CRISPRimmunity

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
CP029843	Lysobacter maris strain HZ9B chromosome, complete genome	4 crisprs	DEDDh,WYL,Cas9_archaeal,csa3,cas3,DinG	0	6	0	0

1. CP029843

CRISPR-Cas detection and classification

Crispr_ID: CP029843_1

• CRISPR_ID: CP029843_1
• CRISPR_location: 1479824-1479920
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of CP029843_1

Consensus_repeat	Method
GTCGCAGCTTACGCAGCTCCTAC	CRISPRCasFinder

spacers of CP029843_1

>1.1|1479847|51|CP029843|CRISPRCasFinder
AGATGCGGAGGCCTTCCCCTGTAGGAGCGGCGGCCTTCATGGGAAGGCCCG

CRISPR arrays and Neighbor proteins around CP029843_1

CRISPR arrays

The CRISPR arrays of CP029843_1

>merge|CP029843|1|1479824-1479920|CRISPRCasFinder
GTCGCAGCTTACGCAGCTCCTACAGATGCGGAGGCCTTCCCCTGTAGGAGCGGCGGCCTTCATGGGAAGGCCCGGTCGCAGCTTGCGCAGCTCCTAC

>CP029843|1|1|1479824-1479920|CRISPRCasFinder
GTCGCAGCTTACGCAGCTCCTAC	AGATGCGGAGGCCTTCCCCTGTAGGAGCGGCGGCCTTCATGGGAAGGCCCG
GTCGCAGCTTGCGCAGCTCCTAC

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
CP029843.1|AWV06908.1|1491046_1491430_-|membrane-protein	unknown	unknown	unknown
CP029843.1|AWV06904.1|1486894_1487845_+|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase	unknown	unknown	gnl|CDD|234893
CP029843.1|AWV06899.1|1480215_1480485_-|30S-ribosomal-protein-S20	unknown	unknown	gnl|CDD|178943
CP029843.1|AWV06901.1|1482529_1483489_+|riboflavin-kinase	unknown	unknown	gnl|CDD|235536
CP029843.1|AWV06889.1|1466890_1467793_+|sulfurtransferase	unknown	unknown	gnl|CDD|225450
CP029843.1|AWV06897.1|1478249_1478510_+|50S-ribosomal-protein-L27	unknown	unknown	gnl|CDD|235464
CP029843.1|AWV06906.1|1489561_1490164_-|hypothetical-protein	unknown	unknown	gnl|CDD|379312
CP029843.1|AWV06895.1|1475186_1477265_-|peptidase-S8	unknown	unknown	gnl|CDD|173820
CP029843.1|AWV06905.1|1488156_1488492_-|hypothetical-protein	unknown	unknown	gnl|CDD|367760
CP029843.1|AWV06890.1|1467894_1468662_-|enoyl-CoA-hydratase	unknown	unknