826831_+|hypothetical-protein
MTGTTTGVSWTQWTLEPIALLAIVVVGGLYLRGGAQGSAAPDQRRRGAALGAALVLLGIAVMSPLDVAAGRLASAHMVQHLLLGLVVAPLLVLAAPGPRVLRAVPRDVVARGMRIGRVLRIVPGPAWWRRMDVAWLANIAVLWGWHAAVPYDAALRNELVHVLQHGSWLLAGWLWWRVVLRHRTAQPGIRLLFVFTTAMATVFLAALMTFAGTAWYDGYRGIADTTGLTPLADQQLAGALMWVPGGLVYPATALWLLVGWLRAIDLESQQPRAAA
>CP031165.1|AXV06242.1|1826806_1827847_-|hypothetical-protein
MTNDLLDTLRAHDPARPRTAAVRSATSDVVSRIADTPRPAARPARALSRGDRAPWAFGAVAAGLVALLVVVVVRVAPAPNAVGDGGTQVFGDVGPHLLLTAEGWNLDRVDVQSDSFGEATFSGPEGSMDLHWRPAEEHSGWLADRRTSTTPLDQIVVDGRQADLMAYAATDHTALWTDDVRSLELRGGGMDAEAFTALAASLAPATPEEWSAALPDSAISPSQRGTVVSQMLDGLPLPPGFDQAALEGAESTNDRYQLGAAVTGAVACGWIEEWIAARGVGDDTRATTARDALASAHGWPILDEMSAEGAYPQVLRQYADAVNADGTIEGGTTLTVEESYAAALGC
>CP031165.1|AXV06243.1|1827843_1828365_-|putative-RNA-polymerase-ECF-subfamily-sigma-factor
MDDNDRLRALHDAHADDLVAYVTRRTASPDDAADVIAETFLVAWRRLDDVPPGHEARLWLFGVARRQLANSRRSTRRRTRLLGRLTDQLGPALAAAPPGSPPDSPVMEAISRLPERDREVLYLVAWEQLSPAEAAVVLGVSPDAARTRLHRARKRLEAELDIPASTPALEGTR
>CP031165.1|AXV06244.1|1828456_1828816_-|DNA-binding-protein
MTLLAGHPTKVGRLAFVDQDYPIVLPVNFRVHRGSVVFRSDTGSKYMAAAMGQKVAFEVDDVDEAWQEGWSVLIQGMCHEITDPHQLKLIDGIGLNAWAGANMHTLEILHHRITGRRIV
>CP031165.1|AXV06245.1|1828860_1828974_-|hypothetical-protein
MQHGRVTGQPAQRAEGPGSSGTFDAGRWTTPCRIVDA
>CP031165.1|AXV06246.1|1829073_1830165_-|Adenylate-cyclase
MASSPEAAAFDASVVRSIGALAEIAVGCALLIDGVVHFVSDEVPLTDVTWTLLSSALRSGATARQDTGAGAEMVVPLVADEETVGFVVARRHDGAFSSAEAALLRLMADAAAEAGVRGRAEHELTDLFSDYLSRDVAVQLLEDPEGGALGGRTMDVSVLFADLQGFTSLSEQIPPADVVDLLNRYFALVVPAITENGGAVSAFIGDAIMALFGAPIPHPEHPLLAARAAIALQDAVNGMIAAEPQMPKLRVGVATGPATVGSIGSPRRRVFTAIGDTVNLASRLESSAAPGTVSISAETYAVVRTFTHTERLDPIRLKGKAEPVLSYRLDGIRDNSDRLVGTGTVATPLSVLRQLPPKRDRPV
>CP031165.1|AXV06247.1|1830249_1831146_+|hypothetical-protein
MDGRILPGPGRVVHHGDVVVVLGDRAPTDLVELLFDAASVADGDGLLDRLRQHPHGDEPSLGVLVCHGDGFTVRIGADLLYRSDHVGYRSTVSGPVDLATADPIRVAIGPADMPIGPAADHPGLREGAWLGTGAWVDTGPTVGASPQQLEGVVCGTCAAFVHPRTLRCRRCDTVLEPPRQAWTQPAVPVASLRMDDGTRHVLNGDVVVGRNPSGHERVQSGAAAPLVVTDSERSVSRSHAELLVQGWSVHLRDLGSPNGTSVRLPSSPRHEPVPTGEVIALLPGTEITMGRRAMTLLT

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Crispr_ID: CP031165_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_12

1853067-1853176

Orphan

Consensus_repeat	Method
CTCGGTCGCACCTTGCGGCGACAACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_12

>merge|CP031165|12|1853067-1853176|CRISPRCasFinder
CTCGGTCGCACCTTGCGGCGACAACGACGGGTTCGAGGCCCGAGTGGCGGGGCAGGGCCGATCGATCGGCCGGTCGAGCGGTGTCTCGGTCGCACCTTGCAGCGACAACG

>CP031165|12|12|1853067-1853176|CRISPRCasFinder
CTCGGTCGCACCTTGCGGCGACAACG	ACGGGTTCGAGGCCCGAGTGGCGGGGCAGGGCCGATCGATCGGCCGGTCGAGCGGTGT
CTCGGTCGCACCTTGCAGCGACAACG

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV06263.1\|1847297_1848416_-\|Glycosyl-transferase,-group-1	unknown	unknown	gnl\|CDD\|340832
CP031165.1\|AXV06270.1\|1855022_1855976_-\|D-3-phosphoglycerate-dehydrogenase	unknown	unknown	gnl\|CDD\|240636
CP031165.1\|AXV06274.1\|1862225_1863629_+\|alkaline-serine-protease,-subtilase-family	unknown	unknown	gnl\|CDD\|173810
CP031165.1\|AXV06268.1\|1853257_1854508_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238038
CP031165.1\|AXV06264.1\|1848487_1849258_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377145
CP031165.1\|AXV06275.1\|1863648_1864872_-\|regulatory-protein	unknown	unknown	gnl\|CDD\|379258
CP031165.1\|AXV06266.1\|1850659_1851631_+\|Quinone-oxidoreductase	unknown	unknown	gnl\|CDD\|176203
CP031165.1\|AXV06265.1\|1849355_1850462_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|340831
CP031165.1\|AXV06267.1\|1851662_1853018_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377111
CP031165.1\|AXV06259.1\|1843482_1844316_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379056
CP031165.1\|AXV06276.1\|1864918_1865578_-\|Transcriptional-regulator,-TetR-family	unknown	unknown	gnl\|CDD\|172294
CP031165.1\|AXV06258.1\|1842822_1843521_+\|Lipolytic-enzyme,-G-D-S-L-precursor	unknown	unknown	gnl\|CDD\|238870
CP031165.1\|AXV06269.1\|1854553_1854682_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06260.1\|1844393_1845203_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|133042
CP031165.1\|AXV06271.1\|1856010_1859436_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235435
CP031165.1\|AXV06277.1\|1865724_1868382_+\|membrane-protein,-putative	unknown	unknown	gnl\|CDD\|223964
CP031165.1\|AXV06272.1\|1859531_1861052_+\|GTP-binding-protein-Obg	unknown	unknown	gnl\|CDD\|237046
CP031165.1\|AXV06262.1\|1846254_1847301_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|367813
CP031165.1\|AXV06261.1\|1845199_1846258_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|340849
CP031165.1\|AXV06273.1\|1861044_1862163_+\|Glutamate-5-kinase-/-RNA-binding-C-terminal-domain-PUA	unknown	unknown	gnl\|CDD\|235460

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV06263.1\|1847297_1848416_-\|Glycosyl-transferase,-group-1	gnl\|CDD\|340832	cd03802, GT4_AviGT4-like, UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.	8.91425e-85
CP031165.1\|AXV06270.1\|1855022_1855976_-\|D-3-phosphoglycerate-dehydrogenase	gnl\|CDD\|240636	cd12159, 2-Hacid_dh_2, Putative D-isomer specific 2-hydroxyacid dehydrogenases. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.	7.25705e-114
CP031165.1\|AXV06274.1\|1862225_1863629_+\|alkaline-serine-protease,-subtilase-family	gnl\|CDD\|173810	cd07484, Peptidases_S8_Thermitase_like, Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.	2.13579e-73
CP031165.1\|AXV06268.1\|1853257_1854508_-\|hypothetical-protein	gnl\|CDD\|238038	cd00085, HNHc, HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.	8.61075e-10
CP031165.1\|AXV06264.1\|1848487_1849258_-\|hypothetical-protein	gnl\|CDD\|377145	pfam03861, ANTAR, ANTAR domain. ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found in bacterial transcription antitermination regulatory proteins. The majority of the domain consists of a coiled-coil.	5.74627e-13
CP031165.1\|AXV06275.1\|1863648_1864872_-\|regulatory-protein	gnl\|CDD\|379258	pfam13556, HTH_30, PucR C-terminal helix-turn-helix domain. This helix-turn-helix domain is often found at the C-terminus of PucR-like transcriptional regulators such as Bacillus subtilis pucR and is likely to be DNA-binding.	3.27652e-10
CP031165.1\|AXV06266.1\|1850659_1851631_+\|Quinone-oxidoreductase	gnl\|CDD\|176203	cd08241, QOR1, Quinone oxidoreductase (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	4.97852e-142
CP031165.1\|AXV06265.1\|1849355_1850462_-\|hypothetical-protein	gnl\|CDD\|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	2.07137e-06
CP031165.1\|AXV06267.1\|1851662_1853018_-\|hypothetical-protein	gnl\|CDD\|377111	pfam03724, META, META domain. Small domain family found in proteins of of unknown function. Some are secreted and implicated in motility in bacteria. Also occurs in Leishmania spp. as an essential gene. Over-expression in L.amazonensis increases virulence. A pair of cysteine residues show correlated conservation, suggesting that they form a disulphide bond.	4.12847e-12
CP031165.1\|AXV06259.1\|1843482_1844316_-\|hypothetical-protein	gnl\|CDD\|379056	pfam13185, GAF_2, GAF domain.	8.68694e-11
CP031165.1\|AXV06276.1\|1864918_1865578_-\|Transcriptional-regulator,-TetR-family	gnl\|CDD\|172294	PRK13756, PRK13756, TetR family transcriptional regulator.	1.33317e-10
CP031165.1\|AXV06258.1\|1842822_1843521_+\|Lipolytic-enzyme,-G-D-S-L-precursor	gnl\|CDD\|238870	cd01832, SGNH_hydrolase_like_1, Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.	1.30506e-19
CP031165.1\|AXV06260.1\|1844393_1845203_-\|hypothetical-protein	gnl\|CDD\|133042	cd06420, GT2_Chondriotin_Pol_N, N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase. Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.	1.23898e-12
CP031165.1\|AXV06271.1\|1856010_1859436_-\|hypothetical-protein	gnl\|CDD\|235435	PRK05371, PRK05371, x-prolyl-dipeptidyl aminopeptidase; Provisional.	2.84642e-50
CP031165.1\|AXV06277.1\|1865724_1868382_+\|membrane-protein,-putative	gnl\|CDD\|223964	COG1033, COG1033, Predicted exporters of the RND superfamily [General function prediction only].	3.00726e-73
CP031165.1\|AXV06272.1\|1859531_1861052_+\|GTP-binding-protein-Obg	gnl\|CDD\|237046	PRK12297, obgE, GTPase CgtA; Reviewed.	0
CP031165.1\|AXV06262.1\|1846254_1847301_-\|hypothetical-protein	gnl\|CDD\|367813	pfam04101, Glyco_tran_28_C, Glycosyltransferase family 28 C-terminal domain. The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.	3.50434e-07
CP031165.1\|AXV06261.1\|1845199_1846258_-\|hypothetical-protein	gnl\|CDD\|340849	cd03822, GT4_mannosyltransferase-like, mannosyltransferases of glycosyltransferase family 4 and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.	2.14602e-07
CP031165.1\|AXV06273.1\|1861044_1862163_+\|Glutamate-5-kinase-/-RNA-binding-C-terminal-domain-PUA	gnl\|CDD\|235460	PRK05429, PRK05429, gamma-glutamyl kinase; Provisional.	1.2851e-180

>CP031165.1|AXV06267.1|1851662_1853018_-|hypothetical-protein
MSLSPGTVGVAAASETMMHLSRLVLFLVTALVLTACAVPQGVQQTALEPAGVPTQPPADSFSQLASLSPDVVAPGDASTEITITADDAPLGSGTYFRIERWDGERWALQHHVWHGEVQPADLEGVNDDGYDIEPGEALVEQLPLDDLDTGVHRVGLEMRAGDDPDVRLDVYARLDVRPGTQDDAPALTQLDGSEWRSVVVEGLDLPAGQQIQLTFSHGRVGARVACNDVDGPYDLIDGHLAVDADEVTSTLIGCPHPEGSWDEWVTGLLLGAPTIELDDEDLRLSAGSDTVVFERYVEPTPTPTDPDAPLSTWVPPADYRYTIWGSCGPDARFFGDREVIVQGGVPSDEAAFLPTLLADAETIRADGADVVTVEHDPDAGHPTAILWDVDPTISTDSEVCYGVTDFEDLTAPPPAEPTDGVTIELDRPLGDPALVDTSTGEAVRVAVQFDS
>CP031165.1|AXV06266.1|1850659_1851631_+|Quinone-oxidoreductase
MRAVQITSLDGPSAVTVADVPDPVRGDDQVLVEVRAAGVSFPDLLQTRGQYQIQPPMPFVPGVEAAGIVRESPEGSAHQPGDRVMAFGMLGGMAELLAVPDATTFALPESLSFEQGAAFPMNYHTAHFSLVRRGRLEAGESVLVHGAAGGVGTASIQVAKGLGARVLAVVSSDDKAAVARDAGADVVLRSDRPWKDEAREATDGRGVDIVMDPVGGDRFTDSIRALAPEGRVLVVGFAGGSIPEVRVNRLLLSNTAVVGCAWGGFLFHDQTLVPDTAAALGPLIRDGSLAPPIGAALPLDEVAEALRLIDEREATGKVVLTVP
>CP031165.1|AXV06265.1|1849355_1850462_-|hypothetical-protein
MTTARPQGPWQAGFEPIDLPRVLHYPDATRYAARMEGHLTRAPASMGDDVAGQHDDHADPPADPYDPMWLREHSQDWDIVHVHVGLPPGTDPRLPIALDTHRRQGTPVLVTVHDLPGSGTIAGDALDMPSVQRVLADAWLVTTFTTGAARTILERTGIRPRVIPHGPMLSGADLLRARRYRTACGGEWGPILVELEPHHPANDVDGALDACALLAGSMPVRLLVHAVHEHAVAGHPGIQAADLVVHHGMAFDQVVDHIAAARALVLPRTAGLHSQRLELAADIGTPVISGRVGHLAEQHPVVGVPVHDGRIDVAALAEAMLTPAEHSVTSRVEDRERAWAEVCMAHERLYSTARSHGAHVPDHSASTP
>CP031165.1|AXV06264.1|1848487_1849258_-|hypothetical-protein
MPPTEGQIRDRKLMQVLLGFAHTMASDYSAQDALDDLLRQAPSLLGVDGLGVMLLDDNDDLRFVSASDDRVRLIEQLQLDYDEGPCLLAYITGTPIYADDLCQDTRFPTFGPVAVESGLVAVHSFPMRVGDTRLGALNLYRTTPGPLDESSKQLGGLFADMASSYLVSARQVDDVSRQVIGIRQALERNGVIEQAKGVLMHGHGLTADAAFDLLRHFARSNRRKVLEVAESFMDGQLTAADLGLDSHQVIEIDHHG
>CP031165.1|AXV06263.1|1847297_1848416_-|Glycosyl-transferase,-group-1
MVSAAPVHQPRAAGSPADAARPLRIAIIAALRHGLREPHAGGLERQTADLAHGLRAAGNGVTVFASADADPDLGVEPIVPRETLLDLSPAAREDVSMLAEGFMVEHDAYLDLMLRLRDADFDVVHDNSLHYIPPATADLLPMPVVKVLHTPPTPWIEAALRRRPENLHVVSVSHDNARRWPITPRAVIHNAIDLDRFEPTGAPVPRSAVWVGRVCPEKGPHHAVRAARRAGFSLDVIGPASDPTYAEEVLRPELDDHRRWVGHLDSADVAARIARASVALVTPCWPEPFGLVVMEALACGTPVAGYRHGALPELVNDDVAVLVDPDDEDGLAEAVLQASTLDRGRCRAHAVAHGSVERMTGDYLALYRELVS
>CP031165.1|AXV06262.1|1846254_1847301_-|hypothetical-protein
MIGWYVHHHGSGHEVRARNVVPLLADEVVCFSSRPLDIPTASVRRLPLDVEPPATAWHAAQPTPTALHYAPLGVAGLRRRMGAMAAWMAESEPAAMVVDVSVEVTLLARLLSVPSIVVRQHGRRTDPPHRTAVDAASLLLAPYPEWLEEPWVPDAMRDRTVYTGGFSRFDHRDADRDDARSALGLDADVQMVVVLPGQGGRVGWPVHEAAAATGSWQWVVLGDVPAGPHVTTPGWVEDPWPWLAAADVIVSHGGHNAVMESVGSGRPVIVVPQDRPFDEQRHKAHLLAAHEVCLVRERWPRAAAWPALLDHAFDHGAPRAADLVDGKGVHRAADAIQSFIRTSRGATP
>CP031165.1|AXV06261.1|1845199_1846258_-|hypothetical-protein
MNRRPRVLSHPPRHPYVDRFDDTVSRVVHRDEPMPRLDAYHDPDWVRRHSGDWDLVHLHFGHEHHPVERMVDVLDAHRSAGTPIVVTVHDLANPHLRPQDDPSLELLGPMVERARVVTTLTVGCANAVAAHTGVHPRIIPHGPILPADRMWRARRLRSASAGPWGPLLLHAKPRRPSHDVRGVLDAVALLDGGVPMRVLVDRDDVDLLRGHRALELVDLVVHDGLEHRELVRQIALSRGLVLPYRWGTHSGMLELAADVGTAVIGTDAGFVAEQHPMAVAPLRRDHVDPIEMADQMISLRDADLVSRAEDRERLGYQVLAAHERVYRAALGTVQTAPRAVDRLATASPGGGV
>CP031165.1|AXV06260.1|1844393_1845203_-|hypothetical-protein
MTVAVCTIVRGRQTHLRRLLEGLRRQTSPPDHVVVAWMGGPDPRPAVPTGMPVDVVDAADPRTPLPLAAARNAARRGAADADVLVFLDVDVIPSSTLVADYARRCRTTGGLWSGQVDYLPEGVPADDAWTEAQLDVAAAPHPARTPPPADTRLGDPDLFWSLSFAMRAVDYDCLGGFDETFVGYGGEDTDFGRRADAAGLTLWRTPAARGWHQHHESTSPPVQHVHDIVGNAHTFHRRWGEWPMRGWLEAFHDQERVLFRPEDGILEAR
>CP031165.1|AXV06259.1|1843482_1844316_-|hypothetical-protein
MGRTADADRRLFQLLLDFATTLASQTDARTNAAGRDGPDDHEVVDHDNGRRSALATLITRSTAVLDIEGIGVMLLDGRDHLAVGAASDAAIDRIEHAQLGFDQGPCVDAFRTDATVTVDDLADDERYPQLASLAEGQGVRGVLSIPMRADGEVLGAMNLYRAATGPFDDDMVQVGRLFADTTSTHLRSAARTAAATEQLLGIRRAMRTHGPIEQAKGAIMHAVGLSDRQAFDLLRQHARRSRQPLLEVVRAFLVGELTTGDLGWTSAGAHDGQVAAE
>CP031165.1|AXV06258.1|1842822_1843521_+|Lipolytic-enzyme,-G-D-S-L-precursor
MTPWEGMRLTSAQVDPYRREWEAANRRALDGEGPLLGVLGDSAAQGIGAPTPFEGWVGQLQRRLEGIDGHRWRVLNLSVSGARAHTVMDEQLPRLWRVGQPVDLVVCAVGGNDMYRSTRRQVHDRFTRLLRALPAPGTWHGDQRTIVTTLPQGLGRRRAGIANDLVRTLGPQRGLEVADLWATTGPPWRGKYAEDMFHPNALGYGHWVDAILGTIRPDRRSLGGDLPVVGTR
>CP031165.1|AXV06268.1|1853257_1854508_-|hypothetical-protein
MVEAGEVTELVTHLHTLASRFDPDAIPDGDVAGLVVDLGRAGRLVDGMLTRAARRAAETSAHETAGAKDAATLIATATGTSTAAAKKMLKTSEQLVDQPDVEKAVTDGTLSTHQAVVVSETVADAPEKADELIGDATSQTLPELRKKARDIRTAADPDRETTRRRHLTRRAFRSWTESDGEWKAFIQGPGDLGARIEAALRGKHDAVFRAAHAAGQREDDACYRFDALLNLLEGHATTGGEQASNDDAPVPTPATKGPRTGRQTKVIIRVDGSALVRGEVEDGETCEIAGIGPVALSAVREQIPDAHITYVITNGHDVTVAHLGRQVTAHQRTALEARGYQCEVPGCTADHLLEIDHVTGWAITKDTRLSDLAWLCTTHHRQKSRRHYRLLGPPGQRTWTTQTGVEISRDPPAEAA
>CP031165.1|AXV06269.1|1854553_1854682_+|hypothetical-protein
MCSSLPHRGSRIACFPSSDAISDEISVVIISASWLVLDRAIH
>CP031165.1|AXV06270.1|1855022_1855976_-|D-3-phosphoglycerate-dehydrogenase
MPDLHLVPDMPSNPVPVAVLPEGLRPHLLDAVVAGGGEVVAPEEARMLVWTDPNDAAGVSDVLAANPDIEVVQLLWAGVEEFAALGLFDDGRTWLCGKGVYADPVAEHALALSLAGLRGLPGRVTARGWGPQWGTSLIGRRVTVLGGGGITESFLRLLGPFESDVTVVRRSGEPLDGAARVVTPDRTLEALDGADLVVLALALTEDSRGVIDEEALAAMPDHSWLVNVARGQHVVTDDLVTALREGTIAGAGLDVTDPEPLPDDHPLWTLDNAIITPHTANTEAMAVPLVSARVTANVRRLGEDRPLIGPVDPALGY
>CP031165.1|AXV06271.1|1856010_1859436_-|hypothetical-protein
MSNTHDMRRSTVLLSCLVLLLSVLPAAAQPSGDGALVFAPAGLSVDQYDVVTTPEVVEVEAHDGVVLHTRVYRPDTGGVATPVILVHSPYYNGLLLGDDTRSLDLVEFFTPKGYTVVLSDLRGTGNSGGCGEQDGPNQAKDFATLVEHFADQPWSSGKVGSYGKSYDAETQHAGAVLDPRGLETMVSVAGIAGLYDVAYFDGVPLALNGVLSATAYELYDLDVPGDVGAMPRRFERHTCQPENFANGADPRGDMTDYWAEREFRAGVDDITASMLMVTGLQDFTVSPINLDGWFDEIPTFRRAIIGQWPHKYPYDAADPIARDDWYDTVHAWFDHELMGLDTGITEWPEVQVQDEDNAWRAVDSFRGMGSEVELPLGEGTVTFGEDGEWSVDLPTPSRHLSGQAYLDAVIALDRPDGHFAVRLDEVRSSGQTRQLVRGYLSAVHRESLLNPIPVTPGHPTPYRIRTYPFDVTLDEGSTLRLTVSGSDSATLPAGTGYTATVDLSRSVLRVPVADDRCGLAVATREAAGPTAGCPDGVPVSTAWTDVPRSFGHDTTARVIGTSVETIGGVDAVREWGYLTMRDGVELAFEVVRPDDDQPHPTLFTYDGYAAGADPDAGYAERYLPDGYALLGVNLRGTSCSGGTFDFFQPAEAHDGYEVVEWAAAQPWSTGRVGMIGKSYPGITQLFVAETQPPHLAAISPGHYYADVYRDIANPGGITNYAFAALWSFISQPGPGVLAAPGESLAGDATCLANQRHHATNAPDNPLLQAETHPHEVMLHAERSPLTHADRIDVPVYQALSWQDEQLMSRNTHFLATLDELGVPYRAVLSNGDHGTYREGPQMAELDRFLEAHLVAPEVLADGTLLEDYLAEPSVSVFWEQGETTAPRWVTELDGWGDQAVAHVEPLSADGGLGGTTVAGSTSWLHNAAGTQGIADGTTLGSDYQTVTTWDRYSPPPGTFAAFTSLPYTEDVALLGSASADLWLTATAPNVDLQVTLTEVRADGTEVFVNQGWLRASQRQLDRARSTALLPVHTHREADVAPLSMTEPSLVRVEVLPFGHVVREGSRLRMWVEAPTAVPQLEGFQLDPTPARVTIHSGADFPSALVLPVAVSAPVPQVYAGQAGQPACGVSQRNHCRTDPLA
>CP031165.1|AXV06272.1|1859531_1861052_+|GTP-binding-protein-Obg
MFTDLVKINVRGGKGGDGVTSFRRQPYEPKGPPEGGDGGDGGDVVLVADEGLSTLIDFHFRPHRKAGNGVNGSGDLRHGARGDDEVLAVPVGTVVSDAETGEVIGDMVHDGQRLLIAEGGRGGRGNAAFRTRQRRAPRFHEFGAEGDEQWVQLELKLIADVALVGFPNGGKSSLISRLSAAKPKIADYPFTTLQPNLGVVTVNDESFVIADVPGLIEGAADGKGLGHEFLRHVERAGALVHVLDCASGYAAEVVRPGTDDIPARRYEQRNPIDDLHQVLDELRSYMPEMLDRPAIVWLNKVDVDPDMAELVKPELEKEGWEVLMGSPVTGQGLDPLRYRLADLVRQARAERADPDHPDPVERPVLRPRQVRNEKDFTIERVALGGDEYGWRVHSDRLERWVAQLDLGNEDAVDYLQGRLKRAGLETALAEAGAHPGDDVELGGAVFVFQPEDWAGDDDDWDDWDGNDDRGQDWEVDETPIEIDLADEPDDDPYEDDEDDKDDEGDG
>CP031165.1|AXV06273.1|1861044_1862163_+|Glutamate-5-kinase-/-RNA-binding-C-terminal-domain-PUA
MADRRYDPARRVVVKVGSSTLTAEDGGLDRQWVDDLCTQLAALRADGVEVVLVSSGAVAAGLRPLGLTQRPTDLGRLQAAASVGQGELVHAYAAALRRHGFVAGQVLLVPDDLVTRDRYLNARTTFSELLAMGALPIVNENDTVATEELRFGDNDRLAALVASMLGVDLLMLLSDVEGLHDGQPSAGAPVINEVHDLSTLDDRHRGGTGSAVGSGGMASKLDAARVATFSGVSCVIARGRRPDVVLDVARGEQVGTWFPPARKRPDSRRLWLAFAHQPAGRLHVDAGAVRALAQRGSSLLAIGVTAVDGTFERGDAIDVVGPDGHPVARGIVAYDAAEVTAMRGRSTEQLTDEQGDAFAAPIVHRDAMVVTA
>CP031165.1|AXV06274.1|1862225_1863629_+|alkaline-serine-protease,-subtilase-family
MDRGHRSPRVLTAVAVLAAFLLVAAAPPNDPLVSQQAHLTIVGAFDAWDTRRGEGAVVAVLDTGVDLDHPDLAGRLVEGIDLVEPDTPPDDPQGHGTIVAGVIAAVADNGRGVSGVAPQAMVMPIRVLDAGGRGTSDIVADGIRHAIEQQVQVINLSLAEVQSEDDDEDEGTTGPPLLPGVSLVQDREVIRAIEEADEAGILVVAAAGNDGRASTPYDADVPVLVVGATDSDDVRWEESNHDDRTLFAPGVAILSTWSEGRYARSDGTSFATPIVAAGAAMLMGAGVSAEDTVTRLVDTAVRLEDDQEAEVGLGRVDLAAAVQGVDPAPPTTPPAVTTPTPAPATTAPAASTPAPTDGVEVVEPVQEVTEPPPAPAQVTEPPPDITQAAPVATTPPPTAVALEPVEVVTVPTTMPTTPSATPATSAEDTAPGLAVDEQDRGPLITVATMLLGVDVLLAGWVLAGRRT
>CP031165.1|AXV06275.1|1863648_1864872_-|regulatory-protein
MSRTFDPLRFDDTALSAEPVAVATRPASRVAAELLHDVDELTESVVRTIQTRLGSYTGRAVPRDDLWWSVRATTGMLVRVLAEDREPTQQEIQTRRALGERRAMQALPVDQLVEAMQVAFGEVWSALSDRAMQQGHETVTDLLSLSRHFWTMMHTVSSVVTEAHHDVAREQVARTRRRSAGFLDILAGLPATETQARHEAAALGLDPDATFVAAVRPPREGDDPLRSCRDGVVMVERPDRVLLLTVATADGAFPLDLVDDPVGIGMARPGLSGAKETVRDAELAHAAASALGRSRLAYADDWFACVSSGELSRVEPLVRDAVAALRADPQMAHTVDAYIRADGKLVAAGEAIDVHANTVAYRLDRFVERAGLDPRTSDGLMRCRLALLIAEASPSRGGGAAEPTPTD
>CP031165.1|AXV06276.1|1864918_1865578_-|Transcriptional-regulator,-TetR-family
MTESTRTAAPLTKDTIVDAALVIVERETMEALSMRRVARELGRAPMSLYRHVGDIDELTELVMARLIADVNPIDHAEDWRRTLRDAAVQVRRVFVRYPGIVEVAMASGIRTDTMLQVLNTIMGAFLTAGLTPEQAVQAHRVLFSTILGDTLMQRSADEVLGATPEAQRTFMDQLTSAADERFPNLRAVAGVWPDVDGDQVFAFAIDRVLDGIAALAAEG
>CP031165.1|AXV06277.1|1865724_1868382_+|membrane-protein,-putative
MNALVIALSRAVRRAPAVVLVVALVLTAAIGAVGFPRIEQGGGNEGFSPDNPELLAQQRVQEVFGSSGDVVLQVLLRAEEGGDVLSAAGVQATLGIQQAVQASEAGQYLVQRPDQPPLISPLLGVLQAAGAQGIDPTALDDATVDQLFAASLAQMPSEQAGFVTGLLPASAGIDAATPVEQPESPLALAILFLDSEALPADDVESAEVVQDIAAIIEGVEVDGVTLEPFAFELLFANQDSFTDEIGRLFAMAIGIILLILGFVYFSKPQADGSWFTSIRRTVADVATTIAVIMMAIIWVQGFAGILGPQGLGWIDALAEPAQLLPVLLVGLGVDYGIHMTSRYRSEVAEGSVPDAIGTATKTVGVALVLATVTTAVGFLTNLTAPVPALADFGVLAAVGIVAAFVLMLTVFPSLRLLLDRRAEAKGTLPRQTLSSNSEGLLPRMMAGVSVFAERLAVPTLIVTAGIGGVLGVIGLMNVSTEFSFTDFLPEDDPLIVTFDTLTEEFGGGAGETTTVVIDGTMTPEAHNALVAAQQELAGVADVQVFGENAQATSPVTVLAQVLASLQPADQAAPSAGLATPVDPALAQQIAGMLEPGGLTVPADTDVEALYDLLLQAAPDVAGQVIAAQDDVVRVSVSTAAGEERAVALGENLDAVFAPVEAELGGDSVVVTSDGIISSRIVTSLRDSQLRSLFIAVLAAMVLLVLNFWVTERRPMLGVVTIAPVALVVLWTFGMMAATGVPVGPVTATIAALAVGIGVPYTIHVSHRFSEDRERFATAEEAIRSTVSHTGGALAGSAMTTIAGFGILVTSSLVPFQQFGLVTVYSIGFALIASTVVLPAMLVLYDRSRRRREGDPTPPAAGPTDGGEADAWWTKPPAPETAVSGG

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Crispr_ID: CP031165_14

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_14

2545885-2546120

Orphan

Consensus_repeat	Method
GGCCCCGATCGCGCCGGTGGCC	CRT

3 spacers

The CRISPR arrays of CP031165_14

>merge|CP031165|14|2545885-2546120|CRT
GGCCCCGATCGCGCCGGTGGCCACCCGGTTCGGCCGGGCGGATCGTGCCGGTACCCACGTAGGGGTGGGTTGGGCCCCGATCGCGCCGGTGGCCACCGGGGCCGGGCGGCGGCGGATCGCGCCGATCATCGGCCCACGGCGACGCAGGCCCCGATCGCGCCGGTGGCCTTTCGGGTCGGCCGAGCGGATCGCGCCGGTGGCCACCCCGACCGGCCACCCCGATCGCGCCGACCGGG

>CP031165|14|1|2545885-2546120|CRT
GGCCCCGATCGCGCCGGTGGCC	ACCCGGTTCGGCCGGGCGGATCGTGCCGGTACCCACGTAGGGGTGGGTTG
GGCCCCGATCGCGCCGGTGGCC	ACCGGGGCCGGGCGGCGGCGGATCGCGCCGATCATCGGCCCACGGCGACGCA
GGCCCCGATCGCGCCGGTGGCC	TTTCGGGTCGGCCGAGCGGATCGCGCCGGTGGCCACCCCGACCGGC
CACCCCGATCGCGCCGACCGGG

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV06852.1\|2541442_2542225_-\|3-oxoacyl-[acyl-carrier-protein]-reductase	unknown	unknown	gnl\|CDD\|180604
CP031165.1\|AXV06851.1\|2540527_2541415_+\|putative-DNA-binding-protein	unknown	unknown	gnl\|CDD\|375319
CP031165.1\|AXV06861.1\|2550427_2551651_+\|two-component-system-sensor-kinase	unknown	unknown	gnl\|CDD\|226951
CP031165.1\|AXV06859.1\|2547046_2548018_-\|Alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|176228
CP031165.1\|AXV06865.1\|2555294_2556152_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06853.1\|2542402_2543089_-\|Rrf2-linked-NADH-flavin-reductase	unknown	unknown	gnl\|CDD\|187555
CP031165.1\|AXV06850.1\|2539001_2540411_-\|putative-transmembrane-transport-protein	unknown	unknown	gnl\|CDD\|129794
CP031165.1\|AXV06857.1\|2546130_2546559_-\|putative-lyase	unknown	unknown	gnl\|CDD\|319924
CP031165.1\|AXV06863.1\|2552388_2553135_-\|Pyridoxamine-5'-phosphate-oxidase	unknown	unknown	gnl\|CDD\|378988
CP031165.1\|AXV06846.1\|2532418_2532727_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|371814
CP031165.1\|AXV06866.1\|2556185_2557298_-\|putative-periplasmic-protein	unknown	unknown	gnl\|CDD\|238867
CP031165.1\|AXV06848.1\|2538390_2538657_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06860.1\|2548014_2550195_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225272
CP031165.1\|AXV06849.1\|2538765_2538996_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV06858.1\|2546560_2547040_-\|Transcriptional-regulator,-AraC-family	unknown	unknown	gnl\|CDD\|197666
CP031165.1\|AXV06855.1\|2543642_2544956_+\|RNA-polymerase-sigma-70-factor,-ECF-subfamily	unknown	unknown	gnl\|CDD\|227277
CP031165.1\|AXV06854.1\|2543268_2543646_+\|PhnB-protein	unknown	unknown	gnl\|CDD\|226318
CP031165.1\|AXV06862.1\|2551667_2552357_+\|DNA-binding-response-regulator,-LuxR-family	unknown	unknown	gnl\|CDD\|225107
CP031165.1\|AXV06864.1\|2553350_2555222_+\|Vancomycin-B-type-resistance-protein-VanW	unknown	unknown	gnl\|CDD\|377286
CP031165.1\|AXV06847.1\|2532788_2537429_+\|Gamma-glutamyltranspeptidase	unknown	unknown	gnl\|CDD\|380277

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV06852.1\|2541442_2542225_-\|3-oxoacyl-[acyl-carrier-protein]-reductase	gnl\|CDD\|180604	PRK06523, PRK06523, short chain dehydrogenase; Provisional.	1.58268e-69
CP031165.1\|AXV06851.1\|2540527_2541415_+\|putative-DNA-binding-protein	gnl\|CDD\|375319	pfam17765, MLTR_LBD, MmyB-like transcription regulator ligand binding domain. This domain is found in a family of actinobacterial transcription factors. The structure shows it has a PAS domain like fold and it is bound to Myristic acid.	1.85604e-48
CP031165.1\|AXV06861.1\|2550427_2551651_+\|two-component-system-sensor-kinase	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	1.80659e-46
CP031165.1\|AXV06859.1\|2547046_2548018_-\|Alcohol-dehydrogenase	gnl\|CDD\|176228	cd08267, MDR1, Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.	3.05886e-108
CP031165.1\|AXV06853.1\|2542402_2543089_-\|Rrf2-linked-NADH-flavin-reductase	gnl\|CDD\|187555	cd05244, BVR-B_like_SDR_a, biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs. Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	9.87349e-17
CP031165.1\|AXV06850.1\|2539001_2540411_-\|putative-transmembrane-transport-protein	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	3.26179e-45
CP031165.1\|AXV06857.1\|2546130_2546559_-\|putative-lyase	gnl\|CDD\|319924	cd07263, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	1.77478e-31
CP031165.1\|AXV06863.1\|2552388_2553135_-\|Pyridoxamine-5'-phosphate-oxidase	gnl\|CDD\|378988	pfam12900, Pyridox_ox_2, Pyridoxamine 5'-phosphate oxidase. Pyridoxamine 5'-phosphate oxidase is a FMN flavoprotein that catalyzes the oxidation of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP). This entry contains several pyridoxamine 5'-phosphate oxidases, and related proteins.	1.79071e-41
CP031165.1\|AXV06846.1\|2532418_2532727_-\|hypothetical-protein	gnl\|CDD\|371814	pfam11950, DUF3467, Protein of unknown function (DUF3467). This family of proteins are functionally uncharacterized. This protein is found in bacteria, archaea and viruses. Proteins in this family are typically between 101 to 118 amino acids in length.	2.75616e-14
CP031165.1\|AXV06866.1\|2556185_2557298_-\|putative-periplasmic-protein	gnl\|CDD\|238867	cd01829, SGNH_hydrolase_peri2, SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.	1.63821e-59
CP031165.1\|AXV06858.1\|2546560_2547040_-\|Transcriptional-regulator,-AraC-family	gnl\|CDD\|197666	smart00342, HTH_ARAC, helix_turn_helix, arabinose operon control protein.	8.55749e-26
CP031165.1\|AXV06860.1\|2548014_2550195_-\|hypothetical-protein	gnl\|CDD\|225272	COG2409, COG2409, Predicted drug exporters of the RND superfamily [General function prediction only].	2.10828e-89
CP031165.1\|AXV06855.1\|2543642_2544956_+\|RNA-polymerase-sigma-70-factor,-ECF-subfamily	gnl\|CDD\|227277	COG4941, COG4941, Predicted RNA polymerase sigma factor containing a TPR repeat domain [Transcription].	1.17341e-134
CP031165.1\|AXV06854.1\|2543268_2543646_+\|PhnB-protein	gnl\|CDD\|226318	COG3795, COG3795, Uncharacterized protein conserved in bacteria [Function unknown].	1.34285e-21
CP031165.1\|AXV06862.1\|2551667_2552357_+\|DNA-binding-response-regulator,-LuxR-family	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	3.82731e-72
CP031165.1\|AXV06864.1\|2553350_2555222_+\|Vancomycin-B-type-resistance-protein-VanW	gnl\|CDD\|377286	pfam04294, VanW, VanW like protein. Family members include vancomycin resistance protein W (VanW). Genes encoding members of this family have been found in vancomycin resistance gene clusters vanB and vanG. The function of VanW is unknown.	4.94084e-50
CP031165.1\|AXV06847.1\|2532788_2537429_+\|Gamma-glutamyltranspeptidase	gnl\|CDD\|380277	NF033435, S-layer_Clost, S-layer protein SlpA. In Clostridiodes difficile, the S-layer protein precursor, SlpA, is one member of a large paralogous family of protein that share several cell wall-binding repeats. SlpA is cleaved into a larger and smaller protein. The S-layer protein itself is important to adhesion, and portions of it are highly variable, and then N-terminal and C-terminal are well-conserved.	9.57216e-19

>CP031165.1|AXV06855.1|2543642_2544956_+|RNA-polymerase-sigma-70-factor,-ECF-subfamily
MTVPDTEWVGRTFQQEAGRSLAALVAAFGDVDLAEDAMQEAFARALDRWPEVGLPANPGGWITTTARRCAIDILRRDRRGSDLLARAHPVDLIGGPPGGDHDRGRGVTASDDGHPSQEEVVVDERLRLLFMCCHPALPLDGRVALTLRLLGGLSTAEVARAFLVSEPTMAQRLVRAKHKIVAATIPFAMPAEADLPERLDAVLGVVYLIHNAGSNAPEDGSRPSPRREAMRLARLLHELMPDEPEVTGLLALLLLADARQHARWDDDGRLVLLRDQDRSRWSPRLVAEGQALVRSCLRRNRPGPYQVQAAISAVHADAVRVEDTDWPQVLALYDHLAELDPSPVVSLNRAVAVAEVHGAASALAQVEALGGLEGYPPWHVTRGEFLARLGNPDGAREALRRALDLASDDGTRRHLQRRLAELDGPPATGGAQTASTS
>CP031165.1|AXV06854.1|2543268_2543646_+|PhnB-protein
MPHYMLSVHMDPTQERPPMTEEDMAGHMTALEALETDMHDKGAWLFSARMHGPESASVVHHRDGTRAVTDGPYIETKEHLGGFYVITAADLDEALEWADRTSATVGMPIEVRPFAGFSEEPHRTQ
>CP031165.1|AXV06853.1|2542402_2543089_-|Rrf2-linked-NADH-flavin-reductase
MRVCIIGASGKLGRYMIEHALERGHEVVGVCRPKSTDKLADVADRITIVPGRTDDPAVIAKAVAGCDGVLVVLVPFGVKGYSSGTAQAVLDHAEPDARVVFSCGWHITRDGQDRYSWRLRLTLPIVTVLARFFRFVDIDDQVEACRRIFASDRRWTVVRGSDLEEGPSEGLPVWSQHVGDPVLESNRTRRTDFALFMVEALTDDTLVGEAPAIVSRMSESALAHSGAR
>CP031165.1|AXV06852.1|2541442_2542225_-|3-oxoacyl-[acyl-carrier-protein]-reductase
MNLDLDGHVVIVTGGTSGIGLATAHELVAEGARVVAVARSEPQPGVLPDTVDFVAADLSDPAAGDHVMTRTLAWYGRIDALVNNAARFETRPSLLGFADEEWRSTFETNLFAPARLARAVVPALRETRGSLVHIGSEAGRMPDPTMAAYAASKAALLSLSKSLAIEFGPDGIRSNVVSPGPTRTALFDAPGGFAEQLADRFDTDPDTAVETFVRDERRLPTGRVGRPEDVAGVIAYLLSPRASQVTGAEWAVDGGALRQL
>CP031165.1|AXV06851.1|2540527_2541415_+|putative-DNA-binding-protein
MERPSSDAVPAGADVHRPVTELGEFLRSRRDRITPEEAGVRSYGRRRVPGLRREELAQLAGVSVTYLTRLEQGQSHNASDAVIDALARALRLDPDERAHVDALVHPRPVRRSHPYRPETARPGAVQLLRSMGEVPAVLLGRFNDILAWNRAGHLLLAGHLDDDAPSRVEGRPNQLTLLFLDPHTRDLYVDWAEEAARAVASLRYVAAQFADDRRLAGLVGELSVKSPEFACLWAGHDVRLCTSGAKRLRHPTVGVLELGFEVLHLPEGNGQRLLTHTAAPGSASSAALRLLVSTA
>CP031165.1|AXV06850.1|2539001_2540411_-|putative-transmembrane-transport-protein
MTDIDTVPPSSTANARAQPLTSAERIAMAVLLTANFTLAVDFSILNVTLPHIGSELGFATSALQWIVTSFALCAAGFTLFFGRVADLYGRKRLFVIGIVLLGLSSLAGGLATEPVLLITARVGQGLATAMVTPTALSLMTTMFAEGPARSRALGLNGALMAAGFTGGAVLGGLLTGTVSWRWAFFVNVVVAIAVVATAPFVLRDPARGPRPALDVPGAVTITLALVALVFGIDTAGHHGWAHPGTWGPVLGAVALFAIFLTIESRVAQPLVEPALLRQRNIAWGNAAGLLAFGTFTSLVFILTLYLQQVLGYSPVTAGLVLGVLGVGTVLGGLVAPKVIDRTNAKTAIVFGLMCQAGATAPLAFAGGNRVWLVPLLVLTFLGGIANLVAIVAYTVASTAGVGADQQGLATGLVTMSQQVGIALGTPVMSAIATSVVAAALLPGLQVAIAVNAAITITAALLVATFLRLP
>CP031165.1|AXV06849.1|2538765_2538996_-|hypothetical-protein
MDRARPGSSGRYGQVERAVGRPLEGPIVTVGEQAEERLLGRLGHGSTGGRPQPGVQSTLFPTSRTIASVSKRSAWP
>CP031165.1|AXV06848.1|2538390_2538657_-|hypothetical-protein
MVLTDHVFDKVRSIDMTLAEFEELLGGGAVIEEAAVDDGVKELVLIIEWTRPLHVVVVVDDIREEERIVTVYEPDKERWSADYKVRKP
>CP031165.1|AXV06847.1|2532788_2537429_+|Gamma-glutamyltranspeptidase
MRAHRQIRAGLPRTAAVWVVVLLGLTAPPDVAAQDEPEPVMDVLRTADGAVPPEDFGTAIGHVVDDAGRIVAFATSVGGVLNDQPDDNDASDVYIWDRTDGRTRLISTANGSDAAADGPATNPRISRDGRYVFYLSDSTNGAPQPNTRDDGSRLGTMLLRYDVDRGTTELVTRSVDDRRACGQVNSNESVFGARAPFEIADDGSAVAFTARCPDLVYPAEDTTAWFNDELYLWREGHGVDWLSEGIPAPTAQDPHVGSGVRHVVRGISSDGAVVTFSAQTSGQRWQAFDRSAFEETANFFLYTWRAGLIEPVFFNNDLSPVGSSFHAMALAGDGRTWAVIPREASQRCGPTPAVCVRRGDSIAADIGPIDLPGPLSQSGIALARNGAGLVLETIGERSDSGAWFHDLETGENILVTRTPDGEPVDTLQPTELIGFNQRDRAVVSDDGTAVVFRGDPALFGFGNADEPFSRPEGSADLFVFDVPTRTVGLVAQPGTASTGGFVHISSFGQVITGSGEVVVFLSSQQLNDDDTDDGVDLYAWGGPVELPDPDPVVEAIEVNQGIQTRVARAGAIDSTVDYPDQDVPFVVGRDTLVRLYPFAGEGADPAVYDVDLRLQVELDIAPGVLPPQVVLETTTVIRPNVFGEPRPVVGPADAELDRQLLVMRADPSRTVEFVLDGDAVLSEGEVVGADLVPRELIRGVWLTPWHEFEDRAVGGTVRVDLQPAEDLRVHLLNFTGPHFRNLTDEFGRPGANADIGRFRREVVPYLERTTPFAGVAVASATDVVLQDPSRPFRARGADGRVRQLAPANDCLRALHLAALAAAGNVAPTAPADYTVTLGYGTTFRACFGLAYGFDGARLGASAATRYGNAWPMVTASLGDSAAHELGHTMGIRHADGSHREADAEAWPYGRGWINPSTSGPERQAFGALMTDLSGQLIATPLGTAVLSNSWTASVLDFCPTTGERTAPCTNGDAQQGAELMSYGSSPPAVDLSPLVTTVRDRWPSDLTWRRMVAAMGGLPTTTPFPPSSPAPEASAPAPRQAPPGADGALVVSVLEQDGERFLLPADHVSGRGAIVEAESDDLVVEARDADGGVLAAAPVIEGVQEEAEAVLHVAVLPAMADVTSLVLVEDGDDAIAWPASANAPTVSLTVPETVTADRATVELAVDDADADDVLGATLSISVDGGETRSLLRHLDPAETGPATIDLSGFPTGPAILRAAVSDGLLVDIADADLVIGPLRRLSGDSRVATAIEVSRASHPEDGSAATAVLARADGFADALSGATLATQVAGPLLLNPTDRLADEVAAELTRLDVDEVVLLGGVSALSAQVAADLGAMGVTVERVAGDSRFATAGAVADRVDSAHAFLVEGANADPGRGWPDAVSASALAAFRGDPVLLATRDELPAATAEALTRNGIGAVTIVGGTAAVGDAVAAALTDLGIAVERVAGPSRFATSGEVAALAQQLGADGNRVWLATGSNFPDALAAGPAAAADGGVLLLVDRDTLDGSPAVGEWIEDHPDLSQVTLVGGTAAISDQVAADLEARAG
>CP031165.1|AXV06846.1|2532418_2532727_-|hypothetical-protein
MLAMSDTDPQQPQPPQQPRVNIKVDDDERFGTYANFLVVSHSAHEFTLDFCQIMPGGEPGKVQAEVVSRVKIAPTMVGKVIRALNTNMTGYEDKFGMVAEIG
>CP031165.1|AXV06857.1|2546130_2546559_-|putative-lyase
MQRMTLALRYCHVTVTDHEAALGFYRDALGLEVRNDVSSGGHRWVTLGIPDQPGTDIVLSDPYGGRSEADGDTIAELVTKGVFGMVVFRTDDLDKVFEAAEASGAEVMQEPTEQPWGPRDCAFRDPAGNMVRIEQTTPAEQA
>CP031165.1|AXV06858.1|2546560_2547040_-|Transcriptional-regulator,-AraC-family
MRSRTSSLGAMQPETLADLANLRRARDFMDREYDRPLDVAAVARRALMSPSHFSRRFRAVYGETPYAYLMTRRIERAMTLLRAGTSVTDACMAVGCSSLGSFSSRFTEVVGMSPSEYRAQEHPAEKAMPTCVAKANTRPPRSPGRRSSRIGEASGISAH
>CP031165.1|AXV06859.1|2547046_2548018_-|Alcohol-dehydrogenase
MKAWTFDRYGSPDVLRLEDVPDPAPGPGEVLVDIRAAALNPYDWRILGSDPLVARVSLGLRRPRAGAILGADLTGEVVALGDGVTDLAVGDRVLGEVELGACAQRAVASADRLVVVPDGVTDIQAAAVPMAGQTAWKAVHAVGRVGAGDRVLVNGASGGVGTFAVQLAVAAGATVTGVCSGGNAELVRSLGAAAVVDYTVTDFTEERTAYDVLIDTKGTHPLRRFLRTLVPDGRLVLVGGGGGKLLGPATHVLLGVLANHLQRRTIGVVGWKPNAADLAAVIGLVADGAVSPVIDRVVPFADVPDALRYLRLGHARGKVVIEV
>CP031165.1|AXV06860.1|2548014_2550195_-|hypothetical-protein
MYQLARRIGDASARRPWVTIAAWLMGIIVVLATAGSIGGAFVDDMTAPGSQSERANQLLADRFPDAAGGSAMAVFAAEDGQPLVAHREVIADALQRIRAVDHVVAVSDPFVDGTVSDDSRIGFATIAFDTPSVDLGPAPLAALDAAVGPARSADLAAELGGDAIFINAETETSGAEAIGLVAALVILVIAFGTVVAALVPIALALTAVAAGLGGITLLAAVMDTSTSAPTIGAMIGLGVGIDYALFVVARYREHRTAGLPNEQALSLAMGSSGSAVVFAGGTVVVAMAALVLTGLGFLGSIGLATSLVVLFAVASALTLLPAILTLLGDRIDAGRLIGRGRAPVPSEDTRWWQFAHRVSGRPWPWLLAATALLVLLAAPAIRMETGFPDAGDDSVETTHRRAHDLLAEGFGPGSNAPLLLVLDLVDTGLAAEDVPTIVAAVRADPGVVMVGQPVTSPGGDAVVVPVVPATDAADPATSATLQRVRAVAPDGLYVAGLTAMTDDLTTQLTDTLPVFVAAILAASFLLLMVVFRSVAVPLKAAVMNLLSIGGAYGVVVAVFQWGWFGGLFGLDGTYLIASPMPTIFFAVLFGLSMDYEVFLLSRIREEYAVTGDNAESVARGMAGTGRVITSAALIMMAVFGSFVGNTSPLVKMMGLGLSTAIVLDATIVRMVIVPATMALMGRANWWLPGWLDRLLPHVDLDHAVASAPAVPVIDVTTRPRSLEEIS
>CP031165.1|AXV06861.1|2550427_2551651_+|two-component-system-sensor-kinase
MSPGSTTAARRNVDTPGPLGAPRPAERVRRSGPFVRWPRTADAVLATVVFVLTTTVTEGPGDTLMTRSVQDVPVPALLAFAVASAALYRRRHEPLVVLAVVLVCFAATLDSGFADAGGTLLIGLYSVGRYAPSQQRGIVGVVVAIVLIAADGLLAGLPWGEVVVSGVAMEVAWSIGRRLRLRGERAVALQREKDVEAHRIVMEERTRIARELHDVVAHRVSSMTVQAGAAKAVAARDPEAALRAMTAVEEAGREALDELRHLLGVLRLEADLDGAGPQPGLQDLPRLVEQTRRAGLEVTLSIDGVAAPLPARVELSAYRIVQESLTNVLKHAGPGARADVTLQADRRRLVVEVLDDGAGVNGEPGSGHGIVGMRERATLLGGSLVAGPRPRGGYLVRAELPIDGDAA
>CP031165.1|AXV06862.1|2551667_2552357_+|DNA-binding-response-regulator,-LuxR-family
MTIRVAVVDDQTLVRSGFAMILGANDDIDVVAEAATGVEAVAVAREHRPDVVLMDIRMPEMDGIEATIRILQEADTTPGHEVRVLILTTFDPDEYVYRALRAGASGFVLKDTPADQLVQAVRTIADGGALLAPSITRRLISRFGQQLSTDRAVADRLDRLTEREREVTAAVARGASNAEIAEALFIGAATVKSHVSNVLTKLGLRDRAQIVVFAYESGLVEPGDIDIGY
>CP031165.1|AXV06863.1|2552388_2553135_-|Pyridoxamine-5'-phosphate-oxidase
MAIGAWAMLSAMSDISPPPRSADRRWTPAEDGRGEPGSDRVKVRRDTKKRGRYDAEAVHAILDATPFCHIAYVHDGHPIVIPTLQARIDDHVYLHASSGSRLGLSADTPWPISLSVTLIDGLVMARSGFHHSINYRSVVVVGDAVLVTDREEMLLALDTTVDHVAPGRAAELRRPTERELSATVVARLPLAEASVKTRTGPPNDEPEDMDLPVWAGVVPMTTTFGPPLPSPDLADDIPVSPSVRLLTG
>CP031165.1|AXV06864.1|2553350_2555222_+|Vancomycin-B-type-resistance-protein-VanW
MRDVTTDTHASDEAGETPSTETPDTEQSASSKASNAGGTGMSRADWHDTMTVEGGGRRWGWMLGLVGSTAVLAVAGVLMAINLPGGTTLAGTSVASVDDAPAALQEAAGTLTSLPLRFSTDAGTELVRTGGDLGLTVDVRGTISPIEQGLPSISAWLRRLPSGPLAAPLQLEPYDGDVLTEVAAAVTAEPINAELDVRASGIDTTPGVDGLDVTSEDVRQALDTALDTIETTDPSTWPETLEVTVAGSTVAPPVTQADIDAVGEVVDRLEAAEVVVTGEVILPADPEADEDEESSEERRGPQAITLSRSELRQLVDVAVDAEAPEGERLRLVPDPDGTPGRLVALMDLARVRPEVTAHVENRSPTPTTDDDPTDVSDITGDLVLDEVEPGFEPDREATLAQVIDAALAGGGEVEIVGETDSEVSLADMGIVEPISTFTSYYTAGQSRVQNIRRIAEIVDGVIVPAGEAFEVNHFVGRRTVENGFTVGGAILDGELVSDIGGGVSQFATTFFNAAWFAGIELVDFKAHSFYFSRYPPGREATINYPNVNLEIRNDTPYDILIDTDSNETSVTVTFWSTPYWDVQTVMGPCGCGGSFRITNERILTAPGGQPVTEEYTTTYSVPR
>CP031165.1|AXV06865.1|2555294_2556152_+|hypothetical-protein
MLMSGCGAIVLLALAAGVRWRAVEYRAGWYAAPMPPRRLRAGVSMSRRIFREAAVMVLAGALVGLLLIGPAARLAMRALAVLAGPEAQGRPIETGTAMGAITVEGTLVVVVFGGLLAGLLLALVHTLLRRLLPDGWRGGSVVGLAVLVVAGPLIDPLRPDNPVFANVGHAWVAVLLFSAIAIAAGAVLAAVHARLSQAVPLPAMRPVRAWLPYVPLAMLVLPDLLLLTELLTAGGVGVVLRRRGVIPLSERTGRLLRVAGVVLVVGVVSWKAPGFALAVSHIVGG
>CP031165.1|AXV06866.1|2556185_2557298_-|putative-periplasmic-protein
MPRSYARTVGEPARRTMPAGRALVVIVVALLLGGLLNVTALTEAADRQPPSLKRDISQVLVWPFEQISGLLGLDQPRALLADRLGRDADAGTAGGTAAATVDAGESAPQEAGDALGAAAALAGREAIDTALGDAVAIPEAGASLEDQPTLTGRLEGPFTETEPLVVGVIGDSLTEQIGPTLIQRMGRPGVPGEAFHDFTYSSGLSRPDFYDWPARAAQLMAEEDPDIWVVMVGANDGQDVIDDGGQFRQLGTDEWEAIYRSRIGGLMDLLTADGRAVIWIGQPVMRDTEFDERMEYLSSLYQSEASARAYVSFVDARRVFAGDDGRYADYLPAGDGSLTQMRLGDGIHLTRSGAERLVSQLLPLLPIETG

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Crispr_ID: CP031165_15

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_15

2932611-2932718

Orphan

Consensus_repeat	Method
GGGCGAGTTCAAGCGAAGCTTGAACTCGTGAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_15

>merge|CP031165|15|2932611-2932718|CRISPRCasFinder
GGGCGAGTTCAAGCGAAGCTTGAACTCGTGACAGGCCGGGGGGCGAACGCGCGGATCCGCCAGGATCTGCGGGTTCGGGCTAGTTCAAGCGAAGCTTGAACTCGTGAC

>CP031165|15|14|2932611-2932718|CRISPRCasFinder
GGGCGAGTTCAAGCGAAGCTTGAACTCGTGAC	AGGCCGGGGGGCGAACGCGCGGATCCGCCAGGATCTGCGGGTTC
GGGCTAGTTCAAGCGAAGCTTGAACTCGTGAC

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV07207.1\|2921043_2922570_+\|Oligopeptide-ABC-transporter,-periplasmic-oligopeptide-binding-protein-OppA	unknown	unknown	gnl\|CDD\|173853
CP031165.1\|AXV07213.1\|2928897_2931303_+\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	unknown	unknown	gnl\|CDD\|238923
CP031165.1\|AXV07220.1\|2938850_2941154_+\|putative-enzyme-of-poly-gamma-glutamate-biosynthesis-(capsule-formation)-like-protein	unknown	unknown	gnl\|CDD\|214858
CP031165.1\|AXV07219.1\|2938264_2938723_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07218.1\|2936692_2938186_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379207
CP031165.1\|AXV07206.1\|2920664_2920895_+\|Preprotein-translocase-subunit-SecG	unknown	unknown	gnl\|CDD\|235881
CP031165.1\|AXV07224.1\|2944459_2945230_+\|regulatory-protein,-LuxR:Response-regulator-receiver	unknown	unknown	gnl\|CDD\|225107
CP031165.1\|AXV07212.1\|2928336_2928492_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07222.1\|2941582_2942872_-\|PspC-domain-protein	unknown	unknown	gnl\|CDD\|377200
CP031165.1\|AXV07209.1\|2924099_2926232_-\|Polyphosphate-kinase	unknown	unknown	gnl\|CDD\|235469
CP031165.1\|AXV07210.1\|2926378_2927989_+\|putative-sulfite-oxidase	unknown	unknown	gnl\|CDD\|239028
CP031165.1\|AXV07211.1\|2928000_2928234_-\|putative-LIPOPROTEIN	unknown	unknown	unknown
CP031165.1\|AXV07223.1\|2943056_2944463_+\|putative-two-component-system-sensor-kinase	unknown	unknown	gnl\|CDD\|226951
CP031165.1\|AXV07208.1\|2922585_2924040_-\|Oligopeptide-ABC-transporter,-periplasmic-oligopeptide-binding-protein-OppA	unknown	unknown	gnl\|CDD\|173853
CP031165.1\|AXV07216.1\|2934877_2935525_-\|putative-MEMBRANE-PROTEIN	unknown	unknown	gnl\|CDD\|377946
CP031165.1\|AXV07204.1\|2918621_2919029_+\|Transcriptional-regulator,-MecI-family	unknown	unknown	gnl\|CDD\|367747
CP031165.1\|AXV07215.1\|2932745_2934746_-\|Cell-division-protein-FtsH	unknown	unknown	gnl\|CDD\|273520
CP031165.1\|AXV07217.1\|2935523_2936666_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225807
CP031165.1\|AXV07205.1\|2919083_2920514_+\|Peptidase-M48,-Ste24p-precursor	unknown	unknown	gnl\|CDD\|320700
CP031165.1\|AXV07221.1\|2941115_2941586_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV07207.1\|2921043_2922570_+\|Oligopeptide-ABC-transporter,-periplasmic-oligopeptide-binding-protein-OppA	gnl\|CDD\|173853	cd00995, PBP2_NikA_DppA_OppA_like, The substrate-binding domain of an ABC-type nickel/oligopeptide-like import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding domain of nickel/dipeptide/oligopeptide transport systems, which function in the import of nickel and peptides, and other closely related proteins. The oligopeptide-binding protein OppA is a periplasmic component of an ATP-binding cassette (ABC) transport system OppABCDEF consisting of five subunits: two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Similar to the ABC-type dipeptide and oligopeptide import systems, nickel transporter is comprised of five subunits NikABCDE: the two pore-forming integral inner membrane proteins NikB and NikC; the two inner membrane-associated proteins with ATPase activity NikD and NikE; and the periplasmic nickel binding NikA, which is the initial nickel receptor that controls the chemotactic response away from nickel. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand binding domains of ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	1.05428e-85
CP031165.1\|AXV07213.1\|2928897_2931303_+\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	gnl\|CDD\|238923	cd01948, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.	1.23215e-96
CP031165.1\|AXV07220.1\|2938850_2941154_+\|putative-enzyme-of-poly-gamma-glutamate-biosynthesis-(capsule-formation)-like-protein	gnl\|CDD\|214858	smart00854, PGA_cap, Bacterial capsule synthesis protein PGA_cap. This protein is a putative poly-gamma-glutamate capsule biosynthesis protein found in bacteria. Poly-gamma-glutamate is a natural polymer that may be involved in virulence and may help bacteria survive in high salt concentrations. It is a surface-associated protein.	3.87208e-78
CP031165.1\|AXV07218.1\|2936692_2938186_-\|hypothetical-protein	gnl\|CDD\|379207	pfam13472, Lipase_GDSL_2, GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.	2.41761e-19
CP031165.1\|AXV07206.1\|2920664_2920895_+\|Preprotein-translocase-subunit-SecG	gnl\|CDD\|235881	PRK06870, secG, preprotein translocase subunit SecG; Reviewed.	2.71685e-10
CP031165.1\|AXV07224.1\|2944459_2945230_+\|regulatory-protein,-LuxR:Response-regulator-receiver	gnl\|CDD\|225107	COG2197, CitB, Response regulator containing a CheY-like receiver domain and an HTH DNA-binding domain [Signal transduction mechanisms / Transcription].	1.97807e-62
CP031165.1\|AXV07222.1\|2941582_2942872_-\|PspC-domain-protein	gnl\|CDD\|377200	pfam04024, PspC, PspC domain. This family includes Phage shock protein C (PspC) that is thought to be a transcriptional regulator. The presumed domain is 60 amino acid residues in length.	3.54324e-15
CP031165.1\|AXV07209.1\|2924099_2926232_-\|Polyphosphate-kinase	gnl\|CDD\|235469	PRK05443, PRK05443, polyphosphate kinase; Provisional.	0
CP031165.1\|AXV07210.1\|2926378_2927989_+\|putative-sulfite-oxidase	gnl\|CDD\|239028	cd02110, SO_family_Moco_dimer, Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). .	1.30816e-80
CP031165.1\|AXV07223.1\|2943056_2944463_+\|putative-two-component-system-sensor-kinase	gnl\|CDD\|226951	COG4585, COG4585, Signal transduction histidine kinase [Signal transduction mechanisms].	3.98635e-27
CP031165.1\|AXV07208.1\|2922585_2924040_-\|Oligopeptide-ABC-transporter,-periplasmic-oligopeptide-binding-protein-OppA	gnl\|CDD\|173853	cd00995, PBP2_NikA_DppA_OppA_like, The substrate-binding domain of an ABC-type nickel/oligopeptide-like import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding domain of nickel/dipeptide/oligopeptide transport systems, which function in the import of nickel and peptides, and other closely related proteins. The oligopeptide-binding protein OppA is a periplasmic component of an ATP-binding cassette (ABC) transport system OppABCDEF consisting of five subunits: two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Similar to the ABC-type dipeptide and oligopeptide import systems, nickel transporter is comprised of five subunits NikABCDE: the two pore-forming integral inner membrane proteins NikB and NikC; the two inner membrane-associated proteins with ATPase activity NikD and NikE; and the periplasmic nickel binding NikA, which is the initial nickel receptor that controls the chemotactic response away from nickel. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand binding domains of ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	3.98367e-63
CP031165.1\|AXV07204.1\|2918621_2919029_+\|Transcriptional-regulator,-MecI-family	gnl\|CDD\|367747	pfam03965, Penicillinase_R, Penicillinase repressor. The penicillinase repressor negatively regulates expression of the penicillinase gene. The N-terminal region of this protein is involved in operator recognition, while the C-terminal is responsible for dimerization of the protein.	3.2738e-28
CP031165.1\|AXV07216.1\|2934877_2935525_-\|putative-MEMBRANE-PROTEIN	gnl\|CDD\|377946	pfam07947, YhhN, YhhN family. The members of this family are similar to the hypothetical protein yhhN expressed by E. coli. Many are annotated as possible transmembrane proteins, and in fact they all have a high proportion of hydrophobic residues. A human member of this family, formerly known as TMEM86B, is a lysoplasmalogenase that catalyzes the hydrolysis of the vinyl ether bond of lysoplasmalogen. Putative conserved active site residues have been proposed for the YhhN family.	6.5158e-19
CP031165.1\|AXV07215.1\|2932745_2934746_-\|Cell-division-protein-FtsH	gnl\|CDD\|273520	TIGR01241, ATP-dependent_zinc_metalloprotease_FtsH, ATP-dependent metalloprotease FtsH. HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides].	4.28227e-84
CP031165.1\|AXV07217.1\|2935523_2936666_+\|hypothetical-protein	gnl\|CDD\|225807	COG3268, COG3268, Uncharacterized conserved protein [Function unknown].	6.73669e-14
CP031165.1\|AXV07205.1\|2919083_2920514_+\|Peptidase-M48,-Ste24p-precursor	gnl\|CDD\|320700	cd07341, M56_BlaR1_MecR1_like, Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase. This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain ?-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized.	9.6401e-25

>CP031165.1|AXV07213.1|2928897_2931303_+|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)
MVTAGVVLAIAFVAVEMWPLTLEIRGDTLNLTLSGVVVIVGLFFTGPLVTLVARMLGAGLSLAFRWHNAPLKLAVNLTAMAVEVWATAAVLALVLPEGRVTDVVQWLGVLLAGVAGELGMGFVVLAAMRMMVGTVQVDTLRALGTGLVASTLMVWVFTVLTLALVEVDPWLLGIVVAAMGLLVHSNRQRNDLNLRYQSLRGLYRFMTRVDEAEDTTAMASRILDEAAEVVGSTRAALYVVDDSRTTRLSNARGSLGVTWVPREQVEALAADVGTTARLVDRSWVQEDYLDLLDHDEQTIVASLGNPDVTGLLVLSGRPRHLPEFDVQDVELAAAVAHHAGASLAEARLLDRLREERYRVEQMGLTDTLTGLRNRDGLMRDVPRMDAGAVIVLGLRDLVEINGALGHEVGERMVLAAAQRLRRMADQHAMIAAAFGGGRFALVAPDVTSVLAGSDLCRQLLQEVSGPMEDGPLALDISPVLGIALAPSHGRDPAELVRAADKALGQALDSGMGVAWFDADYDRESTERLHLAGELRRALDQGHLTVAYQPKVELASGRVVGVEALARWPHAERGMIPPTEFIDVAERTGLIRPLTLAITQQALAQADAWRRQGLDLSMSINLSIAVMQDASMARQIVALVRSHETPPERIIVEITESQVMEDVERGSGMLAIFGAAGVSLSVDDFGTGYSSLSQVKNLPVQELKVDRSFVMDMASNRTDQVIVTSVLRLAEELGLRVVAEGIEDETVRRMLEDLGCEQAQGYLFAKPLPASQIPAAVKDIEARPRPDAAAPLPLRRRFDGLG
>CP031165.1|AXV07212.1|2928336_2928492_-|hypothetical-protein
MAVIIDERVVGGRPERLGPRGPMLPVHATKAKRPRWRQILTTGLGFALPGR
>CP031165.1|AXV07211.1|2928000_2928234_-|putative-LIPOPROTEIN
MTTTTATTTSSAAGPNWAGINWAGINWAGINWAGINWAGINWAGINWAGDSWAGINWAGDSWAGINWAGINWADQQA
>CP031165.1|AXV07210.1|2926378_2927989_+|putative-sulfite-oxidase
MTATHHDVDPAGMPADGTTPSPIPSDGLGRPAVAGLVAAAVALGTTELVAGLLPSAPSLVVAIGNGVVELGAGSRVKEIAIALFGTNEKTALVIGTVVLALAFGAVLGVVGRRRSVAVASAGIGVFGLLGVAATTVNPLDSTAWSLVPAVLGVAAGVLTLRMLLRLDRGITGAAAGHPGVGRGRREFLRIAIGMAAVAGVIGAFGRTLSSRTRINDAREEVVLPEAVRTPAPVDLATEFEGIDGLSPFFTPNDAFYRIDTALTPPMVDVASWEVRIHGMVEQEVVLTYRDLLDLPQVEADVTIACVSNEVGGDLIGTARWQGVRLSDVLDMAGVDPAADQLVGRSVDGWTAGFPTDIAFDGRDCLVALAMNGEPLPIAHGFPARLIVPGLYGYVSATKWLSEIELTTWDAFDGYWVPRGWSKEGPVKTHSRIDVPKQGAPLESGPQVIAGVAWAQQRGVERVEVSIDDGPWQETVLADELNVDTWRQWRFDWDAGPGQHVIRVRATDRTGVTQSADRVPVAPNGAEGYHTRAVTIA
>CP031165.1|AXV07209.1|2924099_2926232_-|Polyphosphate-kinase
MTTQPDLAAARSLPPRGPDGRFRRPEVQDLSDPSLYLNRELSWLEFNRRVLAQAADTAVPLLERLRFISIFHSNLDEFFMIRVAGLKDQVAAGLRLRTPDGMSAVEQLEAISRRVRPMAEQSTVTLHERILPLLARRGVGVVHVADLDERTLGRLHKQFDEQIFPVLTPLAVDPGHPFPYISNLAISLAVSVRDHKTGQRKLARVKVPGVLPRFWQVPGSRRAWVPLEELIRWRLDALFPGMDVESAHLFRVTRNADMDVDEDEAEDLLLAIQAQLSRRRFGSVVRLEVADDMPADTVRTLQEELDISSMHTYPVRGLLGLADVSQLADLDQPTLRFSPWVPVTHPRLRTSADDPVDSPTMFERIAEHDILLRHPYHSFATSVEQFVTAAADDPQVLAIKQTLYRTSGDSPMFRALIHAAEAGKQVVALVELKARFDEEANIEWARILERAGVHVVYGLVGLKTHCKTMLVVRRETEGIRRYVHIGTGNYHPGTAKLYTDLGLLTADVDIAEDVTQLFNYLTGYARHDRYRQLMVAPVSLRDRITELIREQAELGTDGLIRVKLNSLSDRSLIRELYAASRAGATVDLIVRGICGIRPGIPGVSDRIRVMSVLGRLLEHERILQFGQDMWIGSADWLPRNLDRRVEAMVPIEDEDLAKELRRILDVTWQDTRQGWRLRADGTWETPPDVDSVASQARFMAETRAADLEQA
>CP031165.1|AXV07208.1|2922585_2924040_-|Oligopeptide-ABC-transporter,-periplasmic-oligopeptide-binding-protein-OppA
MLLLTTTACSTTLARQPAAVSTKAPLELAVWVGPSPTLHPHQANPQVTAALFSPLVVIDPESHLPTWGPDVPGALLESVSSEDLRRWDVVVKEGWTWHDGTPVVAEDVARGWQAAIEAGLPIVSTVTDIRVRDKATLSFALAAPYGQLPALLANEAFLPLPPMAIDDPARFAEAPVGNGVYRLAGRQGDALVLDAVSGHPAGTAASDRLLAVRTDQPAADQQLVVVPDGVLALPGDADRPHVVRAPGRQLAYLGFPLTDPRFADPDVRVALSQAIDRQALVELLPEGAVVPADRLLGPGMARSDGPVCTACVHDPDRAAELWSAPDGPLSLWYAADAGHDEVIDAIAGAWSTVLGVDDIQLATLPAEDLLARLAQAEVPGPFRLTWAADAASPSRLLEPLFGPRGSANDFRYRADGIGDRLATADLQRDLEEALDAYATVEQQVLDDLPLVPLWFSTVGVAMDENITAGMDGRGLLDWASVERS
>CP031165.1|AXV07207.1|2921043_2922570_+|Oligopeptide-ABC-transporter,-periplasmic-oligopeptide-binding-protein-OppA
MTVAGGTFRWAIGEPTSILPPMASTTDDFAVVDALFDSLTTAGVAGRPAPSAATEWSANDDATVWTFHLRPGATFQDGTPVTAEAFVEAWSTLVAAGPMQHLLRDVVGHAAVASGAATTLSGMRATSEDTLEVTLSRPRGDFPILTSHPSLGPVQPSAVAADPAAHALQPVGNGPFRASEPWVPGEFVRAARWDGWTNGDRPEDGIGEVVFRIADLDTNFLAFRQGRRDLARVPPEALELAAEEYPASPGSYTGPGLVTGATPETYLLAIDRSVEPYEELEVREAASLFVDRQRIAAENDGGNLDPATSLLPPAISRGSAGMCELCTFNPSGAADRLADAGVPGLTLAFNAEGGHERIRDVLREALSDRGYTLVSNWRGAAPTLVEYLDRLASGGIGMFRLPLTADVPSSLDILYPLLHSSQTPDRGGLNYMRYQDPQVDALLDQAAQIVDVDQREALLRRVEEIVVNRDQVIVPVVTSRLAVVVGEDVTGVRVDPFGGVDLTTVRAV
>CP031165.1|AXV07206.1|2920664_2920895_+|Preprotein-translocase-subunit-SecG
MLNIILTVLHVIVSILLIMFILLKSGKGGGLSDMFGGGSMSGGGGSTIAEKNLDRITVLTAVVFAVTTMALALRLV
>CP031165.1|AXV07205.1|2919083_2920514_+|Peptidase-M48,-Ste24p-precursor
MTDGVVGLRDVTDGLGLLLSTQSFAARALIGSLVAAALAAAAVRLGWLKSRRARRGLVLAPIATAVAAAVASAGDAFLPPLVVATTGAGESWEFFGQEYRVLQLEWLLIAYVAVASFLLLRRGLSHLAIRMYVRGAVPCDDPAVIASVRRIASKLGLTSPSLLLIPDCPGGAFTTGLRHPVVCVDPDLVEQLDTRELEGLLAHELAHIARRDVPLNVAIGVIRDLTFFVPPLHLAARWLRQEQEHAADDLASDSTGRPAALASSILKVWEGASRRGVTVVASMACATMVPAPLPVPAGMPARILRQGGLRGGAKQIAARVVRLIEGEARATRTRERIELLALAVVLTALTAVTVVLPAQLADSSLLLGQWSRPVARPVESPALQTFRTLTITETTAFGTSVARPARAATCEDCLTVESTADWRRGVAPAAPVRTAGWAHGGYVWEDGSPVLVTAPRAEPLWGVDARTTRVGVFVVR
>CP031165.1|AXV07204.1|2918621_2919029_+|Transcriptional-regulator,-MecI-family
MAKRNKQLQGLLGPLETDVMEMVWRLGDATVRDVHEELRNRRDLAYTTIMTTMARLASKGLLERDTSGLAHRYRPTVSREVYAKSTVTSVVDWLVQSFPEPAMSYFVEKIDDSGDPDVLSALRASIDAQRSDEDD
>CP031165.1|AXV07215.1|2932745_2934746_-|Cell-division-protein-FtsH
MEAKDHTEGAQPNALSHSVADRLGGALVSAHHADVGQAREHARQHRLKALALLLAIPFLFLWTRIVRGDAINFLQAPTLPDGWQLWLLPMVLILALGAAMLMPLMSGRSPHIRYAPEQIETGFADVVGLDPVVNEVTRTLNTFMGHKLYRGQLGGRPRRGVLFEGPPGTGKTHLAKAMAHEAGVPFLFVSATSFQSMWYGATARRIRSYFAALRKVAREEGGAIGFIEEIDAIATSRSGMRASGFAPAGTNAMSSGCVQATADAFGADGGVSFGGGEATAHSGGLVTNAFGSSEGTAGVVNELLIQMQSFDTPPASIRIRNWWAEKVNAYLPADRQIKAKTSPYNNILVIAATNRAADLDPALVRPGRFDKQLAFDRPAQPARRDLLDYYLARKSHAADLDDPELRDQVASQTLGYTPVMIENLLDEALIVALKNGRDQMTFGDVAQARLDIEVGMATPAPYTDAERRRVATHEAGHAVMAHLSGHRRLEILSIVKRRTSLGLLAHGDTAEVYTRTVKELHDMVDIAMGGKAAEEIWFGAVSTGPGSDLAAATRTACEIIGIHGMGDSLVSLAAVQQSSLSGTNLVGQVLRDQVARPQVETLLHEAHQRTVATLERNRHLVEALRDALLDRDELVGAEIGEVILAAGPPVLEDLTVEVDGVELAAD
>CP031165.1|AXV07216.1|2934877_2935525_-|putative-MEMBRANE-PROTEIN
MLQSSTALLVLTLLAAALDWWAVATDRRRLEEVAKPAVMVLLIGWVLTVPGADPTVRTWVVVALGLSLVGDVLLLPRIDVFVGGLAAFLLGHLAFVPALLPHADGLTGGIAALGLVPAAAFVGRRIADGARQHGGQPLASAVVVYVVAVGATALLAVASRAPLVMLGGLLFATSDGVLGWNRFVAPLPNGRTIVHVTYHLAQVGLATVVTLSTVA
>CP031165.1|AXV07217.1|2935523_2936666_+|hypothetical-protein
MVGIMAHRPTDPQRARGGGGTLCGMRRRIVVVGATGRTGRLVAQELAGRPHVLLVARRADALATLGRTTDLPARCADLDGLGGVLVPGDIVLSCVGPHDVVGDRVVDAAVHVGATYLDVTGEPAFLARLHTDHGPRAASSGVSLLPAVGYEYLPGLLLSELALDAAGPAARRVEVAYLVDGGLDAGSATARRSLVRALTRPTTTFRRGVHHAETVAARRGEFRAGGQLHTTVSLGGLEVWSLPTRHPDLDRVDVHTGWFGAAAPLLQLGALLSGPARMLGVDRLMDGAVAILGDGDDEGLSTGTSRFVVRVRDERGGVLAREEAVAGNAIVLAARLAAATADALAERPLGDVPTGATDPVAALGLQAVGRLAEWAGLVRL
>CP031165.1|AXV07218.1|2936692_2938186_-|hypothetical-protein
MLIFLAVLSALVVGALSWLLIGPTGAAAVAVLILIGGLVAQFGDRSVRRPIGTVLLLALLAGGTYGTIVAVDLVEALTTTDGTVDMADQSQLASAEDKLEGLAGQSSFQLELTEPELQAVVQDGLAAADDVPVRRVDLDLRGATSDVAFRAVFKAGGVEATGNASIAVVDGGIDLELGPLEFGSVQVPSLAAGAIQSLLGAVTDLNAALEDQQAVVQSITVTDDALIVTGTRGTDEVLTDGDLLAAIRDQATGAIDAVQAPPERIGQGRLAGLDEPGEPIVLAIGDSLAANVGVDDNRDGFVSRFHRFVADADGVPYGLVNLGVPGETSGSLLTGGQLEAAEAVLASRPAAYVVVDIGANDLLGHLTSAECGTDLANASCQQLVDETLVTYRSNLEQAMDRLVASAGSARVLFLQTYNPFSLGLGESAQERESSTMVSRLNAVAAEVAASRGIGVADGFSPLQGTTAATTHMLDAEPDIHPNVAGYDVLAGALVDAR
>CP031165.1|AXV07219.1|2938264_2938723_-|hypothetical-protein
MNEPKFTFVEPGRDRRKRKEHLKAVMKHQPGTARAVELANLARDFHENRELNMAMDTARQCLLESEGTVSFLVNAYICHDRDDHAIEDLAMLADLARWLDDDGLQAIVRAMAFERGLGWCGCTDGRERERRIDTLRRRFDDGLANEVDLALI
>CP031165.1|AXV07220.1|2938850_2941154_+|putative-enzyme-of-poly-gamma-glutamate-biosynthesis-(capsule-formation)-like-protein
MLLTVATSAGAGPALAPTVIDTPPARVAGADRTATSAAFLGMLAETAAVERVVVVPRDSTGVALAAAGLAGVLDAGVVLADAVPSDTVTTAVDTVHPIEVLTVGDAARADAWQQDGRVVTVLDAPGGPPALAAEMAREIARRHAEAGTPVPTRVLLASTTGLPDALAASAWAHEEGLPLLLTAASALDPHARFVVEQLGITDVTILGGTAAVSATVEEELRSSGLAVERVAGPTREHTALAVAARRGVGPNRVLVAAGDDPADAAAAGPWASVVGAALLPPGPTVAGALAERCGHGVVVQVAGGPVAVPEGQVAPLLAAAERCDGPNRPLTVRLAVAAPEDPEVVPTVVDVVADARGWNSRRLRIEAVGQDETMGLIVTPDGCGGAAVCRRGRTIVVDATTWRAADPDRRTRLVNLAVAVRLGVTLPDGCTGGVLQPLACPDGAPWPTDDQRRTLADTFVPSATIALTGDVHAERHIGSQAVAGQNPLDPVRDVLTAADVAVVNLETPLSTRGAPVPKTYTFRGPPEMAARLVEAGVDVASLANNHGLDYGPVAMLDTLDHADAVGLHVVGAGADATAAYAPALVETPAGTVAVVGLTRVLHTRTWEATATRAGLASAYDEAAAVAAVRAADAVADHVVVAIHWGAELADCPNADQRHLATLLVDAGADVIAGHHPHVLQGVQPLRDGLVAYSLGNFVWYHNRAPSRYTGVLTVELPLLDQPSWSFLPAEIGSDGRPHPAAGGTAAAITERLTSRSPGGAAGCGFPS
>CP031165.1|AXV07221.1|2941115_2941586_-|hypothetical-protein
MTDRPAPSRPRGLYRHRTDIVSLLFGLAFTAAALSALVQPGEPSAIDVGAVAAVAAVVAGLAVIDSLRSSDTDRTEAPASDPVFDPALPPAPIIPTPEAIRDEDREWFGLDNPLSEVEREILASLEEEDRSEVTGPDGGPPDAPSGGEPTAGGPTG
>CP031165.1|AXV07222.1|2941582_2942872_-|PspC-domain-protein
MDQKKWAGVAAGIGWYFGVDPVLIRIGFVVLGFMAGPVSLGLYVLLWIFLPEATSQRVPMSAPKPAGGRSRGVTAAAIVLGAMIFGQIDLFRGDVLLAAALIGLGVLLFNDRREVPTNPFWSGGASTPPPPAPWAVPTTDSSTGSPSSTMPPPPRPEDATVPLERSAPSRAGDCGPPWRRGPGHGPHQGRTTTAYPTGYTASWSGPPRPPMPATPRRGRTRSHPRSTLFPLSFGVWLLALGGAALLDRMGLVELTLFNAAALSLLVAGLGLLVGTWFGRARRLVPIGLLTGVVMVGAAAAPTIDLPRALEGGLGERQYALTAVGDVQPDYQLLAGQMVLDLTDLELGSETVDIDASVVLGELQVLVGPDVTVEAAGTLSAGDYTVLEETSSGNDLQFDVLDRGLEGAGRIRLDLESTFGEITVTREEPQ
>CP031165.1|AXV07223.1|2943056_2944463_+|putative-two-component-system-sensor-kinase
MVPISTPTPTTTPDPGPVPPPPAASSPDGPAPSSSTLSAVTAPLTDLGITRSTEDRVVSGVAAGVANRIGVDVGVVRLVLVVLATAGGAGVLLYALGHVLLPEPSVDPESAETAPVRTGTVRHAVALGLITAGVLVLLRALGVWFADSLTWSVGLAAIGSAVVWTRASEEEKVRWRHAMDRAVGDRVMPDLASLSRIRLSVGAILLLAGMATFLVTIDLSAAPEVILASLVTIIGVALVIGPWFQALGRQLADERRERIRSEERADMAAHLHDSVLQTLALIQRSGSPEEMSRLARGQERELRAWLFGRRPDDAATRLGQAIQDAAGLVEDRYGVKVEVVLAGDVALDEHLHAMVEAAREAMANAAKHAEVDRVDVFVEVEPDRVEVFVRDEGVGFDPTAVPEDRRGLVESIRGRMQRHGGTATIESVLGEGTEVELHLPLDPSPPVASDAVADAADDDPDPDLDRPL
>CP031165.1|AXV07224.1|2944459_2945230_+|regulatory-protein,-LuxR:Response-regulator-receiver
MTTRQEHTDMATRLDPPSAPDDDPADDPAGDPSRSPASDGPLRVFLVDDHRLFLTGVRTEIGDRFDVVGTAETVDAAVADILALQPDVVLLDVHMPDGGGLAVITRVRESTADVQFLALSVSDAAEDVIALVRAGARGYLTKTVSADELAEGVRRVHGGDAVFSPRLAGFVLDAFSGAPPARPTETSPGEDDLDQLTPREREVLRYIARGYAYKQVASRLHISIKTVESHVSAVLRKLQLSSRYELTRWATDRKIV

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Crispr_ID: CP031165_16

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_16

3053567-3053687

Orphan

Consensus_repeat	Method
GGCGTTCCCCGACGATTGTGGGGAGGGGTGCACCCGCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_16

>merge|CP031165|16|3053567-3053687|CRISPRCasFinder
GGCGTTCCCCGACGATTGTGGGGAGGGGTGCACCCGCGCTCCCGTTCCTACGATCGTGCCCGATTGCCGGGCCTGCCAACGAGGCGTTCGCCGACGATTGTGGGGAGGGGTGCACCCGCGC

>CP031165|16|15|3053567-3053687|CRISPRCasFinder
GGCGTTCCCCGACGATTGTGGGGAGGGGTGCACCCGCGC	TCCCGTTCCTACGATCGTGCCCGATTGCCGGGCCTGCCAACGA
GGCGTTCGCCGACGATTGTGGGGAGGGGTGCACCCGCGC

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV07328.1\|3056150_3056645_-\|Inorganic-pyrophosphatase	unknown	unknown	gnl\|CDD\|376376
CP031165.1\|AXV07317.1\|3042202_3043417_+\|3-oxoacyl-[acyl-carrier-protein]-synthase,-KASII	unknown	unknown	gnl\|CDD\|274452
CP031165.1\|AXV07326.1\|3053801_3054956_-\|transmembrane-efflux-protein	unknown	unknown	gnl\|CDD\|341027
CP031165.1\|AXV07324.1\|3050280_3051804_-\|Exoenzymes-regulatory-protein-AepA-in-lipid-linked-oligosaccharide-synthesis-cluster	unknown	unknown	gnl\|CDD\|238625
CP031165.1\|AXV07320.1\|3045785_3046631_+\|UPF0028-protein-YchK	unknown	unknown	gnl\|CDD\|224666
CP031165.1\|AXV07335.1\|3068013_3068466_+\|Acyl-dehydratase	unknown	unknown	gnl\|CDD\|239534
CP031165.1\|AXV07330.1\|3060630_3062235_+\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	unknown	unknown	gnl\|CDD\|238923
CP031165.1\|AXV07322.1\|3047287_3048625_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07321.1\|3046627_3047266_+\|Leucyl/phenylalanyl-tRNA--protein-transferase	unknown	unknown	gnl\|CDD\|234720
CP031165.1\|AXV07331.1\|3062315_3063740_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274360
CP031165.1\|AXV07327.1\|3055238_3056147_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07319.1\|3044946_3045744_+\|Enoyl-[acyl-carrier-protein]-reductase-[NADH]	unknown	unknown	gnl\|CDD\|236124
CP031165.1\|AXV07316.1\|3041895_3042132_+\|Acyl-carrier-protein	unknown	unknown	gnl\|CDD\|179197
CP031165.1\|AXV07323.1\|3048695_3050234_-\|Cyclohexanone-monooxygenase	unknown	unknown	gnl\|CDD\|224983
CP031165.1\|AXV07329.1\|3056672_3060461_-\|ATP-dependent-helicase-hrpA	unknown	unknown	gnl\|CDD\|182986
CP031165.1\|AXV07325.1\|3051811_3053455_-\|Peptide-chain-release-factor-3	unknown	unknown	gnl\|CDD\|179105
CP031165.1\|AXV07332.1\|3063816_3064746_+\|Exopolyphosphatase-related-protein	unknown	unknown	gnl\|CDD\|223691
CP031165.1\|AXV07334.1\|3066292_3067933_+\|Carboxypeptidase-T-precursor	unknown	unknown	gnl\|CDD\|349432
CP031165.1\|AXV07333.1\|3064868_3066266_+\|putative-membrane-protein	unknown	unknown	gnl\|CDD\|376607
CP031165.1\|AXV07318.1\|3043462_3044908_+\|Acetyl-coenzyme-A-carboxyl-transferase-alpha-chain	unknown	unknown	gnl\|CDD\|227136

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV07328.1\|3056150_3056645_-\|Inorganic-pyrophosphatase	gnl\|CDD\|376376	pfam00719, Pyrophosphatase, Inorganic pyrophosphatase.	6.29533e-77
CP031165.1\|AXV07317.1\|3042202_3043417_+\|3-oxoacyl-[acyl-carrier-protein]-synthase,-KASII	gnl\|CDD\|274452	TIGR03150, fabF, beta-ketoacyl-acyl-carrier-protein synthase II. 3-oxoacyl-[acyl-carrier-protein] synthase 2 (KAS-II, FabF) is involved in the condensation step of fatty acid biosynthesis in which the malonyl donor group is decarboxylated and the resulting carbanion used to attack and extend the acyl group attached to the acyl carrier protein. Most genomes encoding fatty acid biosynthesis contain a number of condensing enzymes, often of all three types: 1, 2 and 3. Synthase 2 is mechanistically related to synthase 1 (KAS-I, FabB) containing a number of absolutely conserved catalytic residues in common. This model is based primarily on genes which are found in apparent operons with other essential genes of fatty acid biosynthesis (GenProp0681). The large gap between the trusted cutoff and the noise cutoff contains many genes which are not found adjacent to genes of the fatty acid pathway in genomes that often also contain a better hit to this model. These genes may be involved in other processes such as polyketide biosyntheses. Some genomes contain more than one above-trusted hit to this model which may result from recent paralogous expansions. Second hits to this model which are not next to other fatty acid biosynthesis genes may be involved in other processes. FabB sequences should fall well below the noise cutoff of this model. [Fatty acid and phospholipid metabolism, Biosynthesis].	0
CP031165.1\|AXV07326.1\|3053801_3054956_-\|transmembrane-efflux-protein	gnl\|CDD\|341027	cd17474, MFS_YfmO_like, Bacillus subtilis multidrug efflux protein YfmO and similar transporters of the Major Facilitator Superfamily. This family is composed of Bacillus subtilis multidrug efflux protein YfmO, bacillibactin exporter YmfD/YmfE, uncharacterized MFS-type transporter YvmA, and similar proteins. YfmO acts to efflux copper or a copper complex, and could contribute to copper resistance. YmfD/YmfE is involved in secretion of bacillibactin. The YfmO-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	3.64437e-20
CP031165.1\|AXV07324.1\|3050280_3051804_-\|Exoenzymes-regulatory-protein-AepA-in-lipid-linked-oligosaccharide-synthesis-cluster	gnl\|CDD\|238625	cd01300, YtcJ_like, YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for photochrome A signalling.	7.8813e-87
CP031165.1\|AXV07320.1\|3045785_3046631_+\|UPF0028-protein-YchK	gnl\|CDD\|224666	COG1752, RssA, Predicted esterase of the alpha-beta hydrolase superfamily [General function prediction only].	3.53427e-38
CP031165.1\|AXV07330.1\|3060630_3062235_+\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	gnl\|CDD\|238923	cd01948, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.	8.40342e-47
CP031165.1\|AXV07321.1\|3046627_3047266_+\|Leucyl/phenylalanyl-tRNA--protein-transferase	gnl\|CDD\|234720	PRK00301, aat, leucyl/phenylalanyl-tRNA--protein transferase; Reviewed.	6.66093e-113
CP031165.1\|AXV07331.1\|3062315_3063740_+\|hypothetical-protein	gnl\|CDD\|274360	TIGR02946, Putative_diacyglycerol_O-acyltransferase_Mb3115, acyltransferase, WS/DGAT/MGAT. This bacteria-specific protein family includes a characterized, homodimeric, broad specificity acyltransferase from Acinetobacter sp. strain ADP1, active as wax ester synthase, as acyl coenzyme A:diacylglycerol acyltransferase, and as acyl-CoA:monoacylglycerol acyltransferase. [Unknown function, Enzymes of unknown specificity].	1.6207e-143
CP031165.1\|AXV07335.1\|3068013_3068466_+\|Acyl-dehydratase	gnl\|CDD\|239534	cd03450, NodN, NodN (nodulation factor N) contains a single hot dog fold similar to those of the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit. Rhizobium and related species form nodules on the roots of their legume hosts, a symbiotic process that requires production of Nod factors, which are signal molecules involved in root hair deformation and meristematic cell division. The nodulation gene products, including NodN, are involved in producing the Nod factors, however the role played by NodN is unclear.	1.91194e-76
CP031165.1\|AXV07319.1\|3044946_3045744_+\|Enoyl-[acyl-carrier-protein]-reductase-[NADH]	gnl\|CDD\|236124	PRK07889, PRK07889, enoyl-[acyl-carrier-protein] reductase FabI.	7.11e-143
CP031165.1\|AXV07316.1\|3041895_3042132_+\|Acyl-carrier-protein	gnl\|CDD\|179197	PRK00982, acpP, acyl carrier protein; Provisional.	8.45815e-17
CP031165.1\|AXV07323.1\|3048695_3050234_-\|Cyclohexanone-monooxygenase	gnl\|CDD\|224983	COG2072, TrkA, Predicted flavoprotein involved in K+ transport [Inorganic ion transport and metabolism].	1.22932e-95
CP031165.1\|AXV07329.1\|3056672_3060461_-\|ATP-dependent-helicase-hrpA	gnl\|CDD\|182986	PRK11131, PRK11131, ATP-dependent RNA helicase HrpA; Provisional.	0
CP031165.1\|AXV07325.1\|3051811_3053455_-\|Peptide-chain-release-factor-3	gnl\|CDD\|179105	PRK00741, prfC, peptide chain release factor 3; Provisional.	0
CP031165.1\|AXV07332.1\|3063816_3064746_+\|Exopolyphosphatase-related-protein	gnl\|CDD\|223691	COG0618, COG0618, Exopolyphosphatase-related proteins [General function prediction only].	2.07363e-15
CP031165.1\|AXV07334.1\|3066292_3067933_+\|Carboxypeptidase-T-precursor	gnl\|CDD\|349432	cd03859, M14_CPT, Peptidase M14 Carboxypeptidase T subfamily. Peptidase M14-like domain of carboxypeptidase (CP) T (CPT), CPT belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT has moderate similarity to CPA and CPB, and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB. CPA and CPB are M14 family peptidases but do not belong to this CPT group. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs. CPT has increased thermal stability in presence of Ca2+ ions, and two disulfide bridges which give an additional stabilization factor.	8.79939e-80
CP031165.1\|AXV07333.1\|3064868_3066266_+\|putative-membrane-protein	gnl\|CDD\|376607	pfam01757, Acyl_transf_3, Acyltransferase family. This family includes a range of acyltransferase enzymes. This domain is found in many as yet uncharacterized C. elegans proteins and it is approximately 300 amino acids long.	1.19725e-10
CP031165.1\|AXV07318.1\|3043462_3044908_+\|Acetyl-coenzyme-A-carboxyl-transferase-alpha-chain	gnl\|CDD\|227136	COG4799, COG4799, Acetyl-CoA carboxylase, carboxyltransferase component (subunits alpha and beta) [Lipid metabolism].	0

>CP031165.1|AXV07325.1|3051811_3053455_-|Peptide-chain-release-factor-3
MSSTPAPSASIATAAFTDAVGRRRTFAIISHPDAGKTTLTEKFLLYAGAVGEAGAVKSRRVARAARSDWMKLEQERGISVSSTVLHFAYGDWRFNLLDTPGHADFSEDTYRTLCAADAAVMVLDIAKGLEPQTLKLFQVCRDRGLPIVTFVNKCDRPGLPPLGLLDEITEQIGLQPVPITWPVADGSDFAGIVDRRTDELVRYDRTAHGARKGQEVVEPWATADPQGCPPDRWDAAKEELELLDMEERVLDQDAFLGGTQTPVFFGSALQNFGVRLLLEGFAELAPPPSASPVDEPADAGARPVAAPFAGQVFKVQANMNPRHRDRMAFLRVNSGTFERGMSATLARTGRTYQLKYAHQLFAADRNTVDLAVAGDIVGLVNAADLVPGDTLYTDDAVTFPPIPTFAPEKFVSVRTTDTKRYKQFRKGLVQLDEEGVIHVLRRPEFGDQEPILAGVGQLQFEVAEHRFEHEFGCPVRMQPLQWEVARRIDASAVDALRGQFKTMVVEDSQGNHMALFASSVALDKAERDHPDIAFEPLGTGLARRVAA
>CP031165.1|AXV07324.1|3050280_3051804_-|Exoenzymes-regulatory-protein-AepA-in-lipid-linked-oligosaccharide-synthesis-cluster
MTEPGVGERVLWVGRGLAAVGGIDPTHRAVLVDGDQIAWTGSDPADAPAHDRVEDLGAVWLTPGFVDAHVHATATGLERVGVALAGARSLEDALARVRAHVERVDPAVVHGTGWDDQSWPEQRPPTADELFDAAGGRPTVLFRVDGHSCVVDRGLLARLDLGAVGQHVMRDIDGLPTGWLLEEAVAVAQGALVGLLGPAAIDRARQETCRAALALGITSIHEMGIPELSDITDALAWATGPWPLEVHAYWADLAWQSGGPLRPGGDLFLDGSIGSCTAAASAPYLANDGVRINGELFHDDEAVTDFFVRATHAGLGAGVHAIGDEATGQAVRALVRAAEVCGVDAVRTARHRIEHLELVSRADVTTLGRLGVVASVQPAFDATWNGPAGLYEHRFGRDRADTTNPFSWLAADGVAMCFSSDSTVTPMDPWSGIRAAQHHHGGLAIDRRTALEAATIGGHVAVGREDLVGALLPGRRADIVAWPGDPLTSDAPWDWTPTAVLVAGHPT
>CP031165.1|AXV07323.1|3048695_3050234_-|Cyclohexanone-monooxygenase
MLSLLLAKVSTPRPTRTLRVVIVGAGFSGMAMALAMKRDGHADEMVIIDAAEDLGGTWRDNTYPGCACDVPSPVYSLRGQPNDWPRFFSEQPDILDYMHRVADHHDLRRHMRFGTEIIRQEWDEARACWLLTTAAGETMEADVVVNGVGPLTRAVIPDIPGRDDFTGPAFHSAHWRDDVDLEGARVGIIGTGASAVQIVPSIVDEVGAMTVFQRTPGWVLPKLDREFSGLERLLLRRVPGAHRVLREVTNLILEHGVWRMLERNPRAAARLRSAGTWNIHRAVEDPDLREKLTPTIEPGCKRLLLSNTYYPALARDHVEVATEGIERITPSGVRLVDGTEVALDVIIWGTGFDAHHFWAPMEVIGRDGQDLHDAWSSHAAAYNSLAAPGFPNTFFLLGPNSGTGHNSVVLMAEAQADYVVQALEHLRAGRADWLEPTQQAADAYAAEMAERHADLVWASGCGSWYLNEDGVNDTLYPGRVGHYQRRVSTFDPESWSFGRRRVAPADAEPAIA
>CP031165.1|AXV07322.1|3047287_3048625_-|hypothetical-protein
MRSLVVPALVAVVVAFGGVAAETDGPRNALDGTVLLRPTTEGSSDEFQAPEGQRYHVDTPHFRIHFTDTGPDAATIAFVKDTATVLEEVWVAEVERLGWPEPLPDEGLGGTDRHGQDLVDVYLVDLDDGPYGYVAADEENPCVLCRSVHGFLVLENDYIGYEPNPPDALRSTAAHEFAHLIHMRMAWDGEPWAYEATAVWMEQAVYPDADARTAYLQDFAARPELPLSDFSLGGGGFDRAYGAYVWNLWLAERYGDDVIRQVWQAASDADSHLLGGYATVLAERGTSLDEEMVAFVAATAAWEVAGFPGEPLPYPTISRAGTLASGEVTEVAVDHAAAHVVDLEGVGDAVTVTVRGPRHVAGGVAVVATGEGRVVQAIDGTLFDGQATVTLVGLADAGRVSLVVVNADAALARPKRAGDDRASYLNDEVVWVVGVDVDPGAPQKR
>CP031165.1|AXV07321.1|3046627_3047266_+|Leucyl/phenylalanyl-tRNA--protein-transferase
MSAMFPDPRQAPADAPLAIGEDFRPSTLVEAYRNGIFPWPDGGGEVFWWSPDPRAVFVVGSVRRSRSLRQVIRRDDLDVTFDTAFPAVMAACADRAEEGTWITQRMQAAYESLHRMGHAHSVEVWRDGVLVGGLYGIAVGGVFTGESMFHRVSNASKVALVALDDHLLDRGFSLIDAQLHTDHLESMGARMVDREAFLDVLHAVRDAPITFL
>CP031165.1|AXV07320.1|3045785_3046631_+|UPF0028-protein-YchK
MTTLGIVLGGGGARGLAHIGVLRALADVDVHPDVLVGVSMGAVVGATYAARSDWLSALQSLDRSALPGHENLVDAEGFDLLRAVVRSAVRMAPKVVSFGVNGYEDFGRRTMAELLGGTPDFADLRMPFAAVATDLAGGRRAVLDAGDVTDAVMASAALPVLTRPLELEQGRYLDGGFADPAPVDVARAMGADVVLMVHVGSAPVGLGEATVDGALKGVLRGLEIGVAEFVQSRLIQADVVVAPPFGAGVSWLSFDRADDLAQMGYDAMRGQLDAVLELLDG
>CP031165.1|AXV07319.1|3044946_3045744_+|Enoyl-[acyl-carrier-protein]-reductase-[NADH]
MTSQTTDLPQLLAGKRLLVTGVLTEASIAFATARMAQQLGAEIVLTGFGKGIRLTTRVAERLPSTPDVLEMDVTDIEQMGAVVAELGDRWGAVDGVVHAIGFAPASAIGGNFLETPWEDVATAVQVSTYSFASLARVMAPLLKAGGGGSYVGLDFDATVAWPSYDWMGVAKAGLESACRYTARELGAQGTRVNLVAAGPLKTMAARQIEGFKSFEDTWGERAPLGWDITDTEPVARVVCSLLGDWMPGVTGEIVHCDGGVHAIGA
>CP031165.1|AXV07318.1|3043462_3044908_+|Acetyl-coenzyme-A-carboxyl-transferase-alpha-chain
MTDTQAPVQRPDARGRIDTLADDGSFVEFGSQARHHVTAFGLADKRPDGDGVVTGTVTVDGRPVALFAQDPTALGGSLGEVHAQKIAMVQDKASRGRIPVVGLLDSGGARIQEGVAALDGYAHIFHRNVRSSGRVPQISVVLGPCAGGAVYSPALTDVVIMARDRAHMFVTGPKVVKAVTFEDVSLADLGGADVHSTTSGVAHLVADDAEGALELTRRVLSYLPSSAWEEPPLAAPVPPEAMPEIPTDHRQPYDVRDVIRGIVDGGSMLELSEAFARNIVTSFARMDGRPVGVVANQPSVLAGCLDIAASEKAARFVRLCDAFGLPLVVLVDVPGFLPGTGQESAGIIRKGAKLLYAFSEATVPRATVILRKAYGGAYIVMNSRNIGADAVYSWPGAEVAVMGAEGAVDVLYRRPIAEDPASRPEYLAKYKAEALRPDLPNEILSVDETIDPGDTRRVLLGTLNAVRGSLEPGFRHDNLPQ
>CP031165.1|AXV07317.1|3042202_3043417_+|3-oxoacyl-[acyl-carrier-protein]-synthase,-KASII
MSTPVAITGIGLVTPGGIGAAASWEAVLRGESTATPDPVLEGMDVDFSCRIPDFDANALLGRRARKLDRFVQLALVAAREAIADADLDHETWDGPRVGVVLGCGMGGAPTWEEQHGVLMERGPNRVSPHLIPRMIPNMAAGHIAMDFGAHGPNLATATACASGATAIGYALDLLRVGRCDIVIAGGTEAGITPLSIAGFNNMTALSTRRDDPTAASRPFDAGRDGFVAAEAAGVLVLERVADADARGVRTYAKLAGYGASADGHHVTAPDPQGAGGEMAVRAALADAGLEPGDIDHVNAHGTSTPLNDVSEARMIARVLGDRPAVTSTKGVTGHALGGAGAIEAAFSALTLHHQVIPPTANLDSQDPEIQIDVVSKAPRETKVEAVISDSFGFGGQNAVLAFTA
>CP031165.1|AXV07316.1|3041895_3042132_+|Acyl-carrier-protein
MSVYTKIVALLDDKFGIAADEVTETTTFEELDLDSLDLVEFSMAAEDELGVKIEDEEAAELKTVGDAVKLLESKGASV
>CP031165.1|AXV07326.1|3053801_3054956_-|transmembrane-efflux-protein
MFGRVADIFGLRRPLVVGVLVMALGAAIAASAPSLPVLLGGRVLQGIGSGAVPVLANGIVAARWTGPARSAVFGSLFAVVSAVSGAGPIIGGGVETLLGWRWVIAIPVVAVLLIRPIVPLAPDTVRGGSFDARGAALVSALVSGVMLLLQAPTAGAAAGMVGACLLLVSLPLLWVHTRRAADGFLPHAVIGNPAIRACSIGGLTLLGGYFAALLAVPSLLAETQGWSSLGIGLAMLPAAAAGAVGSRVVGRLLAGGGHFRTASAVAAGSVATLLLAGFGGGSPWLLVLGVAGASIGFSGGSVALNDRVTLAADDSTLGVALGMVNMVQFVGGAIGTALLGGLSGLVPLHTALGLAAVLPTIGLAVLVRAARRDATDPSPAPAST
>CP031165.1|AXV07327.1|3055238_3056147_+|hypothetical-protein
MTAVHEASGLDRPTRPLGRVVVAAVGVFVLLRLLLPAGDGPDVVALPAEDSVEAAQLSDGTPVWIVRGSGEDIGVIQALAPETVSGVGELVAWCPAGDRFVAGHHGRSFAPDGRRYTGASPSGLPTDHDVPPADLVTHTWTILEGSSDVGDPLRVGPAEPVNHPTELLRPTLRGPLDGLGPPAGCRMDPVVDVPVPSGPAPLDHTAFLAPLQTARDGWQIVEGNVLVQPDGRAIWCQGTAASGPPGCRPDLSVDVDLGVDQRDTRGVSTVLDGPMAVRLDGGRVVQIAVLFGTRWRGGPLRA
>CP031165.1|AXV07328.1|3056150_3056645_-|Inorganic-pyrophosphatase
MMLAMTVDVFVEIPAGSRNKYEWDHEIGGFRLDRMLFSAVHYPGDYGFVPNTLSGDGDPLDALVLLGVPTFPGCTITSRIVGVFDMADDKGEDAKLITVAEADPRWQHVRDLVDLPKHLLDEVEHFFSIYKDLEGKSVRIDGFRDRAAALEQLAEDTERFTATG
>CP031165.1|AXV07329.1|3056672_3060461_-|ATP-dependent-helicase-hrpA
MTSTATGARGGPAGDRTPSIPTPSRPPELPITDRADEIVAAIRDHQVVVVAGETGSGKSTQLPKLCIEAGRGTNGLIGHTQPRRIAARAVAERVAEELNSRVGDLVGYAVRFTDTVSKRSVIKVMTDGILLNELQRDRQLRAYDTIIIDEAHERGLNIDFVLGYLAQLLPKRPDLKLIITSATIDTERFAAHFATDGVPAPIIEVSGRTYPVDVRYRPLEHADSDGNVAELDLVDGIVEAVEELVDQGPGDILVFASGERDIRDAADALGKAKLKGTEILPLYARLSAAEQHRVFSGHKGRRIVIATNIAETSLTVPGIRYVVDPGLARMSRYSRKTKVQRLPIEKISQASANQRSGRCGRLGPGVAIRLYAEEDFEARPAFTEPEILRTNLASVILRMTAIGLGDVDAFPFLEAPDRRQVADGVALLEELGAIVPDASAPGGRALTEVGTRLARLPVDPRLARMVLAAEEEGCVHEVMVIASGLSIQDPRERPQDKAHTAEQYHARFVEPGSDFLTLLNLWDHLRDQQHQLSGNQFRKRCRQEFLHWLRVREWQDVYSQLRRIVKDLGIAISKDPDNHDGIHRSMLAGLLSNVGVRDGDSREYLGTRSTRFVLGRRSALADHPPGWVVAAELVETNRLWASMASAIRPRWIEELAGDLVTRSHSDPEWSRNRAAATTLEKVVFRGLPIVQGRRINLGRIDRAQARAMFIEHALVNGDWDHSHRFLAANADTVARVRELEARLRRPGLLAPEDVLADHYDAHVGADVVNGASFDKWWRGVSRDRPHLLDVTVDQLLAGGHDSLADLTHYPDTWTVGGNDLSLDYAYDPEDPQADGVTVDIPLEMLPRIQPGHFDWQVPGLRHELIVALIRALPKSLRRALVPAPDTATRALQRIGPDDGPLLPALARELTRLSGVTITPQDWAGARLPPHLRMRYRIVGDKGPLASGTDLSALKEGVATHLRSAVRKAAPFPEHRGLTDWTFGDLPRVVSNRAGDVEVRAYPTLVDEGTTAGVRSVTTEAEQARAMAAGTRRLLRLALPTMVRVVAGQLDQQQKLQLTMAPHPDVPAVIEDCLDCVIDAIVEDAGGPAWTAADFAELRKDVRERAPRLVVVTARATAHIVQRAGTVRERLRQPLPPSFDDAKRDVAQQLGRMVYPGFVARTGGSRLPHLPRYLQGMVVRLDTMGRNPDRDREGMALVRDLEEELRLLVDTRGPSLDPIAAQSVRWQLEELRISLFAQQVGTAERISEARVRQRLLDLRTGRA
>CP031165.1|AXV07330.1|3060630_3062235_+|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)
MRARVLVVDDDVAVRTLLSVVLDDDSWDVVVAGTVEEALALVHDGGITVVVLDRHLVDADGIELLEDLGQASETGTIPVILISARADHDSRVAGLDAGALDFVDKEMTPVELKARVRSHVNHAGRLAALVADRARDQDLLIDASAALVRATTAIDVARTATSRALGWPDVDLAVVVGLVGPGSGRVIALSGSTVGVSLSSGATVPPEADRALRAQAEAGPWVEPASGMALSSIIGGAPSLVCAAPLVHGGRTVAVLGTASLRGTRERSRILSGTAGLARAAASRFGELLATEVRTRHDLEALEAAVAGNGVASVFQPVARAGSLRVEGFEALTRFVDGTPPEPRFRSAGLLGVRVELELAAMTQQLRAAEALPTASWVALNLSPSVMLDRRLPAVLARTDRQVVLELTEHDPIEDYAVLLRALATLPGSPKLSIDDAGSGYACLAHVLALEPDFVKLDKAWVREVDTDGARQALISGVRGFAEELGAQVIAEGVERAEELAVLEDLGVAYVQGHLLGEPRSAAEAPRTTGPGLP
>CP031165.1|AXV07331.1|3062315_3063740_+|hypothetical-protein
MRQLSGLDAMFLSLERPNTPLHVGSVVFVDPTTAAEGFTHETVMDVYRNRLHLLPPFRWRLVTTPMGLDHPYWIDDPEFDLEYHVRRIAVPPPGDARTLADIVARIHARPLDRSRPLWETYVIEGMADGMVAIYSKNHHATIDGVSGVDILGVLFDLEPTPPVPGHREAMTGERPPSDAEMLLRSAQGLAKLPGRAGRMAVRAAGALPLLGRMAEQAAPSRMRSRMGEGLLGKPHLQAPPSPFNGTISPHRRWAYASMPLKDIKRLKDAYDCKVNDVVMALTAGALRRWLQRHDALGDQALQAMVPISMRTSAQKGDAGNQVNALIALLPTDVAGVEDRLRSAASSMDVAKGGNAVPASVLRDFTQFASPALAASAARTVARLGWADHMRTPFNVVVSNVPGPPVPLYLGGARMEGIFPVSAIYDGMGLNVTLFSYRDELQFGLVADREMVPDLWEMADDFTAEMAEMAALLDR
>CP031165.1|AXV07332.1|3063816_3064746_+|Exopolyphosphatase-related-protein
MSYRLVTRSDFDGLVCAALLEELGLIDDILFVHPKDMQDGVVEITDRDITTNLPWVEGAHLVFDHHLSETRRVGEQANHIIDPEAPSAARVVFDHYGGADAFPRISDDMMRAVDQADSAQYSLEEILHPTGWTLLNYLMDARTGLGRFRTFRISNYQLMMALIEACRELTIEEILELPDVAERVELYTEQAQAFAEQLRRCTTVRGEVAVLDLRQEETIHAGNRFMIYALFPETTVSVHVLWGKGQQNTVLAVGKSILNRTNDVSIGDLMLAHGGGGHRNAGTCQVAHGDAVATLDTVVDALNGAVVPA
>CP031165.1|AXV07333.1|3064868_3066266_+|putative-membrane-protein
MSTTSSLQPAATAATSTRPDGASHDADRTARLRWVDAVRAASLLVVVLGHYLIAVVVLRDDDVTVSALLDIAPWTHPVTWAVQVMACFFAVGAVVAAPRLADDLGSSTGTVSGSTFRSVWRAHVASRARQLVVPALPLLALWVLGGPAVAGLFGADLVGVASQAALVPLWFLAVYLLVQALLPMAVRVVQRHGALRPIVLLLAAAGAVDALHLAGVPFVGWLNFPIVWMIPSTLGVAVGLGSLDTVRLWRAGAAALVVALGLVALAGYPVPVVGVTDAARSNNSPPSLLLAVHGLAYACTALSVGPRLEAWLGRTATRRRALAVAGRWSMAVYLWHMTGLVALVALAVRVDLPVIDAVLAVEPLTTTWWLVHPVQMAAALVVTLVVIALVSRPSAWLLRRSAVHALPGTTRTVVATLLASGGIADVVLHGTADGRVWGPLALVVATVLLHDVRDETRSSRRRSRT
>CP031165.1|AXV07334.1|3066292_3067933_+|Carboxypeptidase-T-precursor
MHSFSRRSFLAGAAASSAATLLPATGAAALAGDLVSRASRTEPTALLRVRLTDAFREVMAGFDLTEHVHDGQVEVVAWPGDRARLRAAGISWEEVEGDLGARFVADRLAEAADGRARPQERTGYRVLDDYRADMDRLVELAPDLVRPLLLDSPLTHEGRAIHGLVIGADVAVADSDGRPQAMMCGLHHAREWPSGELTIMFAEALVEGWLDGDAEVTGLLEQLCVFVIPVSNPDGFVRSREAVPYVEEIAVVEGLTLLAQEGPYHRKNLLKHTALPGSFEPQQGVDINRNYPYMWGGVGASGTTTSQTHYGPGPGSEPEIEALTGLFRSTQILAAISNHTSGDLVLRPWGWTPAEPPDEAALAALGDDMAGPMGYTSGSWNEALYPGTGIIDDWMYGTLGTYCYTLEHGSSFHPVYGDNVPGYFADNWQAHLKLLRSAVDTAQHAVLVGTAAPGTVLTLAKDISIPLSRAADGATRVEEHLEATMVVGEDGSFAWHVNPSVGAETLESGGQPEHYVLTAQAPDGTVRTWSGVARRGDELEVLTAEG
>CP031165.1|AXV07335.1|3068013_3068466_+|Acyl-dehydratase
MPTTMTLTELAEAGETDLGTSDWLEVTQDMVNQFADATLDHQWIHIDVERAKDGPFGGPIAHGFLTLSFLPHLVGQILQVTEVSAGVNYGLDKLRFTSPVPVGGRVRANGRLLETQQKGQGIMARVEVTVEIEGSDRPALIATWLILRYP

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Crispr_ID: CP031165_17

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_17

3133201-3133299

Orphan

Consensus_repeat	Method
CGTGGTCTGGGCCCCGATCGCGCCGTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_17

>merge|CP031165|17|3133201-3133299|CRISPRCasFinder
CGTGGTCTGGGCCCCGATCGCGCCGTTCCCCACGCGTCCCGACCGATGGGATCGTGCCGGTCCCCACGTCGGCGTGGTCTGGGCCCCGATCGCGCCGTT

>CP031165|17|16|3133201-3133299|CRISPRCasFinder
CGTGGTCTGGGCCCCGATCGCGCCGTT	CCCCACGCGTCCCGACCGATGGGATCGTGCCGGTCCCCACGTCGG
CGTGGTCTGGGCCCCGATCGCGCCGTT

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV07394.1\|3139696_3140344_-\|NAD(P)HX-epimerase-/-NAD(P)HX-dehydratase	unknown	unknown	gnl\|CDD\|367695
CP031165.1\|AXV07388.1\|3132615_3132981_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|314732
CP031165.1\|AXV07382.1\|3127313_3127463_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07391.1\|3136028_3137267_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase,-archaeal-type	unknown	unknown	gnl\|CDD\|179745
CP031165.1\|AXV07387.1\|3132040_3132619_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226648
CP031165.1\|AXV07386.1\|3130780_3131884_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|367829
CP031165.1\|AXV07380.1\|3124206_3126045_+\|Serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
CP031165.1\|AXV07385.1\|3129527_3130769_+\|RecA-superfamily-ATPases-implicated-in-signal-transduction	unknown	unknown	gnl\|CDD\|379062
CP031165.1\|AXV07389.1\|3133431_3134229_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07397.1\|3142536_3143082_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07396.1\|3141640_3142492_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07381.1\|3126264_3127203_+\|Membrane-protein,-putative	unknown	unknown	gnl\|CDD\|377542
CP031165.1\|AXV07379.1\|3122710_3124084_-\|Succinate-semialdehyde-dehydrogenase-[NAD]	unknown	unknown	gnl\|CDD\|143418
CP031165.1\|AXV07383.1\|3127487_3128450_-\|Lipase	unknown	unknown	gnl\|CDD\|369561
CP031165.1\|AXV07395.1\|3140394_3141513_-\|RNA-polymerase-sigma-factor-RpoE	unknown	unknown	gnl\|CDD\|274357
CP031165.1\|AXV07384.1\|3128556_3129327_+\|Methionine-aminopeptidase	unknown	unknown	gnl\|CDD\|238519
CP031165.1\|AXV07390.1\|3134408_3136004_+\|X-Pro-dipeptidyl-peptidase-like	unknown	unknown	gnl\|CDD\|225487
CP031165.1\|AXV07398.1\|3143097_3143568_-\|DUF1794	unknown	unknown	gnl\|CDD\|378046
CP031165.1\|AXV07392.1\|3137337_3137934_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|197714
CP031165.1\|AXV07393.1\|3138072_3139581_-\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV07394.1\|3139696_3140344_-\|NAD(P)HX-epimerase-/-NAD(P)HX-dehydratase	gnl\|CDD\|367695	pfam03853, YjeF_N, YjeF-related protein N-terminus. YjeF-N domain is a novel version of the Rossmann fold with a set of catalytic residues and structural features that are different from the conventional dehydrogenases. YjeF-N domain is fused to Ribokinases in bacteria (YjeF), where they may be phosphatases, and to divergent Sm and the FDF domain in eukaryotes (Dcp3p and FLJ21128), where they may be involved in decapping and catalyze hydrolytic RNA-processing reactions.	1.72747e-39
CP031165.1\|AXV07388.1\|3132615_3132981_-\|hypothetical-protein	gnl\|CDD\|314732	pfam11903, ParD_like, ParD-like antitoxin of type II bacterial toxin-antitoxin system. ParD-like antitoxin is a family of archaeal and bacterial proteins of a type II bacterial toxin-antitoxin system. Many of the cognate toxins for these molecules fall into family ParE-like_toxin, pfam15781. Gene-pairs are expressed from the same operon, the toxin of the pair being expressed first, eg, for UniProtKB:Q3AQ93 and UniProtKB:Q3AQ94.	6.98655e-11
CP031165.1\|AXV07391.1\|3136028_3137267_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase,-archaeal-type	gnl\|CDD\|179745	PRK04135, PRK04135, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.	4.88925e-162
CP031165.1\|AXV07387.1\|3132040_3132619_-\|hypothetical-protein	gnl\|CDD\|226648	COG4185, COG4185, Uncharacterized protein conserved in bacteria [Function unknown].	2.03623e-57
CP031165.1\|AXV07386.1\|3130780_3131884_-\|hypothetical-protein	gnl\|CDD\|367829	pfam04122, CW_binding_2, Putative cell wall binding repeat 2. This repeat is found in multiple tandem copies in proteins including amidase enhancers and adhesins.	2.95402e-10
CP031165.1\|AXV07380.1\|3124206_3126045_+\|Serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.93253e-97
CP031165.1\|AXV07385.1\|3129527_3130769_+\|RecA-superfamily-ATPases-implicated-in-signal-transduction	gnl\|CDD\|379062	pfam13191, AAA_16, AAA ATPase domain. This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.	3.12033e-06
CP031165.1\|AXV07381.1\|3126264_3127203_+\|Membrane-protein,-putative	gnl\|CDD\|377542	pfam05661, DUF808, Protein of unknown function (DUF808). This family consists of several bacterial proteins of unknown function.	1.84759e-138
CP031165.1\|AXV07379.1\|3122710_3124084_-\|Succinate-semialdehyde-dehydrogenase-[NAD]	gnl\|CDD\|143418	cd07100, ALDH_SSADH1_GabD1, Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like. Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.	0
CP031165.1\|AXV07383.1\|3127487_3128450_-\|Lipase	gnl\|CDD\|369561	pfam07859, Abhydrolase_3, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	3.39736e-57
CP031165.1\|AXV07395.1\|3140394_3141513_-\|RNA-polymerase-sigma-factor-RpoE	gnl\|CDD\|274357	TIGR02937, RNA_polymerase_sigma_factor, RNA polymerase sigma factor, sigma-70 family. This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.	2.78364e-35
CP031165.1\|AXV07384.1\|3128556_3129327_+\|Methionine-aminopeptidase	gnl\|CDD\|238519	cd01086, MetAP1, Methionine Aminopeptidase 1. E.C. 3.4.11.18. Also known as methionyl aminopeptidase and Peptidase M. Catalyzes release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.	3.22451e-98
CP031165.1\|AXV07390.1\|3134408_3136004_+\|X-Pro-dipeptidyl-peptidase-like	gnl\|CDD\|225487	COG2936, COG2936, Predicted acyl esterases [General function prediction only].	4.63791e-61
CP031165.1\|AXV07398.1\|3143097_3143568_-\|DUF1794	gnl\|CDD\|378046	pfam08768, DUF1794, Domain of unknown function (DUF1794). This domain forms a beta barrel structure but the function is unknown. The GO annotation for this protein indicates that the protein has a function in nematode larval development and has a positive regulation on growth rate.	7.98751e-52
CP031165.1\|AXV07392.1\|3137337_3137934_-\|hypothetical-protein	gnl\|CDD\|197714	smart00420, HTH_DEOR, helix_turn_helix, Deoxyribose operon repressor.	0.00357981
CP031165.1\|AXV07393.1\|3138072_3139581_-\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	7.83638e-92

>CP031165.1|AXV07388.1|3132615_3132981_-|hypothetical-protein
MGTPVRIDDEVYAAARRVGAVASRSAAQQVDYWVRIGRAVSMAEAGVRNRIDDAIAGRTPLAGLTAEERLLANAEIDAAIEQAAVSTDYADRLAAEGITTVVMDEAGHLVTRFPDGTSTPA
>CP031165.1|AXV07387.1|3132040_3132619_-|hypothetical-protein
MSRLDLVVGPNGAGKSTFVRFTLAPMRPGVPFVNADVIAAERWPDDQQAHAYEAAAMASRIRETLIARGQPFIAETVFSHPSKLDLIERADAAGYDIRLHVVMVPPDLSVARVAHRVRAGGHDVPEDKIRQRHDRLWGLVAQAAHRVPIASFYANHRTGPDLVAVFHHGRPASATEWPTWTHPDLISGLAQN
>CP031165.1|AXV07386.1|3130780_3131884_-|hypothetical-protein
MSTTPRRLLGSAVSCALLTGLLASPASAQDARLASSLDPTIASVDLALEMFEPGSVDVLVLGRNDQFADNLGGSALAGQVGGPLLLTDGGPDAALRPEVLDAIGTLVPRTAGLNCDNEPADVYVLGGDNAVSSGAVEELVIDGYCVERLAGDSRVETSVAVAREMRERGAPRAFLLARADSFADSAAAGAYGARFGWPVLLTSQDALHPASGAYISEDQEPGVVLDVYVWILGGTAAVSQDVEDQVFQQVGPDRVSRVAGATRDETSALIADAFQAAQEEGNASLAVGLVNGFADDGWVYALIGGAISPVTNAPILYVQADGIGDPVARYLDVQKPSSILVLGPPERVSDATAEEARGIAGVAISKE
>CP031165.1|AXV07385.1|3129527_3130769_+|RecA-superfamily-ATPases-implicated-in-signal-transduction
MRSTLNNPFVPGSDTVPEVWAGRGEEISDFHRQVRPRRLAGAYERGRVLIGEPGIGKSVLASRIAAEAREAGDLVLPSLRIPRGGDPIALLAGVVADAVSAYSLGERVGSMATGLLDRITAIRAGVTVTLQGAPAGVPHRELTLALSALARTAMDDGRLLVVHIDEVQNVDRTEHMSQLLVALGDVMAETAEGTDAAGNPHERHLPVAVTLTGLWSFVDGATRAAGATFARRFKAYHLGPLEDVDIRTALAPFTSDGWPILTDDGPAVVTASADAVQMLLEAVCGDPFLFQLVGQAAWNASTGPVIDRADVAAGIREVATEMTHHAERTLERLPRAERDLLDALLSLPGEQRTLTAAGRELGKTPQQVATTAKRLEMRSIIRRGRPIAVTSRVTEALIGGRWPTAPDEDARGR
>CP031165.1|AXV07384.1|3128556_3129327_+|Methionine-aminopeptidase
MLEIMTSSEIARARDTGALVAEILQSAKARTTVGTNLLEIDEWARTMIVDAGAESCYVDYEPSFGRGPFGHYICTSVNDAVLHGLPHDYAVADGDLVTLDLAVSLAGVVADSAISFVVGETAPAGATPMIEATERALAAGIAAAGPGARIGDLSAAIGSVLTEAGYAINTEFGGHGVGSTMHQDPHVANSGRAGRGYKLRPGLLLALEPWVMADTDELVTDDDGWTLRSSTGCLTAHSEHTIAITDDGAEIMTLPR
>CP031165.1|AXV07383.1|3127487_3128450_-|Lipase
MTKDEMHADLRRWAAPLSILPAMMTNRRMVAINNAVADRLLVGRDLKGLDCRTVEVPSSGGTHRIRTRVYRPADHDGPLPVLVYVHGGGYITGNPEMSGTFIKRFVGTRPCMVVAPAYRRAHDAAFPAGFDDCWDVLTWVRDNAEVLGSNDRAVAVGGHSAGGGLTAALSLKARDTGAVDIGFQMPLYPMIDDTQPDDPSREVQAPVWNTDANRAGWAAYLADLRRMGEAIPPYAAPARATDLSGLPPTITFVGTAEPFHLETVAYVEGLRAAGVEVAFREYEGCFHAFEASVPRADVSRDAQDFTYATFGEFHDRYLTG
>CP031165.1|AXV07382.1|3127313_3127463_+|hypothetical-protein
MGRRDRVERGRGRSERRVPEISWDARAQLIWGQDLEIDNTVLARMTVTS
>CP031165.1|AXV07381.1|3126264_3127203_+|Membrane-protein,-putative
MAGGLVGLLDDVVTLAKLAATSLDDIGAAAGRATSKAAGVVIDDAAVTPQYVHGLAANRELPIIKKIAKGSFRNKLLFVVPVLLILSELLPVLLTPLLMLGGGYLCYEAVHKIWGVVAGHEGGHDSAEEMKSEDEVVSGAIRTDLILSAEIMTIALNEVADEPLVSRGLILVVVAIGITILIYGVVALLVRMDDVGLHLAETRQNGMARFGRGLVNAMPKILSALGIIGTAAMLWVGGHIVLIGLDELGLHGPYDLVHGWEEAIHDAVEGLGGFLAWLTNTAASAVLGLVVGAVLVAVLSLRPGADSGASAH
>CP031165.1|AXV07380.1|3124206_3126045_+|Serine/threonine-protein-kinase
MPPLETVVADRYRLIELIGRGGAGEVWRARDERLQRDVAVKRIRLAPLDGEADGQPTTSRAMREARAAARLSHPGVVTIYDVVTTDEETVANLVMELVDAPDLASVVQRDGTLSPERAAAIGGSLLEALTAGHGMGILHRDVKPSNVLLPAGGRPRLTDFGTATIAGEDRLTASGIVVGSPAYMSPEQALGEPVDPRTDLWSLGATLFHAVEGHPPFGAGSPIATARAVTADPPRPAERAGALAPLLAALLTKDPDGRPGVEEVRAALAGVAAGTSSPADIAPVPAGTMPVPADTMPVPADTMPVPADTVPMPAEGSGPLGAAVHHDPARRRRHLVVGGAMALVVVLGVVVIGLVGDGGGDPATSVTAPTAQPADPTEPGAVADAPAPTPIDEGTATAPPTPVPTSSAVATDLPAAEDARPDEDGDQNEENDGEDDDSDDDGDGEDGDDEDGDDEADGGAEFGDGTVPEGWQTHQPEGAPYTVAHPADWVVEPSGGTLTDITDPNGPAYLRLDWTDDPAPDPVADWEAYEQDFAAAHPGYERLRLEPTTFNGEPAAIWEYRYGGGNGTLHAYNLNVSGSDYGYALNFQTSESRWADDVALFEGFTASYAIGS
>CP031165.1|AXV07379.1|3122710_3124084_-|Succinate-semialdehyde-dehydrogenase-[NAD]
MPTSTTVNPATGEDIATYTHHTDDELTQLIDAADNAFDKWRRESFQTRANAIRTLGQLLRDNVDELSALMSEEMGKVIGQGPSEVELCAAICDYTADNGATMLADEDRELDGGRAIVTHQPVGVIYGIQPWNFPIYQVIRYSIPQIMAGNTVLLKHAQNVWGMAERLQELYEDAGLPKGVFTALKISHDQSDEVIANPKVRGVTLTGSDGAGRHVAAVAGKHLKKTVMELGSNDAYVVLSDADIERTVKTCVMGRIVNNGETCVAAKRFIVVDDVYEAFRDAFVERMSGVEMADPTDPKAKLGPMARTELRDTLHDQVTESVEKGATLLLGGEVPDRPGAWYPATVLEDVAPGQPAYDDELFGPAAALIRVKDDAEAMRVANDSRYGLGGGIFSADVDRAIELARTEFDTGMVNINGYNLAKPNLPFGGVKDSGYGREHGGFGIHEFVNTKAVMIVE
>CP031165.1|AXV07389.1|3133431_3134229_-|hypothetical-protein
MSRVLAILFGAALALGGCNSGPDTAGAVAAATAYVQALAATDYDTMASLSVGSANDAARYGQQVLLADPEAFSSRDLVVLEPLTVPDGGDGTYLDGELELSTKGISGAPLRINTITMLSTADGWKVDGYDRDGRSTAELFRNVSTGPHQLAFDGVDVASISATVLLTDVAEDVVLLPIGVTAGAQQVTIVPERSTFTLGGRQIQVTDIIGTATVESLHEQIMVLLARQAPTTTASDADAVLIGVEMDGTDVGPLNVELRTQPPSQ
>CP031165.1|AXV07390.1|3134408_3136004_+|X-Pro-dipeptidyl-peptidase-like
MQRRMFGSLLPRPAGQVLMRARRAATVRIRTDDGHELATDVHRPSTDTPVPTVLIRTSYGRNGLTGVPMVAQAKALATLGYAVVLQDVRGRFDSTGEFVPMVNEVADARATIDWVTDQSWSDGTIGAWGLSYLGGTAWAAAVAAPDRVKALSVGITHSAVGLPEASGLVFVDTGLRWLRSLDAMARTDESAARRLANLVRFRLPGASDDEAFSHLPLLELDELVLGTRSPIWRTWAEHPDASDPFWQPGDLRHGVADVAPTSHLTGWWDLFVDRHLDDIDRQAPAGRADRVVVGPWGHLDGAVQVRAFAEMRRHFDQHLRGIDRNGPAVELWIGGADRWWTGDRWPTTRTESIPFDLLRGPTHTLVFDPAAPTPKTGGRTLSIDAGPVDCTALADRRDVVTLTGPPLPHHLTVIGRPTVTVELDADTGHTDLWVRLAEVDIHGLARSVSDGFLRLRDLRGRHTAVVELHPVGHRFSAGHRLRVHVAGGAFPHHDRNLGLDGDRLHLVDHRPTTVRIHDGRIDLPVAGPMDT
>CP031165.1|AXV07391.1|3136028_3137267_-|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase,-archaeal-type
MIDFDRYTPLLQDGGRILLLVVDGLGGYPEADRGSELEDAHTPNLDALAARGITGLTEPAGPGITVGSGPGHLALFGYDPWRYDLGRGVLAAVGTGFPLQPGDVAARGNLAFLNDDSLVSDRRAGRISDDRAAPLTERVQQRLDADPPVAGVEVFLRHVSEHRVLLVLRGEGLDARLADMDPQDTGLAPLQARPLGSADARTASVVDAVDAAVRAALAEESDEASPDVALFRGFDGLREMPDFGERTGLRAAAIASYPMYRGVAQLVGMEVLHGPDGPPSSMADQIALARAARDTHDFLFVHYKYADAAGHDGNREAKVEALERLDVDLPALLEAADADVVVVSGDHASPAAVSGHSWHPVPTLLAGGSAGVDDVTTFGERACAGGLLGLRPTEHLLPLALGAAGRLAKYGA
>CP031165.1|AXV07392.1|3137337_3137934_-|hypothetical-protein
MEALQDPNTAVDWDEVEELAAQIAEATDPVRRVLLRAEWRRASDPATYMPDLEADYIAFAAQWAQANRVTGDDFFYEGVPLQVLREAGLGISEEARAYADGDDDMDVSDDAAPAGPAPAAAESDGDEPMFEEGSAMESVYSAIGNEPFTINDLVDRADASRSTVRAVLDKLEEAGKLEELPPLDTGTAGRAPKRYQLT
>CP031165.1|AXV07393.1|3138072_3139581_-|serine/threonine-protein-kinase
MNTESAVLADRYRLTDSIGRGGMADVYAAEDTSSGRMVAVKIMRVGEQADPDRFASEMRILDRLSHPAIVRLFDSGTTDDASPYFVMQLVDGESLSARLRAEGPLADEDAEEIGARVASALAHAHDTGVIHRDIKPANILIDTDGGAYLTDFGVARLADATLVTRAGTTIGTAAYLAPEQLQDSQVGPAADVYSFGLVLLESLTGTRAFRGTGVEAAMARLSRDPVVPDDLQGPWAPLLVAMTRRDPTQRPTAAEVELIIRAELPAPEVSAEEMASRAGGSRNTDEDPTAISQPFDGPSSGSGPWEPPSSDSAQSVAVVPPTPPPTPALGLPVAEASAHPTVPAPAPFLEDLPRRGMDAIRSRALLVGLLLGVVVVLGGFGVFRLLQPVDETDMVSGTDPVDEAARQVLAILDASERLRAADPSLQRELVSLADNIVESVNDDRWDSALLGVVAMTSTTRDAIDTLDIEPVALNGLLEALRDLTREIELLAGAEASGTDPPE
>CP031165.1|AXV07394.1|3139696_3140344_-|NAD(P)HX-epimerase-/-NAD(P)HX-dehydratase
MREVDRRMIEEVGIDLPRMMENAGRHLADVATTMFAPRHVVVLYGSGGNGGGALVAARHLVNRGVEVTLVPSSSALTPVPAVQHAILERMGVLESAGRTPPSCDLVIDGMVGYSLAGAPSGRVAELIGWAGAQKAPVLSLDVPTGFSASSGTTASPHITAAATVTLGLPKAGLVGNAATGRLYLADISVPPVVWADMALEVPRDLFGPGQIVQLV
>CP031165.1|AXV07395.1|3140394_3141513_-|RNA-polymerase-sigma-factor-RpoE
MTAVHPGQHTLPDDDSGLIEAHLVGIEGAFDELFRRYHHRLVTYLTHRVGDAATADDLAQESLIRAMHALERFDTSRPLWPWLRRIATNAAIDWSRSNSRSRMLVNTLSLEPPRTHDGPDFAERELMARAMDAVPDRQRHALEKCYVEGWRPVDVADQFGVGSNAFEQLLHRARRNLRRAYVRQDDGGDRAAGFIWLAMLASPFARAFNAVRRLGVAGPRVLEVAAASVAIGAVVAVGPTGTPAPRTVVDAPVERVDRTAVPADVQPIDLPAAAAGVAGTVDAVAAPAVSGPASAVPSGAGRPAPVAPDAPPADTAAQQPAAPSFDDNPLDRDAEPTSPAAPDGPQSFPELIGGCGSAVRGALCTTVGVVLE
>CP031165.1|AXV07396.1|3141640_3142492_+|hypothetical-protein
MSQDVNRDRLERIRSDLAALRAAADIEDAAPPAPAPVNGATRDGEPVEPATVEAPATDAPPEAAHRPATTTTTAPTGLLGRPRIPRPPRRNPFRRRARRPSKRLAVPAPIPVRRRPVWLAGPRWPVADALSSTVIVLVMVPVVAQMANRLWVATNETSVLLGADPSRADALRAAAGVAGGGITVALAVFALAVVRGRPGYIAGGVAVLLLFVAFPYVAYTANAGIVSAPIPTLGEMVVPRGWERANQLGAVFLLAAGVLTAALVDLAYRSVLALRDGVQQTRS
>CP031165.1|AXV07397.1|3142536_3143082_-|hypothetical-protein
MVIAVALATAVFLAGFVAGRASLPSASEDRVVDPDAAAMRPGSEGDPIEIGSPAAVGPWEVEVTGFDPDAIDRVLAANQFNVEPAKGQTYVTVEVSLTRRAAGPGILRGSVAPALVTPSGRSFALGSDCGVISAPVDAERLLAQGEVLDGEWCWRVPVAEVDKVALRVGGTGGGAVWFAVR
>CP031165.1|AXV07398.1|3143097_3143568_-|DUF1794
MTHPDIAPLEFLVGTWRGRGRGDYPTIDGFDYVEEISFSTMPKPFLAYQQRTTRADDGQPLHAETGYVRPVQDGPELVICQPTGIVEAHRGRLEEQQIIWDSHRVAMTPTAESHRVTKVRRELRVEGDELRYELHMGAVGQPLQLHLRATLHRVEA

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Crispr_ID: CP031165_18

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_18

3575524-3575618

Orphan

Consensus_repeat	Method
CCGTCGCAGGAACCCGACACGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_18

>merge|CP031165|18|3575524-3575618|CRISPRCasFinder
CCGTCGCAGGAACCCGACACGCGGCCGGGGTGCCGCGCCGCGTGACCGGACGCGTGTCGGAAAGGGGGCCGCCCGTCGAAGGAACCCGACACGCG

>CP031165|18|17|3575524-3575618|CRISPRCasFinder
CCGTCGCAGGAACCCGACACGCG	GCCGGGGTGCCGCGCCGCGTGACCGGACGCGTGTCGGAAAGGGGGCCGC
CCGTCGAAGGAACCCGACACGCG

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV07782.1\|3564140_3565763_+\|N-methylhydantoinase-B	unknown	unknown	gnl\|CDD\|376810
CP031165.1\|AXV07799.1\|3585205_3586375_+\|L-rhamnose-isomerase	unknown	unknown	gnl\|CDD\|274239
CP031165.1\|AXV07791.1\|3576271_3577774_-\|putative-L-lactate-dehydrogenase,-Iron-sulfur-cluster-binding-subunit-YkgF	unknown	unknown	gnl\|CDD\|224062
CP031165.1\|AXV07781.1\|3562165_3564148_+\|N-methylhydantoinase-A	unknown	unknown	gnl\|CDD\|223223
CP031165.1\|AXV07795.1\|3581351_3582410_+\|putative-L-rhamnose-ABC-transporter,-transmembrane-component-2	unknown	unknown	gnl\|CDD\|224093
CP031165.1\|AXV07797.1\|3583563_3584751_+\|putative-L-rhamnose-ABC-transporter,-substrate-binding-component	unknown	unknown	gnl\|CDD\|380655
CP031165.1\|AXV07784.1\|3567408_3568674_-\|putative-peptidase	unknown	unknown	gnl\|CDD\|366703
CP031165.1\|AXV07783.1\|3565759_3567178_+\|Cell-envelope-associated-transcriptional-attenuator-LytR-CpsA-Psr,-subfamily-A1	unknown	unknown	gnl\|CDD\|224235
CP031165.1\|AXV07790.1\|3575621_3576275_-\|putative-L-lactate-dehydrogenase,-hypothetical-protein-subunit-YkgG	unknown	unknown	gnl\|CDD\|224473
CP031165.1\|AXV07788.1\|3573845_3574997_-\|Sulfur-carrier-protein-adenylyltransferase-ThiF	unknown	unknown	gnl\|CDD\|181156
CP031165.1\|AXV07785.1\|3568902_3570897_+\|Vancomycin-B-type-resistance-protein-VanW	unknown	unknown	gnl\|CDD\|377286
CP031165.1\|AXV07786.1\|3571147_3572515_+\|Magnesium-and-cobalt-efflux-protein-CorC	unknown	unknown	gnl\|CDD\|224173
CP031165.1\|AXV07796.1\|3582399_3583446_+\|putative-L-rhamnose-ABC-transporter,-transmembrane-component-1	unknown	unknown	gnl\|CDD\|119321
CP031165.1\|AXV07789.1\|3575065_3575473_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07793.1\|3578516_3579623_-\|Transcriptional-regulator-of-rhamnose-utilization,-LacI-family	unknown	unknown	gnl\|CDD\|224525
CP031165.1\|AXV07792.1\|3577770_3578520_-\|putative-L-lactate-dehydrogenase,-Fe-S-oxidoreductase-subunit-YkgE	unknown	unknown	gnl\|CDD\|223325
CP031165.1\|AXV07794.1\|3579852_3581355_+\|putative-L-rhamnose-ABC-transporter,-ATP-binding-component	unknown	unknown	gnl\|CDD\|224053
CP031165.1\|AXV07780.1\|3561550_3562123_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07787.1\|3572511_3573837_+\|Magnesium-and-cobalt-efflux-protein-CorC	unknown	unknown	gnl\|CDD\|224173
CP031165.1\|AXV07798.1\|3584822_3585209_+\|L-rhamnose-mutarotase	unknown	unknown	gnl\|CDD\|377501

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV07782.1\|3564140_3565763_+\|N-methylhydantoinase-B	gnl\|CDD\|376810	pfam02538, Hydantoinase_B, Hydantoinase B/oxoprolinase. This family includes N-methylhydaintoinase B which converts hydantoin to N-carbamyl-amino acids, and 5-oxoprolinase EC:3.5.2.9 which catalyzes the formation of L-glutamate from 5-oxo-L-proline. These enzymes are part of the oxoprolinase family and are related to pfam01968.	0
CP031165.1\|AXV07799.1\|3585205_3586375_+\|L-rhamnose-isomerase	gnl\|CDD\|274239	TIGR02635, putative_xylose_isomerase, L-rhamnose isomerase, Streptomyces subtype. This clade of sequences is closely related to the L-rhamnose isomerases found in Pseudomonas stutzeri and in a number of the Rhizobiales (TIGR02629). The genes of the family represented here are found in similar genomic contexts which contain genes apparently involved in rhamnose catabolism such as rhamnulose-1-phosphate aldolase (TIGR02632), sugar kinases, and sugar transporters. [Energy metabolism, Sugars].	0
CP031165.1\|AXV07792.1\|3577770_3578520_-\|putative-L-lactate-dehydrogenase,-Fe-S-oxidoreductase-subunit-YkgE	gnl\|CDD\|223325	COG0247, GlpC, Fe-S oxidoreductase [Energy production and conversion].	2.25991e-53
CP031165.1\|AXV07781.1\|3562165_3564148_+\|N-methylhydantoinase-A	gnl\|CDD\|223223	COG0145, HyuA, N-methylhydantoinase A/acetone carboxylase, beta subunit [Amino acid transport and metabolism / Secondary metabolites biosynthesis, transport, and catabolism].	1.10002e-159
CP031165.1\|AXV07795.1\|3581351_3582410_+\|putative-L-rhamnose-ABC-transporter,-transmembrane-component-2	gnl\|CDD\|224093	COG1172, AraH, Ribose/xylose/arabinose/galactoside ABC-type transport systems, permease components [Carbohydrate transport and metabolism].	7.70576e-75
CP031165.1\|AXV07797.1\|3583563_3584751_+\|putative-L-rhamnose-ABC-transporter,-substrate-binding-component	gnl\|CDD\|380655	cd20000, PBP1_ABC_rhamnose, rhamnose ABC transporter substrate-binding protein. Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.	2.19176e-155
CP031165.1\|AXV07784.1\|3567408_3568674_-\|putative-peptidase	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	2.39411e-40
CP031165.1\|AXV07783.1\|3565759_3567178_+\|Cell-envelope-associated-transcriptional-attenuator-LytR-CpsA-Psr,-subfamily-A1	gnl\|CDD\|224235	COG1316, LytR, Transcriptional regulator [Transcription].	1.81896e-49
CP031165.1\|AXV07790.1\|3575621_3576275_-\|putative-L-lactate-dehydrogenase,-hypothetical-protein-subunit-YkgG	gnl\|CDD\|224473	COG1556, COG1556, Uncharacterized conserved protein [Function unknown].	6.52889e-29
CP031165.1\|AXV07788.1\|3573845_3574997_-\|Sulfur-carrier-protein-adenylyltransferase-ThiF	gnl\|CDD\|181156	PRK07878, PRK07878, molybdopterin biosynthesis-like protein MoeZ; Validated.	0
CP031165.1\|AXV07785.1\|3568902_3570897_+\|Vancomycin-B-type-resistance-protein-VanW	gnl\|CDD\|377286	pfam04294, VanW, VanW like protein. Family members include vancomycin resistance protein W (VanW). Genes encoding members of this family have been found in vancomycin resistance gene clusters vanB and vanG. The function of VanW is unknown.	3.26803e-54
CP031165.1\|AXV07786.1\|3571147_3572515_+\|Magnesium-and-cobalt-efflux-protein-CorC	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	5.56868e-120
CP031165.1\|AXV07796.1\|3582399_3583446_+\|putative-L-rhamnose-ABC-transporter,-transmembrane-component-1	gnl\|CDD\|119321	cd06579, TM_PBP1_transp_AraH_like, Transmembrane subunit (TM) of Escherichia coli AraH and related proteins. E. coli AraH is the TM of a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of the monosaccharide arabinose. This group also contains E. coli RbsC, AlsC, and MglC, which are TMs of other monosaccharide transporters, the ribose transporter, the D-allose transporter and the galactose transporter, respectively. The D-allose transporter may also be involved in low affinity ribose transport. These transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Proteins in this subgroup have a single TM which homodimerizes to generate the transmembrane pore.	7.13575e-67
CP031165.1\|AXV07793.1\|3578516_3579623_-\|Transcriptional-regulator-of-rhamnose-utilization,-LacI-family	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	1.5443e-102
CP031165.1\|AXV07794.1\|3579852_3581355_+\|putative-L-rhamnose-ABC-transporter,-ATP-binding-component	gnl\|CDD\|224053	COG1129, MglA, ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism].	0
CP031165.1\|AXV07787.1\|3572511_3573837_+\|Magnesium-and-cobalt-efflux-protein-CorC	gnl\|CDD\|224173	COG1253, TlyC, Hemolysins and related proteins containing CBS domains [General function prediction only].	4.0456e-120
CP031165.1\|AXV07791.1\|3576271_3577774_-\|putative-L-lactate-dehydrogenase,-Iron-sulfur-cluster-binding-subunit-YkgF	gnl\|CDD\|224062	COG1139, COG1139, Uncharacterized conserved protein containing a ferredoxin-like domain [Energy production and conversion].	0
CP031165.1\|AXV07798.1\|3584822_3585209_+\|L-rhamnose-mutarotase	gnl\|CDD\|377501	pfam05336, rhaM, L-rhamnose mutarotase. This family contains L-rhamnose mutarotase which is a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer. In Escherichia coli this enzyme is the product of the rhaM gene (also known as yiiL). The tertiary structure has been solved, in complex with L-rhamnose, and the catalytic mechanism determined. His22 is the proton donor. The enzyme naturally exists as a dimer.	2.17245e-33

>CP031165.1|AXV07789.1|3575065_3575473_-|hypothetical-protein
MTCMTADARPNDHAVIAHVGDAATAEAAVADLAESGVDRDAIAHGTGESFAARLEAGDEDSHPAGRLVKFLLSLGQEREELMRLGEEARSGRHAIVVNDVEESHRDSIADVLARHDARDIVWFGDWQTEDLSIQR
>CP031165.1|AXV07788.1|3573845_3574997_-|Sulfur-carrier-protein-adenylyltransferase-ThiF
MEPLIAEPAPLTNDEIRRYSRHLIMPNIGMDGQGRLKAAKVLLVGTGGLGSPAAMYLAAAGVGEIGLVDYDTVDESNLHRQVIHGTKDIGKRKTESARETILDINPTVKVNIHETLLRSENALEIIEPYDLVIDGTDNFPTRYLVNDACAILGKPNVYGSIFRFEGQLSVFWNEVGPNYRDLFPEPPPPGMVPSCAEGGVFGVLCASIGAGQVTEAIKLITGIGEPLIGKMKLYDALDHDWRTITVRKDPDAKPITELIDYEEFCGVPANDHVSDDVDSDFDLQITPVEFEKIRDEVTLIDVRDPHEYEISRIEGSTLIPLGDLPSRMHELDSSDEIVLQCKSGQRSMQALNILRDAGFRKLRNLQGGINGYSRQVDSSIPTY
>CP031165.1|AXV07787.1|3572511_3573837_+|Magnesium-and-cobalt-efflux-protein-CorC
MTGPTGAIVAIVLLAVNGAFVAAEFALLAVRRSRIQQLADADDARATAALKGLKELSVTLAGAQLGITMASLGLGYVAEPLVAGFFEHLLAESTPLPEPAAVTIGFAIGLSIVVFLHMVVGEMAPKSWAIADAERSSLLLARPFLLFVSIFRPVILLLNGMANALVRAVGVEPQEELAVAHAPSDLLMVLRESYNEGTIAGEDHELLSRALELSGLDAESIMIPRREVVAVAATATAAEVMAVASATGRSRLPVHGGDLDQVLGVLTVKDLVLRPDRFGPETPAARLARPAMVVPESRPIEDLLLDMRQQRQHIAMVADEYGSVSGLVSLEDVIEELIGEFDDETDRLSRRLRRRPDGRLVVAGNLRAHELAEQTGLELPDGPWETLAGFIEHRTGNVPQVGATASLGGVRLTVTTVDRFRIIEVELRPAKPTGATTPERQ
>CP031165.1|AXV07786.1|3571147_3572515_+|Magnesium-and-cobalt-efflux-protein-CorC
MSTVLGLLAVLLLIFGNAWFVAAEFALVTARRGRLEAAHEGGDRRAGRALQLLGRLSFALSGAQLGITVTSLAVGFIAEPVFTALFEPLLSPLGIRPALVPVIAVSLGLVVSTAGQMVLGELGPKNLAIAKAEDVAKSLAGGQILYLRLFGPIIHLFDSAANRLLRLVGIEPSEEIDNSVTVEELEHIITSSSASGTLGEGVSALLQRSIEFRDLHADDAMRPRADVVSISGDATCEELTALGVRTGHSRFPVTGPEGLDDLLGVVNIKDLLDVPVAERAITPVRTLAEPELAVPESASLRDVLLLLRDTHTQLAVVVDEFGGTEGIVTLEDIVEELVGDIRDEHDRAERQAVLRADGSWRVPGSWRIDEVRRDTGIELPQGEHDTISGLLMATLSRVPVVGDTLRLDGITIEVLAVQRHVAQTVRLSTDPDHAPDGDEPPVPAPVHVHDKETER
>CP031165.1|AXV07785.1|3568902_3570897_+|Vancomycin-B-type-resistance-protein-VanW
MDTTQDAVDRGTGRRATSGPRRRPPQRGSSRSPVREAIATVVGLVVVLAVVFLGLRAARADTALPGLTVAGVDVGGQSSDAVTTAIAGLDDARRTRTITVTRGTDEVVSTAEELGYALDVEATVAAVMDRGRQANPLLAFRDQVRATFVPLTVPPIAAFDSIAFERWIDRIADDLALPPIEADLVITGTTVEVVQPQPGETIDVEALRSAALDALQDGGDATIEVPTVVTTPSTDPEAIADLAAAAELAISAPVTLIRGDVRLSLTGERIGALLQVRAEAVSEGGDADLELVIDPDRLLAMLPAEQFAALAQPPQDASIEVTGGQVVVTPSVDGFAFDAVAAAEQVLEVATTPGARSAELTGELTEPEVTTEDIEAMGIVEQVATFTTEHPCCQSRVTNIQRMADIVRGTIVMPGETFSLNGLVGPRTTDKGFVGGGAISGGEFVEQIGGGVSQFTTTMFNTIYFGGYDIVEFKPHSYYISRYPLGREATLNYDPPVDLKFTNDSPHAIWIDTTYTDTSITVSFWSTEYAEVTSTTGDRYGLREPREEREESDELPAGEERVVQSGRDGFSVDFTRTIAYVDGRTATETYTTVYLAEPRIVMVGTGEGQDDEEPTEEPTQPAPDPTEEPDPEPTAPAPAPTEEPAPAPAPTAAPEPAPSDGGGG
>CP031165.1|AXV07784.1|3567408_3568674_-|putative-peptidase
MILSSSIHSPLSRAVLLLLVLAMAIATSGPASATGSEESRISQTREELERVRGELNAARGEADDDMIALEDADAQLEAVFTAVETAQQAVGRQEDAVAEAERELAVAQGELVEQQQRMALRINRLYRQARPDPLITVLDASTVSDAVEQSAYITAIGRQDRALVEGLENAQSRVEGRQRALDEETVALDRVLVEQQALLVEVEEIRNDRELIAAASQDLVARLQSREEHLEEEAIELLREQAQAEARAVAEAAAKEAAEQLAAEVIADDEAEGEDDEAEIEEATAPPPAPAPVAAPSGGGGLQWPAGGTVTSGFGPRWGRNHNGIDIAAGSGAPIVAARGGTVTKAENWSGSGFGNVVIIAHGNGLTTLYAHMSSIAVSAGQSVGGGTYLGGMGCTGSCTGTHLHFEVWAGGTPVDPMGYL
>CP031165.1|AXV07783.1|3565759_3567178_+|Cell-envelope-associated-transcriptional-attenuator-LytR-CpsA-Psr,-subfamily-A1
MSQDDYDYDRTYGERWGGDGHRPDDFGPAMTGRHRRVSFTKALGGVFNIAFSALMIVLLALGGLAVYASSQIQREPVEGLVSGGPTLNVLVVGSDSRDGFTPEQLLELGTEAVDGRRTDTIFLLSIDGGRAAMLSFPRDLFVEQCDGVQGRVNAAFARGGPSCLVQTVSNASGIPIDHYVEVNLFGFVQIVDAVGGVPVFLDEPLQDQFAAVDLPAGCHVLDGTQAIGFVRARHVDSDLGRIARQQRFLRSLAQQVVSPSTLVNVPRLFRVAGSAGRTLIADEGLGLIELAQLARAARGLAGSGLATYTVPANAANIGGAAVLVPDPDAAGALYASFADGSVLSLNPGEDVQALQPGDVPVRVLNATGTEGLAATVRDFLTARGFDIVGIGNADPTDGTVVRYAGPNVAAAQLVAEQIPGATLQQDDSLTEVVLIVGSAIDVSAPPPPPMTEDPGAAEEVPVGAAAVPDECS
>CP031165.1|AXV07782.1|3564140_3565763_+|N-methylhydantoinase-B
MADPRPPADPARLQVTRHALDGVAEQMGVALERSAYSPNITERLDLSAAIFSPSGEMVAQAEHIPVHLGSMPASVDSILGAFDLSPGMTAVVNDPYRGGSHLPDITLVGAVGDREDGRSGQLIGYVANRAHHADIAGAAPGSMPADATDIAMEGLRIPPLLLVDDHGERTDVIEMLAANSRTPTERHGDLRAQFAANHAGAARLCEMAAERGRDGLLADMDALVDYAERRIRAALAEMPDGEWTFSDWLEVAADGSMDAAAQAVGLELHTTVAIRGDQLVVDLTRCPPQVPANVNAVRAVTESAALFVLRLVTDPDAPANAGTARAMTVQTTPGTIVDAVFPAPVATGNVETSQRLVDLLLGALAQAVPDRVPAASQGTMNNILIGSSGQGTPFAYYETIGGGEGGTPGRPGMDGVHTGMTNTRNTPVEALEVAYPLRVVRSELRSGTGGEGLHPGGDGIVREIEVLTDARVTVQTERRARGPWGLGGGRAGQPGRNTLIRPDGTTQALPAKVTLTVQAGDRIRLETPGGGGWGTQAAHQ
>CP031165.1|AXV07781.1|3562165_3564148_+|N-methylhydantoinase-A
MPQQSPPPSPTAPLVAGVDVGGTFTDAVVLTADGPRLAKVPTTPSDQGEGLVAAVEAAGQRPTVDLQALAHGTTTATNAVLERTLDRAVLLVTEGFADVLTIARQNRPSLYDLSAVRPAPTIPRDMVVPVPERITVDGEVLTPLTEAAIEAVVARTVALQPDAVAICLLFGWADPSHEHRLATAVAAALPDVHITVSADLVGSIREYERASTCALNAAVGPTMGRYLQRLSDRLPDTDVTVMTSGGGTADLDRMVAEPVHTLLSGPAGGVVAAAAAARSAGFDDAIAFDMGGTSTDVCLIRGGEPVVSLAGTIDGLPIGTSTIGIHTVGAGGGSIAALDAGGALRVGPRSAGSDPGPACYGRGGTQPTVTDAHAVLGHLDSLAGGTMTADVAAAERAIARIEGVTATGILDVVRAAMARALRRVSTEAGVDPDSLALVAYGGAGPLHASALARMLGCRATVLAPAPGVLSAVGLLTAPQRREWSRTVMVPPERLRDTLELLPLDESVTGSIPDAAATVRTVADLRYVGQAHELRIDVDPDAGEDLGTLAAFHRRHEQVYGYALHDADVVVVTVRRISQRPALHTEAVTGWDLGPSTPTTTRTADLGDGPEAVSVVARGSLRPGDTVSGSAILVQPDSTGLLLHGDVGTVDDHLNLVIRHG
>CP031165.1|AXV07780.1|3561550_3562123_+|hypothetical-protein
MHVVTYTRGSSEDSRAYRIDRILDAQPDHEQYTSVTRFGDGQAGSADPRHPQRKAMLAACEGGQFDLLVVNTLWDLHAPGTDADVNTLVALLHRGDLDEIRFADGTSWVATDPATVAAERFLGDADEVVAAMEVLRQAAPDRFLDAAAELYRAVVGDAATRRARGADADTAADLVVEHDSDSASTDSLRG
>CP031165.1|AXV07790.1|3575621_3576275_-|putative-L-lactate-dehydrogenase,-hypothetical-protein-subunit-YkgG
MSLPSDPARTEVLARIVDALGPAPAAVDVPRDYDIDPPADVDLLERFVDRVEDYRATVHRVGSDDLAATIGRILDAAVSDRVARVVVAHDLDEAVLPEGVERHIDSPEVPLPVDGSGGLDAMDAVVTTSAAAIADTGTIVLDGGPGQGRRAITLVPDLHVCIVRAEDVHATVPLAVRALDATRPQTWISGPSATSDIELDRVEGVHGPRTLHVVLLT
>CP031165.1|AXV07791.1|3576271_3577774_-|putative-L-lactate-dehydrogenase,-Iron-sulfur-cluster-binding-subunit-YkgF
MTPQVPPGRTSLPVVSPRGVGQLRGAQSFPDAARGALADPQLRRNLGNATATIRAKREAVVGEVPDWQALRAAGAAIKDDTLRRLPELLVRLEERVTAAGGTVHWARDAAEANAIVTRLVRATGADEVVKVKSMATQEIGLNEALAEAGIHALETDLAELIVQLADDRPSHILVPAIHRNRTEIRDIFLAHMADVDPDLTDEPRALAMAARRYLRRKFLTARVAVSGANFAVADTGTLSVVESEGNGRMCLTLPETLITVMGIEKLVPTWEDLEVFLQLLPRSATGERMNPYTSFWTGVHPGDGPQDVHLVLLDNGRTAVLADEYGRDALRCIRCSACLNVCPVYERTGGHAYGSVYPGPIGAVLSPQLTGVEDNASLPYASSLCGACFDACPVAIDIPSMLVHLREQHVEAQAAARTVPTVEAAAMKAAAWMMSDASRWSGAQRAARVGRLIGRDRGDGDRRIRTLPPPMNGWTATRDAPVPASQSFRDWWRGREEGTT
>CP031165.1|AXV07792.1|3577770_3578520_-|putative-L-lactate-dehydrogenase,-Fe-S-oxidoreductase-subunit-YkgE
MRIALFVTCLADTLFPDVGRAVVTVLERLGHEVVFPASQTCCGQAHTNTGYGPMALPLVRNHVEAFEDCDVVVGPSGSCVGSVRHQHAGIARAAGDEALARRADAVASRTFELSELLVDQLGVTDVGAVFPHRVTYHPTCHSLRLLRVDDKPLQLLRAVEGIDLVELPRADECCGFGGTFAVKNADTSSAMLADKMRHVRATGAEYVTAGDASCLMHIGGGLSRSRAGVRTLHLAEILASTGDRAGVAP
>CP031165.1|AXV07793.1|3578516_3579623_-|Transcriptional-regulator-of-rhamnose-utilization,-LacI-family
MTRFNGGVRSAASVRADSEGSLLVSIKEVAHRAGVSVGTVSNVLNRPGNVNEDTLQRVRTAISELGYVRNESARQLRAGQSRTIGLVVLDVANPFFTDLARGVESLAHDADMVVTLCNSDNDGGRQARHLDVLAQQRVRGVLITPLDTHAPSIQHLVDHGIPVVLVDRGSEDATRCSVSVDDVHGGRLAGAHLAGEGHDRIAFVGGPFDIRQVSDRLEGLREGAPDADVQVVEVNGLSVADGREAARHVIDMPVDRRPTAVLCANDLIALGMLQEVVRAGLRVPQDLALVGYDDIDFAAAAVVPLSSVRQPREQLGRAAAELLLEEAGDAAGQHIHRQVVFRPELVVRTSSGGPDGFGTETVTGEGTA
>CP031165.1|AXV07794.1|3579852_3581355_+|putative-L-rhamnose-ABC-transporter,-ATP-binding-component
MSQPVLELRDIEKSFGAVRALRDAQLELHAGEAHALVGENGAGKSTLVKILAGAHRQDTGRVLLDGEPLELTGPADARAAGIAVIYQEPTLFPDLSVAENIFMGRQPQRSLGRIDHDAMHAAATALFDRLGHHLDPRRPARGLSIADQQLVEIAKALSFDARVLIMDEPTAALSGVEVERLFAVARSLRESGAAILFISHRFDEVFGLCDRITVMRDGAHVSTDPTAGLTVDEVVRRMVGREVGSLFPKVEAEIGEVALSVRGLTRHGIFRDVSFDVRRGEIVALAGLVGAGRSEVIRAVFGVDGRNAGEVLVHGTPLAGGDPRAAMRAGLALVPEDRRQQGLVMELSVERNTTVTSRRTLARFGLLSGAAEHAWAADWTRRLEVKAGSLDAPVSTLSGGNQQKVVLAKWLSTDPSILIVDEPTRGIDVGTKAEVHRLLSALAADGLAVLMVSSELPEVLGMADRILVMHEGRLTADIPRIDATEESVMRAATGQVEVVA
>CP031165.1|AXV07795.1|3581351_3582410_+|putative-L-rhamnose-ABC-transporter,-transmembrane-component-2
MTAQITDPPANTTDMTASPLRTAPGPVSRILHARELGIVLALVALVTVTALRNPRFLSPQSLRDLLLSASIVAVLAVGQTAVIVTRNVDLSVGSILGLTAFGIGKLFIAAPGLPVAIGILVAVLGGALLGALNGGLIAAARVPALVVTLGTLYIFRGVDFAWASGQQINAADMPDTLLTLGTQTVLGVPVLAITAVVVAALASWYLASYRSGRELYAIGSDPDAARLYGIDVGRRVLGAFVFSGATAGLAGAMYAARFGTLDATAGRGIELEVVAAAVVGGVAIFGGSGTAYGAAIGALLLTTISTSLAVLRINPFWQQAVVGLLILLAIGLDRLLTLRAERSLRRRSPHGR
>CP031165.1|AXV07796.1|3582399_3583446_+|putative-L-rhamnose-ABC-transporter,-transmembrane-component-1
MAADIAPTAPSSWTRRSPWASLRSWDGAITLVLLLVLAVAAVSVENFTNTGNLKFLLLDSITIALIALPMTLIVITGEIDLSVASTLGLTSAVMGSLWTANVPLELAVIGVVLLGALLGAVNGVFVTRFGLPSLAVTIGTLAAYRGLAFVVLGSRAVADFPIGWTSTTTEAIGSTFVPLALIPLALLGLAFAVVLHRTATGRAMYVIGHNDEAATFSGIDPARTRFWLFVTSGAVSGLAGVFWTLRYASARADNAQGLELAVVAAVLLGGVSIFGGKGSLPGVIAAVLLLGTIRNALQLQNVSADVLDIVTGLLLIVSVLTPNVIARVSASRHRRALARGASPSPETA
>CP031165.1|AXV07797.1|3583563_3584751_+|putative-L-rhamnose-ABC-transporter,-substrate-binding-component
MSTTILRRRSAMFAAMLALLLLVTACSGTTREDDTADAPEEDSAATTEEEADAPTEDEATDEPAATENTPEAAATTEDAGDDTADGATAIEEGIEIAFLPKQINNPYFTTADGGGEEAVGEFAGSYSEVGPSEASASSQVSYINTLTQQGVGAIAISANDPNAVCPALNEARDAGIAVVTYDSDTDPSCRDLFINQASAEGIARVQVEMVAEQIGGAGEIAVLSATPNATNQNAWIELMEGILADEYPDIELVTVAYGNDDDQDSFTETQALLQSYPDLAGIVSPTTVGISAAARYLSGSEFKGEVALTGLGTPNQMREFVEDGTVTAFALWNPADLGYLAAYAGGALASGLITGAEGDTFEAGKLGSYTVEADGSVLLGPPTVFDIDNIGDFDF
>CP031165.1|AXV07798.1|3584822_3585209_+|L-rhamnose-mutarotase
MPRYCFTLQVDPRHLDAYRRDHAAVWPEMLRALADAGWRNYSLHLRDDGLLIGIVETEDFQRALDAMDATAVNDRWQAAMASYFADLDGPDGQHTAPDRAMQLVPEIFHLETQLAAADAHPTPEENPR
>CP031165.1|AXV07799.1|3585205_3586375_+|L-rhamnose-isomerase
MTTVPEHVAAGLRAMEVEVPSWAYGNSGTRFKVFAQAGVPRDPYEKVADAAQVHRFTGAAPSVSLHIPWDRVEDYGKLTQHAEDLGVRLGVINANVFQDDDYMLGSVTHPDPRVRRKATDHLLECVDVMDATGSTDLKLWFSDGTNYPGQDDIRARQDRLAEALREVYDRLGDDQRMLLEYKLFEPAFYTMDVPDWGTAFAHCIALGEKAEVVVDTGHHAPGTNIEFIVATLLRAGRLGAFDFNSRFYADDDLMVGSADPFQLFRILHECVVGGAVTAESTVRFMLDQCHNIEPKIPGQIRSVMNVQESTAKALLVDHDALAAAQSAGDVLGANAVLMDAFDTDVRPLLAAFREEQGLDPDPMAAYAASGYADAIVADRVGGTQAGWGA

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Crispr_ID: CP031165_19

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_19

3629721-3629819

Orphan

Consensus_repeat	Method
CGACGGGCGGCCCGGAATCCGACACGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_19

>merge|CP031165|19|3629721-3629819|CRISPRCasFinder
CGACGGGCGGCCCGGAATCCGACACGCGCAACCCGGTGGGGGCCGACCCCTTGCCCGCGTGTCGGGTGTTCACGACTGGCGGCCCGGAATCCGACACGC

>CP031165|19|18|3629721-3629819|CRISPRCasFinder
CGACGGGCGGCCCGGAATCCGACACGC	GCAACCCGGTGGGGGCCGACCCCTTGCCCGCGTGTCGGGTGTTCA
CGACTGGCGGCCCGGAATCCGACACGC

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV07842.1\|3636136_3636562_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07834.1\|3628172_3628904_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223445
CP031165.1\|AXV07835.1\|3628912_3629701_+\|Cobalamin-synthase	unknown	unknown	gnl\|CDD\|234697
CP031165.1\|AXV07840.1\|3634592_3635639_+\|TsaC-protein	unknown	unknown	gnl\|CDD\|223088
CP031165.1\|AXV07839.1\|3633981_3634596_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07846.1\|3638143_3640366_-\|RecD-like-DNA-helicase-YrrC	unknown	unknown	gnl\|CDD\|273632
CP031165.1\|AXV07844.1\|3636880_3637585_-\|Dienelactone-hydrolase-family	unknown	unknown	gnl\|CDD\|223489
CP031165.1\|AXV07828.1\|3622492_3623476_+\|L-proline-glycine-betaine-binding-ABC-transporter-protein-ProX	unknown	unknown	gnl\|CDD\|270324
CP031165.1\|AXV07827.1\|3621698_3622466_+\|Glycine-betaine-ABC-transport-system-permease-protein	unknown	unknown	gnl\|CDD\|224095
CP031165.1\|AXV07831.1\|3624521_3625502_+\|Quinone-oxidoreductase	unknown	unknown	gnl\|CDD\|176180
CP031165.1\|AXV07826.1\|3621015_3621687_+\|Permease-protein-of-ABC-transporter	unknown	unknown	gnl\|CDD\|224095
CP031165.1\|AXV07845.1\|3637676_3638147_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07833.1\|3627742_3627937_-\|Translation-initiation-factor-1	unknown	unknown	gnl\|CDD\|178954
CP031165.1\|AXV07830.1\|3624024_3624390_-\|SSU-ribosomal-protein-S1p	unknown	unknown	gnl\|CDD\|224023
CP031165.1\|AXV07838.1\|3632027_3633851_+\|Acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173842
CP031165.1\|AXV07832.1\|3625595_3627653_+\|Gamma-glutamyltranspeptidase	unknown	unknown	gnl\|CDD\|225218
CP031165.1\|AXV07829.1\|3623512_3623998_-\|DNA-binding-response-regulator	unknown	unknown	gnl\|CDD\|381116
CP031165.1\|AXV07843.1\|3636586_3636787_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV07841.1\|3635635_3636019_-\|Large-conductance-mechanosensitive-channel	unknown	unknown	gnl\|CDD\|376605
CP031165.1\|AXV07837.1\|3630858_3631701_+\|putative-undecaprenyl-phosphate-glycosyl-1-phosphate-transferase	unknown	unknown	gnl\|CDD\|376775

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV07834.1\|3628172_3628904_-\|hypothetical-protein	gnl\|CDD\|223445	COG0368, CobS, Cobalamin-5-phosphate synthase [Coenzyme metabolism].	4.05327e-07
CP031165.1\|AXV07835.1\|3628912_3629701_+\|Cobalamin-synthase	gnl\|CDD\|234697	PRK00235, cobS, cobalamin synthase; Reviewed.	6.78095e-50
CP031165.1\|AXV07840.1\|3634592_3635639_+\|TsaC-protein	gnl\|CDD\|223088	COG0009, SUA5, Putative translation factor (SUA5) [Translation, ribosomal structure and biogenesis].	9.56954e-81
CP031165.1\|AXV07846.1\|3638143_3640366_-\|RecD-like-DNA-helicase-YrrC	gnl\|CDD\|273632	TIGR01448, recD_rel, helicase, putative, RecD/TraA family. This model describes a family similar to RecD, the exodeoxyribonuclease V alpha chain of TIGR01447. Members of this family, however, are not found in a context of RecB and RecC and are longer by about 200 amino acids at the amino end. Chlamydia muridarum has both a member of this family and a RecD. [Unknown function, Enzymes of unknown specificity].	5.28244e-157
CP031165.1\|AXV07844.1\|3636880_3637585_-\|Dienelactone-hydrolase-family	gnl\|CDD\|223489	COG0412, COG0412, Dienelactone hydrolase and related enzymes [Secondary metabolites biosynthesis, transport, and catabolism].	1.15426e-55
CP031165.1\|AXV07828.1\|3622492_3623476_+\|L-proline-glycine-betaine-binding-ABC-transporter-protein-ProX	gnl\|CDD\|270324	cd13606, PBP2_ProX_like, Bacterial substrate-binding protein ProX of ABC-type osmoregulated transporter and its related proteins; the type 2 periplasmic-binding protein fold. This group includes periplasmic substrate-binding component of ABC transport systems from gram-negative and -positive bacteria that are involved in uptake of osmoprotectants (also termed compatible solutes) such as betaine, choline, proline betaine, carnitine, and L-proline. To counteract the efflux of water, many microorganisms accumulate the compatible solutes for a sustained adjustment to high osmolarity surroundings. This substrate-binding domain belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	2.16958e-100
CP031165.1\|AXV07827.1\|3621698_3622466_+\|Glycine-betaine-ABC-transport-system-permease-protein	gnl\|CDD\|224095	COG1174, OpuBB, ABC-type proline/glycine betaine transport systems, permease component [Amino acid transport and metabolism].	4.09629e-40
CP031165.1\|AXV07831.1\|3624521_3625502_+\|Quinone-oxidoreductase	gnl\|CDD\|176180	cd05276, p53_inducible_oxidoreductase, PIG3 p53-inducible quinone oxidoreductase. PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	2.61553e-171
CP031165.1\|AXV07826.1\|3621015_3621687_+\|Permease-protein-of-ABC-transporter	gnl\|CDD\|224095	COG1174, OpuBB, ABC-type proline/glycine betaine transport systems, permease component [Amino acid transport and metabolism].	1.17052e-56
CP031165.1\|AXV07833.1\|3627742_3627937_-\|Translation-initiation-factor-1	gnl\|CDD\|178954	PRK00276, infA, translation initiation factor IF-1; Validated.	6.88785e-44
CP031165.1\|AXV07830.1\|3624024_3624390_-\|SSU-ribosomal-protein-S1p	gnl\|CDD\|224023	COG1098, VacB, Predicted RNA binding protein (contains ribosomal protein S1 domain) [Translation, ribosomal structure and biogenesis].	4.32815e-34
CP031165.1\|AXV07838.1\|3632027_3633851_+\|Acyl-CoA-dehydrogenase	gnl\|CDD\|173842	cd01153, ACAD_fadE5, Putative acyl-CoA dehydrogenases similar to fadE5. Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.	3.53547e-159
CP031165.1\|AXV07832.1\|3625595_3627653_+\|Gamma-glutamyltranspeptidase	gnl\|CDD\|225218	COG2340, COG2340, Uncharacterized protein with SCP/PR1 domains [Function unknown].	5.86899e-10
CP031165.1\|AXV07829.1\|3623512_3623998_-\|DNA-binding-response-regulator	gnl\|CDD\|381116	cd17574, REC_OmpR, phosphoacceptor receiver (REC) domain of OmpR family response regulators. OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	2.2548e-37
CP031165.1\|AXV07841.1\|3635635_3636019_-\|Large-conductance-mechanosensitive-channel	gnl\|CDD\|376605	pfam01741, MscL, Large-conductance mechanosensitive channel, MscL.	2.72851e-42
CP031165.1\|AXV07837.1\|3630858_3631701_+\|putative-undecaprenyl-phosphate-glycosyl-1-phosphate-transferase	gnl\|CDD\|376775	pfam02397, Bac_transf, Bacterial sugar transferase. This Pfam family represents a conserved region from a number of different bacterial sugar transferases, involved in diverse biosynthesis pathways.	4.89959e-75

>CP031165.1|AXV07835.1|3628912_3629701_+|Cobalamin-synthase
MIAHRPAMMATPVHPRLFLVALQLLTRLPVGDPMESDRDVADSVAWYAVVGALVGGLSGFVWWMAALALPTRAAAVLAVGATVMLTGALHEDGLADTADGLFGGRTPTDRLRIMKDSATGAYGVLALVLIVLLRVNLLAALSPVAGAAALVVAGSLSRGVTAIAMLNAVPARRDGSGAVLLDHLRPGPAIAAGVTAVVATSLFAGLEAIPVVLAAGAAAFAVRVSAVRRLGGLTGDTIGAMILLSDAAVLSLLVALEVGAGL
>CP031165.1|AXV07834.1|3628172_3628904_-|hypothetical-protein
MRAALALFTALPVEWDGDDLDRSWLLAPVVGMLIGLVWFVFHQLTVGLVGPVVAGAFVVAISAALTGSRGFRGLVGLADAMGGVPAGPGAPPMVGVGALAVAIVVVVEANLLQRVNLAPEMIVIVPMVARGVQSLLLRAGDDMVGVTPPSPRAKLGIGIVLLGLLALPIPLQSLVRPERLNGPLDAVGYLTLGVAALVGAFVVGGITRAWTLARFGPLDPRGWHAIGLFAEVAALVVVAVRID
>CP031165.1|AXV07833.1|3627742_3627937_-|Translation-initiation-factor-1
MEGVIEEALPNTMFRVKLDNGHSILGHISGKMRKHYIRILPGDRVTVEVSPYDLTRGRITYRYK
>CP031165.1|AXV07832.1|3625595_3627653_+|Gamma-glutamyltranspeptidase
MLPLSERTAFNDRETRMTFLRRPLAVLALLASLALVPAPVLGQDPTPTSDSTPPEQLLPVPAANPLLPPLATDDVSRVADSSDAVEVGVTLSKAAFADATPWVAHDPRYTGATGVVLARDDVFPDSLAAAAVAGTDRPILYTTGGPDAFLDSAVADELWRVLGPGRGCADGGHEVIVVGGAQAVSPAVVEQVEAMGYCTARLAGPSRVDTSVVLATAAIARTGATTLLLARADNWADAATGGAVAARYGLPLAITGADALHPAVADLIGSGGITDVVLLGGEAALSATVATQVEALGVSVQRVAGPGREETAAAIAEELWEDDDVEGAVLLNGRAEDGWVYALAAAPFSARSGRPQLYGHTDGVPTPSADVVAGVPAVTVVGPVASVDDSVITALRTMLAAPDDRVGADLAGLRSGDSLDALNYWRRVSGMPEVDAWDPDLSRGAFEHARYTVKEDDPGHAQDPTSPWSTPAGRGEEPEAAGGEVYNGHDGPDTAHHAVTGWVRTPFHGAGMLDPSASHYGIGSYAEDLGQGTTAATAVRLRYDWQNGGLPDSDGDGVITHFPVDGSVLALSAYWGGEYPEPLDICGYDNPVGQPLWLHLAEPLPVGDVDVVLEVDGQPVEHCAFLHYDDATESRRMYVMARRPLRAGGEYTVTAAIPGGRTFTWSFEVLRSPIDGGLAGTAPNI
>CP031165.1|AXV07831.1|3624521_3625502_+|Quinone-oxidoreductase
MRAVIAPSPGGVEALELVELPDPEPGPEDLLVEVAATAVNRADILQRRGMYPPPPGAPDTLGLELSGRVVGMGADVTGWQEGDEVCAVVGGGGYASMAVVPARTAMPLPPGLDVVSAAAVPEVYATAYDNVFLRAGLTAGETVLLHGGSSGVGTAGILLATRAGADVVVTVGTEEKAAACRELGADLAIDYKAVDSFADAIREARDGRGVDVVLDIIGGPYLKQNLSVLEPDGRMVTIGLMGGAKAEINLGLVLSKRLSVMGSTLRARSVDAKAALAERLVADVWPGFADGTLRPIIHSRHALADVAAAHEELESSTHIGKILLVV
>CP031165.1|AXV07830.1|3624024_3624390_-|SSU-ribosomal-protein-S1p
MSAQVGDVVTGKVVKLQDFGAFVEIDAETTGLVHISEVHRDFVDNIHAYLTEGQEVEVKVVGIKEDGRIDLSIKRAEPDWSDEPKPRPTAKVDKEFNQRLRKFMHQSDMIQGEVRKRKRST
>CP031165.1|AXV07829.1|3623512_3623998_-|DNA-binding-response-regulator
MVRVLVVDDDPNVRFTVRVALEGSPPSGQPMAVVEAANGVEALQATQHDTYDLVLLDIMMPGLDGFAVLHALRQHGDDPPVVMLTARGREVDIVNAFRAGADGYVTKPFDVDELAYLVADLTGREVSERRAMRVKELERAELLLQLEHGFGAEPPEASNPA
>CP031165.1|AXV07828.1|3622492_3623476_+|L-proline-glycine-betaine-binding-ABC-transporter-protein-ProX
MTTSTRSRMAAFLLMLVLALVASACASDDDGSDDAAGDASESADGTTDEGAETAEELGDITVGSTNFDEQELVAEMYALALEDAGYTVERRYQLGSREVVLPALTSGEIDVYPEYVGTALEFLNEGAGEATGDTEASTELLRERFAEQGVDVLEPSDAQDKNGLVVRQETADTYGLSTVSDLADVAGDLTLGGPPECPERPLCIPGYESAYGVTFGDFRSLDAGSPVTIEALSAGEIDVALLFTTDGVIAANDWVLLDDDQDLQPAENIVPVIRSEANTDAATEALDAVSAVLTTENVTEMIRQLRVDLADPAEVAETFLTDQGVLG
>CP031165.1|AXV07827.1|3621698_3622466_+|Glycine-betaine-ABC-transport-system-permease-protein
MLAQAAEQTLTEEILAWLRGEDFRSVDGIPQLIGDHLALSAAALGLACAVAIPLALFLAHGHRAPVLSINMANAFRAIPAFGLLLVAFQLGGFSLPLLVLVFALVGVAPIFANAYIGVRQVDPEIVDAAVGMGLTGRQVLMEVELPLASPVLMAGVRTAAVNIVATVTLAAVVGFGGLGFPIIAGLNRGLQFSSSARTLAIGGALLVALLSIGTEAVLGLVQARIVPEGLRLRDAAREARAEAVTEPTLRTEPSP
>CP031165.1|AXV07826.1|3621015_3621687_+|Permease-protein-of-ABC-transporter
MSPLLLAQSRPFPDWEWIRRNGDTILEQGIEHVQLTLMAVALGFVIAFPLAVLASRRRRLQTPVLQVTGILFTIPSLALFVGLVPLTGLSTTTALIPLTLYTLLILVRNTIAGLDSVPTEVVEAARAMGYREWTLLRAVELPLALPVIIAGIRIATVTTIGLVVVTAVIGQGGWGQMMYSDGFQRQNLTPTLLGFLLSVALAIVLDLALVALERRLSPWAKAR
>CP031165.1|AXV07837.1|3630858_3631701_+|putative-undecaprenyl-phosphate-glycosyl-1-phosphate-transferase
MLVHPDNSPSGSSADVIDGHAVDVDVQPASAAGHADPDVVAVVAAPRVVSEEEKATIARLQAQVDGTDRPDGTYVKVIKPALDRFAGGVLLLLTLPLLLAGMLAVRVTMGKGVIFRQERIGLDGRRFTVLKLRTMGHDRRSTSQKDLEALAEGRWDGIERRQTHKTDADPRHTGVGRTLRKLSIDELPQLINVVRGDMSLVGPRPELPVVINRHYEPWMHRRHAVKPGVTGLWQISMRGEGDMHEHVDVDLDYVDRVSLREDLRILFATPFAALGAHKGV
>CP031165.1|AXV07838.1|3632027_3633851_+|Acyl-CoA-dehydrogenase
MTHYKSNLRDMFFNLFEVNRVQDHLGTGPYEQMDADSAKDVLREVDRLAREDFAASFVAGDRTPLQLDAENGEVTLPKEINETLDAFFDNDWHLLYVPPHLGGYGASPSITWSASELLLGANASAMLYTAGPFFATILDSVCNDEQRTRFVEPMIEHKWGATMVLTEPEAGSDVGAGRAKAVDNGDGTWTITGNKRFITSGDFDWPDNVIHLVLARPEGAGPGTKGLSLYVVPKYWVNEDGSLGERNGVWVRAIEDKMGIKASATAELYFSDTDVPARGILVGEVHDGIAQMFRVIEYARMLVGTKAISTLSTGYLNALEYAKERVQGPDLKKAMDKTAPRVEIMRHPDVRRNLMMQKAHVEGMRALVMYTGWVQDQIAMARHNGDDEAAEGWEQMNDLLLPMVKGYGSEKSYELLAVALQVFGGSGFTRDVPLEQYIRDAKIDTLYEGTTGIQGMDLFFRKIGKDQGATLTRLLTEVQNFAKDGKPDDGLQAERQRLATALEDVQGMLGSLVQFLGEDLYKVGLSTTPFLMSLSEVVVGWLSLRGADVALTQLNSEDVSDADRDFYTGKVAAARWFAHNVLPQLSSRREIMAATSMEVMEVADAAF
>CP031165.1|AXV07839.1|3633981_3634596_+|hypothetical-protein
MANWRRTRPAPSRLEEGREVYTLALDVAKALDRAGLDLWAAGIRACLDAPSSLARQQHLTVELVRLRDTGDLRRAGCAEDIESALSRLELGLGSIDVPQQPLYTATRNLADHLELNGGRRWLARLRTVITDPDRGAAARVERLDALTERMVPGADGLPEGSASLVRAVRGRLNRHLDMDAVALHLAFALTPPAPSRIRDDQQPR
>CP031165.1|AXV07840.1|3634592_3635639_+|TsaC-protein
MTASLLAIPDDLPDGDLRALLASPAAALRDGGLVAFPTETVYGLGADALSTRAVERIFHAKGRPSDNPLIVHLADASWMDRVAVVTPLARALAERFWPGPLTLVLARRDRVPEATAAGLDSVAVRVPASRVARLLIDTAGTPVAAPSANRSGRPSPTTAAHVATDLGEDLDWIIDGGPCEIGIESTVVDARGDAPVVLREGSVTREMLGDRGAIGDPSRSPGTRHAHYQPRAAVRIAPVGRGQEVAADVASTGARVGLVTGDAIGVPSAVTLLAAPVDDDAMARELYAALRRADDLGLDVVVVEAVTDTGVGRAVMDRLRRAGTPNDPAAAGSSRGASRPQAGGTPER
>CP031165.1|AXV07841.1|3635635_3636019_-|Large-conductance-mechanosensitive-channel
MVKEFKEFLMKGNVIDLAVAVVIGAAFAAIISALVEGIINPIIAAIVGQPDITEVTTSIGSAELLTGQVIGAIINFVLVGLVLFLLVKAANKAMDARKKEPEEVEVVADPEEILLLREIRDSLSTRA
>CP031165.1|AXV07842.1|3636136_3636562_+|hypothetical-protein
MTTTTAEWLLEISGLTIGCNDSTDVVSRGHHLAAQVRSAAAAFCAATSCGPDGCVAGCPLATYDGGFTACHLASELAPDTPRNTTIDAHRAAMLYVQALRAASTAVFHCRRQAHPAGECWFSTDGTARCGDVLAVTHRLGG
>CP031165.1|AXV07843.1|3636586_3636787_-|hypothetical-protein
MDHVTPKLRSITGVARALIATVGVEEAVTILLTQFGWDIAFSAVSHVEGPEGARAMWLTLERVGTA
>CP031165.1|AXV07844.1|3636880_3637585_-|Dienelactone-hydrolase-family
MADRTPHQNVTFPSNGHEAHGYLTTPDNGSGPGLIVIQEWWGLTDHIADVCDRFARQGYVALAPDLYGGSITHDADEAGQMMQDLPEDRAATDLAGAVDHLLSLDAVTSERVGVVGFCMGGGFVIQLAAQQGDRIGAAVPFYGVLQSEPDFSAITAPVLGHYAETDDFAPPTKALEMGQAIRDAGGSAAINVYGGTNHAFFNDENRLGTHEPDAAAVAWARTLSFLSTHLGHQD
>CP031165.1|AXV07845.1|3637676_3638147_-|hypothetical-protein
MTMSSWPVTGTRRFGSTPLPPELQVSLVPLLEDAHASDPFVPHQPREGIVRAAELVRSVGLAVVTIRGSLLVGGVEVDHVWLAVTDHSGEPWVLDTAFPLHRESFLDVLPGWVAGDVSTDVLAAAADGAALLDRVLASFPDGTGYIGGPVWSSGRR
>CP031165.1|AXV07846.1|3638143_3640366_-|RecD-like-DNA-helicase-YrrC
MENTLLPAPERVAGEVVYVVYADDASGFGVVSMDEDRDGAIKASGPLASLTPGQAVTLVGRWTEHPKHGRTFEADFYELATPRTKKGLKTFLASDRFPGVGDAIAERLVKTFGTGLAEVIANQPERLAGVTGVSTALAGRIHGSWVSAGLLPQVVQLLAAVDLGPAVARAAVKRFGDEAAEMLTTDPYAYLSLPGVRWKHADALGRAAGIDDDDPRRLAAGAAGFLRGACWRGGHTVMAEEELLARLPSALGGGIDRARLAIDEAVDNGEIRREDQPLGDLPVPRVSPPPLHDAELAVADRIRVLTDADGSGNPLRNAEGNDDKLTDEQAHAVEAVSDHAVTILTGGPGTGKTFAVTELVRRATAAGANVALCAPTGRAAKRLEEVTGHAATTVHRLLEARPEPGEGFVFGRTADNPLPHDLVVADEWSMADVHLAAALLDALAPPSHLLLVGDPDQLPPVGPGATLRDLLAARNVPVTRLTKVHRQAAQSRIVTLAHELNAGGEPIVVGRDGDVFAVPERTPAIPARIAEIVAERAPAYFDCTPADVQVLAPMYRGAAGVDALNTALKERLNPAGTRRAVSGWHEGDRVVATRNDPEVDIANGDIGEVAGTDAKDGVVSVSFPQGIVELSGDRLNHLAPAWCLTVHKSQGGEWPVVVLVLDRSQMSMLTRELVYTAITRARRGLLLVGDAGLLVPAARRVGGGMAARHTTLSARLAANDAGATGAQGDGDTVDEEGQEA

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Crispr_ID: CP031165_21

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_21

4151482-4151576

Orphan

Consensus_repeat	Method
CCGGTCGCACCTTGCAGCGACAACCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_21

>merge|CP031165|21|4151482-4151576|CRISPRCasFinder
CCGGTCGCACCTTGCAGCGACAACCGCAGCACCCGCCACCTTGGCCCAGCGCGCGACCAAGAAGGAGGCCGGTCGCACCTTGCAGCGACAACCGC

>CP031165|21|20|4151482-4151576|CRISPRCasFinder
CCGGTCGCACCTTGCAGCGACAACCGC	AGCACCCGCCACCTTGGCCCAGCGCGCGACCAAGAAGGAGG
CCGGTCGCACCTTGCAGCGACAACCGC

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV08289.1\|4143633_4145358_-\|Urease-alpha-subunit	unknown	unknown	gnl\|CDD\|237304
CP031165.1\|AXV08299.1\|4154938_4155067_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV08297.1\|4152260_4153001_-\|putative-lipoprotein	unknown	unknown	gnl\|CDD\|367619
CP031165.1\|AXV08292.1\|4147290_4148172_-\|Uricase-(urate-oxidase)	unknown	unknown	gnl\|CDD\|274554
CP031165.1\|AXV08303.1\|4156930_4159303_+\|Xanthine-dehydrogenase,-molybdenum-binding-subunit	unknown	unknown	gnl\|CDD\|132240
CP031165.1\|AXV08293.1\|4148180_4148510_-\|5-Hydroxyisourate-Hydrolase-(HIUase)	unknown	unknown	gnl\|CDD\|274364
CP031165.1\|AXV08294.1\|4148506_4150039_-\|Allantoicase	unknown	unknown	gnl\|CDD\|106738
CP031165.1\|AXV08302.1\|4156406_4156928_+\|Xanthine-dehydrogenase-iron-sulfur-subunit	unknown	unknown	gnl\|CDD\|224991
CP031165.1\|AXV08305.1\|4160581_4161847_+\|drug-resistance-transporter,-EmrB/QacA-family	unknown	unknown	gnl\|CDD\|340882
CP031165.1\|AXV08301.1\|4155570_4156410_+\|Xanthine-dehydrogenase,-FAD-binding-subunit	unknown	unknown	gnl\|CDD\|224238
CP031165.1\|AXV08287.1\|4142171_4142852_-\|Urease-accessory-protein-UreG	unknown	unknown	gnl\|CDD\|349776
CP031165.1\|AXV08295.1\|4150038_4151403_-\|Allantoinase	unknown	unknown	gnl\|CDD\|238640
CP031165.1\|AXV08288.1\|4142884_4143586_-\|Urease-accessory-protein-UreF	unknown	unknown	gnl\|CDD\|223900
CP031165.1\|AXV08298.1\|4153006_4154956_-\|putative-secreted-protein	unknown	unknown	gnl\|CDD\|293789
CP031165.1\|AXV08304.1\|4159299_4160604_+\|Guanine-deaminase	unknown	unknown	gnl\|CDD\|236184
CP031165.1\|AXV08296.1\|4151612_4151924_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV08290.1\|4145350_4146043_-\|Urease-gamma-subunit	unknown	unknown	gnl\|CDD\|183886
CP031165.1\|AXV08286.1\|4140550_4141408_+\|Sirohydrochlorin-cobaltochelatase	unknown	unknown	gnl\|CDD\|225049
CP031165.1\|AXV08291.1\|4146079_4147303_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225184
CP031165.1\|AXV08300.1\|4155032_4155254_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV08289.1\|4143633_4145358_-\|Urease-alpha-subunit	gnl\|CDD\|237304	PRK13206, ureC, urease subunit alpha; Reviewed.	0
CP031165.1\|AXV08304.1\|4159299_4160604_+\|Guanine-deaminase	gnl\|CDD\|236184	PRK08203, PRK08203, hydroxydechloroatrazine ethylaminohydrolase; Reviewed.	0
CP031165.1\|AXV08297.1\|4152260_4153001_-\|putative-lipoprotein	gnl\|CDD\|367619	pfam03713, DUF305, Domain of unknown function (DUF305). Domain found in small family of bacterial secreted proteins with no known function. Also found in Paramecium bursaria chlorella virus 1. This domain is short and found in one or two copies. The domain has a conserved HH motif that may be functionally important. This domain belongs to the ferritin superfamily. It contains two sequence similar repeats each of which is composed of two alpha helices.	9.00383e-35
CP031165.1\|AXV08292.1\|4147290_4148172_-\|Uricase-(urate-oxidase)	gnl\|CDD\|274554	TIGR03383, Structure_Of_Uricase, urate oxidase. Members of this protein family are urate oxidase, also called uricase. This protein contains two copies of the domain described by the uricase model pfam01014. In animals, this enzyme has been lost from primates and birds. [Central intermediary metabolism, Other].	8.85947e-107
CP031165.1\|AXV08303.1\|4156930_4159303_+\|Xanthine-dehydrogenase,-molybdenum-binding-subunit	gnl\|CDD\|132240	TIGR03196, pucD, xanthine dehydrogenase D subunit. This gene has been characterized in B. subtilis as the molybdopterin binding-subunit of xanthine dehydrogenase (pucD), acting in conjunction with pucC, the FAD-binding subunit and pucE, the FeS-binding subunit. The more common XDH complex (GenProp0640) includes the xdhB gene which is related to pucD. It appears that most of the relatives of pucD outside of this narrow clade are involved in other processes as they are found in unrelated genomic contexts, contain the more common XDH complex and/or do not appear to process purines to allantoin.	0
CP031165.1\|AXV08293.1\|4148180_4148510_-\|5-Hydroxyisourate-Hydrolase-(HIUase)	gnl\|CDD\|274364	TIGR02962, Probable_5-hydroxyisourate_hydrolase_R09H10.3, hydroxyisourate hydrolase. Members of this family, hydroxyisourate hydrolase, represent a distinct clade of transthyretin-related proteins. Bacterial members typically are encoded next to ureidoglycolate hydrolase and often near either xanthine dehydrogenase or xanthine/uracil permease genes and have been demonstrated to have hydroxyisourate hydrolase activity. In eukaryotes, a clade separate from the transthyretins (a family of thyroid-hormone binding proteins) has also been shown to have HIU hydrolase activity in urate catabolizing organisms. Transthyretin, then, would appear to be the recently diverged paralog of the more ancient HIUH family. [Purines, pyrimidines, nucleosides, and nucleotides, Other].	4.4756e-49
CP031165.1\|AXV08294.1\|4148506_4150039_-\|Allantoicase	gnl\|CDD\|106738	PRK13797, PRK13797, allantoicase.	8.08025e-156
CP031165.1\|AXV08302.1\|4156406_4156928_+\|Xanthine-dehydrogenase-iron-sulfur-subunit	gnl\|CDD\|224991	COG2080, CoxS, Aerobic-type carbon monoxide dehydrogenase, small subunit CoxS/CutS homologs [Energy production and conversion].	1.09245e-57
CP031165.1\|AXV08301.1\|4155570_4156410_+\|Xanthine-dehydrogenase,-FAD-binding-subunit	gnl\|CDD\|224238	COG1319, CoxM, Aerobic-type carbon monoxide dehydrogenase, middle subunit CoxM/CutM homologs [Energy production and conversion].	6.92773e-60
CP031165.1\|AXV08287.1\|4142171_4142852_-\|Urease-accessory-protein-UreG	gnl\|CDD\|349776	cd05540, UreG, urease accessory protein UreG. UreG is one of the four accessory proteins of urease. Urease is an enzyme which catalyzes the decomposition of urea to form ammonia and carbon dioxide. Bacterial urease is a trimer of three subunits which are encoded by genes ureA, ureB, and ureC. Up to four accessory proteins (ureD, ureE, ureF, and ureG) are required for urease catalytical function. UreG may play an important role in nickel incorporation of the urease metallocenter. UreG is a member of the Fer4_NifH superfamily which contains an ATP-binding domain. Proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.	1.75059e-106
CP031165.1\|AXV08295.1\|4150038_4151403_-\|Allantoinase	gnl\|CDD\|238640	cd01315, L-HYD_ALN, L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.	0
CP031165.1\|AXV08288.1\|4142884_4143586_-\|Urease-accessory-protein-UreF	gnl\|CDD\|223900	COG0830, UreF, Urease accessory protein UreF [Posttranslational modification, protein turnover, chaperones].	1.0155e-21
CP031165.1\|AXV08298.1\|4153006_4154956_-\|putative-secreted-protein	gnl\|CDD\|293789	sd00042, LVIVD, LVIVD repeat. LVIVD repeats are mainly found in bacterial and archaeal cell surface proteins, many of them hypothetical. Structurally, LVIVD repeats have been predicted to form a beta-propeller, with each repeat forming one four-stranded anti-parallel beta-sheet blade.	1.03429e-09
CP031165.1\|AXV08290.1\|4145350_4146043_-\|Urease-gamma-subunit	gnl\|CDD\|183886	PRK13192, PRK13192, bifunctional urease subunit gamma/beta; Reviewed.	9.99682e-102
CP031165.1\|AXV08286.1\|4140550_4141408_+\|Sirohydrochlorin-cobaltochelatase	gnl\|CDD\|225049	COG2138, COG2138, Sirohydrochlorin ferrochelatase [Inorganic ion transport and metabolism].	1.04242e-35
CP031165.1\|AXV08291.1\|4146079_4147303_-\|hypothetical-protein	gnl\|CDD\|225184	COG2301, CitE, Citrate lyase beta subunit [Carbohydrate transport and metabolism].	0.00873021
CP031165.1\|AXV08305.1\|4160581_4161847_+\|drug-resistance-transporter,-EmrB/QacA-family	gnl\|CDD\|340882	cd17324, MFS_NepI_like, Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily. This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	4.54217e-25

>CP031165.1|AXV08295.1|4150038_4151403_-|Allantoinase
MSELDARSLPADLVLRARQVVTPEGIRPAAVHVRDGMIVAVTDGVPRGTDVVDLDDRLVLLPGLVDSHVHVNEPGRTRWEGFFTATRAAAAGGITTIVDMPLNCIPPTVDVAALQAKRDAAEGKLHVDVAVWGGAVPGNAAELAALHDAGVRGFKAFLCDSGVPEYGCVHPTDVSPLLQRIADLGSTLIVHAEDPDVCADAAASLDLRNPRSYNTWLDSRPPEAEVAAVRALVAAVRETGGRVHVLHLSAAEAGEVIGDARAEGLPITVETCPHYLTLHAGDIPDGATAFKCAPPIRDRANADRLWDLLADGVIDAIVSDHSPCPPEDKAPDTGDFLAAWGGIASLQIGLPLVWTAAKERGHDITDVVRWMGEGPARIAGLTDRGRIAPGARADLVVVDPDVEWTIAGAALEHRHPVTPYQGRTVVGAVDTTWLAGTPIVENGRPVGPPRGRMR
>CP031165.1|AXV08294.1|4148506_4150039_-|Allantoicase
MHDPADQTRPDPTRPDPTGLVDLAARRLGGMVLAANDEFFAAKENLLEPLPPVFDPLAYSDRGKVMDGWETRRRRDPSGDPGHDWCIVRLGVTGVIDAVLVDTSHFRGNFPAAFELWGTLTDGGPPGDDADWVQLRPRTELRGDAAQRFDVDAPLRVSHVRFVIHPDGGVARLRLLGRPLVDLRRAADHSGRLDLAAIINGGRAVGCSDAFFSAPTNLLMVGDGRDMGDGWETTRRRGPGHDFAIVELATTGRVERIELDTTNFKGNHPDRCDVLAIDAADADPAELPTDGWTPLVLDHPMQPHARHVIDVEEPTVATHLQLRIHPDGGVARLRARGFVTDEGWQRSTVALLDAATDDRAREVLLACCGSTAWVDAMLARRPFGRPSRLLGAADACWTNVGPDDVLEALSAHPRIGERSASRWSTREQADARAGEQAILDRIAEGNRLYEERFGHVFLIRAAGRSAEEILDALEERLDHPHQTEIAVAAEEQRQITALRLQALLREGVPG
>CP031165.1|AXV08293.1|4148180_4148510_-|5-Hydroxyisourate-Hydrolase-(HIUase)
MSLSTHVLDTANGAPAAGVSVVAERAHDDGWVLVGRGTTDADGRVPELADGLVAGTHRLTFEVGRWFAEADTPTFWSDVVIAFVVADPDEHHHVPLLLSPYGYSTYRGS
>CP031165.1|AXV08292.1|4147290_4148172_-|Uricase-(urate-oxidase)
MSSLPMGPNRYGKSGIRLAVVDRSRPQHDFTDLEVEVRLQGDFDAAHVDGDNSGVLPTDTMRGTCFALARDGIDSVVGYGVRLVDRFLTASPGVDRALVTLTQHPWEAVVVDGAPHAHTFRPAAGGRPTWTVTRDRGEQATVTGGILGARVLKTTGSAFSGFLRDEYTTLPETRDRVMATTVDARWGTTGPDADHTGMAIDVPATILAAFAGHDASESVQHTLHVMGTAVLDAHPDVTWIRFLLPNEHHILSDLSAYGLDNPGVVYLVADRPYGVIEGVVAREGVTPEVPWDG
>CP031165.1|AXV08291.1|4146079_4147303_-|hypothetical-protein
MGRLTPAATRSLLAGVAEADAAHRREWPGRPTTRQPVQVLYVPAHRLPEDPVATLGGEARRLLARHAPDGVALASAVDLPGAMGDRVHARVRAKLDREPIEDLRVDFEDGYVGHDEAEEDADAVRTGRIVGRMLVEDRCTPFVGLRVKSFTDGLASRSVATLDAFLEALLGEAGRLPDGFVVTFPKIVAVAHVAAFVDVLAALEEAHGLAPDTLGFEAQIETTASVLGPDGRVVLRDIRDAGAGRLRAVHFGVFDYTAALGVPPEQQRLDHPGCDIARHLMQVTFAGTEVRLSDGSTNVVPADDTTPTVHTAWHVHAGHVRHSLLHGFEQGWDLHPAHLVSRYAAVFGHLLDGIDEILARLDAWEAGRRGGAVMDEPATVAVLRRRVDRAVACGALEAGNTPDTSGP
>CP031165.1|AXV08290.1|4145350_4146043_-|Urease-gamma-subunit
MRLTPHEQERLMVHVAAGLARHRRDRGLTLNHPEAVALLTSFVLEGARDGRSVAQLMDTGRHVLTEADVMDGVADLVGEVQVEATFPDGTKLVTLHDPIGPPPDGSSDTGPPPGAVVVDGDPIVLNLGRGTLVLTVENTGDRPVQIGSHYHFAEANPALSFDRAAARGHRLDVPAGTAVRFEPGVTRDVDLVPLVGRRAVWGLRGEVAGSLDPAPDAEPDTRIDPGAVDG
>CP031165.1|AXV08289.1|4143633_4145358_-|Urease-alpha-subunit
MGELSRDRYADLFGPTTGDRVRLADTDLWIRVEEDRSGGGALAGDEVVFGGGKVIRESMGQSIATRAEGTPDTVITGALVVDHWGIVKADIGIRDGLIVALGKAGNPDTMDGVHPELVIGPSTEIIAGNGRILTAGAVDSHVHLIAPQLLATALASGITTVVGGGTGPAEGTKATTVTPGAWHLASMLRATDGWPVNLALLGKGNTTSRDALVEQARAGAAGFKMHEDWGTTPAIIDACLAACDELGVQAAIHTDTLNEAGYVDSTLDAIAGRSIHAYHTEGAGGGHAPDIITVASHPNVLPSSTNPTRPHTVNTVDEHLDMLMVCHHLNPSVPEDLAFAESRIRPSTIAAEDVLHDLGAISMIGSDSQAMGRIGEVILRTWQTAHVMKRRRGALPGDDDRADNTRVRRYVAKYTIAPAVAHGLDDHVGSVEPGKLADLVLWDPRFFGVKPDLVLKGGAIAWAQVGDMNASIPTPQPVLPRPMFGAAATVAPTLSVSWVAPIALDDGLPDRLGLGRRLVGVKDCRGIGKADMPGNTATPDIRVDPDTFAVTVDGELMESDPATELPLAQRYFLF
>CP031165.1|AXV08288.1|4142884_4143586_-|Urease-accessory-protein-UreF
MTTDPLLLLLADGRFPSGAHAHSFGLEAAVNAGLLSGVEDLSAWAVGCMHTTWLVDATAAVRAARLGEDVGRWVALDDEVQARLLSSHARTVSRTLGRQMLRTGRAIWPHVALRAAAAVHRDGPSAPLGLGAVIRAAGLPEAHAAELSMHHAVQSAATAAVRLLGLDPFAVTRLVARMGSDIATTSAHAVELADADADADADADVGALPSAGAPMVDLLLTHHHHADGRLFAS
>CP031165.1|AXV08287.1|4142171_4142852_-|Urease-accessory-protein-UreG
MQIAPDQTTRDGELTVNRRRTLRVGIGGPVGTGKTALVAELCRRLAGTLEVAVVTNDIFTTEDADALKRAGVLDEDRIRAVETGCCPHTAIRDDIAANLDAVEQLEARYPALDLVLVESGGDNLTAVFSRALVDLQLFVLDVAGGDKVPRKGGPGVTTADLLVVNKIDLAPLVGASLEVMARDARERRGDKPTVLTSLVADDGARPVLRWLTARLAEHAEALQQDA
>CP031165.1|AXV08286.1|4140550_4141408_+|Sirohydrochlorin-cobaltochelatase
MAMTSAPGLLLIAHGTRDPRGAEEMAELAELVQERVDGPVGNAWLEDFSDPQGVEGARPLVEAGVSRIVTLPMLNFAAYHAKTDVPEQLAEIHEAFPDVAISHGRVLGVHHDLLTLGWERIDAVSPKEGREEEVLIVAASGSSDPDANGELAKAARMLAEGSGHRWVEHSVAGVTWPRTDDVLRRVHRAGATRAVVFSWSLLAGLLEARVWDAVDAVEEETGLEIGRAGRFGPDPRVADALVGRYREALEGDIRANCDTCVYRVPFPGKEDRVGAPSAGGAAPRT
>CP031165.1|AXV08296.1|4151612_4151924_-|hypothetical-protein
MRELLVIVLLESGGSWSCAELADTVEERGFLIAGRAGKVISDQLRYELARGRARRVGRGRYVVGTVTKQAKSRMNARLRALRATAAVAGVPCETCRAGRMPTG
>CP031165.1|AXV08297.1|4152260_4153001_-|putative-lipoprotein
MGTTHRTGGGGRLPAPSGAHHPLLALLVVVLAVFGSGCTRGQDAAAAPTSGPVVLQAGAPGEAPERISAEAAAAIEPPPHTPADVAFVAGMLHHHAQALDMTALVADRTSIDALASFAERMDISQYDEIDLMVSWLEARGEPVPDVGPGSAHARGDHGEHMMPGMLTGEQMDRLAAADGVEFDLLFLDAMTFHHEGALLMVEDLYALEDGSGQDNDLFTMASHIDADQRIEIDRMAELREEVVAGS
>CP031165.1|AXV08298.1|4153006_4154956_-|putative-secreted-protein
MHPSTHRTTTTQPPGRLVVLALSVLLVLGLAVPAAALPTAGEDLPADDGDGQPLDESHGMESIGAEEAALAPEYPTTDDPRVGLPGGPGNTAGEASLNMQRLASMPLAPGASTNSDLAFFERDGRRYAVSGNYNGFNLYDVTDPAAPVHTTSVICPGSQNDVSVHGNLLFMSVESTAAKIDCSAGGGATAETRFRGIRIWDISDLTTPVQLPGVQTCRGSHTHTIVTKPGVEDTLWIYVSMTSSVRAATELPGCSSASSLVDPNTSNFSITVIEVPLAAPETAAIVNRNARIMSTCGDNSCEADHANGSLNGLAFPNPQPNYPEGSGREPGGQSASQTSACHDITSYPAIGLAAGACQGDGLLLDITDPPNPRRIANVRDFNFAYWHSATFNNDGTKVIFTDEWGGGSGARCRATDPLSWGANAIFDIVQTPDGPTMEWRSYFKLPMVQTAQENCVAHNGSLVPVPGRDIMVQAWYQGGTTVFDFTDSANPVEIAYFDRGPVDPTRLLTGGFWSSYWWNGTIVGNEIARGVDTFALTPSPALTQLELDAARQVVTSTTNVQHQQPIVWPTTYLTVRAWHAAADRAGVLAANTSANVKKFVDRAEAATSPASRNNAAAQLRAVSNQVSGDSSQEVGLRNALLALADVVAR
>CP031165.1|AXV08299.1|4154938_4155067_+|hypothetical-protein
MGRWMHFGVLFLYVRGLPGGGIAADAAVRVGVTHDLGGPGPP
>CP031165.1|AXV08300.1|4155032_4155254_-|hypothetical-protein
MNTLVVALMLVAPPITSEAAPRPAVDVSARAIDVVHLDAPWCWLPGRSPDRALPELGGAWLDPTEDQGPPSRG
>CP031165.1|AXV08301.1|4155570_4156410_+|Xanthine-dehydrogenase,-FAD-binding-subunit
MTIARPTDLPSALDALTTMPGARPLAGGTDLQVEVNLGHRQPDAIVALRRIGELQGIGTTADVLDLGALTTYAQVEADLGDAAPGLAMAARTVGSPQIRNAGTIGGNLGTASPAGDTLPWLLAMDATVRLVGPRGTRDLGVAELVTGPKRTAMAADELITRVLVPRVDGPQHVAKVGPRTAMAIAIASVAVIVDTTSRRVRVGLGSVGPTPIRPTAAEAMIDDAMDWAALHAPHDAITRFGDLCAAAASPISDHRSTADYRRHAVGVIAARTLERCLQR
>CP031165.1|AXV08302.1|4156406_4156928_+|Xanthine-dehydrogenase-iron-sulfur-subunit
MTDPSVDPYPLSVNGADHAVRTSWLGESLLYVLRERLGFPGSKNACDQGECGSCTVLMDGLPVCACCVMAADAVDAEITTVEGLAAGGAPTDVQQAFLDAGAVQCGFCTPGLIVATTDLLDRVPDADVPTIREALSGNLCRCTGYGRIIEAVEMVRDRRRVDTGVPDAGTEDS
>CP031165.1|AXV08303.1|4156930_4159303_+|Xanthine-dehydrogenase,-molybdenum-binding-subunit
MIVTGLSDTATPTTPLTGALGDSADRPDGMPKVTGDFAFSSDLHAEGMLWGRTLRSPHAAARIRSIDTSRATAMAGVHAVLLAEDVPGSPTYGMEHRDQPVFASDVVRYHGEPVAAVAADHPELAVRALAAIEVDYEPLIPLADADAAITAPPIHPDGNVFRHIPLRHGDPDGVDTSDLVTVEGTYEVGMQDQAFLGPESGMAIPDGDGGVDLWISTQWLHVDRDQVADCLGLPRGKVRLALAGVGGAFGGREDVSLQIHACLLALATGRPVKMLYSREESFYGHVHRHPARLWYRHHATRDGDLVKVEARVLLDGGAYASSSTAVIANATCFAAGPYRIPHAAIDGWAVRTNNPPCGAMRGFGAVQTCFAHEAQMDRLAEALDMDPVALRLRNALATGDTLLTGQVITGTAPVKEVIEAAMAHPLPPVHSGDDPPQLLPGGTGMTSTADHVRRGVGMAVGFKNLMFSEGFDDHSTAAVTLELDANGHPVATAQCAAAEVGQGFHTLALQILRSELGVQQVMLGPTDTSIGSAGSTSASRQTWMSGGAVQLACHAVRDELFARASARWDIPTAGARRRMLALRDGEVVEVDGARRIPLADLLADGPIRMIREHHHPPTEPLDANGQGNAHVSFAFAAHRAVVDVDPDLGLLRVVQVTTGQDVGRVLNPRAVVGQIEGGIAQGVGLAIMEEVLVHDGLVRNPSFTDYLIPTMLDMPEVLATVIEQPEPGAPFGAKGVGEPPTISSTPAVVAAIRDATGAALIRVPVRPQDIALPSMASGSASAPADGAEAR
>CP031165.1|AXV08304.1|4159299_4160604_+|Guanine-deaminase
MTDATGRLVVRGARHPGDIAVRDGWIEAIGTVEAQEGDTVLHVDGDIVTAGLVNTHHHLYQWMTRGRATGCNLFDWLTTLYPIWARIDVEDVLAAARVGLAELALSGCTTAADHHYLVPRGDDSVFDALATATTEVGTRLHLARGSMDLGESRGGLPPDDVVEDLDDILASTERVIGRWHDAERIVVTVAPCSPFSVSERLMRESADLARRHGLRLHTHLAETREEEADCLARFGKRPLAVLDGWGWVAPDVWFAHGIHFDDDEIARLAAVGAGVAHCPSSNARLAAGFCRTPELRAAGVPVGLGVDGVASNEQGTLITELRQALWSARQGAQDPSALSAAEALEMGTIGGAACLGRRDIGRLAVGARADLVVWPGDDVADIPDPVEAIVLGPDRRARHVLVGGQPIVTDGTLLGMDLHAARTDLAVRARRLWG
>CP031165.1|AXV08305.1|4160581_4161847_+|drug-resistance-transporter,-EmrB/QacA-family
MPGGCGADRVSSARNGRPPGAAGPSGPDGTPDPGGTSAGLSREVRLALVAVVIARLGINGGIRVVFPFLPAIARGLGTTLAVMGVLVAARSLVGTMAPLAASLGERTGRRAVMLGGLAATAIGSAVIGLAPSVVVAAVGFVLVGLGKPLFDVPMQGWFGARVPYAKRGRVLGITELTWAGGLLATVPLSGWLISRTSWRIQFLPVIVLVVAGLLAVAVLMRNDRPPSRVRTTLALTRPRVAMLAVVGLFSFAAESLFVVYGAWLEADLGFDVGAIGAFTVLVVAAELTGEGGVAALGDRIGLHRAVRVALVVSTVAYLTLLTVGNSVPLAILAVVIWFVGYEVSIVASVPLVTELGGEGRDRLLGLMVGVLAGGRAVGALVAPQLFALGGIGAMAVVSAVSVAIAAVLMATLVPVPRRWVG

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Crispr_ID: CP031165_22

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_22

5248122-5248239

Orphan

Consensus_repeat	Method
CGCGTGTCGAGCAATCGGCCGCCCGTCGCAGGAACCCGACAAGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_22

>merge|CP031165|22|5248122-5248239|CRISPRCasFinder
CGCGTGTCGAGCAATCGGCCGCCCGTCGCAGGAACCCGACAAGCGACCGGGGCCGGCCCACCCCTCGAACCCACGCGTGTCGGGCAATCGGCCGCCCGTCGCAGGAACCCGACAAGCG

>CP031165|22|21|5248122-5248239|CRISPRCasFinder
CGCGTGTCGAGCAATCGGCCGCCCGTCGCAGGAACCCGACAAGCG	ACCGGGGCCGGCCCACCCCTCGAACCCA
CGCGTGTCGGGCAATCGGCCGCCCGTCGCAGGAACCCGACAAGCG

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV09279.1\|5256183_5256756_-\|Thiol:disulfide-oxidoreductase-related-to-ResA	unknown	unknown	gnl\|CDD\|239264
CP031165.1\|AXV09263.1\|5237849_5239040_+\|O-succinylbenzoic-acid--CoA-ligase	unknown	unknown	gnl\|CDD\|341285
CP031165.1\|AXV09278.1\|5255371_5256187_-\|Cytochrome-c-type-biogenesis-protein-CcdA	unknown	unknown	gnl\|CDD\|280792
CP031165.1\|AXV09266.1\|5240457_5243184_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224054
CP031165.1\|AXV09268.1\|5244043_5245864_-\|acyltransferase-family-protein	unknown	unknown	gnl\|CDD\|224748
CP031165.1\|AXV09261.1\|5236857_5237718_-\|1,4-dihydroxy-2-naphthoate-polyprenyltransferase	unknown	unknown	gnl\|CDD\|235695
CP031165.1\|AXV09272.1\|5249044_5249566_+\|Shikimate-kinase-I	unknown	unknown	gnl\|CDD\|238260
CP031165.1\|AXV09271.1\|5248289_5249048_+\|Transcriptional-regulator,-TetR-family	unknown	unknown	gnl\|CDD\|224228
CP031165.1\|AXV09275.1\|5251834_5252095_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237910
CP031165.1\|AXV09264.1\|5239100_5239355_+\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV09262.1\|5237714_5237858_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV09269.1\|5246097_5246826_-\|Aspartate-racemase	unknown	unknown	gnl\|CDD\|224707
CP031165.1\|AXV09277.1\|5253534_5255064_-\|Ccs1/ResB-related-putative-cytochrome-C-type-biogenesis-protein	unknown	unknown	gnl\|CDD\|377471
CP031165.1\|AXV09276.1\|5252380_5253538_-\|Cytochrome-c-type-biogenesis-protein-CcsA/ResC	unknown	unknown	gnl\|CDD\|274447
CP031165.1\|AXV09267.1\|5243215_5244019_+\|putative-integral-membrane-protein	unknown	unknown	gnl\|CDD\|372253
CP031165.1\|AXV09280.1\|5256752_5257592_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV09273.1\|5249588_5250896_+\|archaeal-ATPase,-fused-to-C-terminal-DUF234-domain	unknown	unknown	gnl\|CDD\|224586
CP031165.1\|AXV09270.1\|5246944_5248114_+\|Membrane-protein	unknown	unknown	gnl\|CDD\|366370
CP031165.1\|AXV09274.1\|5251023_5251698_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV09265.1\|5239368_5240421_+\|internalin,-putative	unknown	unknown	gnl\|CDD\|225156

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV09279.1\|5256183_5256756_-\|Thiol:disulfide-oxidoreductase-related-to-ResA	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	1.93158e-31
CP031165.1\|AXV09263.1\|5237849_5239040_+\|O-succinylbenzoic-acid--CoA-ligase	gnl\|CDD\|341285	cd17630, OSB_MenE-like, O-succinylbenzoic acid-CoA ligase. This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.	1.58201e-73
CP031165.1\|AXV09266.1\|5240457_5243184_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	3.71999e-86
CP031165.1\|AXV09268.1\|5244043_5245864_-\|acyltransferase-family-protein	gnl\|CDD\|224748	COG1835, COG1835, Predicted acyltransferases [Lipid metabolism].	5.17595e-57
CP031165.1\|AXV09261.1\|5236857_5237718_-\|1,4-dihydroxy-2-naphthoate-polyprenyltransferase	gnl\|CDD\|235695	PRK06080, PRK06080, 1,4-dihydroxy-2-naphthoate octaprenyltransferase; Validated.	1.21878e-96
CP031165.1\|AXV09272.1\|5249044_5249566_+\|Shikimate-kinase-I	gnl\|CDD\|238260	cd00464, SK, Shikimate kinase (SK) is the fifth enzyme in the shikimate pathway, a seven-step biosynthetic pathway which converts erythrose-4-phosphate to chorismic acid, found in bacteria, fungi and plants. Chorismic acid is a important intermediate in the synthesis of aromatic compounds, such as aromatic amino acids, p-aminobenzoic acid, folate and ubiquinone. Shikimate kinase catalyses the phosphorylation of the 3-hydroxyl group of shikimic acid using ATP.	1.47421e-33
CP031165.1\|AXV09271.1\|5248289_5249048_+\|Transcriptional-regulator,-TetR-family	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	2.12698e-13
CP031165.1\|AXV09275.1\|5251834_5252095_+\|hypothetical-protein	gnl\|CDD\|237910	PRK15103, PRK15103, membrane integrity-associated transporter subunit PqiA.	0.00231403
CP031165.1\|AXV09277.1\|5253534_5255064_-\|Ccs1/ResB-related-putative-cytochrome-C-type-biogenesis-protein	gnl\|CDD\|377471	pfam05140, ResB, ResB-like family. This family includes both ResB and cytochrome c biogenesis proteins. Mutations in ResB indicate that they are essential for growth. ResB is predicted to be a transmembrane protein.	8.26899e-92
CP031165.1\|AXV09276.1\|5252380_5253538_-\|Cytochrome-c-type-biogenesis-protein-CcsA/ResC	gnl\|CDD\|274447	TIGR03144, cytochrome_c_biogenesis_protein_chloroplast, cytochrome c-type biogenesis protein CcsB. Members of this protein family represent one of two essential proteins of system II for c-type cytochrome biogenesis. Additional proteins tend to be part of the system but can be replaced by chemical reductants such as dithiothreitol. This protein is designated CcsB in Bordetella pertussis and some other bacteria, resC in Bacillus (where there is additional N-terminal sequence), and CcsA in chloroplast. We use the CcsB designation here. Member sequences show regions of strong sequence conservation and variable-length, poorly conserved regions in between; sparsely filled columns were removed from the seed alignment prior to model construction. [Energy metabolism, Electron transport, Protein fate, Protein modification and repair].	2.59006e-50
CP031165.1\|AXV09269.1\|5246097_5246826_-\|Aspartate-racemase	gnl\|CDD\|224707	COG1794, RacX, Aspartate racemase [Cell envelope biogenesis, outer membrane].	2.81748e-89
CP031165.1\|AXV09267.1\|5243215_5244019_+\|putative-integral-membrane-protein	gnl\|CDD\|372253	pfam12679, ABC2_membrane_2, ABC-2 family transporter protein. This family is related to the ABC-2 membrane transporter family.	4.81998e-08
CP031165.1\|AXV09273.1\|5249588_5250896_+\|archaeal-ATPase,-fused-to-C-terminal-DUF234-domain	gnl\|CDD\|224586	COG1672, COG1672, Predicted ATPase (AAA+ superfamily) [General function prediction only].	1.16816e-21
CP031165.1\|AXV09270.1\|5246944_5248114_+\|Membrane-protein	gnl\|CDD\|366370	pfam00924, MS_channel, Mechanosensitive ion channel. Two members of this protein family of M. jannaschii have been functionally characterized. Both proteins form mechanosensitive (MS) ion channels upon reconstitution into liposomes and functional examination by the patch-clamp technique. Therefore this family are likely to also be MS channel proteins.	1.40065e-21
CP031165.1\|AXV09278.1\|5255371_5256187_-\|Cytochrome-c-type-biogenesis-protein-CcdA	gnl\|CDD\|280792	pfam02683, DsbD, Cytochrome C biogenesis protein transmembrane region. This family consists of the transmembrane (i.e. non-catalytic) region of Cytochrome C biogenesis proteins also known as disulphide interchange proteins. These proteins posses a protein disulphide isomerase like domain that is not found within the aligned region of this family.	2.18845e-36
CP031165.1\|AXV09265.1\|5239368_5240421_+\|internalin,-putative	gnl\|CDD\|225156	COG2247, LytB, Putative cell wall-binding domain [Cell envelope biogenesis, outer membrane].	3.14301e-11

>CP031165.1|AXV09270.1|5246944_5248114_+|Membrane-protein
MPEAEIVEQATNAALSVGVLVVAGFLALGVHLLAVRGIFRLGRSDRFAQEATARAKWPARTTSILLGLLGGMLFTELPDGVTEGLTHTLLVLAIIGGTVTLMRLAVAVEVSILSGLDMDAEDNSWARGRTTRAILLRRISSALIIMVGVGSVLLTFETARTVGTSLLASAGILGLVVGVAAQSTLANIVAGIQIAVAEPIRIDDVVVVEGQWGNIEQLSLTYVVVRTWDRRRVVLPTSYFVSTPFENWSMYGQQIIGDVVWQLDHRVPMNAMRQEFHRMVDAHDLWDGDVAVLQVIEVTGPTVKVRGLVSAHNSHNAWDLRCALREGILVWLAEHHPYALPTTRLLEAAEDPSARRPTSPPPPPMRSPGPDDVPNPDPARTGEWPVVDR
>CP031165.1|AXV09269.1|5246097_5246826_-|Aspartate-racemase
MTTNRCLGLLGGMAWPSTLEAYRRLNRLVHDELGGVHSADLVVRSFDFAAVEALQADGDWDGAGRLLGAAAGGLRACGAQAVMICTNTMHRVEADVRRISGLPVLHIADATAAAVRDAGVERVGLLGTAYTMEGDFYRGRLAAHGLDVVVPDEPGRAAIHAIIYDELVNDVVTEDSRRVARQLVTDLVADGAQGVIAGCTEIELLIGSDDVDVHWFPTTEIHVDTAGGWLLGRPFPGPPPGV
>CP031165.1|AXV09268.1|5244043_5245864_-|acyltransferase-family-protein
MPALDGLRALAVMAVIVYHADAAWLPGGYLGVEVFFAISGYLITALLITEFDRTDRIDFVDFWKRRAKRLLPALAVLLIGVALLAMFTARDALGSLWGQSVAASTYVMNWSLIATEQSYFESFGRPPLLQHLWSLAIEEQFYLLMPTLFLAGRRLLGRRITLGVVLAGIVASVALMWTGFDPTVDPSRLYYGTDTRAAGILVGVAMAMVWRPWVAGGPLTERLRASAWPDIAGVVGLLVIGHQLWTLGAYDARLYRGGFLLIAIATVAVVAAVANPGSLVAVPLSAKPLRWIGQRSYGLYLWHWPVFMVLRPGVDTIVSEPWLTVLRLSATVALAELSFTFIERPVREGRFGQQVIALFRSAPETPALRRGVAIVAISGVSLFAVGNVQLARQSPAAAAPIELATTDGTTPSYIPKGVRGGVMVAEHVDGPPTPLSTEEPAGEPVVDPDTLPAYDFPQVFVVGDSVMVGAAEQVETLDGVVMDARIGRQWHELLEMPEVDPGPDDAVVIHLGNNGAVTTDTLDAVLERFADAGRVVLVTVRVPRPWESQVNRALSGATGRYPNTVLADWQGASDGTPNWFGGDGVHLTQSGAKALRDTIAYALRVD
>CP031165.1|AXV09267.1|5243215_5244019_+|putative-integral-membrane-protein
MGAELSRQLRRRRTLLGLGGLALVPVLLALAFALTTGDGDGGGGDPTGLFDLTRLSALNFTITCVAATAPFLLLSVIALFTGDPVSSEASWGSLRYLLTRPVSRTRLLGRKLVVGLGLSVAAGLVVVVSGLIAGTIAFGWGPVETPFGALAEGEAIVRILAILGYVLWNGAWVACLAFALSVVTDEPVGAVAGTIVLVIVVQILDNITALGDVRQWLPVHESAAWLGLLADPPRWGDLVRGMWLQIPWAALFLGFAWWRFLRRDVLS
>CP031165.1|AXV09266.1|5240457_5243184_+|ABC-transporter-ATP-binding-protein
MRRALAGVAVLVLAVVGLVIAGRDTPVAEESLTVEVSSPAGDPSVTLDAGLYVADGVTLPAPALLLAHGFGSDRSSLDETARAWAREGHVVLTWSARGFGASGGTIGLNDPDREIADVSELVDLLVGRPEVQQDATGDPRVALAGGSYGGGAALMAGTTEPRLDAIVAVAAWHDLARALSPAATGGTGVLKEQWVSLLFTSALLGGIDEPAPSSIPAQATPAVPGLCGRFDPAICALYVEAARTGVLAPEDAALLTARSPAGRLADAAAPTLLVHAMDDTLFSLGQSLANAEELVTADVPFALRWVAGEHGGLPGPDSPAGREMAMWLDRWLAGEDDGVPPTFSWYDAVAGGDVTPEAEPGTVLGPTASTSWVLADGTLVPRSEVEDDRPEDSDGVAGSLVVAHPPGGLPAALSSLPGLGALAGLLPAIDVPGQSVSVETAALDDDLVLVGRPTLDLEITGLEQPAPSTADAPAPALLAKLYDVTPGGSATLLHSTVTPLRATVGRLEVPLEPVAHRFVAGNRLRLVLATTDQALSTGRDPSIVMADGSTLSLVLPVTTPPRTTTLPALVRVLVPVVLVVAAALLAALVLRRRDAHVAAAAARPDAPAVVIERLAKRYADGKVAVDGLDLVVERGQVFGLLGPNGAGKTTTMRMLLGLITPTEGTVEVLGHRMTPGHPVLHRVGVLVEGPGFAPYLSGRRNLETYWRVAGRDPAEADMDRALSVADLGDAIDRPVRTYSHGMTQRLAIAQSLLGGPDLLVLDEPTDGLDPEQIRGMRQLLARLGREGITVLVSSHLLAEVEQMCTHAAVVQHGRVLVSGPVAELRGASRSIVVRTDDHDRAATVLAAALDLDRIDVEGDGLVVHLGDDGRVTSPAVLAALVAAGIGVESLTPRGRLEDVFLDLTGGTP
>CP031165.1|AXV09265.1|5239368_5240421_+|internalin,-putative
MRRRDPDDQQGWGDVPTSRLEHPFFRLVQVLVLAAVILYGLNELGLLSREIRDVRVVRVTGEDPIRVAASAAREAHGGRAETVVIVSVDALADGVAATGLAGILEAPILLNEATLVSPQTRDVIRELDTERAILIGGTSALNGVVERTFADEMGLETIRIAGNSRFDTAVRVAQLFTDNGEVGVLDGLRTALVVPAEDVATGLAAGGLAAGRAAPLPVLYSQSGALPGPTVDALARMGIEQVVTASPITVFDGRVITVSGPVDVADTATELREFQPSRVVIVPDGDDARALVGGPVAGLESGVIMPFSLAQDWLEANCGTVAELFVIAEDTVVTDADLEVLRRAATACGD
>CP031165.1|AXV09264.1|5239100_5239355_+|hypothetical-protein
MAAIPAEPTSPVIANLVVLAGFVAIFSTFVTDSPFSWIVGAIMVVAGGIWAGFVGNGTVDEAVVPDTAGTHVDASEGQTNGGAA
>CP031165.1|AXV09263.1|5237849_5239040_+|O-succinylbenzoic-acid--CoA-ligase
MTHDGSATHGSGRLLLAVEATPEKMDAALRDAWAGGPAVLPLDPRLPPRARGGLVADLKPGAIVKPGGLIALPGGQPVPDDTVVVVPTSGSTGKPKGVMLSRSAVEASTTLGLDATGSDPDVPWLCCLPTSHVAGVLVLLRAIVTGTPAVLHDGFDVEAIRALDGPVHLAVVPTMLRRLLDAGADPDGWGTVLVGGARLTDGLVERVPGLTTTYGSSETSGGCVYDGVPLPGVDVGTTDDGRLTIGGPTLMTGYRTTTPGTGQGLVDGRFVTSDVGEVGADGRVTVIGRADDVIVTGGEKVVAASVASLLEQHPAIAEAEVVGVPDAEWGQRAVAVVVPDQVGAVLSLAILRSFVAERMPRYAAPRDLVVVNALPRLPSGKVDRLALQRAVAAEAQ
>CP031165.1|AXV09262.1|5237714_5237858_-|hypothetical-protein
MGHGAVVSHGRHGIRPMPPPHRGWRSTRCGPVGRVCHPDLYPYDLNP
>CP031165.1|AXV09261.1|5236857_5237718_-|1,4-dihydroxy-2-naphthoate-polyprenyltransferase
MNPYVEAARPRTLTAAVAPVIVGTATAATFVAWRALAALIVSVSVQVAVNYANDYFDGVKGVDTEARLGPRRAVASGMISPPAMKRAIRNAFVVTGLAGLALAAATTWWLLAVGALCFLAALGYSGGPKPYASAALGEVFVFVFFGLVATVGSAFVQDEAVTVTAVLAAVPVGLFAVAILIANNLRDIPTDELAGKRTLAVVLGDRGTRHLLTGTIIGAFAFLGVIGLSVGSAWPFLALLAAVPIARPLEDVREGAAGPGLIPVLGGIARTQLAFAVLLTIALVLA
>CP031165.1|AXV09271.1|5248289_5249048_+|Transcriptional-regulator,-TetR-family
MPSASPVGRRPDTGTRGDRTRAAVVAAARDRFAAEGFERATGARIAADAGVSEPSIAFHFGSKAGLLVAVMQDYYDDLLQRMDAVIDSADAPLDRLRAFARWWMPHTAAHQPLMAVFGRQGRRTTSDEVVEAFRACNRRVTRVMDRLIDDLVHTGVLRPEVSTRVVRDAFFGTTEHLLLGHAATGRPTDLAAAADDVVDLLINGAGIAPDAGRSTRPTHTPDAPDLATMDAKLDRVLARLDELGTSQDRPPR
>CP031165.1|AXV09272.1|5249044_5249566_+|Shikimate-kinase-I
MTDRPVVVLGLMGAGKTTVARLIAQHLGRPLRDSDADIEAATGHTAATLAAGPDGRRRLHDLEAEHVLSALAEGPVVVAAAASVVERPVVRTALAPACVLWLDAPPEVLAARMTSSTHRPDYGEPLEVVQALDRRRRPLFTAVADVVIDASKPTETVQRNALAAVDVTPPPYT
>CP031165.1|AXV09273.1|5249588_5250896_+|archaeal-ATPase,-fused-to-C-terminal-DUF234-domain
MPKFVNREQELRALTRACNPGMAVVSGRRRVGKTALLDHFSTERASVFLPGTRAPIGEALRRLEERVRAVVPPLAGDLLDLGHFETWDTALGYLIARSSDDPLLLVLDEFPYLCEADPSLPSTLQARWDHRGESQLSIILAGSHVGLMEELVSTDAPLFGRPDMHLRLGPFSWQHAPLLVGGDDPDVWMEAYVTLGGMPRYLALWDPRHDAATNLAELLDGPGAPLGDEGTVVLQELTPGSAAARVLELVALDASTFTTIRDRAGLAPATTSEALTSLERLGLLDRITPAGEDPRRTRKVRYRVRDPFLRLWLGVVLPHRDAFELGRGAAVLRRKADRIAASQAAAWRSVAADWMAEQTGVSCGEWWGGPGEDVVDVLGVDGAHPVVAASCHWAAGVDGGVWRDRLVQAMSATPDEVHVMARSGTGVLTPAALHR
>CP031165.1|AXV09274.1|5251023_5251698_-|hypothetical-protein
MRARLSTLIALFAIAALALPAGATPVPGDPDFLPTLRTEQTFFHCASAVKVQNVDAIQGNTPSWDTTAPTTSFTAGGGCGFYDNILSGTAVAGPTNSAIWTGTFDGNLDSIEVELHRLLAGAGGSVTFPALVMTLTVDGSVVYDGDVEGFMWLPSSTGASESATMTFTDLGYLTEHGDGFETREITLQVDSYNEAQTAWVFDASEVPAGLTFNPATATFPTVKV
>CP031165.1|AXV09275.1|5251834_5252095_+|hypothetical-protein
MGFVTNDPKKSDEQQPGATGLIVDLGLMSCPECRREVPEWQDDCPDCGVRAVPRASLGSQVPDVPAHLLGDDDDDDDDDTSSDTDG
>CP031165.1|AXV09276.1|5252380_5253538_-|Cytochrome-c-type-biogenesis-protein-CcsA/ResC
MTDLALAETSNSLFNVAFFVYLIAMIAYFFRLAFTRVSADGVQTSTVAGRRVGHFGLAVLLGGFAVHLTSFVMRGVAAGRVPWGNMYEYGSGIALLSIATALVVVQRRYGHLVGFVIAGSLLMMTTSLLLFTDAGPLVPALESYWLQIHVSAMMFSSSVFIVGFVATALYLVKDRAETKLARTSSFTGSTVGAARSATVTPRGEGDIEGRVADVDVDPEEVQVASATAQRDVLNPVLFPVIPFVGVLLFVLVVWRAPVPAMLAASVAALIGSSVWYAVPYLPPAAKLDNLAYRTTAFAFPLITFGIMCGAIWAEEAWGRYWGWDPKETGSFVTWVLYASYLHARSTYGWRGRRAAWVGVTAFTALLITYYAVNLFVVGLHSYAGV
>CP031165.1|AXV09277.1|5253534_5255064_-|Ccs1/ResB-related-putative-cytochrome-C-type-biogenesis-protein
MSTALVLLFALAVATLIATFIPQEPVIASTVRLWRTGEEGPGAAVSGVLDALSLYDVFGSWWFGVLTVLLFVSLTGCLVPRWAAFARNVRKPPVRGRNLDRLTHRAELSVPPGMSESDVLDRAGRAFRTYRTRVITSEQHAPQLAIERGHWREFGSLVFHSSFYVLLIGVTLGAAFTFTGQIDFEEGARFADTPVGYDTFTAGTLWDTDRHNGHTTTLDAFEVTYLPDGFTPDDFVSTVTFTSADGERTVTEDIRVNHPVHFDGLTYYQRAFGFAPTVALRSGLNGAELFEDQLILRQDGGFWTGRGKVSVGNPAADPPLPQIAVEVLFLPDAEFAEDGTVQFNSPEANDPRLLVTLYLDDDLGLDRTVPISRLDWPESAVVDRAMIVPGTPVALAGGLFEVEFADLSMWSGLQISHQPYRWLILTGASMVLMGLIPSLYAYRRRLWVEVRDDRIVVAGVALHRRDRFAETFDDVVDRVAGTLGTDRIPAPSRSNPPSTPQIDPQGSHT
>CP031165.1|AXV09278.1|5255371_5256187_-|Cytochrome-c-type-biogenesis-protein-CcdA
MIPMPAQLVFAQAGDIAQQAQSAITDANLLVAAGVALIAGIVSFASPCVVPLVPGYLAYMTGLSGADIREGGGGAAARARVLSGGLLFVLGFAIPFTLLGLTAGSLSRTLATRPWQIGLGLMVMLLGIAFTGLLPFDFLRREARITDNAIDKGVLGALPLGFVFGVGWTPCIGPALAAILTLSVTSGGGSSVRGGVLAFVYAVGLGLPFILFGLLFNRLGRVLGFLRRNAGRLQIGGGVMLALVGLAIATGLWDRFIEWTRPFISGFEPPI
>CP031165.1|AXV09279.1|5256183_5256756_-|Thiol:disulfide-oxidoreductase-related-to-ResA
MIRHAFTRTSAALLLAFAVFGSACTLGISENEAGAGSTFIGSLELIDPADREPAPDVCGTTTADEELCLDALVGTPTLVNFWASWCGPCAREIPELVELDSTRDDLHIVGVNVQDSIVNARSFERDQGVTYPSWFDEGSIIAGAFGGIAPEALPSTILLDREHRVAIRLFGAVTMADLVPFLDQLSSETG
>CP031165.1|AXV09280.1|5256752_5257592_-|hypothetical-protein
MSTLTSLIVLATEGGIPADSPWAKLAVPLGILLFVGPIFMLLRSNLGTRLGYLVMSVTLWGSIFLFALFWTFGAPGTPAFTGPQNLPGQELDEYLPIWVPLAQDALAVTEEGSPYSVIAGYPDGFQDEPTIEEDLLEDGISEIGNVFAGLSEPYTSLLTGLEEPVEVQYATSDNDRPIIAVTYADTCQMDNDGNLPAGCEEVGAIAPEGSDARGEDITLFAFFDAGAPAFPSYLMLGGTALLFGLHMVLLARDESRTTREQMAEAEESVEVEEKATVSA

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Crispr_ID: CP031165_24

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031165_24

5460437-5460550

Orphan

Consensus_repeat	Method
CCGCTTGTCGGGTTTCGGGCCGCCCGTCGCAGGAACCCGACA	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP031165_24

>merge|CP031165|24|5460437-5460550|CRISPRCasFinder
CCGCTTGTCGGGTTTCGGGCCGCCCGTCGCAGGAACCCGACACGCGGCCGCGGGGCCGGCCGACACGACCACCCGCTTGTCGGGTTTCGGGCCGCCCGTCGCAGGAACCCGACA

>CP031165|24|23|5460437-5460550|CRISPRCasFinder
CCGCTTGTCGGGTTTCGGGCCGCCCGTCGCAGGAACCCGACA	CGCGGCCGCGGGGCCGGCCGACACGACCAC
CCGCTTGTCGGGTTTCGGGCCGCCCGTCGCAGGAACCCGACA

Protein	Signature genes	Signature genes Name	Protein_function
CP031165.1\|AXV09449.1\|5456906_5457818_+\|6-phosphogluconate-dehydrogenase,-decarboxylating	unknown	unknown	gnl\|CDD\|236582
CP031165.1\|AXV09461.1\|5465006_5465264_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|340560
CP031165.1\|AXV09454.1\|5461083_5461530_-\|Integral-membrane-protein	unknown	unknown	gnl\|CDD\|379566
CP031165.1\|AXV09444.1\|5451674_5452142_+\|Thiol-peroxidase,-Bcp-type	unknown	unknown	gnl\|CDD\|224146
CP031165.1\|AXV09455.1\|5461569_5462304_-\|Phosphoadenylyl-sulfate-reductase	unknown	unknown	gnl\|CDD\|234997
CP031165.1\|AXV09458.1\|5463032_5463344_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV09460.1\|5464374_5465004_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV09452.1\|5460058_5460436_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224955
CP031165.1\|AXV09453.1\|5460580_5461084_-\|thioredoxin	unknown	unknown	gnl\|CDD\|239245
CP031165.1\|AXV09445.1\|5452234_5453737_+\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	unknown	unknown	gnl\|CDD\|238923
CP031165.1\|AXV09448.1\|5455999_5456722_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV09457.1\|5462682_5463036_-\|hypothetical-protein	unknown	unknown	unknown
CP031165.1\|AXV09446.1\|5453733_5454627_+\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	unknown	unknown	gnl\|CDD\|143635
CP031165.1\|AXV09450.1\|5457911_5459363_+\|Glucose-6-phosphate-1-dehydrogenase	unknown	unknown	gnl\|CDD\|237234
CP031165.1\|AXV09451.1\|5459362_5460019_+\|6-phosphogluconolactonase,-eukaryotic-type	unknown	unknown	gnl\|CDD\|238694
CP031165.1\|AXV09459.1\|5463345_5464317_-\|putative-TRANSCRIPTIONAL-REGULATORY-PROTEIN	unknown	unknown	gnl\|CDD\|376492
CP031165.1\|AXV09462.1\|5465342_5466023_+\|GlnR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223816
CP031165.1\|AXV09447.1\|5454664_5455594_-\|Folate-dependent-protein-for-Fe/S-cluster-synthesis/repair-in-oxidative-stress	unknown	unknown	gnl\|CDD\|223431
CP031165.1\|AXV09443.1\|5450688_5451636_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237974
CP031165.1\|AXV09456.1\|5462297_5462675_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376874

Protein	Function_ID	Function_description	E-value
CP031165.1\|AXV09449.1\|5456906_5457818_+\|6-phosphogluconate-dehydrogenase,-decarboxylating	gnl\|CDD\|236582	PRK09599, PRK09599, NADP-dependent phosphogluconate dehydrogenase.	0
CP031165.1\|AXV09461.1\|5465006_5465264_-\|hypothetical-protein	gnl\|CDD\|340560	cd17040, Ubl_MoaD_like, ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins. Ubiquitin-like (Ubl) domain found in a group of small sulfide carrier proteins This family includes ThiS, MoaD, CysO, QbsE, and their homologs, which are structurally homologous to ubiquitin (Ub) and may function as the sulfide donor for the biosynthesis of thiamin, molybdopterin, cysteine, thioquinolobactin, and other sulfur-containing natural products. Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Ubiquitination is comprised of a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of Ub and the epsilon-amino group of a substrate lysine. Like Ub, small sulfide carrier proteins in this family are adenylated at a diglycyl C-terminus by specific activating proteins. The adenylated C-terminus is subsequently converted to a thiocarboxylate, serving as the sulfide source. Those activating proteins are diverse and show little sequence similarity. This family also includes the small archaeal modifier protein (SAMP), including SAMP1, SAMP2 and SAMP3, which are Ub-like proteins that function as protein modifiers and are required for the production of sulfur-containing biomolecules in the archaeon Haloferax volcanii. SAMP1 and SAMP2 are involved in sulfur transfer during molybdenum cofactor biosynthesis and tRNA thiolation much like MoaD and Urm1, respectively. They can form covalent conjugates with their protein targets through an isopeptide linkage via their C-terminal diglycine motif in a streamlined archaeal E1-dependent pathway. SAMP2 also forms homo-conjugates through the intermolecular isopeptide bond between the C-terminal Gly and the Lys58 side chain, a feature that likely resembles polyubiquitination. SAMP3 conjugates are dependent on the Ub-activating E1 enzyme homolog of archaea (UbaA) for synthesis and are cleaved by the JAMM/MPN+ domain metalloprotease HvJAMM1.	2.558e-14
CP031165.1\|AXV09454.1\|5461083_5461530_-\|Integral-membrane-protein	gnl\|CDD\|379566	pfam14340, DUF4395, Domain of unknown function (DUF4395). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 142 and 168 amino acids in length. There are two completely conserved C residues that may be functionally important.	1.64822e-31
CP031165.1\|AXV09444.1\|5451674_5452142_+\|Thiol-peroxidase,-Bcp-type	gnl\|CDD\|224146	COG1225, Bcp, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones].	6.82837e-76
CP031165.1\|AXV09455.1\|5461569_5462304_-\|Phosphoadenylyl-sulfate-reductase	gnl\|CDD\|234997	PRK02090, PRK02090, phosphoadenylyl-sulfate reductase.	1.648e-97
CP031165.1\|AXV09452.1\|5460058_5460436_+\|hypothetical-protein	gnl\|CDD\|224955	COG2044, COG2044, Predicted peroxiredoxins [General function prediction only].	4.08596e-05
CP031165.1\|AXV09453.1\|5460580_5461084_-\|thioredoxin	gnl\|CDD\|239245	cd02947, TRX_family, TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.	1.48154e-14
CP031165.1\|AXV09445.1\|5452234_5453737_+\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	gnl\|CDD\|238923	cd01948, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.	5.43698e-91
CP031165.1\|AXV09462.1\|5465342_5466023_+\|GlnR-family-transcriptional-regulator	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	3.11617e-41
CP031165.1\|AXV09446.1\|5453733_5454627_+\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	5.82625e-57
CP031165.1\|AXV09450.1\|5457911_5459363_+\|Glucose-6-phosphate-1-dehydrogenase	gnl\|CDD\|237234	PRK12854, PRK12854, glucose-6-phosphate 1-dehydrogenase; Provisional.	0
CP031165.1\|AXV09451.1\|5459362_5460019_+\|6-phosphogluconolactonase,-eukaryotic-type	gnl\|CDD\|238694	cd01400, 6PGL, 6PGL: 6-Phosphogluconolactonase (6PGL) subfamily; 6PGL catalyzes the second step of the oxidative phase of the pentose phosphate pathway, the hydrolyzation of 6-phosphoglucono-1,5-lactone (delta form) to 6-phosphogluconate. 6PGL is thought to guard against the accumulation of the delta form of the lactone, which may be toxic through its reaction with endogenous cellular nucleophiles.	7.24752e-37
CP031165.1\|AXV09459.1\|5463345_5464317_-\|putative-TRANSCRIPTIONAL-REGULATORY-PROTEIN	gnl\|CDD\|376492	pfam01206, TusA, Sulfurtransferase TusA. This family includes the TusA sulfurtransferases.	4.45741e-10
CP031165.1\|AXV09447.1\|5454664_5455594_-\|Folate-dependent-protein-for-Fe/S-cluster-synthesis/repair-in-oxidative-stress	gnl\|CDD\|223431	COG0354, COG0354, Predicted aminomethyltransferase related to GcvT [General function prediction only].	1.44902e-32
CP031165.1\|AXV09443.1\|5450688_5451636_+\|hypothetical-protein	gnl\|CDD\|237974	PRK15489, nfrB, glycosyl transferase family protein.	1.77925e-07
CP031165.1\|AXV09456.1\|5462297_5462675_-\|hypothetical-protein	gnl\|CDD\|376874	pfam02635, DrsE, DsrE/DsrF-like family. DsrE is a small soluble protein involved in intracellular sulfur reduction. This family also includes DsrF.	1.10013e-07

>CP031165.1|AXV09452.1|5460058_5460436_+|hypothetical-protein
MPDPAPPRLLVVKATHAADDPERANLACNVAAAGVAGGAEVHLFLAMEGVRLALPNIGRVIEVEHAAGVEELLEAVYAAGSVTVCTPCAARRGLEPAAFRDGTAMGGSALFVELATRPNATALVY
>CP031165.1|AXV09451.1|5459362_5460019_+|6-phosphogluconolactonase,-eukaryotic-type
MADTPTLEVLPDEAAVAARTAELITDVLAQPLPAGRTAPRAVALSGGGTPKAMYPLMAAVGTVPWSDVHVLQVDERQVGEDDPARNWLAIRDTLVIPTGAVGHPMPLEGDDYPVPEVVDVAQLGIGTDGHTASLIPGDPVLDVTGVDVARAGPYQGAVRLTLTAEAINRVGVLVWQIVGADKHEALERLMDGDTSIPAGLIRRGPRVVVVADRAAARG
>CP031165.1|AXV09450.1|5457911_5459363_+|Glucose-6-phosphate-1-dehydrogenase
MGDRDLTPPDAVIVLFGGNGDLARRKLIPSLWDLHRAGLMPEQWVLIGASRSDMADEAYGEFAREALAEFDREVSADDQDAFTEFASHLRYRGGGFDADDPSRIADAVAEAEQEMGGEPTRLFYLAVPPSAFGPITEGIGAAGLDQRARVVFEKPFGTDAESFAELDDTVRSVLTEEQIYRIDHFLGKETLQNVLALRFANGMFEPVWNRQHIDHIQIDSPESIDIGSRASFYESTGALRDMVVTHLFQVLSIIALEPPVSLDPSPLMDEKRKVFESMSTLRCEDVVFGQYEGYTESEGVAADSTTETFVAARIEIDNWRWAGVPIYLRTGKAMAEKRQTMTLAFKRPPRQMFAAHGLRADAHDHLTLDMAGDQGVTVSFLAKRPGPRLRLGQASMRFSYEQDFGATGGVQLDAYERLLHDALLGDRTLFTRADGIGRTWELVKPILERPPRVLPYARGSWGPEAATELIAPRTWHLPEDHEH
>CP031165.1|AXV09449.1|5456906_5457818_+|6-phosphogluconate-dehydrogenase,-decarboxylating
MQIGMVGLGKMGGNMTVRLLRGGHDVVAHDVSAEAVASAAEAGATGVDSLEALVAAMPAPRIVWVMVPSGEITERTVRTLGGLMDAGDVIVDGGNSRFSDSVALAASLAEDGVLMVDAGTSGGIWGLEEGYCLMVGGTNEAIERLSPALETLAPPDGWAHVGPVGAGHYVKMIHNGVEYAMMQAYAEGFELMAAGDFGIDLHQVAEVWRHGSVVRSWLLDLTARALDADPGLEELDAWVPDSGEGRWTVQTAVDLAVPTPTIAAALFNRFASREDNAFGQRLLAALRNQFGGHAVKPAEGGHE
>CP031165.1|AXV09448.1|5455999_5456722_-|hypothetical-protein
MEVIMLTTRFRTLGFVLAAFGMVFLIGGGYAWTQVSAGYDSLEAFSEAQNVTLSYNEDGQLIDRGETAGAEAIMTLLTEDWGYPVVEADFDPADPLVNTASEYMYQMATVGYHVLHGTQTVVLDEPVEFNGETFDAGTYEFDVDGRYWTGFDRTHPIEGPAREMAWSGTVHGLFGELGVGTVTASTLQLGTGIAALVAGIGATLVVLGLGLAWAAGGRLREDEAAAVPGVTIPERELIKG
>CP031165.1|AXV09447.1|5454664_5455594_-|Folate-dependent-protein-for-Fe/S-cluster-synthesis/repair-in-oxidative-stress
MTQPTDLLIDTPAIHRRTDGVIRVAGPDRIAYLHSLLSQDVEGTKPGDVADFLYLDAKGEHLAAGTMVVHAEHVLLLVPAEIAAAVAERLDRFRFMMQVEVSDLTGEWSLASLRGPGEVDAPGARSQPGTAAPHGDGLVIRDRDGGVDLLGPTSWVTDRVEELVEDRDLPLASAEDWERHRIATGRPGWGSEIATGRRTQELGLLPTHVHLRKGCYPGQESIAKIFNLGRPRRALAVIEADHVLAAGDTLGEGRRPGEVTSAAATGDGRTVALALLPLVDGELPETVDTPDGVVRVRTRVGAGMPLRGA
>CP031165.1|AXV09446.1|5453733_5454627_+|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)
MTPSSDLPPWLISGVADIVLTSSPTPTGVLNLELRHVMVNQALGKLYGVDPRTATGSTPVQLLGHLGGQIEQRCRAVVGTGRAELGHVVTGVPSTAPEGEVHWQVDCLPVSHENGPPGALLLVVTDITARTRAMRSLNEQRRSLAYQASHDPVTGLANRFQLLEVLQYHLSGQSFPNVLMVDLDGFKEVNDVHGHAAGDQVLATIADRLRNSVRTEDLVARYGGDEFVLVIRPNVDARAFAERLVDLIAEPIPWAGKQLSVGASIGVAEAGPGDSVSGLLHRADEAMYEVKADRKGT
>CP031165.1|AXV09445.1|5452234_5453737_+|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)
MVMSVVGADGPEGDRPLVWAARGRSVALGVLVVCLAVLGVVVQQRAPAALAAVATGLLAVAVLVRGAGAKPPEPEEPTVEVPEELPGRPEFVAAAEVMLSEGEGNPAVLVVLLDGFRDVQTVLGDTPAEEVLAAVGVRVAEVAQDWPAGSLGGERFAVAMRARPFLPAHHLARRIREHIAEPMVIGGVSLRLRAFVGIAQGEGGAEVLTTRATIAAATAQDTNEGLVVHQREDPAVVRRRLDIVSSLSEALEKPDERGFRPLFQPIVDGDGVLISAEALARWDDPKLGAITPDTFIPLAERTGLVAPLFTVMLAQSLLDCRRWRDGGVEAGLSINVSPVNLRDPLLTSELTARLEDVGLSPSDVTLEITESAVIDDYSWALVTLRELRKLGFGVALDDFGMGYSSLGRLHDLPVSVVKLDRSFVAGLPGDERSVGIVRATVDVCRLLGLVVVAEGVETDQQADMILEMGVDRMQGFLFSPAISVDEIVAGPVVAGWEGNR
>CP031165.1|AXV09444.1|5451674_5452142_+|Thiol-peroxidase,-Bcp-type
MNVAAGDTAPDFELPDQDGNPVSLSSLRGQPVLLYFYPRDETPGCTIQAQHIRDSWSDFTDAGVAVLGVSPDTVDSHRSFCDNHDLPHTLLADPDHEVMEAYGAWGEKTLYGRTSIGPIRSSVLIDAEGTVVKVWKRAQAKAHAERALKAISQLL
>CP031165.1|AXV09443.1|5450688_5451636_+|hypothetical-protein
MESGRLQNEPTSVVCRRLATESRTGCLHLLPDEASGEHEVRIWFRDGRIHTAVAQEGRRRLGEILVADSGLPQGSLDRALDQQRREPGGVRIGDVLVAMGLVDRETLRDAVREQILETLALAVGRRHGAWRFVPDAAVKWDVPLGSGMQDALMEASRRLDAPEVIAWRLGGMDAVVDFGSDDADVRLSLRAREWAMLTHIDGRNSIAEIARRAGEDPVTTARVVHGLHAAGVVHVLRPPAPTFDDLRADLVGVSDRPAPAVRPAEPSPGLVVVPVPPPPPIPPPPRPPPTAEPTSEPAVTSSAALFADLADDPAD
>CP031165.1|AXV09453.1|5460580_5461084_-|thioredoxin
MDRVVVLLLVIAATGAFSAWWKARDGRVRTTDAARPAGGDRSGQDRPDPVAGSSVSRWSTLPVEAADIAAAIAPASPLVFVEFTAPNCQPCVATREVLDRVTAGRSDVGIVALDVAEALDLVRAHRVMRAPTTLLITEEGHLLGRVSGVPREDELLALLDSTTPQPA
>CP031165.1|AXV09454.1|5461083_5461530_-|Integral-membrane-protein
MSEPTSSQPLMIDVRGPRFSAALTFVVLATAYLTQSAAVLSVQVAVFAVAAIAGLRWSPYGNVFRFVKRRFDLGPPPETEPEAGPRFSQVMGLIFSGAGLAAVLAGATALGWGLVLVVVALSGLLAATGICVGCEMYAVGQRLRGGTA
>CP031165.1|AXV09455.1|5461569_5462304_-|Phosphoadenylyl-sulfate-reductase
MVTDTLVPALSDIDVEEAAHELEGAPAIDILRWARACIPRFAVTSSFGADAATLLSLVAEVDADLPVLFLDTGFHFAESLAYRHLLANRLGLRNVIDVRPDLTVAQQADRYGPAMYLRDPDVCCALRKVAPLDEALEGYDGWATGVRRSQTPDRASTPVVATADRDGRTLLKVAPLAAWTAADVAGHRRLHDLPPHPLANRGFGSIGCAPCTRPTAPGEDDRAGRWAGRAKTECGIHLESTTSA
>CP031165.1|AXV09456.1|5462297_5462675_-|hypothetical-protein
MPRRLVSLIRHAPGAPRGAEPSLEANAYAVTQDVDLVVVLLEDAVRLAVADGETPPRRIGDAPFPPAAAAHDLRALLESGIRVVAHQPAMARQGIGPEDLLAGIDVVGDDDVASAIADAEGVLTW
>CP031165.1|AXV09457.1|5462682_5463036_-|hypothetical-protein
MIASAALVLNAGSANEQTITALGLVERLVERGVTVRVFAHDEAAVLSAGTHPVARAVEGLIRKGVLGGPLQWIVETDASVALGVDGRQATGVIEGDHAELWGVVRDADLVLSVGVGS
>CP031165.1|AXV09458.1|5463032_5463344_-|hypothetical-protein
MRTTVLLSAGDCWPLHLSALLSQKGEEVTVVLLDRGADLARPAHPSNDRVATALAAGAAVLVDTDALRRRGIPPTAVADGIKPTDIPSVGDLLVDATDKAVWL
>CP031165.1|AXV09459.1|5463345_5464317_-|putative-TRANSCRIPTIONAL-REGULATORY-PROTEIN
MSGTVSVTRALGSSTRAGIYDHLRQVDGALTVRDVADTFDLHPNVARTHLGLLAEAGLLTVGQRKHPGGGRPARVYRARPEVEDDHAVLDGAAQPAGGAAAALMVRLLVTLLDRPGGPPLVARALEASRDEGRRLVSALPGDPPTSRATSDAAQRAVRAIRAYAPDARVDRAGSDWAEVSGLSPAVALVERLDPALAEALERGLLAGATEGSGVMVDLAETSGGIHGRVWRMRATGGRAPRSTISPAATLDARGQTRDSGVVEAMRAMTDLRAGDILEVLAEGPGSPASFARWADRAGHALVAVERAQDAGGRPAIRLLIEKA
>CP031165.1|AXV09460.1|5464374_5465004_-|hypothetical-protein
MPSDAGAASVATGLALAVMGLVAVELAARAAVRARTAALIADVIDPSDDLAVTVPIVPLLPSLLRRRVPFVLASCQRAVLPGVEMEQVRLSLVGLVIGTRLDVVAGSGLLVAHIPAAEVLRRAGVPGSLEIGDGAVTVRWPRTGFAGMPRVGMRLRPTLVGDRIRLLPTPLSMSLPPLPGGTTLTTVEAGDAALVVTARLELPTLLNAR
>CP031165.1|AXV09461.1|5465006_5465264_-|hypothetical-protein
MDTPVVTVKLFAALRDAAGTGEVSVAAPTTLPTLLQELSERFGQRFADRLRVAAVMVDGMPTDPESERPVPAGAEVALLPPFAGG
>CP031165.1|AXV09462.1|5465342_5466023_+|GlnR-family-transcriptional-regulator
MQLLVLIGGTGRPTELLPALEFLDHTLVAATLEPDSLTAAPDCEVIVVDATSNLAGASQTCRAAATSEVQRPILVVVGEGGLAALKPTWGFDDIILPKAGPAELETRIRLLAERESATGGNVSRVGDLSIDENTYVVRLRGEPVDLTFREFELLSYLAANPGRVFTRSQLLAEVWGYDYFGGTRTVDVHVRRLRAKLGHDYDMMIGTVRGVGYKLDPQAAQGAADT

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
CP031165_4	4.2\|367617\|19\|CP031165\|CRISPRCasFinder	367617-367635	19	CP031165.1	186700-186718	1	0.947
CP031165_4	4.2\|367617\|19\|CP031165\|CRISPRCasFinder	367617-367635	19	CP031165.1	367647-367665	2	0.895
CP031165_4	4.2\|367617\|19\|CP031165\|CRISPRCasFinder	367617-367635	19	CP031165.1	869906-869924	2	0.895
CP031165_4	4.2\|367617\|19\|CP031165\|CRISPRCasFinder	367617-367635	19	CP031165.1	1923182-1923200	2	0.895
CP031165_4	4.2\|367617\|19\|CP031165\|CRISPRCasFinder	367617-367635	19	CP031165.1	3768770-3768788	2	0.895
CP031165_4	4.2\|367617\|19\|CP031165\|CRISPRCasFinder	367617-367635	19	CP031165.1	4156166-4156184	2	0.895
CP031165_4	4.2\|367617\|19\|CP031165\|CRISPRCasFinder	367617-367635	19	CP031165.1	5206596-5206614	2	0.895

1. spacer 4.2|367617|19|CP031165|CRISPRCasFinder matches to position: 186700-186718, mismatch: 1, identity: 0.947

ccgacgcccacccccacac	CRISPR spacer
ccgacgcccaccccgacac	Protospacer
************** ****

2. spacer 4.2|367617|19|CP031165|CRISPRCasFinder matches to position: 367647-367665, mismatch: 2, identity: 0.895

ccgacgcccacccccacac	CRISPR spacer
cccacccccacccccacac	Protospacer
** ** *************

3. spacer 4.2|367617|19|CP031165|CRISPRCasFinder matches to position: 869906-869924, mismatch: 2, identity: 0.895

ccgacgcccacccccacac	CRISPR spacer
ccgaggcccacccacacac	Protospacer
**** ******** *****

4. spacer 4.2|367617|19|CP031165|CRISPRCasFinder matches to position: 1923182-1923200, mismatch: 2, identity: 0.895

ccgacgcccacccccacac	CRISPR spacer
ccgatggccacccccacac	Protospacer
****.* ************

5. spacer 4.2|367617|19|CP031165|CRISPRCasFinder matches to position: 3768770-3768788, mismatch: 2, identity: 0.895

ccgacgcccacccccacac	CRISPR spacer
ccgacgccgaccccgacac	Protospacer
******** ***** ****

6. spacer 4.2|367617|19|CP031165|CRISPRCasFinder matches to position: 4156166-4156184, mismatch: 2, identity: 0.895

ccgacgcccacccccacac	CRISPR spacer
ccgaggcccacccgcacac	Protospacer
**** ******** *****

7. spacer 4.2|367617|19|CP031165|CRISPRCasFinder matches to position: 5206596-5206614, mismatch: 2, identity: 0.895

ccgacgcccacccccacac	CRISPR spacer
ccgacccccacgcccacac	Protospacer
***** ***** *******

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NC_008271	Rhodococcus jostii RHA1 plasmid pRHL3, complete sequence	69540-69569	5	0.833
CP031165_22	22.1\|5248167\|28\|CP031165\|CRISPRCasFinder	5248167-5248194	28	NZ_AP014801	Rhodovulum sulfidophilum plasmid Plasmid1 DNA, complete genome, strain: DSM 2351	31806-31833	6	0.786
CP031165_22	22.1\|5248167\|28\|CP031165\|CRISPRCasFinder	5248167-5248194	28	MT711975	Streptomyces phage Alderaan, complete genome	3372-3399	6	0.786
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NZ_CP027299	Streptomyces sp. SGAir0924 plasmid unnamed_5	190528-190557	6	0.8
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NC_019848	Sinorhizobium meliloti GR4 plasmid pRmeGR4c, complete sequence	129569-129598	6	0.8
CP031165_9	9.1\|1397814\|33\|CP031165\|CRISPRCasFinder	1397814-1397846	33	NC_016585	Azospirillum lipoferum 4B plasmid AZO_p1, complete sequence	362571-362603	7	0.788
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NZ_CP016083	Streptomyces sp. SAT1 plasmid unnamed3, complete sequence	648431-648460	7	0.767
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NZ_CP019037	Massilia putida strain 6NM-7 plasmid unnamed2, complete sequence	35571-35600	7	0.767
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NZ_CP041766	Tomitella sp. HY188 plasmid unnamed, complete sequence	57701-57730	7	0.767
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NC_007337	Cupriavidus pinatubonensis JMP134 plasmid 1, complete sequence	44730-44759	7	0.767
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NZ_CP039340	Ralstonia solanacearum strain UW386 plasmid pUW386, complete sequence	1169856-1169885	7	0.767
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NZ_LT984809	Cupriavidus taiwanensis isolate Cupriavidus taiwanensis STM 8555 plasmid I, complete sequence	16437-16466	7	0.767
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NZ_LT984809	Cupriavidus taiwanensis isolate Cupriavidus taiwanensis STM 8555 plasmid I, complete sequence	494873-494902	7	0.767
CP031165_9	9.1\|1397814\|33\|CP031165\|CRISPRCasFinder	1397814-1397846	33	NZ_AP018921	Pseudonocardia autotrophica strain NBRC 12743 plasmid pPA12743CP, complete sequence	97486-97518	8	0.758
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NC_017585	Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCATT, complete sequence	1789402-1789431	8	0.733
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NC_016113	Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCAT, complete sequence	23716-23745	8	0.733
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	MN234172	Mycobacterium phage ThulaThula, complete genome	507-536	8	0.733
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	KR080195	Mycobacterium phage Phayonce, complete genome	507-536	8	0.733
CP031165_9	9.1\|1397814\|33\|CP031165\|CRISPRCasFinder	1397814-1397846	33	NZ_CP031599	Roseovarius indicus strain DSM 26383 plasmid pRIdsm_01, complete sequence	122177-122209	9	0.727
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NZ_CP034351	Streptomyces sp. W1SF4 plasmid p1, complete sequence	177426-177455	9	0.7
CP031165_24	24.1\|5460479\|30\|CP031165\|CRISPRCasFinder	5460479-5460508	30	NZ_CP013379	Burkholderia pseudomultivorans strain SUB-INT23-BP2 plasmid pINT23, complete sequence	42588-42617	14	0.533

1. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NC_008271 (Rhodococcus jostii RHA1 plasmid pRHL3, complete sequence) position: , mismatch: 5, identity: 0.833

cgcggccgcggggccggccgacacg-accac	CRISPR spacer
ttcggcggcggggccggccgagacgcacca-	Protospacer
. **** ************** *** ****

2. spacer 22.1|5248167|28|CP031165|CRISPRCasFinder matches to NZ_AP014801 (Rhodovulum sulfidophilum plasmid Plasmid1 DNA, complete genome, strain: DSM 2351) position: , mismatch: 6, identity: 0.786

accggggccggcccacccctcgaaccca	CRISPR spacer
aacggggccggcccaccccccgaccgat	Protospacer
* *****************.*** *

3. spacer 22.1|5248167|28|CP031165|CRISPRCasFinder matches to MT711975 (Streptomyces phage Alderaan, complete genome) position: , mismatch: 6, identity: 0.786

accggggccggcccacccctcgaaccca	CRISPR spacer
accggggcgggcccgcccctcgaccagg	Protospacer
******** *****.******** *  .

4. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NZ_CP027299 (Streptomyces sp. SGAir0924 plasmid unnamed_5) position: , mismatch: 6, identity: 0.8

cgcggccgcggggccggccgacacgaccac-	CRISPR spacer
aaccgccgcggggccggccgacacg-ctgca	Protospacer
 .* ********************* *..*

5. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NC_019848 (Sinorhizobium meliloti GR4 plasmid pRmeGR4c, complete sequence) position: , mismatch: 6, identity: 0.8

-cgcggccgcggggccggccgacacgaccac	CRISPR spacer
tcgcgctta-ggggccggccgactcgaccac	Protospacer
 **** ... ************* *******

6. spacer 9.1|1397814|33|CP031165|CRISPRCasFinder matches to NC_016585 (Azospirillum lipoferum 4B plasmid AZO_p1, complete sequence) position: , mismatch: 7, identity: 0.788

gggggtgcgggggcggtcgccccg-gacggttgg	CRISPR spacer
gggggtgcggcggcggtcgccgcgctgctgctg-	Protospacer
********** ********** **  .* *.**

7. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NZ_CP016083 (Streptomyces sp. SAT1 plasmid unnamed3, complete sequence) position: , mismatch: 7, identity: 0.767

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
cgcggccgcggggccagccgacctgcttgc	Protospacer
***************.****** .* ...*

8. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NZ_CP019037 (Massilia putida strain 6NM-7 plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.767

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
gcagagcgcggggccggccgatacggccac	Protospacer
   *. ***************.***.****

9. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NZ_CP041766 (Tomitella sp. HY188 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
cccggccgcggggcctgccgagacgattca	Protospacer
* ************* ***** ****..

10. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NC_007337 (Cupriavidus pinatubonensis JMP134 plasmid 1, complete sequence) position: , mismatch: 7, identity: 0.767

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
cgcggccgcggggccggcagccagcagcga	Protospacer
****************** * **  * *.

11. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NZ_CP039340 (Ralstonia solanacearum strain UW386 plasmid pUW386, complete sequence) position: , mismatch: 7, identity: 0.767

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
aacggccgcggcgccggccgccacggcacc	Protospacer
 .********* ******** ****.*  *

12. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NZ_LT984809 (Cupriavidus taiwanensis isolate Cupriavidus taiwanensis STM 8555 plasmid I, complete sequence) position: , mismatch: 7, identity: 0.767

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
cgcggccgcggggctggccgagcccgcagc	Protospacer
**************.******  * .* .*

13. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NZ_LT984809 (Cupriavidus taiwanensis isolate Cupriavidus taiwanensis STM 8555 plasmid I, complete sequence) position: , mismatch: 7, identity: 0.767

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
cgcggccgcggggctggccgagcccgcagc	Protospacer
**************.******  * .* .*

14. spacer 9.1|1397814|33|CP031165|CRISPRCasFinder matches to NZ_AP018921 (Pseudonocardia autotrophica strain NBRC 12743 plasmid pPA12743CP, complete sequence) position: , mismatch: 8, identity: 0.758

gggggtgcgggggcggtcgccccggacggttgg	CRISPR spacer
gagtatgcgggggcggtctcgccggacgggacg	Protospacer
*.* .************* * ********   *

15. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NC_017585 (Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCATT, complete sequence) position: , mismatch: 8, identity: 0.733

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
gatcatcgcggggccggccgccaccaccac	Protospacer
 .. ..************** *** *****

16. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NC_016113 (Streptomyces cattleya NRRL 8057 = DSM 46488 plasmid pSCAT, complete sequence) position: , mismatch: 8, identity: 0.733

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
gatcatcgcggggccggccgccaccaccac	Protospacer
 .. ..************** *** *****

17. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to MN234172 (Mycobacterium phage ThulaThula, complete genome) position: , mismatch: 8, identity: 0.733

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
cgcggctgcggggccggcagacacccgagt	Protospacer
******.*********** *****    ..

18. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to KR080195 (Mycobacterium phage Phayonce, complete genome) position: , mismatch: 8, identity: 0.733

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
cgcggctgcggggccggcagacacccgagt	Protospacer
******.*********** *****    ..

19. spacer 9.1|1397814|33|CP031165|CRISPRCasFinder matches to NZ_CP031599 (Roseovarius indicus strain DSM 26383 plasmid pRIdsm_01, complete sequence) position: , mismatch: 9, identity: 0.727

gggggtgcgggggcggtcgccccggacggttgg	CRISPR spacer
agggcggcgggggcggtcgccccggcctggccc	Protospacer
.***  ******************* * * .

20. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NZ_CP034351 (Streptomyces sp. W1SF4 plasmid p1, complete sequence) position: , mismatch: 9, identity: 0.7

cgcggccgcggggccggccgacacgaccac	CRISPR spacer
gagagccgcgcggccggccggcacgacggg	Protospacer
 . .****** *********.****** .

21. spacer 24.1|5460479|30|CP031165|CRISPRCasFinder matches to NZ_CP013379 (Burkholderia pseudomultivorans strain SUB-INT23-BP2 plasmid pINT23, complete sequence) position: , mismatch: 14, identity: 0.533

cgcggccgcggggccggccgacacgaccac----	CRISPR spacer
----gccagcgtgccggccggcgccgcggccggg	Protospacer
    ***.  * ********.*.* .* .*

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

604725 : 615399

Bacillus_virus(25.0%)

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
AXV05194.1\|604725_605586_-	diguanylate cyclase/phosphodiesterase (GGDEF & EAL domains) with PAS/PAC sensor(s)	G3MA91	Bacillus_virus	7.4e-10	40.5
AXV05195.1\|605578_606457_-	diguanylate cyclase/phosphodiesterase (GGDEF & EAL domains) with PAS/PAC sensor(s)	G3MA91	Bacillus_virus	2.1e-15	30.9
AXV05196.1\|606550_608590_+	Transcriptional activator of maltose regulon, MalT	G9BWE0	Planktothrix_phage	2.9e-12	31.7
AXV05197.1\|608635_609553_+	Transcriptional activator of maltose regulon, MalT	A0A1B1IUU3	uncultured_Mediterranean_phage	1.2e-21	34.8
AXV05198.1\|609809_610085_+	Mobile element protein	B6ETC4	Enterobacteria_phage	2.0e-17	58.0
AXV05199.1\|610081_610993_+	Mobile element protein	Q6H9S3	Enterobacteria_phage	6.3e-76	55.6
AXV05200.1\|611020_612163_-	Mobile element protein	W5R8L2	Staphylococcus_phage	2.4e-40	34.3
AXV05201.1\|612304_613363_-	Malyl-CoA lyase	NA	NA	NA	NA
AXV05202.1\|613435_613870_-	Peptide methionine sulfoxide reductase MsrB	NA	NA	NA	NA
AXV05203.1\|613979_614279_+	Methylated-DNA-[protein]-cysteine S-methyltransferase family protein	NA	NA	NA	NA
AXV05204.1\|614325_615399_+	DNA polymerase I	F8WQ40	Bacillus_phage	3.6e-14	26.8

DBSCAN-SWA_2

1606369 : 1618049

Catovirus(12.5%)

protease

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
AXV06052.1\|1606369_1607122_+	Endonuclease IV	A0A1V0SBL9	Catovirus	2.1e-08	24.6
AXV06053.1\|1607146_1607836_-	Outer membrane protein	NA	NA	NA	NA
AXV06054.1\|1607995_1608682_+	Cell division transporter, ATP-binding protein FtsE	F2Y1V6	Organic_Lake_phycodnavirus	5.2e-14	28.4
AXV06055.1\|1608686_1609565_+	Cell division protein FtsX	NA	NA	NA	NA
AXV06056.1\|1609677_1610967_+	Peptidase, M23/M37 family	A8ATH6	Listeria_phage	9.7e-22	52.3
AXV06057.1\|1611034_1612297_+\|protease	Carboxyl-terminal protease	A0A0R6PIZ1	Moraxella_phage	1.7e-23	31.4
AXV06058.1\|1612333_1612801_+	tmRNA-binding protein SmpB	W5RAM5	Staphylococcus_phage	4.3e-28	44.5
AXV06059.1\|1612832_1615016_-	diguanylate cyclase/phosphodiesterase (GGDEF & EAL domains) with PAS/PAC sensor(s)	A9J564	Pseudomonas_phage	8.7e-07	37.3
AXV06060.1\|1615046_1615184_+	hypothetical protein	NA	NA	NA	NA
AXV06061.1\|1615692_1616490_+	hypothetical protein	M1HRP1	Paramecium_bursaria_Chlorella_virus	1.5e-09	23.9
AXV06062.1\|1616522_1618049_-	DNA helicase	U5PT02	Bacillus_phage	2.7e-07	20.3

DBSCAN-SWA_3

2128997 : 2136133

Staphylococcus_phage(50.0%)

tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
AXV06493.1\|2128997_2129537_+	Peptide deformylase	E3SLL2	Synechococcus_phage	2.5e-16	41.5
AXV06494.1\|2129575_2130457_+\|tRNA	Methionyl-tRNA formyltransferase	NA	NA	NA	NA
AXV06495.1\|2130453_2131809_+	16S rRNA (cytosine(967)-C(5))-methyltransferase	NA	NA	NA	NA
AXV06496.1\|2131805_2132744_+	DNA-binding response regulator mtrA	W8CYM9	Bacillus_phage	2.7e-21	44.5
AXV06497.1\|2132774_2133791_+	Diaminohydroxyphosphoribosylaminopyrimidine deaminase	A0A2I2L4R9	Orpheovirus	1.2e-43	34.2
AXV06498.1\|2133794_2134427_+	Riboflavin synthase eubacterial/eukaryotic	A0A2H4PQS5	Staphylococcus_phage	5.8e-36	43.1
AXV06499.1\|2134419_2135688_+	3,4-dihydroxy-2-butanone 4-phosphate synthase	A0A2H4PQS2	Staphylococcus_phage	2.4e-89	44.7
AXV06500.1\|2135674_2136133_+	6,7-dimethyl-8-ribityllumazine synthase	A0A2H4PQS3	Staphylococcus_phage	1.1e-28	45.6

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage

2. CP031166

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Crispr_ID: CP031166_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031166_1

112998-113147

TypeI-E

Consensus_repeat	Method
GCAAGGGATCACCCCCGCCTGCGCGGGGAGAAG	PILER-CR
GGGATCACCCCCGCCTGCGCGGGAGAAG	CRISPRCasFinder

2 spacers

cas3,cas8e,cse2gr11,cas7,cas5,cas6e,cas1,cas2

The CRISPR arrays of CP031166_1

>merge|CP031166|1|112998-113147|PILER-CR,CRISPRCasFinder
GGGCTGACCCCCGCCTGCGCGGGGAGAAGGCCGAGCAGGACCGGCTGACGATCGCTGGCCAGGGATCACCCCCGCCTGCGCGGGAGAAGTGGTCGCCGGCCTCATGCGCCGGAGGCCGCAGGGGATCACCCCCGCCTGCGCTGGGAGAAG

>CP031166|1|1|112998-113147|PILER-CR
GGGCTGACCCCCGCCTGCGCGGGGAGAAGGCCG	AGCAGGACCGGCTGACGATCGCTGGCCA
GGGATCACCCCCGCCTGCGCGGGAGAAGTGGTC	GCCGGCCTCATGCGCCGGAGGCCGCAGGGGATC
ACCCCCGCCTGCGCTGGGAGAAG

>CP031166|1|1|112998-113146|CRISPRCasFinder
GGGCTGACCCCCGCCTGCGCGGGGAGAA	GGCCGAGCAGGACCGGCTGACGATCGCTGGCCA
GGGATCACCCCCGCCTGCGCGGGAGAAG	TGGTCGCCGGCCTCATGCGCCGGAGGCCGCAG
GGGATCACCCCCGCCTGCGCTGGGAGAA

Protein	Signature genes	Signature genes Name	Protein_function
CP031166.1\|AXV09896.1\|107752_107896_-\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09899.1\|109759_111565_+\|Cell-division-protein-FtsH	unknown	unknown	gnl\|CDD\|273520
CP031166.1\|AXV09894.1\|102435_104166_+\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09892.1\|99892_100546_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372434
CP031166.1\|AXV09895.1\|104364_107727_+\|Serine-protease,-subtilase-family	unknown	unknown	gnl\|CDD\|310150
CP031166.1\|AXV09893.1\|100726_102154_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|198389
CP031166.1\|AXV09908.1\|120620_121601_+\|CRISPR-associated-protein-Cas1	cas1	cd09719_cas1_CAS-I-E	gnl\|CDD\|274693
CP031166.1\|AXV09907.1\|120003_120621_+\|CRISPR-associated-protein,-Cse3-family	cas6e	cd09727_cas6e_CAS-I-E	gnl\|CDD\|187858
CP031166.1\|AXV09905.1\|118133_119255_+\|CRISPR-associated-protein,-Cse4-family	cas7	pfam09344_cas7_CAS-I-E	gnl\|CDD\|378153
CP031166.1\|AXV09897.1\|108567_109212_+\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09902.1\|113339_115922_+\|CRISPR-associated-helicase-Cas3	cas3	cd09639_cas3_CAS-I	gnl\|CDD\|182031
CP031166.1\|AXV09891.1\|99124_99763_+\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09909.1\|121600_121882_+\|CRISPR-associated-protein,-Cas2	cas2	pfam09707_cas2_CAS-I-E	gnl\|CDD\|378244
CP031166.1\|AXV09903.1\|115918_117529_+\|hypothetical-protein	cas8e	pfam09481_cas8e_CAS-I-E	gnl\|CDD\|187860
CP031166.1\|AXV09904.1\|117525_118119_+\|hypothetical-protein	cse2gr11	mkCas0096_cse2gr11_CAS-I-E	gnl\|CDD\|274193
CP031166.1\|AXV09910.1\|123007_123991_+\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09906.1\|119251_120007_+\|CRISPR-associated-protein,-Cas5e-family	cas5	cd09645_cas5_CAS-I-E	gnl\|CDD\|273842
CP031166.1\|AXV09900.1\|111772_112018_+\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09898.1\|109367_109718_+\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09911.1\|123966_124116_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
CP031166.1\|AXV09899.1\|109759_111565_+\|Cell-division-protein-FtsH	gnl\|CDD\|273520	TIGR01241, ATP-dependent_zinc_metalloprotease_FtsH, ATP-dependent metalloprotease FtsH. HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides].	7.70519e-154
CP031166.1\|AXV09907.1\|120003_120621_+\|CRISPR-associated-protein,-Cse3-family	gnl\|CDD\|187858	cd09727, Cas6_I-E, CRISPR/Cas system-associated RAMP superfamily protein Cas6e. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6e is an endoribonuclease that generates crRNA; This family is specific for CRISPR/Cas system I-E subtype; Homologous to Cas6 (RAMP superfamily protein); Possesses double RRM/ferredoxin fold; also known as Cse3 family.	2.17597e-28
CP031166.1\|AXV09895.1\|104364_107727_+\|Serine-protease,-subtilase-family	gnl\|CDD\|310150	pfam05345, He_PIG, Putative Ig domain. This alignment represents the conserved core region of ~90 residue repeat found in several haemagglutinins and other cell surface proteins. Sequence similarities to (pfam02494) and (pfam00801) suggest an Ig-like fold (personal obs:C. Yeats). So this family may be similar in function to the (pfam02639) and (pfam02638) domains. This domain is also found in the WisP family of proteins of Tropheryma whipplei.	0.000952475
CP031166.1\|AXV09908.1\|120620_121601_+\|CRISPR-associated-protein-Cas1	gnl\|CDD\|274693	TIGR03638, cas1_ECOLI, CRISPR-associated endonuclease Cas1, subtype I-E/ECOLI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 protein particular to the ECOLI subtype of CRISPR/Cas system.	1.62685e-63
CP031166.1\|AXV09904.1\|117525_118119_+\|hypothetical-protein	gnl\|CDD\|274193	TIGR02548, CRISPR_system_Cascade_subunit_CasB, CRISPR type I-E/ECOLI-associated protein CasB/Cse2. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model family is found in Ecoli subtype CRISPR/Cas regions of many bacteria, most of which are mesophiles, and not in Archaea. It was designated Cse2 originally, and renamed CasB based on its characterization in the CASCADE complex.	7.53363e-05
CP031166.1\|AXV09893.1\|100726_102154_+\|hypothetical-protein	gnl\|CDD\|198389	cd10442, GIY-YIG_PLEs, Catalytic GIY-YIG endonuclease domain of penelope-like elements and similar proteins. This model corresponds to the EN domain of PLEs that contains catalytic module of the GIY-YIG endonucleases of group I bacterial/organellar introns, as well as bacterial UvrC DNA repair proteins. It can cleave DNA with low nucleotide sequence specificity. However, the PLEs EN domain is distinct from other GIY-YIG endonucleases by the presence of a well-conserved CCHH motif (CX(2-7)CX(33-39)HX(3-5)H, X can be any residue). The role of the CCHH motif has not yet been identified. Penelope-like elements (PLEs) represent a novel class of eukaryotic retroelements, which do not belong to either long terminal repeat (LTR) retrotransposons or non-LTR retrotransposons (often called LINEs), but instead form a sister clade to telomerase reverse transcriptases (TERTs), highly specialized non-mobile reverse transcriptases (RTs) which are responsible for the addition of telomeric repeats to the ends of eukaryotic chromosomes. The single open reading frame (ORF) encoded by PLE consists of two principal domains, RT domain and endonuclease (EN) domain, jointed by a linker region of variable length. Both of these two domains are functionally active.	0.00155839
CP031166.1\|AXV09905.1\|118133_119255_+\|CRISPR-associated-protein,-Cse4-family	gnl\|CDD\|378153	pfam09344, Cas_CT1975, CT1975-like protein. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This family is represented by CT1975 of Chlorobium tepidum.	2.88447e-78
CP031166.1\|AXV09892.1\|99892_100546_+\|hypothetical-protein	gnl\|CDD\|372434	pfam13023, HD_3, HD domain. HD domains are metal dependent phosphohydrolases.	2.48639e-15
CP031166.1\|AXV09902.1\|113339_115922_+\|CRISPR-associated-helicase-Cas3	gnl\|CDD\|182031	PRK09694, PRK09694, CRISPR-associated helicase/endonuclease Cas3.	4.64995e-75
CP031166.1\|AXV09909.1\|121600_121882_+\|CRISPR-associated-protein,-Cas2	gnl\|CDD\|378244	pfam09707, Cas_Cas2CT1978, CRISPR-associated protein (Cas_Cas2CT1978). This entry represents a minor branch of the Cas2 family of CRISPR-associated protein which are found in IPR003799. Cas proteins are found adjacent to a characteristic short, palindromic repeat cluster termed CRISPR, a probable mobile DNA element.	1.2151e-23
CP031166.1\|AXV09903.1\|115918_117529_+\|hypothetical-protein	gnl\|CDD\|187860	cd09729, Cse1_I-E, CRISPR/Cas system-associated protein Cse1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; subunit of the Cascade complex; signature gene for I-E subtype; also known as Cse1/CasA/YgcL family.	1.31355e-19
CP031166.1\|AXV09906.1\|119251_120007_+\|CRISPR-associated-protein,-Cas5e-family	gnl\|CDD\|273842	TIGR01868, hypothetical_protein, CRISPR-associated protein Cas5/CasD, subtype I-E/ECOLI. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This family is part of the ECOLI subtype CRISPR/Cas locus, and now characterized as part of the CASCADE complex of that system. It shares a small N-terminal homology region with members of several other CRISPR/Cas subtypes, and we view the families that share this region as being Cas5.	1.46338e-25

>CP031166.1|AXV09900.1|111772_112018_+|hypothetical-protein
MATPDGRPPDLQPAGTLYINQGGRVTCTTHGGGYLQAAAGQQRYVDGDHITTPLDDWEVFSPEVVAEDGLECETCARGGHR
>CP031166.1|AXV09899.1|109759_111565_+|Cell-division-protein-FtsH
MKRLRERLRTPRQPEARAGHLAVGFALFVSVVFAVQTFASDPTADHVPIAEVLAAAEDAGADLVVYDENAGTITVTSDGQETTAGVPVRNADPILQHLLDAKAPLEIRAAQPPSYLGSLILAVAPMLLLGAALLLYLRNRQGGGPVNDAERPDVRLDDVIGIDEAKAEATEIVGYLADPSAYDRVGARPPVGVLLTGPPGVGKTMLAKAIAGDAGVPFFKISGSDFVEMFAGLGSRRVRSLFTAARKAAQSAGGAIVFIDELDAVGRRRSEHAGSGGHREAEQTLNALLVELDGFTGRDGVIILAATNRPDVLDPALTRPGRFDRTITLGLPDLHARTRLLDHLLDQAPVPTQVDTAGHARRMTGSSGAALTNLINQAKIEAARTGYGIITDRHVDAAWDRLQIGTPRPDAVIDPSDRQTTVIHEAGHAVAGLLLPDAPAPTRVSALPHGSGVGGVTITDGTDRQMLTHDQALARLTVLMAGRAAEQLVLGPGATSNGAAGDIASATDLARAMITQWGWGTFGTVHLDGLGPDGTLAADVADGVATMLDAALQRAKDLLAHNRPFLDEVADTLDQFDTLTGQDLTALRNATDGTDVVPAVP
>CP031166.1|AXV09898.1|109367_109718_+|hypothetical-protein
MANDLSWARLARLAANPPYLAADLTHRDLDAVMVWLTDVTVAARRVPARIHTTAASTLWLRCAVLTDRLGHADDDEIERRVNEVVSRYEHIRAELAARLAERIPVAATSRQHQIAA
>CP031166.1|AXV09897.1|108567_109212_+|hypothetical-protein
MLAALALTGCATEPEPVEDPFQVVFDQLATVELGCRGLPDEGQRRFGDVLALSSSCTTVVDDTDVELTVVIDDFDTLQSAANSLTTSTFVITPGALVVVDANPARLAELVGGLIAGELDGQLVAHDDSDRFCELAEEMADLVDDALRVAHDTDSTTADILALEYQVGQLATELEEEAPEAIADIYDSPLESDQAAIRDYIHDQCGVDVNFVEPG
>CP031166.1|AXV09896.1|107752_107896_-|hypothetical-protein
MASKELSRDTAAILVGLVGRPDRLPFLDHRASLVGVADVAVGLAGSG
>CP031166.1|AXV09895.1|104364_107727_+|Serine-protease,-subtilase-family
MVLLATLAPMSAYAQDTGGDTTPPTITSFELIDTTGDTDVGPVQIRMRATATDDLSGPSSVTAYFRSEDGRNTGASLLRTQTPGEFQGSAHFPQYREGGVYTLVGLAAGDQVGNVTNINGAALTQQFGTHTFTIAGQGDTTPPTITSFELIDTTGDTDVGPVQIRMRATATDDLSGPSSVTAYFRSEDGRNTGASLLRTQTPGEFQGSAHFPQYREGGVYTLVGLAAGDQVGNVTNINGAALTQQFGTHTFTIAGQGDTTPPTITGFELIDEVADAGAGPVLIRVRATATDDLSGPSSVTAYFRSEDGRNTGASLSPTQTPGEFQGGVHFPQYSPTGVFTLVGLAAGDHAGNVTNVNGAALTQQFGNPTFRVGNAPTGNHVPVATVQGPYTVPEGETVTVSVFATDADGDTLTYAWDLDGDGAPDHDTNRPSVTFASGDRPIGTQVQIYADVCDTYGVCARARSSVTVVSPVSITTASPLPSGSIGQPYATTLTAAGGTTPYTWAVASGTLPAGLALDSGTGEIVGTPTAAGTFGFVITVTDANGATASAPLTTGNAPATTQPGTDINTPVIVTPTNPDGTPVVDSDGNTVLCDSYELANDSDPLPDGITLDPSTGLLSGSATSGGTYRVIVECSYNIDGQIGAAVAEFTITIAADTTPPAVTCTTPPHPETGWFTEPVTVTCTATDNSGSVSPATQTIIVDTEGPDQAITSDPACDPSDNCVTATVTVSIDLSNPDVTTTVDPAPNDHGWHRTPVTIAATCTDAISGIATCDEPVTVIADGAEQTFIHTGTDLAGRTSRAVTTINLDQVAPQITLTSVEDGASVHDRDETAPSCEATDSLSGTIGDCTVTVIRTPTGGADTVTVTATARDAAGNETTISRTYTVIYDSDAPTITATFNVTPNSADWYRIAPTVTFTCDDPSGVVDCPDPVTFSLDGANQSVTVTAADPWGNTATLTVGGINVDQTAPTLQLTGARDSYTVADRITIECSVDDLTSGVATLDCPGIDTPGTTYGPGAHTITATAVDVAGNTTSMSHTFTVTADVDSIMALVDSYLDASNRPGAQGISNALRSKLASGDYGAFINQVEAQCCIDAPGGNGKRFTRSQADALITLATYLRDR
>CP031166.1|AXV09894.1|102435_104166_+|hypothetical-protein
MTTSNSRAKGLARRLAELGNCTYQQALGHVAEHDTTFGAEQTNRWVANRELAAVLRTEEPGFTANDGAGDAHTLTGPIRRDGTCVWTLRVNTDLLRWTIIATNPTTGSTADIWTSAFHAPDGDTYAFADYHRDQSVRDRVAVTLAGLLVSTRSHLALPAETPGTDTIAGTTPVTPHTFADDTIPDVCYDAVADLVVAQFRHDADDWTGPIPTADNLHDLCDGNMAVHAAIEAVFGPTDVNGNDQVFTDRFNTAYDRVMTHPSVDDAADPGRVEAIYRAMWGRGTGSTTPVPTPFADETFTDVTIGPDGIADGNSSRNGHTTGFSADPVMAIIREAFHLTNEAADALWSLQDGMAGIDGDAAGWDWSALRDSSGTAIATMFDLARQYVTPRDLADAWDVDPDAIKTAIRTRLAHHDRNRTEPGRPFLVDPTTGTVTRIGTATLDVPDTPAAVGHDVLDLIADTARGAADGSGATVTVTNIDHGSTGVVVELDGWTLHWWKADPGVWGWSWFSDDGNDLSFGNLADADGTRLAADFVAGSTAVMLAEAVGWVTAAFVANPTAGGPTGPDPIGVHDQGE
>CP031166.1|AXV09893.1|100726_102154_+|hypothetical-protein
MAFMPTEEQLAFRDAVEFTKPPPKGMAYIYVVKSEGCGCPIYVGETTTSLRARFTGHVRDKVRRIREYPHQDHHRDVQAVTIHLEAVVASRGRRDVEAAVIARYAADGWHLVNDSRYDPSMVEATLATIRIDGCAVATEDARERWRAHVAEQEAASTALSGYLEGHGVSWDGRPNEAVVFAVWAYQRVHGGLPDAALPLVIRHGHMEYRGRPLSKVLELPEATLQGTLDYFADHEARGWSTHMGTSAAMALGWLGEANGGNVHRYDEAIDRLMREADNGFWQDIQSGDADPDPVPSRSTAMSRDFLRDYMGVGSVTGPTLNTDGFHRQWWACDGLGIGIRTAPTPRVTWWGTVGDDGTEYGSDFLQNVHHPLEVSVLRDDWALHWEKVAELATELRDAAGTRDQARWTAAVRRVCLGVEDDVMWLGWRGGFAVLLACVEFGWGTERWQAARGPAGVIAGLSADHGFTAPVIPRTK
>CP031166.1|AXV09892.1|99892_100546_+|hypothetical-protein
MNTHTNTAPVTTGGDTATTADAMLDMAGFAMAFGAIQRATLLPDGTTREDDATHTVMLGMIACSLAARFFPALDVGNVAQYALVHDAPERYAGDVDTLTATEDERAAKAADEAAATDRIDEEFGQTLPWLPNTIRAYESMADPEARFVKAVDKLLPLLTEVLSGMAGTRRRGVDAAALATHYDRQVDEIALYASDFPVVFEVRRLLVAETLRILAAG
>CP031166.1|AXV09891.1|99124_99763_+|hypothetical-protein
MTVQPDRAPYEATMSDGSPNLGSYEFAGYVGAVTKARAILVECGTDPADVDPKIVRALAGVIADMADRVQHRLRAKVITARRLDIAADNAARNGQEFGEADAAAVRAKVWESALVDRQGGSHTRARSCVYTAMEDFPFPADADAQAVADWTERVENRAFGLLVIAVDLAYDDRSHETFEDRVSALGGLLAPTPADADEQDAPAAEQAATADA
>CP031166.1|AXV09902.1|113339_115922_+|CRISPR-associated-helicase-Cas3
MAHLVDTAAVASALVDRWVPSRLLDDPTREAVVAAAGLHDLGKAGPVFQGQLMARRRDSRFADHLAGLSTAGLGCPGPVLSGVRLAAGEEQALLRRHEVLSAAILAGRVEDAGAEGLAALVAGHHGCWRLPFDDYGAVPVALEAVRSDPGWSAWHRDAIAVIEGLVGGAGTSAVDPVVVPVAAGVVVVADWLASHLADVDPSGVEGADGDWEVWFERRVGDAHRLVEDLLGVPVRPAGSVEDILGVPSLRPVQQAVSASTARGLRLVMAPTGEGKTEAAFGRWLAHHAGAGSGLLFALPTMATTDAMLERVRPLFADTDARGALAHGRSILNGFNRPAGPLHGSVHNGPGGLSPSWWFNGRGRQVLAPVTVCTVDQVLLSVLAHRHNFVRLLGVFSKMVVVDEVHTFDPYMSGLLERFLRWAGRFGVDVVLMSATLPAERQRTYVEAYADGPAGLPAAVYPSVVTCTGGVVDVSPVAMSRPARTVVIDRMSFGGPDDIARYVAGVVAAHPDAKVGVILNTVGRVQQVATALHALLGCSGTHADGRCGTLWTAHSRFPAAVRSRQTAAMLGEFGPDSTTGAAVLVATQVVEMSLDIDLDLLITDLCPAPSLVQRIGRLHRHTHDPAVRRRPGGMRHPRVVLVTPDPWPDGPAGWLPYPAPVIGATWEHGLGGGAVNELVVPNDVQAFVDRSHLPVTALYGPEGEGLADELVTHLLGESAKAQRAGRAAIPTPEAMTSRTAAALEKFANAEVDGLRLSTRWDDTPTALVLLHNPDGPPGASTNGVWGGPIPSAPGYDEQAELLGCTVTISGRQAFDVTPRDDIGRPSPGRWDGTLLHDVVPLPLPSPDWDPDPLTGLTRRDQ
>CP031166.1|AXV09903.1|115918_117529_+|hypothetical-protein
MSTTTTTKLHDRIVGLLPATPTYNLTVERWIPVIGPDGPDTVGLAGLLDRAHRLDLDDAGHGPLWRHSMERLLIGIGHLIAQAAPGHDWAAVANSGLPLPADGATSVLARLADRLWLHHPTSPFLQRLDVLSHMDDKPDKPIVEVTDPFWALLPDVPSKSNSAWFNRADPDAKTGPADAANALLVRHTWAVPGNETKNGVGKARSEGGSAGQGANDLTHLTIGGPTVAATIARNLIGDWVDRGQRLWFENPAGAVGVLAADDPDPLWLYTATTASTVLIPMFGGYRVVRSPMPEPPEVAKQLGTTLKANNPHTVRFTSVDGKTTPTLRLPVPSCGSDLLRRYHSRLAGGRPLTPSVLDLRGLHVRPARRPMVRALIVIGAGQAAGARVGDVAVAASELADLTLPAPAAVRFAELARIIFGPSPSVRSRTATAISTVRGADGEDDRKQIRASVEHDLTVAADAVVFRLLSACRRNADGDLPDRIPVPDSRLLIDTALGCFDRHVAPLTHRPATAATAVVQRRRLVRHLTRLLSEETP
>CP031166.1|AXV09904.1|117525_118119_+|hypothetical-protein
MTDTARPPRTVDALIALRADTGARTAMRRGLSQATEHYAYPYLAHRWQGRPWARTPTLRIAGLIAVTSLADEPAGDRIGTTLRRVALADRPAPGDATDRALDRIGKRLLWAQTGDLAKFHQVLTGLLPNAPLGRIDWQELHDTYLRWGHPHPDARRRIRLRVIEDFYSPVPRAEREPDPGPADENADAPKPTQPTLI
>CP031166.1|AXV09905.1|118133_119255_+|CRISPR-associated-protein,-Cse4-family
MIRYANFHILHPLAFSNPNRDDTGAPKTTTYGGTVRGRMSSQSQKRAARTAFEGQTTADRTHRSKYAADRLLDTTTTLLAANGTTLTPDQTEKLHKSVRTEIGKLTGKADDAKATLVWLAEAELNGLAAKLAVKAGAEMTKDDIDAALSTTTDSLTIAAFGRMFASRADLAIEAAAQVGHAFTTHAQANDLDYLTAFDDLQASYDTPDDDGNVKGAGAGHLDVNEFHSGVFYRYFNLNRDDLTDNWRPLTNQGAPGTTERLEAFLREMTIQLPTGRDATAAHQTPPAYVMVTFTERAATLAPAFETPVAGGANDGYLPGSIAALTGYADAIARIYGPDHRIVVNLTDPDAQTTLADLTGAVANWVVSGTLSTP
>CP031166.1|AXV09906.1|119251_120007_+|CRISPR-associated-protein,-Cas5e-family
MTTILLRLAAPLMAFGTTSRFDNRATDADPSLSAVHGLLTAAAGITRDQPRPDWITHALPAIRVDRDGHTLPDYQTVNQPPLRRYRELSDHDLRKVYTVAMPDGSRKPNSTKTKQPATVQSRRGYLTDATFLITLPDPTGNLNEALARPRFHLYAGRKGCPVTEPFLLGTTTDDPVAALTTTPTPRTGPDDTGERRAVLFANPADNSRHEDRNDLPSGGRRHRTARRWHTTVTAPLTDNWFTTITHIKAAA
>CP031166.1|AXV09907.1|120003_120621_+|CRISPR-associated-protein,-Cse3-family
MTHLTTTPMTHPAFAQARWHDARWTHKAVMGLFPTPLPDNGTGPRATSRILYRTEPDVAGGRILIQSDIPPVVDGVRTRPMDDVFVRYRPGGTVALLLHANTVRTINRTRDDGNVRTHRARVPDTLLNGWLKDRLEGAATLHGHIDTSPLERALGPRRRGRQQIITIYRATATITNPTRLIDLCTAGIGRNKAYGCGLLTALPTN
>CP031166.1|AXV09908.1|120620_121601_+|CRISPR-associated-protein-Cas1
MGYSPEAQTLRQPRIVDLPRSGDRISHLHLDRAKVFQDETGVAATLDTGDTVRIPAGSLAVLMLGQGCSITTPAQATLHRAGCNIMLSGADGTTAITTARPLTGRAKWAEAQARMWTAPNGRADAARILYSHQFPDLDWPATATIQRMRGLEGHQVKLLYKQHAARTKHRNWRRDTNGEDQPNRLLNLANAILYASATAAVTALGLNPALGIIHQGAVGALLFDLADIHKATASIPLAFDCSRDDDPAFHLRRRMRAYLHRNRVLAQHLRVLDEILTPHLDATDDVLLDEHGVVAGHTNHAPDADPIDTRPPPPDMEQLRQAVEDY
>CP031166.1|AXV09909.1|121600_121882_+|CRISPR-associated-protein,-Cas2
MQAVLHATAIPDHLRGYVSRLLQEVHTGLYIGIVTPKVADGLWDAVTTYAKEGTATLITTTNANEFGFDVRLHNSSTHRMTDFDGLQLPTERS
>CP031166.1|AXV09910.1|123007_123991_+|hypothetical-protein
MATKWGNHGFSVDDVAVWAATGATPFQAAEYRAAGFGPEETAAWMAVPDGLATFPPTGPMARRWMESPIYHDGITPADAHAWRGAGIESPDRAAEAFGWADRLGYADNADGDKWEPEDGPYPAEVQASVWARARFAPAEAQQWQQAGFTFDDGRGPSVARVWAGHIDDAEGAAAWRRVVGNNPGSAAALVRLGVTPDTYVTGDETFVSGPEAIGVFKARAFWRDIGVTDGREAQGWFAVGFDPWTAGEWKAADPTIDPATAASWKHHGFSPSVTAAWLAAFPFRCNPTQALRMSEAGWSPDTVKDELAGMPAEEAVRFADHAPVRAR
>CP031166.1|AXV09911.1|123966_124116_-|hypothetical-protein
MSGSRVPLHAAPIPALPEHRRAETALLMPPPFRPSLPGSAPGYRARTGA

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Crispr_ID: CP031166_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP031166_2

121901-122722

TypeI-E

Consensus_repeat	Method
GGATCACCCCCGCCTGCGCGGGGAGAAG	PILER-CR
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	CRISPRCasFinder
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	CRT

13 spacers

cas2,cas1,cas6e,cas5,cas7,cse2gr11,cas8e,cas3

The CRISPR arrays of CP031166_2

>merge|CP031166|2|121901-122722|PILER-CR,CRISPRCasFinder,CRT
CTTCTCCCCGCGCAGGCGGGGGTGATCCTGCGGGCATGAGGCCGGTTGTTGGGTTGGACTTCTTCTCCCCGCGCAGGCGGGGGTGATCCCAGTGCCTCCTCAACGAGGGAGGTCAGCTGGTCCTTCTCCCCGCGCAGGCGGGGGTGATCCCTTCCTGGCCGTCACCCAAACGGTCGCATCCGTCTTCTCCCCGCGCAGGCGGGGGTGATCCCGGCCGCCAGCCGGCGCTGACCGGATGCCGTTTCTTCTCCCCGCGCAGGCGGGGGTGATCCCCCGTCTGGCCTGCCCCGTTCCCGAGGTCCGCCCTTCTCCCCGCGCAGGCGGGGGTGATCCCTTGCCGGTCCACCCGGATTTCGCCGGCGGCCACTTCTCCCCGCGCAGGCGGGGGTGATCCTGGCCAGTTCTTCGCCGGCGCCATCTGGGGTGGCTTCTCCCCGCGCAGGCGGGGGTGATCCCTTAGTCCCGTTTTTTGGGTGGGGGCTGTTGGGCTTCTCCCCGCGCAGGCGGGGGTGATCCCTCAACCCACTCCGGCAGGTAGTCGCCGCGAGGTTTCTCCCCGCGCAGGCGGGGGTGATCCCGGGAGGTCGACCCGGCCCTCGGGGCATGGCCGCTTCTCCCCGCGCAGGCGGGGGTGATCCCTGGATCCTGCGCGGATCGCCGGGCACTCCCTTCTTCTCCCCGCGCAGGCGGGGGTGATCCCCTCGGCGACGCCGGCCTTGTGGAGACCCATCTCTTCTCCCCGCGCAGGCGGGGGTGATCCCCTGCCCGCGTGCGCCTCTCAGGGGAAGTGGCGCTTCTCCCCGCGCAGGCGGGGGTGATCCC

>CP031166|2|2|121901-122721|PILER-CR
CTTCTCCCCGCGCAGGCGGGGGTGATCC	TGCGGGCATGAGGCCGGTTGTTGGGTTGGACTT
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CAGTGCCTCCTCAACGAGGGAGGTCAGCTGGTC
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CTTCCTGGCCGTCACCCAAACGGTCGCATCCGT
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CGGCCGCCAGCCGGCGCTGACCGGATGCCGTTT
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CCCGTCTGGCCTGCCCCGTTCCCGAGGTCCGCC
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CTTGCCGGTCCACCCGGATTTCGCCGGCGGCCA
CTTCTCCCCGCGCAGGCGGGGGTGATCC	TGGCCAGTTCTTCGCCGGCGCCATCTGGGGTGG
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CTTAGTCCCGTTTTTTGGGTGGGGGCTGTTGGG
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CTCAACCCACTCCGGCAGGTAGTCGCCGCGAGG
TTTCTCCCCGCGCAGGCGGGGGTGATCC	CGGGAGGTCGACCCGGCCCTCGGGGCATGGCCG
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CTGGATCCTGCGCGGATCGCCGGGCACTCCCTT
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CCTCGGCGACGCCGGCCTTGTGGAGACCCATCT
CTTCTCCCCGCGCAGGCGGGGGTGATCC	CCTGCCCGCGTGCGCCTCTCAGGGGAAGTGGCG
CTTCTCCCCGCGCAGGCGGGGGTGATCC

>CP031166|2|2|121901-122722|CRISPRCasFinder
CTTCTCCCCGCGCAGGCGGGGGTGATCCT	GCGGGCATGAGGCCGGTTGTTGGGTTGGACTT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	AGTGCCTCCTCAACGAGGGAGGTCAGCTGGTC
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TTCCTGGCCGTCACCCAAACGGTCGCATCCGT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	GGCCGCCAGCCGGCGCTGACCGGATGCCGTTT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	CCGTCTGGCCTGCCCCGTTCCCGAGGTCCGCC
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TTGCCGGTCCACCCGGATTTCGCCGGCGGCCA
CTTCTCCCCGCGCAGGCGGGGGTGATCCT	GGCCAGTTCTTCGCCGGCGCCATCTGGGGTGG
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TTAGTCCCGTTTTTTGGGTGGGGGCTGTTGGG
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TCAACCCACTCCGGCAGGTAGTCGCCGCGAGG
TTTCTCCCCGCGCAGGCGGGGGTGATCCC	GGGAGGTCGACCCGGCCCTCGGGGCATGGCCG
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TGGATCCTGCGCGGATCGCCGGGCACTCCCTT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	CTCGGCGACGCCGGCCTTGTGGAGACCCATCT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	CTGCCCGCGTGCGCCTCTCAGGGGAAGTGGCG
CTTCTCCCCGCGCAGGCGGGGGTGATCCC

>CP031166|2|1|121901-122722|CRT
CTTCTCCCCGCGCAGGCGGGGGTGATCCT	GCGGGCATGAGGCCGGTTGTTGGGTTGGACTT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	AGTGCCTCCTCAACGAGGGAGGTCAGCTGGTC
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TTCCTGGCCGTCACCCAAACGGTCGCATCCGT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	GGCCGCCAGCCGGCGCTGACCGGATGCCGTTT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	CCGTCTGGCCTGCCCCGTTCCCGAGGTCCGCC
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TTGCCGGTCCACCCGGATTTCGCCGGCGGCCA
CTTCTCCCCGCGCAGGCGGGGGTGATCCT	GGCCAGTTCTTCGCCGGCGCCATCTGGGGTGG
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TTAGTCCCGTTTTTTGGGTGGGGGCTGTTGGG
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TCAACCCACTCCGGCAGGTAGTCGCCGCGAGG
TTTCTCCCCGCGCAGGCGGGGGTGATCCC	GGGAGGTCGACCCGGCCCTCGGGGCATGGCCG
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	TGGATCCTGCGCGGATCGCCGGGCACTCCCTT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	CTCGGCGACGCCGGCCTTGTGGAGACCCATCT
CTTCTCCCCGCGCAGGCGGGGGTGATCCC	CTGCCCGCGTGCGCCTCTCAGGGGAAGTGGCG
CTTCTCCCCGCGCAGGCGGGGGTGATCCC

Protein	Signature genes	Signature genes Name	Protein_function
CP031166.1\|AXV09913.1\|125348_126038_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379326
CP031166.1\|AXV09907.1\|120003_120621_+\|CRISPR-associated-protein,-Cse3-family	cas6e	cd09727_cas6e_CAS-I-E	gnl\|CDD\|187858
CP031166.1\|AXV09901.1\|112014_113004_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372196
CP031166.1\|AXV09917.1\|128135_130778_+\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09914.1\|126169_126625_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378815
CP031166.1\|AXV09908.1\|120620_121601_+\|CRISPR-associated-protein-Cas1	cas1	cd09719_cas1_CAS-I-E	gnl\|CDD\|274693
CP031166.1\|AXV09904.1\|117525_118119_+\|hypothetical-protein	cse2gr11	mkCas0096_cse2gr11_CAS-I-E	gnl\|CDD\|274193
CP031166.1\|AXV09912.1\|124353_125160_+\|ADP-ribose-pyrophosphatase	unknown	unknown	gnl\|CDD\|223979
CP031166.1\|AXV09905.1\|118133_119255_+\|CRISPR-associated-protein,-Cse4-family	cas7	pfam09344_cas7_CAS-I-E	gnl\|CDD\|378153
CP031166.1\|AXV09916.1\|126954_127716_-\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	unknown	unknown	gnl\|CDD\|143635
CP031166.1\|AXV09915.1\|126677_126911_-\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09919.1\|131192_131987_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|163057
CP031166.1\|AXV09902.1\|113339_115922_+\|CRISPR-associated-helicase-Cas3	cas3	cd09639_cas3_CAS-I	gnl\|CDD\|182031
CP031166.1\|AXV09909.1\|121600_121882_+\|CRISPR-associated-protein,-Cas2	cas2	pfam09707_cas2_CAS-I-E	gnl\|CDD\|378244
CP031166.1\|AXV09903.1\|115918_117529_+\|hypothetical-protein	cas8e	pfam09481_cas8e_CAS-I-E	gnl\|CDD\|187860
CP031166.1\|AXV09910.1\|123007_123991_+\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09906.1\|119251_120007_+\|CRISPR-associated-protein,-Cas5e-family	cas5	cd09645_cas5_CAS-I-E	gnl\|CDD\|273842
CP031166.1\|AXV09918.1\|131032_131206_-\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09900.1\|111772_112018_+\|hypothetical-protein	unknown	unknown	unknown
CP031166.1\|AXV09911.1\|123966_124116_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
CP031166.1\|AXV09913.1\|125348_126038_+\|hypothetical-protein	gnl\|CDD\|379326	pfam13673, Acetyltransf_10, Acetyltransferase (GNAT) domain. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	0.00126409
CP031166.1\|AXV09907.1\|120003_120621_+\|CRISPR-associated-protein,-Cse3-family	gnl\|CDD\|187858	cd09727, Cas6_I-E, CRISPR/Cas system-associated RAMP superfamily protein Cas6e. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Cas6e is an endoribonuclease that generates crRNA; This family is specific for CRISPR/Cas system I-E subtype; Homologous to Cas6 (RAMP superfamily protein); Possesses double RRM/ferredoxin fold; also known as Cse3 family.	2.17597e-28
CP031166.1\|AXV09901.1\|112014_113004_+\|hypothetical-protein	gnl\|CDD\|372196	pfam12569, NARP1, NMDA receptor-regulated protein 1. This domain family is found in eukaryotes, and is approximately 40 amino acids in length. The family is found in association with pfam07719, pfam00515. There is a single completely conserved residue L that may be functionally important. NARP1 is the mammalian homolog of a yeast N-terminal acetyltransferase that regulates entry into the G(0) phase of the cell cycle.	0.00578752
CP031166.1\|AXV09914.1\|126169_126625_+\|hypothetical-protein	gnl\|CDD\|378815	pfam12120, Arr-ms, Rifampin ADP-ribosyl transferase. This protein is found in bacteria. Proteins in this family are typically between 136 to 150 amino acids in length. The opportunistic pathogen Mycobacterium smegmatis is resistant to rifampin because of the presence of a chromosomally encoded rifampin ADP-ribosyltransferase (Arr-ms). Arr-ms is a small enzyme whose activity thus renders rifamycin antibiotics ineffective.	0.000249641
CP031166.1\|AXV09908.1\|120620_121601_+\|CRISPR-associated-protein-Cas1	gnl\|CDD\|274693	TIGR03638, cas1_ECOLI, CRISPR-associated endonuclease Cas1, subtype I-E/ECOLI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 protein particular to the ECOLI subtype of CRISPR/Cas system.	1.62685e-63
CP031166.1\|AXV09904.1\|117525_118119_+\|hypothetical-protein	gnl\|CDD\|274193	TIGR02548, CRISPR_system_Cascade_subunit_CasB, CRISPR type I-E/ECOLI-associated protein CasB/Cse2. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This model family is found in Ecoli subtype CRISPR/Cas regions of many bacteria, most of which are mesophiles, and not in Archaea. It was designated Cse2 originally, and renamed CasB based on its characterization in the CASCADE complex.	7.53363e-05
CP031166.1\|AXV09912.1\|124353_125160_+\|ADP-ribose-pyrophosphatase	gnl\|CDD\|223979	COG1051, COG1051, ADP-ribose pyrophosphatase [Nucleotide transport and metabolism].	3.25592e-23
CP031166.1\|AXV09905.1\|118133_119255_+\|CRISPR-associated-protein,-Cse4-family	gnl\|CDD\|378153	pfam09344, Cas_CT1975, CT1975-like protein. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This family is represented by CT1975 of Chlorobium tepidum.	2.88447e-78
CP031166.1\|AXV09919.1\|131192_131987_-\|hypothetical-protein	gnl\|CDD\|163057	TIGR02881, Stage_V_sporulation_protein_K, stage V sporulation protein K. Members of this protein family are the stage V sporulation protein K (SpoVK), a close homolog of the Rubisco expression protein CbbX (TIGR02880) and a members of the ATPase family associated with various cellular activities (pfam00004). Members are strictly limited to bacterial endospore-forming species, but are not universal in this group and are missing from the Clostridium group. [Cellular processes, Sporulation and germination].	1.99038e-83
CP031166.1\|AXV09902.1\|113339_115922_+\|CRISPR-associated-helicase-Cas3	gnl\|CDD\|182031	PRK09694, PRK09694, CRISPR-associated helicase/endonuclease Cas3.	4.64995e-75
CP031166.1\|AXV09909.1\|121600_121882_+\|CRISPR-associated-protein,-Cas2	gnl\|CDD\|378244	pfam09707, Cas_Cas2CT1978, CRISPR-associated protein (Cas_Cas2CT1978). This entry represents a minor branch of the Cas2 family of CRISPR-associated protein which are found in IPR003799. Cas proteins are found adjacent to a characteristic short, palindromic repeat cluster termed CRISPR, a probable mobile DNA element.	1.2151e-23
CP031166.1\|AXV09903.1\|115918_117529_+\|hypothetical-protein	gnl\|CDD\|187860	cd09729, Cse1_I-E, CRISPR/Cas system-associated protein Cse1. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Large proteins, some contain Zn-finger domain; subunit of the Cascade complex; signature gene for I-E subtype; also known as Cse1/CasA/YgcL family.	1.31355e-19
CP031166.1\|AXV09916.1\|126954_127716_-\|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	3.85852e-44
CP031166.1\|AXV09906.1\|119251_120007_+\|CRISPR-associated-protein,-Cas5e-family	gnl\|CDD\|273842	TIGR01868, hypothetical_protein, CRISPR-associated protein Cas5/CasD, subtype I-E/ECOLI. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This family is part of the ECOLI subtype CRISPR/Cas locus, and now characterized as part of the CASCADE complex of that system. It shares a small N-terminal homology region with members of several other CRISPR/Cas subtypes, and we view the families that share this region as being Cas5.	1.46338e-25

>CP031166.1|AXV09909.1|121600_121882_+|CRISPR-associated-protein,-Cas2
MQAVLHATAIPDHLRGYVSRLLQEVHTGLYIGIVTPKVADGLWDAVTTYAKEGTATLITTTNANEFGFDVRLHNSSTHRMTDFDGLQLPTERS
>CP031166.1|AXV09908.1|120620_121601_+|CRISPR-associated-protein-Cas1
MGYSPEAQTLRQPRIVDLPRSGDRISHLHLDRAKVFQDETGVAATLDTGDTVRIPAGSLAVLMLGQGCSITTPAQATLHRAGCNIMLSGADGTTAITTARPLTGRAKWAEAQARMWTAPNGRADAARILYSHQFPDLDWPATATIQRMRGLEGHQVKLLYKQHAARTKHRNWRRDTNGEDQPNRLLNLANAILYASATAAVTALGLNPALGIIHQGAVGALLFDLADIHKATASIPLAFDCSRDDDPAFHLRRRMRAYLHRNRVLAQHLRVLDEILTPHLDATDDVLLDEHGVVAGHTNHAPDADPIDTRPPPPDMEQLRQAVEDY
>CP031166.1|AXV09907.1|120003_120621_+|CRISPR-associated-protein,-Cse3-family
MTHLTTTPMTHPAFAQARWHDARWTHKAVMGLFPTPLPDNGTGPRATSRILYRTEPDVAGGRILIQSDIPPVVDGVRTRPMDDVFVRYRPGGTVALLLHANTVRTINRTRDDGNVRTHRARVPDTLLNGWLKDRLEGAATLHGHIDTSPLERALGPRRRGRQQIITIYRATATITNPTRLIDLCTAGIGRNKAYGCGLLTALPTN
>CP031166.1|AXV09906.1|119251_120007_+|CRISPR-associated-protein,-Cas5e-family
MTTILLRLAAPLMAFGTTSRFDNRATDADPSLSAVHGLLTAAAGITRDQPRPDWITHALPAIRVDRDGHTLPDYQTVNQPPLRRYRELSDHDLRKVYTVAMPDGSRKPNSTKTKQPATVQSRRGYLTDATFLITLPDPTGNLNEALARPRFHLYAGRKGCPVTEPFLLGTTTDDPVAALTTTPTPRTGPDDTGERRAVLFANPADNSRHEDRNDLPSGGRRHRTARRWHTTVTAPLTDNWFTTITHIKAAA
>CP031166.1|AXV09905.1|118133_119255_+|CRISPR-associated-protein,-Cse4-family
MIRYANFHILHPLAFSNPNRDDTGAPKTTTYGGTVRGRMSSQSQKRAARTAFEGQTTADRTHRSKYAADRLLDTTTTLLAANGTTLTPDQTEKLHKSVRTEIGKLTGKADDAKATLVWLAEAELNGLAAKLAVKAGAEMTKDDIDAALSTTTDSLTIAAFGRMFASRADLAIEAAAQVGHAFTTHAQANDLDYLTAFDDLQASYDTPDDDGNVKGAGAGHLDVNEFHSGVFYRYFNLNRDDLTDNWRPLTNQGAPGTTERLEAFLREMTIQLPTGRDATAAHQTPPAYVMVTFTERAATLAPAFETPVAGGANDGYLPGSIAALTGYADAIARIYGPDHRIVVNLTDPDAQTTLADLTGAVANWVVSGTLSTP
>CP031166.1|AXV09904.1|117525_118119_+|hypothetical-protein
MTDTARPPRTVDALIALRADTGARTAMRRGLSQATEHYAYPYLAHRWQGRPWARTPTLRIAGLIAVTSLADEPAGDRIGTTLRRVALADRPAPGDATDRALDRIGKRLLWAQTGDLAKFHQVLTGLLPNAPLGRIDWQELHDTYLRWGHPHPDARRRIRLRVIEDFYSPVPRAEREPDPGPADENADAPKPTQPTLI
>CP031166.1|AXV09903.1|115918_117529_+|hypothetical-protein
MSTTTTTKLHDRIVGLLPATPTYNLTVERWIPVIGPDGPDTVGLAGLLDRAHRLDLDDAGHGPLWRHSMERLLIGIGHLIAQAAPGHDWAAVANSGLPLPADGATSVLARLADRLWLHHPTSPFLQRLDVLSHMDDKPDKPIVEVTDPFWALLPDVPSKSNSAWFNRADPDAKTGPADAANALLVRHTWAVPGNETKNGVGKARSEGGSAGQGANDLTHLTIGGPTVAATIARNLIGDWVDRGQRLWFENPAGAVGVLAADDPDPLWLYTATTASTVLIPMFGGYRVVRSPMPEPPEVAKQLGTTLKANNPHTVRFTSVDGKTTPTLRLPVPSCGSDLLRRYHSRLAGGRPLTPSVLDLRGLHVRPARRPMVRALIVIGAGQAAGARVGDVAVAASELADLTLPAPAAVRFAELARIIFGPSPSVRSRTATAISTVRGADGEDDRKQIRASVEHDLTVAADAVVFRLLSACRRNADGDLPDRIPVPDSRLLIDTALGCFDRHVAPLTHRPATAATAVVQRRRLVRHLTRLLSEETP
>CP031166.1|AXV09902.1|113339_115922_+|CRISPR-associated-helicase-Cas3
MAHLVDTAAVASALVDRWVPSRLLDDPTREAVVAAAGLHDLGKAGPVFQGQLMARRRDSRFADHLAGLSTAGLGCPGPVLSGVRLAAGEEQALLRRHEVLSAAILAGRVEDAGAEGLAALVAGHHGCWRLPFDDYGAVPVALEAVRSDPGWSAWHRDAIAVIEGLVGGAGTSAVDPVVVPVAAGVVVVADWLASHLADVDPSGVEGADGDWEVWFERRVGDAHRLVEDLLGVPVRPAGSVEDILGVPSLRPVQQAVSASTARGLRLVMAPTGEGKTEAAFGRWLAHHAGAGSGLLFALPTMATTDAMLERVRPLFADTDARGALAHGRSILNGFNRPAGPLHGSVHNGPGGLSPSWWFNGRGRQVLAPVTVCTVDQVLLSVLAHRHNFVRLLGVFSKMVVVDEVHTFDPYMSGLLERFLRWAGRFGVDVVLMSATLPAERQRTYVEAYADGPAGLPAAVYPSVVTCTGGVVDVSPVAMSRPARTVVIDRMSFGGPDDIARYVAGVVAAHPDAKVGVILNTVGRVQQVATALHALLGCSGTHADGRCGTLWTAHSRFPAAVRSRQTAAMLGEFGPDSTTGAAVLVATQVVEMSLDIDLDLLITDLCPAPSLVQRIGRLHRHTHDPAVRRRPGGMRHPRVVLVTPDPWPDGPAGWLPYPAPVIGATWEHGLGGGAVNELVVPNDVQAFVDRSHLPVTALYGPEGEGLADELVTHLLGESAKAQRAGRAAIPTPEAMTSRTAAALEKFANAEVDGLRLSTRWDDTPTALVLLHNPDGPPGASTNGVWGGPIPSAPGYDEQAELLGCTVTISGRQAFDVTPRDDIGRPSPGRWDGTLLHDVVPLPLPSPDWDPDPLTGLTRRDQ
>CP031166.1|AXV09901.1|112014_113004_+|hypothetical-protein
MSRNEAETGEWVLPSAEVARVKKALRAAHNGVAEAAYREAKAFWKQHGTQSATKYAEAADRFVAQISPRPPSLYGRPDPRAAHQRAVADAVREVLDRIAWHARGGGQALHGATWDDMDGVGWGRKTNRDTTFGDAEASVRINEKTRTLRWTVEENNHAVEHAHDGLLGKTLFGHLAKVKWTRGTGGIVRYLSEYDTDGFGLSNGSRLSQWHGPRGAEVWKQETGHYPYDSPQGKAEAAKAQEKERKKAAAARKRAAAKRQKQAQQAAQKQAAGSSYCGAVKKDASGLCGRKLASGKCPDHGTIGAQMAIGVTTVGSVVPAAAVTADPMG
>CP031166.1|AXV09900.1|111772_112018_+|hypothetical-protein
MATPDGRPPDLQPAGTLYINQGGRVTCTTHGGGYLQAAAGQQRYVDGDHITTPLDDWEVFSPEVVAEDGLECETCARGGHR
>CP031166.1|AXV09910.1|123007_123991_+|hypothetical-protein
MATKWGNHGFSVDDVAVWAATGATPFQAAEYRAAGFGPEETAAWMAVPDGLATFPPTGPMARRWMESPIYHDGITPADAHAWRGAGIESPDRAAEAFGWADRLGYADNADGDKWEPEDGPYPAEVQASVWARARFAPAEAQQWQQAGFTFDDGRGPSVARVWAGHIDDAEGAAAWRRVVGNNPGSAAALVRLGVTPDTYVTGDETFVSGPEAIGVFKARAFWRDIGVTDGREAQGWFAVGFDPWTAGEWKAADPTIDPATAASWKHHGFSPSVTAAWLAAFPFRCNPTQALRMSEAGWSPDTVKDELAGMPAEEAVRFADHAPVRAR
>CP031166.1|AXV09911.1|123966_124116_-|hypothetical-protein
MSGSRVPLHAAPIPALPEHRRAETALLMPPPFRPSLPGSAPGYRARTGA
>CP031166.1|AXV09912.1|124353_125160_+|ADP-ribose-pyrophosphatase
MLAGYDLGRWPSRDTVDIVLVDPAGRVLMIERGKPPYAGHGALPGGFVDHGEEPQDAAVRELAEETGLDVSADDVVFVMNSSDISRDPRGPIRTTVYAARVPAEVLDRAVGADDARDARPVHAHDLAGMKLAFDHRNLLAHALGMEQMRDRVNWRDAERLLAGVASDAARNWSFSDEVRAARAGRIASELAGHGIDTSVIGGQVVCRRQRHPGWPVHEMRWDTVMTGPAGRPIVFCVDGRKVREEPAPGPDGVAAQLADLFDRHDPRR
>CP031166.1|AXV09913.1|125348_126038_+|hypothetical-protein
MHREVDAGDVAYRAVAAFVDGAEVGRLTWQEAPDYSHYPETGWPDDAEETATIAMVKVDEDHRRRGVATGMLAAARAAVDEDGYSIHHSGDLWPDGAAWAAAVDGQSASEVVVDLVGRFGRLEPGLVARWADPVGASAQCTDAAERFRDWAWDNDVDATIRVHHDPTGEVRRPKGWAGRVGHVTVSVDGATVDFTAAQFWPDAPCPLVEPDDVYAARWSETADRDPQVR
>CP031166.1|AXV09914.1|126169_126625_+|hypothetical-protein
MVTADPFAAPAPASDPEPKGRTVTARWVGDPDDPRRHFTRFFHGTTVVLDEGEEILPAEETGAKRAHWNMGHGTMAYATGTEDDGWRWAELAWNNTDGGRPRVYEVEPVGAWLGDDEDDAGSLAVMSPHGWRVVRAVGFPPEWGGEDADWE
>CP031166.1|AXV09915.1|126677_126911_-|hypothetical-protein
MRKSARPHRALGLPNRSRQPADPQNLRTSPRAGGGDPWFGDDDDDAGSLSPRRRGRSPQAVALARARTLPRAGGAIL
>CP031166.1|AXV09916.1|126954_127716_-|diguanylate-cyclase/phosphodiesterase-(GGDEF-&-EAL-domains)-with-PAS/PAC-sensor(s)
MWAVRTVPTRIAALSVLLDGPVDAVTCDLGLPDNDGHDVVADIATHLPDLPLVVLSGQEEAGMGLRSLRAGATDYLPKSQIDRLPEILDMAIHRNEHELMCRQLASTDPLTGSANRDALTDAWNATGHDTAVVIVLADLDRFKQVNDQHGHNTGDLVLRELAGHLRGAVRPTDIVARIGGDEFVVLAEMPHDSVSGFLDRLHQQMGAPVRVGDISVTSSIGAATKCIDDTLDDALSRADQAMYAAKRDRHHTI
>CP031166.1|AXV09917.1|128135_130778_+|hypothetical-protein
MTSSLADARTAYLAALADAAAIELAAFLADFGRPGATVIVVEPDLFLRSVELIEVVFADGTTMGRDDLDDVDVPLCVHQGFDNVEALGEWAANAALGNIEELRVPSDRAVRDAINGMRAAIDTAASHDAASLSDLIGATNGVVAALRSAGTDSPMTQAALNAMDGWHADIDAGCTECFGNGGFDADGDATEHFDPDDGGSACGNCEGSGSEPDDVVTAATIELFTARWEAVNAAYGGHTAPRAPEAYTPLHVADECDECGADLTGTTAMQSWAHDRTCSLFPANEVGYGQVFATLAADAMGGSAAWHGSRPTRLTVRADVSDSEVGTGRGVFDVIGAKGPDYERAYRGNDWWGLCVPADVADPTRRALSMAAGGLLADMPEGLFVFDLDVPPAGPDDGDGGLVPDGDGPEGRLAAALAGEIERRTGDRPVRIDVAAEVAVDQVGSGSGDVFVLNYRTTDGAVHVREQTAGWALHPLADDSVAHVAEVRGATERFLVDMPAGVTPANLVVPQPCGWCGAAGGAVTQRADHAADCAAREAFCAACDQIVRGIDWGHLPEAHANGCPDPVAPARLTTPASPHADPCRCGGVEECECPPPKPCDHCQVEFDDHAAATRPALGHDPACPFTLATFTDPLMADVAVALAGRAPAGEAGRLVRAIAAHAEELADHPVVLSRLLPMIDAAADAQPVGTRPDGLAGSVADALVARGVEPGRANGLCADGEAWARWIGPMVEDVGAWVGPLGGMSDAAVADAAVEAVKRTRGVNAKAARRLIGQLGGPHADDTVRRVVAAAVGPVTLHTVDELLARLLPEGWTVAGGDGRVVLVRPDGIDVFLVGHDDWSVAAVRGADGRHWSVSTGLPADGGSHPVKAARRIAALAERD
>CP031166.1|AXV09918.1|131032_131206_-|hypothetical-protein
MRPGDFPDDDLIVCAVESGREDVLRAWLMAVPTRPHPRPAPTTPKPGINHPPSQSQA
>CP031166.1|AXV09919.1|131192_131987_-|hypothetical-protein
MGALENLIGLEDIKTQVRGIANLLKVSALRRAEGLPAVDVAHHYIFTGPPGTGKTTVARLMGRIFAAAGELSRGHLVEIDRSGLIGGYLGQTALKTNEIIDTALDGVLFIDEAYSLAADTDRYGSEAIASLLKRMEDDRDRLVVIAAGYPKPMKTFLDSNPGLASRFTETVEFPPYAVDELVALLYGHIIKHGYHLDGSGEEAVRQLLVQKVAEANDAFGNGRYVRNLFDDLITAHANRIAGTAAPTRTALMTITSEDVNDAAG

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	113027-113054	0	1.0
CP031166_1	1.2\|113092\|33\|CP031166\|PILER-CR	113092-113124	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	113082-113114	0	1.0
CP031166_1	1.3\|113026\|33\|CP031166\|CRISPRCasFinder	113026-113058	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	113026-113058	0	1.0
CP031166_1	1.4\|113087\|32\|CP031166\|CRISPRCasFinder	113087-113118	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	113087-113118	0	1.0
CP031166_2	2.1\|121929\|33\|CP031166\|PILER-CR	121929-121961	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	121929-121961	0	1.0
CP031166_2	2.2\|121990\|33\|CP031166\|PILER-CR	121990-122022	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	121990-122022	0	1.0
CP031166_2	2.3\|122051\|33\|CP031166\|PILER-CR	122051-122083	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122051-122083	0	1.0
CP031166_2	2.4\|122112\|33\|CP031166\|PILER-CR	122112-122144	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122112-122144	0	1.0
CP031166_2	2.5\|122173\|33\|CP031166\|PILER-CR	122173-122205	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122173-122205	0	1.0
CP031166_2	2.6\|122234\|33\|CP031166\|PILER-CR	122234-122266	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122234-122266	0	1.0
CP031166_2	2.7\|122295\|33\|CP031166\|PILER-CR	122295-122327	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122295-122327	0	1.0
CP031166_2	2.8\|122356\|33\|CP031166\|PILER-CR	122356-122388	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122356-122388	0	1.0
CP031166_2	2.9\|122417\|33\|CP031166\|PILER-CR	122417-122449	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122417-122449	0	1.0
CP031166_2	2.10\|122478\|33\|CP031166\|PILER-CR	122478-122510	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122478-122510	0	1.0
CP031166_2	2.11\|122539\|33\|CP031166\|PILER-CR	122539-122571	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122539-122571	0	1.0
CP031166_2	2.12\|122600\|33\|CP031166\|PILER-CR	122600-122632	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122600-122632	0	1.0
CP031166_2	2.13\|122661\|33\|CP031166\|PILER-CR	122661-122693	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122661-122693	0	1.0
CP031166_2	2.14\|121930\|32\|CP031166\|CRISPRCasFinder,CRT	121930-121961	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	121930-121961	0	1.0
CP031166_2	2.15\|121991\|32\|CP031166\|CRISPRCasFinder,CRT	121991-122022	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	121991-122022	0	1.0
CP031166_2	2.16\|122052\|32\|CP031166\|CRISPRCasFinder,CRT	122052-122083	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122052-122083	0	1.0
CP031166_2	2.17\|122113\|32\|CP031166\|CRISPRCasFinder,CRT	122113-122144	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122113-122144	0	1.0
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122174-122205	0	1.0
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122235-122266	0	1.0
CP031166_2	2.20\|122296\|32\|CP031166\|CRISPRCasFinder,CRT	122296-122327	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122296-122327	0	1.0
CP031166_2	2.21\|122357\|32\|CP031166\|CRISPRCasFinder,CRT	122357-122388	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122357-122388	0	1.0
CP031166_2	2.22\|122418\|32\|CP031166\|CRISPRCasFinder,CRT	122418-122449	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122418-122449	0	1.0
CP031166_2	2.23\|122479\|32\|CP031166\|CRISPRCasFinder,CRT	122479-122510	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122479-122510	0	1.0
CP031166_2	2.24\|122540\|32\|CP031166\|CRISPRCasFinder,CRT	122540-122571	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122540-122571	0	1.0
CP031166_2	2.25\|122601\|32\|CP031166\|CRISPRCasFinder,CRT	122601-122632	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122601-122632	0	1.0
CP031166_2	2.26\|122662\|32\|CP031166\|CRISPRCasFinder,CRT	122662-122693	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	122662-122693	0	1.0
CP031166_3	3.1\|126706\|36\|CP031166\|CRISPRCasFinder	126706-126741	36	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	126706-126741	0	1.0
CP031166_3	3.2\|126765\|38\|CP031166\|CRISPRCasFinder	126765-126802	38	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	126765-126802	0	1.0
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NC_012586	Sinorhizobium fredii NGR234 plasmid pNGR234b, complete sequence	1820460-1820487	4	0.857
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP019319	Tateyamaria omphalii strain DOK1-4 plasmid pDOK1-4-7, complete sequence	28577-28604	4	0.857
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP050953	Rhodococcus sp. DMU1 plasmid unnamed	410401-410428	4	0.857
CP031166_1	1.4\|113087\|32\|CP031166\|CRISPRCasFinder	113087-113118	32	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	348242-348273	4	0.875
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP017076	Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence	878740-878767	5	0.821
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP035514	Haematobacter massiliensis strain OT1 plasmid pOT1-4, complete sequence	19591-19618	5	0.821
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP013635	Rhizobium sp. N324 plasmid pRspN324e, complete sequence	173498-173525	5	0.821
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP020952	Rhizobium sp. CIAT894 plasmid pRheCIAT894e, complete sequence	284340-284367	5	0.821
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP007795	Azospirillum brasilense strain Az39 plasmid AbAZ39_p2, complete sequence	742698-742725	5	0.821
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP054028	Rhizobium sp. JKLM19E plasmid pPR19E01, complete sequence	127249-127276	5	0.821
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP032323	Azospirillum brasilense strain MTCC4035 plasmid p2, complete sequence	346768-346795	5	0.821
CP031166_2	2.4\|122112\|33\|CP031166\|PILER-CR	122112-122144	33	NZ_CP013110	Sinorhizobium americanum strain CFNEI 73 plasmid C, complete sequence	816652-816684	5	0.848
CP031166_2	2.4\|122112\|33\|CP031166\|PILER-CR	122112-122144	33	NZ_CP029452	Sinorhizobium fredii CCBAU 25509 plasmid pSF25509b, complete sequence	856360-856392	5	0.848
CP031166_2	2.4\|122112\|33\|CP031166\|PILER-CR	122112-122144	33	NZ_CP013054	Sinorhizobium americanum CCGM7 plasmid C, complete sequence	1576760-1576792	5	0.848
CP031166_2	2.4\|122112\|33\|CP031166\|PILER-CR	122112-122144	33	NZ_CP023071	Sinorhizobium fredii CCBAU 83666 plasmid pSF83666b, complete sequence	815677-815709	5	0.848
CP031166_2	2.7\|122295\|33\|CP031166\|PILER-CR	122295-122327	33	KM233689	Pseudomonas phage H70, complete genome	20636-20668	5	0.848
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP016452	Sinorhizobium sp. RAC02 plasmid pBSY16_1, complete sequence	2026015-2026046	5	0.844
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP017422	Arthrobacter sp. ZXY-2 plasmid pZXY21, complete sequence	34782-34809	6	0.786
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_AP022593	Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence	3196540-3196567	6	0.786
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	AP021850	Deinococcus grandis ATCC 43672 plasmid: pDEGR-1 DNA, complete genome	279393-279420	6	0.786
CP031166_2	2.23\|122479\|32\|CP031166\|CRISPRCasFinder,CRT	122479-122510	32	NZ_CP032325	Azospirillum brasilense strain MTCC4035 plasmid p4, complete sequence	27688-27719	6	0.812
CP031166_2	2.23\|122479\|32\|CP031166\|CRISPRCasFinder,CRT	122479-122510	32	NZ_CP032349	Azospirillum brasilense strain MTCC4039 plasmid p3, complete sequence	317917-317948	6	0.812
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NC_019846	Sinorhizobium meliloti GR4 plasmid pRmeGR4a, complete sequence	7188-7215	7	0.75
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	MG962366	Rhodococcus phage Finch, complete genome	107083-107110	7	0.75
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP045386	Ruegeria sp. THAF33 plasmid pTHAF33_b, complete sequence	134906-134933	7	0.75
CP031166_1	1.3\|113026\|33\|CP031166\|CRISPRCasFinder	113026-113058	33	NZ_CP019319	Tateyamaria omphalii strain DOK1-4 plasmid pDOK1-4-7, complete sequence	28573-28605	7	0.788
CP031166_1	1.4\|113087\|32\|CP031166\|CRISPRCasFinder	113087-113118	32	NZ_AP022593	Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence	3660039-3660070	7	0.781
CP031166_2	2.4\|122112\|33\|CP031166\|PILER-CR	122112-122144	33	AB967974	Aurantimonas phage AmM-1 DNA, complete sequence	45619-45651	7	0.788
CP031166_2	2.10\|122478\|33\|CP031166\|PILER-CR	122478-122510	33	MT723933	Streptomyces phage Keanu, complete genome	72943-72975	7	0.788
CP031166_2	2.12\|122600\|33\|CP031166\|PILER-CR	122600-122632	33	NZ_CP024314	Rhizobium sp. NXC24 plasmid pRspNXC24c, complete sequence	1617102-1617134	7	0.788
CP031166_2	2.17\|122113\|32\|CP031166\|CRISPRCasFinder,CRT	122113-122144	32	AB967974	Aurantimonas phage AmM-1 DNA, complete sequence	45619-45650	7	0.781
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	NZ_CP023455	Rhodobacteraceae bacterium QY30 plasmid unnamed, complete sequence	17376-17407	7	0.781
CP031166_2	2.20\|122296\|32\|CP031166\|CRISPRCasFinder,CRT	122296-122327	32	NZ_CP017076	Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence	721279-721310	7	0.781
CP031166_2	2.23\|122479\|32\|CP031166\|CRISPRCasFinder,CRT	122479-122510	32	MT723933	Streptomyces phage Keanu, complete genome	72943-72974	7	0.781
CP031166_2	2.24\|122540\|32\|CP031166\|CRISPRCasFinder,CRT	122540-122571	32	NZ_CP033228	Sphingobium yanoikuyae strain SJTF8 plasmid pF2, complete sequence	111186-111217	7	0.781
CP031166_2	2.25\|122601\|32\|CP031166\|CRISPRCasFinder,CRT	122601-122632	32	NC_009620	Sinorhizobium medicae WSM419 plasmid pSMED01, complete sequence	363262-363293	7	0.781
CP031166_2	2.25\|122601\|32\|CP031166\|CRISPRCasFinder,CRT	122601-122632	32	NZ_CP024314	Rhizobium sp. NXC24 plasmid pRspNXC24c, complete sequence	1617102-1617133	7	0.781
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP017427	Methylobacterium sp. XJLW plasmid unnamed1, complete sequence	81137-81164	8	0.714
CP031166_1	1.1\|113031\|28\|CP031166\|PILER-CR	113031-113058	28	NZ_CP029174	Methylobacterium sp. DM1 plasmid pLVM1, complete sequence	237604-237631	8	0.714
CP031166_1	1.2\|113092\|33\|CP031166\|PILER-CR	113092-113124	33	NZ_CP031166	Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence	348237-348269	8	0.758
CP031166_1	1.3\|113026\|33\|CP031166\|CRISPRCasFinder	113026-113058	33	NC_012586	Sinorhizobium fredii NGR234 plasmid pNGR234b, complete sequence	1820459-1820491	8	0.758
CP031166_1	1.4\|113087\|32\|CP031166\|CRISPRCasFinder	113087-113118	32	MH673674	Thermus phage phiMa, complete genome	15668-15699	8	0.75
CP031166_2	2.6\|122234\|33\|CP031166\|PILER-CR	122234-122266	33	NZ_CP022762	Ralstonia solanacearum strain T95 plasmid unnamed, complete sequence	1112220-1112252	8	0.758
CP031166_2	2.6\|122234\|33\|CP031166\|PILER-CR	122234-122266	33	NZ_CP014703	Ralstonia solanacearum strain KACC 10722 plasmid, complete sequence	1111317-1111349	8	0.758
CP031166_2	2.6\|122234\|33\|CP031166\|PILER-CR	122234-122266	33	NZ_CP022771	Ralstonia solanacearum strain T51 plasmid unnamed, complete sequence	1112212-1112244	8	0.758
CP031166_2	2.6\|122234\|33\|CP031166\|PILER-CR	122234-122266	33	NZ_CP022777	Ralstonia solanacearum strain T11 plasmid unnamed, complete sequence	1111568-1111600	8	0.758
CP031166_2	2.6\|122234\|33\|CP031166\|PILER-CR	122234-122266	33	NZ_CP022799	Ralstonia solanacearum strain SL2064 plasmid unnamed, complete sequence	1112203-1112235	8	0.758
CP031166_2	2.9\|122417\|33\|CP031166\|PILER-CR	122417-122449	33	NZ_AP014705	Methylobacterium aquaticum strain MA-22A plasmid pMaq22A_1p, complete sequence	427967-427999	8	0.758
CP031166_2	2.11\|122539\|33\|CP031166\|PILER-CR	122539-122571	33	NZ_CP033228	Sphingobium yanoikuyae strain SJTF8 plasmid pF2, complete sequence	111186-111218	8	0.758
CP031166_2	2.12\|122600\|33\|CP031166\|PILER-CR	122600-122632	33	NC_009620	Sinorhizobium medicae WSM419 plasmid pSMED01, complete sequence	363261-363293	8	0.758
CP031166_2	2.12\|122600\|33\|CP031166\|PILER-CR	122600-122632	33	NZ_CP006991	Rhizobium sp. IE4771 plasmid pRetIE4771e, complete sequence	701750-701782	8	0.758
CP031166_2	2.12\|122600\|33\|CP031166\|PILER-CR	122600-122632	33	NZ_CP043499	Rhizobium grahamii strain BG7 plasmid unnamed, complete sequence	1397441-1397473	8	0.758
CP031166_2	2.12\|122600\|33\|CP031166\|PILER-CR	122600-122632	33	NZ_CP021128	Rhizobium sp. Kim5 plasmid pRetKim5d, complete sequence	642259-642291	8	0.758
CP031166_2	2.12\|122600\|33\|CP031166\|PILER-CR	122600-122632	33	CP007645	Rhizobium etli bv. phaseoli str. IE4803 plasmid pRetIE4803d, complete sequence	700671-700703	8	0.758
CP031166_2	2.17\|122113\|32\|CP031166\|CRISPRCasFinder,CRT	122113-122144	32	NZ_CP007130	Gemmatirosa kalamazoonesis strain KBS708 plasmid 2, complete sequence	337302-337333	8	0.75
CP031166_2	2.17\|122113\|32\|CP031166\|CRISPRCasFinder,CRT	122113-122144	32	NZ_CP017242	Rhizobium etli 8C-3 plasmid pRsp8C3a, complete sequence	185445-185476	8	0.75
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	NZ_CP012185	Pseudonocardia sp. EC080619-01 plasmid pBCI1-2, complete sequence	206856-206887	8	0.75
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	NZ_CP012182	Pseudonocardia sp. EC080610-09 plasmid pBCI2-1, complete sequence	130209-130240	8	0.75
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP022762	Ralstonia solanacearum strain T95 plasmid unnamed, complete sequence	1112221-1112252	8	0.75
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NC_017966	Tistrella mobilis KA081020-065 plasmid pTM2, complete sequence	88807-88838	8	0.75
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP014703	Ralstonia solanacearum strain KACC 10722 plasmid, complete sequence	1111318-1111349	8	0.75
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP022771	Ralstonia solanacearum strain T51 plasmid unnamed, complete sequence	1112213-1112244	8	0.75
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP022777	Ralstonia solanacearum strain T11 plasmid unnamed, complete sequence	1111569-1111600	8	0.75
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP022799	Ralstonia solanacearum strain SL2064 plasmid unnamed, complete sequence	1112204-1112235	8	0.75
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP019940	Ketogulonicigenium robustum strain SPU_B003 plasmid unnamed3, complete sequence	4501-4532	8	0.75
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP022567	Rhizobium leguminosarum bv. viciae strain BIHB 1148 plasmid pSK03, complete sequence	144785-144816	8	0.75
CP031166_2	2.20\|122296\|32\|CP031166\|CRISPRCasFinder,CRT	122296-122327	32	NC_014309	Ralstonia solanacearum CFBP2957 plasmid RCFBPv3_mp, complete genome	984398-984429	8	0.75
CP031166_2	2.22\|122418\|32\|CP031166\|CRISPRCasFinder,CRT	122418-122449	32	NZ_AP014705	Methylobacterium aquaticum strain MA-22A plasmid pMaq22A_1p, complete sequence	427968-427999	8	0.75
CP031166_2	2.23\|122479\|32\|CP031166\|CRISPRCasFinder,CRT	122479-122510	32	NZ_CP041605	Streptomyces sp. S1D4-14 plasmid pS1D4-14.1, complete sequence	16879-16910	8	0.75
CP031166_2	2.25\|122601\|32\|CP031166\|CRISPRCasFinder,CRT	122601-122632	32	NZ_CP043499	Rhizobium grahamii strain BG7 plasmid unnamed, complete sequence	1397441-1397472	8	0.75
CP031166_2	2.25\|122601\|32\|CP031166\|CRISPRCasFinder,CRT	122601-122632	32	NZ_CP006991	Rhizobium sp. IE4771 plasmid pRetIE4771e, complete sequence	701750-701781	8	0.75
CP031166_2	2.25\|122601\|32\|CP031166\|CRISPRCasFinder,CRT	122601-122632	32	NZ_CP021128	Rhizobium sp. Kim5 plasmid pRetKim5d, complete sequence	642259-642290	8	0.75
CP031166_2	2.25\|122601\|32\|CP031166\|CRISPRCasFinder,CRT	122601-122632	32	CP007645	Rhizobium etli bv. phaseoli str. IE4803 plasmid pRetIE4803d, complete sequence	700671-700702	8	0.75
CP031166_1	1.2\|113092\|33\|CP031166\|PILER-CR	113092-113124	33	MH673674	Thermus phage phiMa, complete genome	15663-15695	9	0.727
CP031166_1	1.4\|113087\|32\|CP031166\|CRISPRCasFinder	113087-113118	32	NZ_CP017105	Rhizobium gallicum strain IE4872 plasmid pRgalIE4872d, complete sequence	1040121-1040152	9	0.719
CP031166_2	2.4\|122112\|33\|CP031166\|PILER-CR	122112-122144	33	NZ_CP007130	Gemmatirosa kalamazoonesis strain KBS708 plasmid 2, complete sequence	337301-337333	9	0.727
CP031166_2	2.6\|122234\|33\|CP031166\|PILER-CR	122234-122266	33	NZ_CP023017	Ralstonia solanacearum strain SL3022 plasmid unnamed, complete sequence	1171943-1171975	9	0.727
CP031166_2	2.6\|122234\|33\|CP031166\|PILER-CR	122234-122266	33	NC_017966	Tistrella mobilis KA081020-065 plasmid pTM2, complete sequence	88806-88838	9	0.727
CP031166_2	2.10\|122478\|33\|CP031166\|PILER-CR	122478-122510	33	NZ_CP041605	Streptomyces sp. S1D4-14 plasmid pS1D4-14.1, complete sequence	16879-16911	9	0.727
CP031166_2	2.12\|122600\|33\|CP031166\|PILER-CR	122600-122632	33	NZ_CP032346	Azospirillum brasilense strain MTCC4039 plasmid p1, complete sequence	1765843-1765875	9	0.727
CP031166_2	2.17\|122113\|32\|CP031166\|CRISPRCasFinder,CRT	122113-122144	32	NC_007949	Polaromonas sp. JS666 plasmid 1, complete sequence	255773-255804	9	0.719
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	NZ_CP020440	Paracoccus yeei strain FDAARGOS_252 plasmid unnamed2, complete sequence	165912-165943	9	0.719
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	NZ_CP044082	Paracoccus yeei strain FDAARGOS_643 plasmid unnamed4, complete sequence	156755-156786	9	0.719
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	NZ_CP031080	Paracoccus yeei strain CCUG 32053 plasmid pYEE2, complete sequence	48391-48422	9	0.719
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	JX872508	Stenotrophomonas phage IME15, complete genome	36640-36671	9	0.719
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	NC_047942	Escherichia phage Ebrios, complete genome	37953-37984	9	0.719
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP023017	Ralstonia solanacearum strain SL3022 plasmid unnamed, complete sequence	1171944-1171975	9	0.719
CP031166_2	2.20\|122296\|32\|CP031166\|CRISPRCasFinder,CRT	122296-122327	32	NZ_CP025613	Niveispirillum cyanobacteriorum strain TH16 plasmid unnamed1, complete sequence	923817-923848	9	0.719
CP031166_2	2.20\|122296\|32\|CP031166\|CRISPRCasFinder,CRT	122296-122327	32	NZ_CP017105	Rhizobium gallicum strain IE4872 plasmid pRgalIE4872d, complete sequence	1310940-1310971	9	0.719
CP031166_2	2.25\|122601\|32\|CP031166\|CRISPRCasFinder,CRT	122601-122632	32	NZ_CP032346	Azospirillum brasilense strain MTCC4039 plasmid p1, complete sequence	1765844-1765875	9	0.719
CP031166_2	2.25\|122601\|32\|CP031166\|CRISPRCasFinder,CRT	122601-122632	32	NZ_CP029833	Azospirillum ramasamyi strain M2T2B2 plasmid unnamed3, complete sequence	158611-158642	9	0.719
CP031166_3	3.2\|126765\|38\|CP031166\|CRISPRCasFinder	126765-126802	38	MK433264	Gordonia phage Tiamoceli, complete genome	5739-5776	9	0.763
CP031166_3	3.2\|126765\|38\|CP031166\|CRISPRCasFinder	126765-126802	38	MT952843	Gordonia phage Twonlo, complete genome	4356-4393	9	0.763
CP031166_3	3.2\|126765\|38\|CP031166\|CRISPRCasFinder	126765-126802	38	MK977704	Gordonia Terrae phage RoadKill, complete genome	4356-4393	9	0.763
CP031166_3	3.2\|126765\|38\|CP031166\|CRISPRCasFinder	126765-126802	38	NZ_CP009294	Novosphingobium pentaromativorans US6-1 plasmid pLA1, complete sequence	94441-94478	9	0.763
CP031166_3	3.2\|126765\|38\|CP031166\|CRISPRCasFinder	126765-126802	38	NZ_CP011772	Croceicoccus naphthovorans strain PQ-2 plasmid p2, complete sequence	54395-54432	9	0.763
CP031166_2	2.4\|122112\|33\|CP031166\|PILER-CR	122112-122144	33	NC_007949	Polaromonas sp. JS666 plasmid 1, complete sequence	255773-255805	10	0.697
CP031166_2	2.18\|122174\|32\|CP031166\|CRISPRCasFinder,CRT	122174-122205	32	NC_011368	Rhizobium leguminosarum bv. trifolii WSM2304 plasmid pRLG201, complete sequence	351367-351398	10	0.688
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP012185	Pseudonocardia sp. EC080619-01 plasmid pBCI1-2, complete sequence	43223-43254	10	0.688
CP031166_2	2.19\|122235\|32\|CP031166\|CRISPRCasFinder,CRT	122235-122266	32	NZ_CP012182	Pseudonocardia sp. EC080610-09 plasmid pBCI2-1, complete sequence	816872-816903	10	0.688
CP031166_2	2.22\|122418\|32\|CP031166\|CRISPRCasFinder,CRT	122418-122449	32	LN997843	Streptomyces reticuli genome assembly TUE45, plasmid : II	581791-581822	11	0.656
CP031166_3	3.2\|126765\|38\|CP031166\|CRISPRCasFinder	126765-126802	38	NZ_CP029232	Sinorhizobium fredii CCBAU 45436 plasmid pSF45436b, complete sequence	807448-807485	11	0.711

1. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
gccgagcaggaccggctgacgatcgctg	Protospacer
****************************

2. spacer 1.2|113092|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

agaagtggtcgccggcctcatgcgccggaggcc	CRISPR spacer
agaagtggtcgccggcctcatgcgccggaggcc	Protospacer
*********************************

3. spacer 1.3|113026|33|CP031166|CRISPRCasFinder matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ggccgagcaggaccggctgacgatcgctggcca	CRISPR spacer
ggccgagcaggaccggctgacgatcgctggcca	Protospacer
*********************************

4. spacer 1.4|113087|32|CP031166|CRISPRCasFinder matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

tggtcgccggcctcatgcgccggaggccgcag	CRISPR spacer
tggtcgccggcctcatgcgccggaggccgcag	Protospacer
********************************

5. spacer 2.1|121929|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

tgcgggcatgaggccggttgttgggttggactt	CRISPR spacer
tgcgggcatgaggccggttgttgggttggactt	Protospacer
*********************************

6. spacer 2.2|121990|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

cagtgcctcctcaacgagggaggtcagctggtc	CRISPR spacer
cagtgcctcctcaacgagggaggtcagctggtc	Protospacer
*********************************

7. spacer 2.3|122051|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

cttcctggccgtcacccaaacggtcgcatccgt	CRISPR spacer
cttcctggccgtcacccaaacggtcgcatccgt	Protospacer
*********************************

8. spacer 2.4|122112|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

cggccgccagccggcgctgaccggatgccgttt	CRISPR spacer
cggccgccagccggcgctgaccggatgccgttt	Protospacer
*********************************

9. spacer 2.5|122173|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

cccgtctggcctgccccgttcccgaggtccgcc	CRISPR spacer
cccgtctggcctgccccgttcccgaggtccgcc	Protospacer
*********************************

10. spacer 2.6|122234|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

cttgccggtccacccggatttcgccggcggcca	CRISPR spacer
cttgccggtccacccggatttcgccggcggcca	Protospacer
*********************************

11. spacer 2.7|122295|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

tggccagttcttcgccggcgccatctggggtgg	CRISPR spacer
tggccagttcttcgccggcgccatctggggtgg	Protospacer
*********************************

12. spacer 2.8|122356|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

cttagtcccgttttttgggtgggggctgttggg	CRISPR spacer
cttagtcccgttttttgggtgggggctgttggg	Protospacer
*********************************

13. spacer 2.9|122417|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ctcaacccactccggcaggtagtcgccgcgagg	CRISPR spacer
ctcaacccactccggcaggtagtcgccgcgagg	Protospacer
*********************************

14. spacer 2.10|122478|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

cgggaggtcgacccggccctcggggcatggccg	CRISPR spacer
cgggaggtcgacccggccctcggggcatggccg	Protospacer
*********************************

15. spacer 2.11|122539|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ctggatcctgcgcggatcgccgggcactccctt	CRISPR spacer
ctggatcctgcgcggatcgccgggcactccctt	Protospacer
*********************************

16. spacer 2.12|122600|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

cctcggcgacgccggccttgtggagacccatct	CRISPR spacer
cctcggcgacgccggccttgtggagacccatct	Protospacer
*********************************

17. spacer 2.13|122661|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

cctgcccgcgtgcgcctctcaggggaagtggcg	CRISPR spacer
cctgcccgcgtgcgcctctcaggggaagtggcg	Protospacer
*********************************

18. spacer 2.14|121930|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

gcgggcatgaggccggttgttgggttggactt	CRISPR spacer
gcgggcatgaggccggttgttgggttggactt	Protospacer
********************************

19. spacer 2.15|121991|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

agtgcctcctcaacgagggaggtcagctggtc	CRISPR spacer
agtgcctcctcaacgagggaggtcagctggtc	Protospacer
********************************

20. spacer 2.16|122052|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ttcctggccgtcacccaaacggtcgcatccgt	CRISPR spacer
ttcctggccgtcacccaaacggtcgcatccgt	Protospacer
********************************

21. spacer 2.17|122113|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ggccgccagccggcgctgaccggatgccgttt	CRISPR spacer
ggccgccagccggcgctgaccggatgccgttt	Protospacer
********************************

22. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ccgtctggcctgccccgttcccgaggtccgcc	CRISPR spacer
ccgtctggcctgccccgttcccgaggtccgcc	Protospacer
********************************

23. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
ttgccggtccacccggatttcgccggcggcca	Protospacer
********************************

24. spacer 2.20|122296|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ggccagttcttcgccggcgccatctggggtgg	CRISPR spacer
ggccagttcttcgccggcgccatctggggtgg	Protospacer
********************************

25. spacer 2.21|122357|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ttagtcccgttttttgggtgggggctgttggg	CRISPR spacer
ttagtcccgttttttgggtgggggctgttggg	Protospacer
********************************

26. spacer 2.22|122418|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

tcaacccactccggcaggtagtcgccgcgagg	CRISPR spacer
tcaacccactccggcaggtagtcgccgcgagg	Protospacer
********************************

27. spacer 2.23|122479|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

gggaggtcgacccggccctcggggcatggccg	CRISPR spacer
gggaggtcgacccggccctcggggcatggccg	Protospacer
********************************

28. spacer 2.24|122540|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

tggatcctgcgcggatcgccgggcactccctt	CRISPR spacer
tggatcctgcgcggatcgccgggcactccctt	Protospacer
********************************

29. spacer 2.25|122601|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ctcggcgacgccggccttgtggagacccatct	CRISPR spacer
ctcggcgacgccggccttgtggagacccatct	Protospacer
********************************

30. spacer 2.26|122662|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

ctgcccgcgtgcgcctctcaggggaagtggcg	CRISPR spacer
ctgcccgcgtgcgcctctcaggggaagtggcg	Protospacer
********************************

31. spacer 3.1|126706|36|CP031166|CRISPRCasFinder matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

agggttcgtgcacgtgcgagggctacggcctgtggg	CRISPR spacer
agggttcgtgcacgtgcgagggctacggcctgtggg	Protospacer
************************************

32. spacer 3.2|126765|38|CP031166|CRISPRCasFinder matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 0, identity: 1.0

gaggctgccggcatcgtcgtcatcgtcgccgaaccagg	CRISPR spacer
gaggctgccggcatcgtcgtcatcgtcgccgaaccagg	Protospacer
**************************************

33. spacer 1.1|113031|28|CP031166|PILER-CR matches to NC_012586 (Sinorhizobium fredii NGR234 plasmid pNGR234b, complete sequence) position: , mismatch: 4, identity: 0.857

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
gccgagccggaccgcctgacgatcgacg	Protospacer
******* ****** ********** .*

34. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP019319 (Tateyamaria omphalii strain DOK1-4 plasmid pDOK1-4-7, complete sequence) position: , mismatch: 4, identity: 0.857

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
gccgagcgggaccggctgaccatcgtgg	Protospacer
*******.************ ****. *

35. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP050953 (Rhodococcus sp. DMU1 plasmid unnamed) position: , mismatch: 4, identity: 0.857

--gccgagcaggaccggctgacgatcgctg	CRISPR spacer
ctgcc--gcaggaacggctgacgatcgcgg	Protospacer
  ***  ****** ************** *

36. spacer 1.4|113087|32|CP031166|CRISPRCasFinder matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 4, identity: 0.875

tggtcgccggcctcatgcgccggaggccgcag	CRISPR spacer
agctcgccggcctcatgagccggaggcagcag	Protospacer
 * ************** ********* ****

37. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP017076 (Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence) position: , mismatch: 5, identity: 0.821

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
gacgagcagaaccggctgacgatcacgt	Protospacer
* *******.**************.*

38. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP035514 (Haematobacter massiliensis strain OT1 plasmid pOT1-4, complete sequence) position: , mismatch: 5, identity: 0.821

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
ctcgaggaggactggctgacgatcgcgg	Protospacer
 .**** *****.************* *

39. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP013635 (Rhizobium sp. N324 plasmid pRspN324e, complete sequence) position: , mismatch: 5, identity: 0.821

gccgagcaggaccggctgacg----atcgctg	CRISPR spacer
gccgcgcaggaccggctgacgggatatc----	Protospacer
**** ****************    ***

40. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP020952 (Rhizobium sp. CIAT894 plasmid pRheCIAT894e, complete sequence) position: , mismatch: 5, identity: 0.821

gccgagcaggaccggctgacg----atcgctg	CRISPR spacer
gccgcgcaggaccggctgacgggatatc----	Protospacer
**** ****************    ***

41. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP007795 (Azospirillum brasilense strain Az39 plasmid AbAZ39_p2, complete sequence) position: , mismatch: 5, identity: 0.821

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
gtcgagaaggaccggctggcgatcgacg	Protospacer
*.**** ***********.****** .*

42. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP054028 (Rhizobium sp. JKLM19E plasmid pPR19E01, complete sequence) position: , mismatch: 5, identity: 0.821

gccgagcaggaccggctgacg----atcgctg	CRISPR spacer
gccgcgcaggaccggctgacggggtatc----	Protospacer
**** ****************    ***

43. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP032323 (Azospirillum brasilense strain MTCC4035 plasmid p2, complete sequence) position: , mismatch: 5, identity: 0.821

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
gtcgagaaggaccggctggcgatcgacg	Protospacer
*.**** ***********.****** .*

44. spacer 2.4|122112|33|CP031166|PILER-CR matches to NZ_CP013110 (Sinorhizobium americanum strain CFNEI 73 plasmid C, complete sequence) position: , mismatch: 5, identity: 0.848

cggccgccagccggcgctgaccgg-atgccgttt	CRISPR spacer
cgcccgccagcgggcgctgaccggcatggcctt-	Protospacer
** ******** ************ *** * **

45. spacer 2.4|122112|33|CP031166|PILER-CR matches to NZ_CP029452 (Sinorhizobium fredii CCBAU 25509 plasmid pSF25509b, complete sequence) position: , mismatch: 5, identity: 0.848

cggccgccagccggcgctgaccgg-atgccgttt	CRISPR spacer
cgcccgccagcgggcgctgaccggcatggcctt-	Protospacer
** ******** ************ *** * **

46. spacer 2.4|122112|33|CP031166|PILER-CR matches to NZ_CP013054 (Sinorhizobium americanum CCGM7 plasmid C, complete sequence) position: , mismatch: 5, identity: 0.848

cggccgccagccggcgctgaccgg-atgccgttt	CRISPR spacer
cgcccgccagcgggcgctgaccggcatggcctt-	Protospacer
** ******** ************ *** * **

47. spacer 2.4|122112|33|CP031166|PILER-CR matches to NZ_CP023071 (Sinorhizobium fredii CCBAU 83666 plasmid pSF83666b, complete sequence) position: , mismatch: 5, identity: 0.848

cggccgccagccggcgctgaccgg-atgccgttt	CRISPR spacer
cgcccgccagcgggcgctgaccggcatggcctt-	Protospacer
** ******** ************ *** * **

48. spacer 2.7|122295|33|CP031166|PILER-CR matches to KM233689 (Pseudomonas phage H70, complete genome) position: , mismatch: 5, identity: 0.848

tggccagttcttcgccggcgccatctggggtgg-	CRISPR spacer
tgtccaggtcttcgccggcgccatc-gtcgtggc	Protospacer
** **** ***************** *  ****

49. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP016452 (Sinorhizobium sp. RAC02 plasmid pBSY16_1, complete sequence) position: , mismatch: 5, identity: 0.844

-ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
cttgcc-gtccagccggatttcgccggaggtcg	Protospacer
 ***** ***** ************** **.*.

50. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP017422 (Arthrobacter sp. ZXY-2 plasmid pZXY21, complete sequence) position: , mismatch: 6, identity: 0.786

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
gccggacaggaccggctgacgatggtca	Protospacer
****..***************** *...

51. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_AP022593 (Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence) position: , mismatch: 6, identity: 0.786

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
ggcgagcaggaccgtctgccgatcgaac	Protospacer
* ************ *** ******

52. spacer 1.1|113031|28|CP031166|PILER-CR matches to AP021850 (Deinococcus grandis ATCC 43672 plasmid: pDEGR-1 DNA, complete genome) position: , mismatch: 6, identity: 0.786

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
gtcgtgcaggaccggctgacgaacggcc	Protospacer
*.** ***************** ** .

53. spacer 2.23|122479|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP032325 (Azospirillum brasilense strain MTCC4035 plasmid p4, complete sequence) position: , mismatch: 6, identity: 0.812

gggaggtcgacccggccctcggggcatggccg-	CRISPR spacer
gcgaggtcggcccggccttcggggcg-gcccgt	Protospacer
* *******.*******.*******. * ***

54. spacer 2.23|122479|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP032349 (Azospirillum brasilense strain MTCC4039 plasmid p3, complete sequence) position: , mismatch: 6, identity: 0.812

gggaggtcgacccggccctcggggcatggccg-	CRISPR spacer
gcgaggtcggcccggccttcggggcg-gcccgt	Protospacer
* *******.*******.*******. * ***

55. spacer 1.1|113031|28|CP031166|PILER-CR matches to NC_019846 (Sinorhizobium meliloti GR4 plasmid pRmeGR4a, complete sequence) position: , mismatch: 7, identity: 0.75

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
aaggagcacgaccggctgacgctcgcaa	Protospacer
.  ***** ************ **** .

56. spacer 1.1|113031|28|CP031166|PILER-CR matches to MG962366 (Rhodococcus phage Finch, complete genome) position: , mismatch: 7, identity: 0.75

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
accgaggaggaccggctgacggtctggt	Protospacer
.***** **************.**

57. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP045386 (Ruegeria sp. THAF33 plasmid pTHAF33_b, complete sequence) position: , mismatch: 7, identity: 0.75

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
agaatgcaggacaggctgacgatcgttg	Protospacer
.  . ******* ************.**

58. spacer 1.3|113026|33|CP031166|CRISPRCasFinder matches to NZ_CP019319 (Tateyamaria omphalii strain DOK1-4 plasmid pDOK1-4-7, complete sequence) position: , mismatch: 7, identity: 0.788

ggccgagcaggaccggctgacgatcgctggcca	CRISPR spacer
cgccgagcgggaccggctgaccatcgtggccga	Protospacer
 *******.************ ****. * * *

59. spacer 1.4|113087|32|CP031166|CRISPRCasFinder matches to NZ_AP022593 (Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence) position: , mismatch: 7, identity: 0.781

tggtcgccggcctcatgcgccggaggccgcag--	CRISPR spacer
tggccgccgggctcatgcgccg--gctcgccggt	Protospacer
***.****** ***********  * .*** *

60. spacer 2.4|122112|33|CP031166|PILER-CR matches to AB967974 (Aurantimonas phage AmM-1 DNA, complete sequence) position: , mismatch: 7, identity: 0.788

cggccgccagccggcgctgaccggatgccgttt	CRISPR spacer
ccgccgacagccggcgcagaccggatgcatcct	Protospacer
* **** ********** **********  ..*

61. spacer 2.10|122478|33|CP031166|PILER-CR matches to MT723933 (Streptomyces phage Keanu, complete genome) position: , mismatch: 7, identity: 0.788

cgggaggtcgacccggccctc-ggggcatggccg	CRISPR spacer
cgggaggtcgtccccgccctcgggggtgcggac-	Protospacer
********** *** ****** ****...** *

62. spacer 2.12|122600|33|CP031166|PILER-CR matches to NZ_CP024314 (Rhizobium sp. NXC24 plasmid pRspNXC24c, complete sequence) position: , mismatch: 7, identity: 0.788

cctcggcgacgccggccttgtggagacccatct	CRISPR spacer
cctcggcgatgccggccttctggaagagcttct	Protospacer
*********.********* ****..  * ***

63. spacer 2.17|122113|32|CP031166|CRISPRCasFinder,CRT matches to AB967974 (Aurantimonas phage AmM-1 DNA, complete sequence) position: , mismatch: 7, identity: 0.781

ggccgccagccggcgctgaccggatgccgttt	CRISPR spacer
cgccgacagccggcgcagaccggatgcatcct	Protospacer
 **** ********** **********  ..*

64. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP023455 (Rhodobacteraceae bacterium QY30 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.781

ccgtc--tggcctgccccgttcccgaggtccgcc	CRISPR spacer
--gtcgatcacctgccccgtgcccgaggcccgca	Protospacer
  ***  * .********** *******.****

65. spacer 2.20|122296|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP017076 (Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence) position: , mismatch: 7, identity: 0.781

ggccagttcttcgccggcgccatctggggtgg-	CRISPR spacer
cgccagtccttcgccggcgcgatc-aacgtggt	Protospacer
 ******.************ *** .. ****

66. spacer 2.23|122479|32|CP031166|CRISPRCasFinder,CRT matches to MT723933 (Streptomyces phage Keanu, complete genome) position: , mismatch: 7, identity: 0.781

gggaggtcgacccggccctc-ggggcatggccg	CRISPR spacer
gggaggtcgtccccgccctcgggggtgcggac-	Protospacer
********* *** ****** ****...** *

67. spacer 2.24|122540|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP033228 (Sphingobium yanoikuyae strain SJTF8 plasmid pF2, complete sequence) position: , mismatch: 7, identity: 0.781

tggatcctgcgcggatcgccgggcactccctt	CRISPR spacer
cagatcctgcgcggaccgcagggcacgctgtt	Protospacer
..*************.*** ****** *. **

68. spacer 2.25|122601|32|CP031166|CRISPRCasFinder,CRT matches to NC_009620 (Sinorhizobium medicae WSM419 plasmid pSMED01, complete sequence) position: , mismatch: 7, identity: 0.781

ctcggcgacgccggccttgtggagacccatct	CRISPR spacer
gccggcgacgacggccttgtcgagaccaagcg	Protospacer
 .******** ********* ****** * *

69. spacer 2.25|122601|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP024314 (Rhizobium sp. NXC24 plasmid pRspNXC24c, complete sequence) position: , mismatch: 7, identity: 0.781

ctcggcgacgccggccttgtggagacccatct	CRISPR spacer
ctcggcgatgccggccttctggaagagcttct	Protospacer
********.********* ****..  * ***

70. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP017427 (Methylobacterium sp. XJLW plasmid unnamed1, complete sequence) position: , mismatch: 8, identity: 0.714

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
ctgaagcaggaccggccgacgatcgtct	Protospacer
 . .************.********..

71. spacer 1.1|113031|28|CP031166|PILER-CR matches to NZ_CP029174 (Methylobacterium sp. DM1 plasmid pLVM1, complete sequence) position: , mismatch: 8, identity: 0.714

gccgagcaggaccggctgacgatcgctg	CRISPR spacer
ctgaagcaggaccggccgacgatcgtct	Protospacer
 . .************.********..

72. spacer 1.2|113092|33|CP031166|PILER-CR matches to NZ_CP031166 (Euzebya sp. DY32-46 plasmid pEDY32-46I, complete sequence) position: , mismatch: 8, identity: 0.758

agaagtggtcgccggcctcatgcgccggaggcc	CRISPR spacer
atggcagctcgccggcctcatgagccggaggca	Protospacer
* ..  * ************** *********

73. spacer 1.3|113026|33|CP031166|CRISPRCasFinder matches to NC_012586 (Sinorhizobium fredii NGR234 plasmid pNGR234b, complete sequence) position: , mismatch: 8, identity: 0.758

ggccgagcaggaccggctgacgatcgctggcca	CRISPR spacer
agccgagccggaccgcctgacgatcgacgtcac	Protospacer
.******* ****** ********** .* *

74. spacer 1.4|113087|32|CP031166|CRISPRCasFinder matches to MH673674 (Thermus phage phiMa, complete genome) position: , mismatch: 8, identity: 0.75

tggtcgccggcctcatgcgccggaggccgcag	CRISPR spacer
ccgtggccggcctcatgcgccggggggggacg	Protospacer
. ** ******************.**  *  *

75. spacer 2.6|122234|33|CP031166|PILER-CR matches to NZ_CP022762 (Ralstonia solanacearum strain T95 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.758

cttgccggtccacccggatttcgccggcggcca	CRISPR spacer
cgcgctcccccccccggatttcgccggcgacca	Protospacer
* .**.  .** *****************.***

76. spacer 2.6|122234|33|CP031166|PILER-CR matches to NZ_CP014703 (Ralstonia solanacearum strain KACC 10722 plasmid, complete sequence) position: , mismatch: 8, identity: 0.758

cttgccggtccacccggatttcgccggcggcca	CRISPR spacer
cgcgctcccccccccggatttcgccggcgacca	Protospacer
* .**.  .** *****************.***

77. spacer 2.6|122234|33|CP031166|PILER-CR matches to NZ_CP022771 (Ralstonia solanacearum strain T51 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.758

cttgccggtccacccggatttcgccggcggcca	CRISPR spacer
cgcgctcccccccccggatttcgccggcgacca	Protospacer
* .**.  .** *****************.***

78. spacer 2.6|122234|33|CP031166|PILER-CR matches to NZ_CP022777 (Ralstonia solanacearum strain T11 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.758

cttgccggtccacccggatttcgccggcggcca	CRISPR spacer
cgcgctcccccccccggatttcgccggcgacca	Protospacer
* .**.  .** *****************.***

79. spacer 2.6|122234|33|CP031166|PILER-CR matches to NZ_CP022799 (Ralstonia solanacearum strain SL2064 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.758

cttgccggtccacccggatttcgccggcggcca	CRISPR spacer
cgcgctcccccccccggatttcgccggcgacca	Protospacer
* .**.  .** *****************.***

80. spacer 2.9|122417|33|CP031166|PILER-CR matches to NZ_AP014705 (Methylobacterium aquaticum strain MA-22A plasmid pMaq22A_1p, complete sequence) position: , mismatch: 8, identity: 0.758

ctcaacccactccggcaggtagtcgccgcgagg	CRISPR spacer
cagcacccgctccgccaggtagtcgccgaggcg	Protospacer
*   ****.***** ************* *. *

81. spacer 2.11|122539|33|CP031166|PILER-CR matches to NZ_CP033228 (Sphingobium yanoikuyae strain SJTF8 plasmid pF2, complete sequence) position: , mismatch: 8, identity: 0.758

ctggatcctgcgcggatcgccgggcactccctt	CRISPR spacer
gcagatcctgcgcggaccgcagggcacgctgtt	Protospacer
 ..*************.*** ****** *. **

82. spacer 2.12|122600|33|CP031166|PILER-CR matches to NC_009620 (Sinorhizobium medicae WSM419 plasmid pSMED01, complete sequence) position: , mismatch: 8, identity: 0.758

cctcggcgacgccggccttgtggagacccatct	CRISPR spacer
agccggcgacgacggccttgtcgagaccaagcg	Protospacer
  .******** ********* ****** * *

83. spacer 2.12|122600|33|CP031166|PILER-CR matches to NZ_CP006991 (Rhizobium sp. IE4771 plasmid pRetIE4771e, complete sequence) position: , mismatch: 8, identity: 0.758

cctcggcgacgccggccttgtggagacccatct	CRISPR spacer
cctcggcgatgccggccttgtcgaaggcttcct	Protospacer
*********.*********** **.. *. .**

84. spacer 2.12|122600|33|CP031166|PILER-CR matches to NZ_CP043499 (Rhizobium grahamii strain BG7 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.758

cctcggcgacgccggccttgtggagacccatct	CRISPR spacer
cgctggcgacgccggccttgtcgagcccgaggt	Protospacer
* ..***************** *** ** *  *

85. spacer 2.12|122600|33|CP031166|PILER-CR matches to NZ_CP021128 (Rhizobium sp. Kim5 plasmid pRetKim5d, complete sequence) position: , mismatch: 8, identity: 0.758

cctcggcgacgccggccttgtggagacccatct	CRISPR spacer
cctcggcgatgccggccttgtcgaaggcttcct	Protospacer
*********.*********** **.. *. .**

86. spacer 2.12|122600|33|CP031166|PILER-CR matches to CP007645 (Rhizobium etli bv. phaseoli str. IE4803 plasmid pRetIE4803d, complete sequence) position: , mismatch: 8, identity: 0.758

cctcggcgacgccggccttgtggagacccatct	CRISPR spacer
cctcggcgatgccggccttgtcgaaggcttcct	Protospacer
*********.*********** **.. *. .**

87. spacer 2.17|122113|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP007130 (Gemmatirosa kalamazoonesis strain KBS708 plasmid 2, complete sequence) position: , mismatch: 8, identity: 0.75

ggccgccagccggcgctgaccggatgccgttt	CRISPR spacer
aaccgccagccggcgctgtccggacgcggcgc	Protospacer
..**************** *****.** *. .

88. spacer 2.17|122113|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP017242 (Rhizobium etli 8C-3 plasmid pRsp8C3a, complete sequence) position: , mismatch: 8, identity: 0.75

ggccgccagccggcgctgaccggatgccgttt	CRISPR spacer
tgctgggggccggcgctgcccagatgccgttg	Protospacer
 **.*  .********** **.*********

89. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP012185 (Pseudonocardia sp. EC080619-01 plasmid pBCI1-2, complete sequence) position: , mismatch: 8, identity: 0.75

ccgtctg-gcctgccccgttcccgaggtccgcc	CRISPR spacer
-cgcgggcacctgccccgtacccgaggaccgcg	Protospacer
 **.  * .********** ******* ****

90. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP012182 (Pseudonocardia sp. EC080610-09 plasmid pBCI2-1, complete sequence) position: , mismatch: 8, identity: 0.75

ccgtctg-gcctgccccgttcccgaggtccgcc	CRISPR spacer
-cgcgggcacctgccccgtacccgaggaccgcg	Protospacer
 **.  * .********** ******* ****

91. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP022762 (Ralstonia solanacearum strain T95 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.75

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
gcgctcccccccccggatttcgccggcgacca	Protospacer
 .**.  .** *****************.***

92. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NC_017966 (Tistrella mobilis KA081020-065 plasmid pTM2, complete sequence) position: , mismatch: 8, identity: 0.75

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
ctgccgggccatccggatttcgccgacatgct	Protospacer
.****** ***.*************.*.  *

93. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP014703 (Ralstonia solanacearum strain KACC 10722 plasmid, complete sequence) position: , mismatch: 8, identity: 0.75

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
gcgctcccccccccggatttcgccggcgacca	Protospacer
 .**.  .** *****************.***

94. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP022771 (Ralstonia solanacearum strain T51 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.75

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
gcgctcccccccccggatttcgccggcgacca	Protospacer
 .**.  .** *****************.***

95. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP022777 (Ralstonia solanacearum strain T11 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.75

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
gcgctcccccccccggatttcgccggcgacca	Protospacer
 .**.  .** *****************.***

96. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP022799 (Ralstonia solanacearum strain SL2064 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.75

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
gcgctcccccccccggatttcgccggcgacca	Protospacer
 .**.  .** *****************.***

97. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP019940 (Ketogulonicigenium robustum strain SPU_B003 plasmid unnamed3, complete sequence) position: , mismatch: 8, identity: 0.75

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
gggcagagccacccggatttcgcgggcgacct	Protospacer
  ** *. *************** ****.**

98. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP022567 (Rhizobium leguminosarum bv. viciae strain BIHB 1148 plasmid pSK03, complete sequence) position: , mismatch: 8, identity: 0.75

--ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
cacgaccg--ccacccggatttcgccgccgccct	Protospacer
  . .***  ***************** ** **

99. spacer 2.20|122296|32|CP031166|CRISPRCasFinder,CRT matches to NC_014309 (Ralstonia solanacearum CFBP2957 plasmid RCFBPv3_mp, complete genome) position: , mismatch: 8, identity: 0.75

ggccagttcttcgccggcgccatctggggtgg	CRISPR spacer
cccgcgttcgtcgccggcgccatcggggttcg	Protospacer
  *  **** ************** *** * *

100. spacer 2.22|122418|32|CP031166|CRISPRCasFinder,CRT matches to NZ_AP014705 (Methylobacterium aquaticum strain MA-22A plasmid pMaq22A_1p, complete sequence) position: , mismatch: 8, identity: 0.75

tcaacccactccggcaggtagtcgccgcgagg	CRISPR spacer
agcacccgctccgccaggtagtcgccgaggcg	Protospacer
   ****.***** ************* *. *

101. spacer 2.23|122479|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP041605 (Streptomyces sp. S1D4-14 plasmid pS1D4-14.1, complete sequence) position: , mismatch: 8, identity: 0.75

gggaggtcgacccggccctcggggcatggccg-----	CRISPR spacer
aggaggtcgacccggccctgg-----cggccgtcctc	Protospacer
.****************** *     .*****

102. spacer 2.25|122601|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP043499 (Rhizobium grahamii strain BG7 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.75

ctcggcgacgccggccttgtggagacccatct	CRISPR spacer
gctggcgacgccggccttgtcgagcccgaggt	Protospacer
 ..***************** *** ** *  *

103. spacer 2.25|122601|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP006991 (Rhizobium sp. IE4771 plasmid pRetIE4771e, complete sequence) position: , mismatch: 8, identity: 0.75

ctcggcgacgccggccttgtggagacccatct	CRISPR spacer
ctcggcgatgccggccttgtcgaaggcttcct	Protospacer
********.*********** **.. *. .**

104. spacer 2.25|122601|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP021128 (Rhizobium sp. Kim5 plasmid pRetKim5d, complete sequence) position: , mismatch: 8, identity: 0.75

ctcggcgacgccggccttgtggagacccatct	CRISPR spacer
ctcggcgatgccggccttgtcgaaggcttcct	Protospacer
********.*********** **.. *. .**

105. spacer 2.25|122601|32|CP031166|CRISPRCasFinder,CRT matches to CP007645 (Rhizobium etli bv. phaseoli str. IE4803 plasmid pRetIE4803d, complete sequence) position: , mismatch: 8, identity: 0.75

ctcggcgacgccggccttgtggagacccatct	CRISPR spacer
ctcggcgatgccggccttgtcgaaggcttcct	Protospacer
********.*********** **.. *. .**

106. spacer 1.2|113092|33|CP031166|PILER-CR matches to MH673674 (Thermus phage phiMa, complete genome) position: , mismatch: 9, identity: 0.727

agaagtggtcgccggcctcatgcgccggaggcc	CRISPR spacer
ctacgccgtggccggcctcatgcgccggggggg	Protospacer
  * *. ** ******************.**

107. spacer 1.4|113087|32|CP031166|CRISPRCasFinder matches to NZ_CP017105 (Rhizobium gallicum strain IE4872 plasmid pRgalIE4872d, complete sequence) position: , mismatch: 9, identity: 0.719

tggtcgccggcctcatgcgccggaggccgcag	CRISPR spacer
gggtcgccgacctcattcgccggaccgtgcgc	Protospacer
 ********.****** *******   .**.

108. spacer 2.4|122112|33|CP031166|PILER-CR matches to NZ_CP007130 (Gemmatirosa kalamazoonesis strain KBS708 plasmid 2, complete sequence) position: , mismatch: 9, identity: 0.727

cggccgccagccggcgctgaccggatgccgttt	CRISPR spacer
gaaccgccagccggcgctgtccggacgcggcgc	Protospacer
 ..**************** *****.** *. .

109. spacer 2.6|122234|33|CP031166|PILER-CR matches to NZ_CP023017 (Ralstonia solanacearum strain SL3022 plasmid unnamed, complete sequence) position: , mismatch: 9, identity: 0.727

cttgccggtccacccggatttcgccggcggcca	CRISPR spacer
ccgcgctccccccccggatttcgccggcgacca	Protospacer
*.   *  .** *****************.***

110. spacer 2.6|122234|33|CP031166|PILER-CR matches to NC_017966 (Tistrella mobilis KA081020-065 plasmid pTM2, complete sequence) position: , mismatch: 9, identity: 0.727

cttgccggtccacccggatttcgccggcggcca	CRISPR spacer
actgccgggccatccggatttcgccgacatgct	Protospacer
 .****** ***.*************.*.  *

111. spacer 2.10|122478|33|CP031166|PILER-CR matches to NZ_CP041605 (Streptomyces sp. S1D4-14 plasmid pS1D4-14.1, complete sequence) position: , mismatch: 9, identity: 0.727

cgggaggtcgacccggccctcggggcatggccg-----	CRISPR spacer
aaggaggtcgacccggccctgg-----cggccgtcctc	Protospacer
 .****************** *     .*****

112. spacer 2.12|122600|33|CP031166|PILER-CR matches to NZ_CP032346 (Azospirillum brasilense strain MTCC4039 plasmid p1, complete sequence) position: , mismatch: 9, identity: 0.727

cctcggcgacgccggccttgtggagacccatct	CRISPR spacer
cctcggcgtcgccggccttgcggaggaggcgcg	Protospacer
******** ***********.****.     *

113. spacer 2.17|122113|32|CP031166|CRISPRCasFinder,CRT matches to NC_007949 (Polaromonas sp. JS666 plasmid 1, complete sequence) position: , mismatch: 9, identity: 0.719

ggccgccagccggcgctgaccggatgccgttt	CRISPR spacer
tgccgccagccggcgctgagcgcattgcaacc	Protospacer
 ****************** ** **  *. ..

114. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP020440 (Paracoccus yeei strain FDAARGOS_252 plasmid unnamed2, complete sequence) position: , mismatch: 9, identity: 0.719

ccgtctggcctgc------cccgttcccgaggtccgcc	CRISPR spacer
ccgcctggcctgcccccttcccgtttccgaag------	Protospacer
***.*********      ******.****.*

115. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP044082 (Paracoccus yeei strain FDAARGOS_643 plasmid unnamed4, complete sequence) position: , mismatch: 9, identity: 0.719

ccgtctggcctgc------cccgttcccgaggtccgcc	CRISPR spacer
ccgcctggcctgcccccttcccgtttccgaag------	Protospacer
***.*********      ******.****.*

116. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP031080 (Paracoccus yeei strain CCUG 32053 plasmid pYEE2, complete sequence) position: , mismatch: 9, identity: 0.719

ccgtctggcctgc------cccgttcccgaggtccgcc	CRISPR spacer
ccgcctggcctgcccccttcccgtttccgaag------	Protospacer
***.*********      ******.****.*

117. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to JX872508 (Stenotrophomonas phage IME15, complete genome) position: , mismatch: 9, identity: 0.719

ccgtctggcctgccccgttcccgaggtccgcc	CRISPR spacer
tcatctggcctgccctgtacccgaggagccgt	Protospacer
.*.************.** *******  *  .

118. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to NC_047942 (Escherichia phage Ebrios, complete genome) position: , mismatch: 9, identity: 0.719

ccgtctggcctgccccgttcccgaggtccgcc	CRISPR spacer
tcatctggcctgccctgtacccgaggagccgt	Protospacer
.*.************.** *******  *  .

119. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP023017 (Ralstonia solanacearum strain SL3022 plasmid unnamed, complete sequence) position: , mismatch: 9, identity: 0.719

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
cgcgctccccccccggatttcgccggcgacca	Protospacer
.   *  .** *****************.***

120. spacer 2.20|122296|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP025613 (Niveispirillum cyanobacteriorum strain TH16 plasmid unnamed1, complete sequence) position: , mismatch: 9, identity: 0.719

ggccagttcttcgccggcgccatctggggtgg	CRISPR spacer
gtgcccgccttcgcccgcgccatcgggggtgc	Protospacer
*  *   .******* ******** ******

121. spacer 2.20|122296|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP017105 (Rhizobium gallicum strain IE4872 plasmid pRgalIE4872d, complete sequence) position: , mismatch: 9, identity: 0.719

ggccagttcttcgccggcgccatctggggtgg	CRISPR spacer
ggccagtacttcgccgccgccatatcacgact	Protospacer
******* ******** ****** * . *

122. spacer 2.25|122601|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP032346 (Azospirillum brasilense strain MTCC4039 plasmid p1, complete sequence) position: , mismatch: 9, identity: 0.719

ctcggcgacgccggccttgtggagacccatct	CRISPR spacer
ctcggcgtcgccggccttgcggaggaggcgcg	Protospacer
******* ***********.****.     *

123. spacer 2.25|122601|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP029833 (Azospirillum ramasamyi strain M2T2B2 plasmid unnamed3, complete sequence) position: , mismatch: 9, identity: 0.719

ctcggcgacgccggccttgtggagacccatct	CRISPR spacer
ctcggcgacgccggcgttgcggacgcgggcca	Protospacer
*************** ***.*** .*  ..*

124. spacer 3.2|126765|38|CP031166|CRISPRCasFinder matches to MK433264 (Gordonia phage Tiamoceli, complete genome) position: , mismatch: 9, identity: 0.763

gaggctgccggcatcgtcgtcatcgtcgccgaaccagg	CRISPR spacer
gccgctgccggcatcgtcgtcgccgtcgccgcatgcga	Protospacer
*  ******************..******** *.  *.

125. spacer 3.2|126765|38|CP031166|CRISPRCasFinder matches to MT952843 (Gordonia phage Twonlo, complete genome) position: , mismatch: 9, identity: 0.763

gaggctgccggcatcgtcgtcatcgtcgccgaaccagg	CRISPR spacer
gcagctgccggcatcgtcgtcgccgtcgccgcatgcga	Protospacer
* .******************..******** *.  *.

126. spacer 3.2|126765|38|CP031166|CRISPRCasFinder matches to MK977704 (Gordonia Terrae phage RoadKill, complete genome) position: , mismatch: 9, identity: 0.763

gaggctgccggcatcgtcgtcatcgtcgccgaaccagg	CRISPR spacer
gcagctgccggcatcgtcgtcgccgtcgccgcatgcga	Protospacer
* .******************..******** *.  *.

127. spacer 3.2|126765|38|CP031166|CRISPRCasFinder matches to NZ_CP009294 (Novosphingobium pentaromativorans US6-1 plasmid pLA1, complete sequence) position: , mismatch: 9, identity: 0.763

gaggctgccggcatcgtcgtcatcgtcgccgaaccagg	CRISPR spacer
gagcggtgcggtatcgtcgtcatcttcgccgaacccgt	Protospacer
***     ***.************ ********** *

128. spacer 3.2|126765|38|CP031166|CRISPRCasFinder matches to NZ_CP011772 (Croceicoccus naphthovorans strain PQ-2 plasmid p2, complete sequence) position: , mismatch: 9, identity: 0.763

gaggctgccggcatcgtcgtcatcgtcgccgaaccagg	CRISPR spacer
gagcggtgcggtatcgtcgtcatcttcgccgaacccgt	Protospacer
***     ***.************ ********** *

129. spacer 2.4|122112|33|CP031166|PILER-CR matches to NC_007949 (Polaromonas sp. JS666 plasmid 1, complete sequence) position: , mismatch: 10, identity: 0.697

cggccgccagccggcgctgaccggatgccgttt	CRISPR spacer
gtgccgccagccggcgctgagcgcattgcaacc	Protospacer
  ****************** ** **  *. ..

130. spacer 2.18|122174|32|CP031166|CRISPRCasFinder,CRT matches to NC_011368 (Rhizobium leguminosarum bv. trifolii WSM2304 plasmid pRLG201, complete sequence) position: , mismatch: 10, identity: 0.688

ccgtctggcctgccccgttcccgaggtccgcc	CRISPR spacer
tgagcgactctgcccctttcctgaggtccgcc	Protospacer
. . * . .******* ****.**********

131. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP012185 (Pseudonocardia sp. EC080619-01 plasmid pBCI1-2, complete sequence) position: , mismatch: 10, identity: 0.688

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
gcccgacaccacccggatctcgtcggcggccg	Protospacer
 . * .  **********.***.********.

132. spacer 2.19|122235|32|CP031166|CRISPRCasFinder,CRT matches to NZ_CP012182 (Pseudonocardia sp. EC080610-09 plasmid pBCI2-1, complete sequence) position: , mismatch: 10, identity: 0.688

ttgccggtccacccggatttcgccggcggcca	CRISPR spacer
gcccgacaccacccggatctcgtcggcggccg	Protospacer
 . * .  **********.***.********.

133. spacer 2.22|122418|32|CP031166|CRISPRCasFinder,CRT matches to LN997843 (Streptomyces reticuli genome assembly TUE45, plasmid : II) position: , mismatch: 11, identity: 0.656

tcaacccactccggcaggtagtcgccgcgagg	CRISPR spacer
caggtccactccggccggtagtggccgctctt	Protospacer
. ...********** ****** *****

134. spacer 3.2|126765|38|CP031166|CRISPRCasFinder matches to NZ_CP029232 (Sinorhizobium fredii CCBAU 45436 plasmid pSF45436b, complete sequence) position: , mismatch: 11, identity: 0.711

gaggctgccggcatcgtcgtcatcgtcgccgaaccagg	CRISPR spacer
ggcactgccttcatcgtcgtcatcgtcgccgagatgat	Protospacer
*. .*****  *********************. ...

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

325448 : 334086

Bacillus_virus(33.33%)

tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
AXV10139.1\|325448_326879_-\|tRNA	tRNA nucleotidyltransferase	G3MAR3	Bacillus_virus	8.2e-22	35.1
AXV10140.1\|327100_327790_-	putative Nudix-like regulator	A0A0E3JJF3	Streptomyces_phage	7.5e-05	31.5
AXV10141.1\|327786_328209_-	hypothetical protein	NA	NA	NA	NA
AXV10142.1\|328205_329087_-	hypothetical protein	NA	NA	NA	NA
AXV10143.1\|329083_330844_-	NAD synthetase / Glutamine amidotransferase chain of NAD synthetase	A0A2L0UZF5	Agrobacterium_phage	1.0e-61	32.7
AXV10144.1\|330840_331248_-	hypothetical protein	A0A2D2W2R2	Stenotrophomonas_phage	1.1e-16	38.4
AXV10145.1\|331244_331604_-	hypothetical protein	NA	NA	NA	NA
AXV10146.1\|331669_332572_-	Nicotinamidase	A0A2K9L6K4	Tupanvirus	6.8e-06	26.9
AXV10147.1\|332590_332770_-	hypothetical protein	NA	NA	NA	NA
AXV10148.1\|332778_334086_-	Nicotinate phosphoribosyltransferase	G3MA18	Bacillus_virus	2.5e-41	36.2

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. CP031165

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. CP031166

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection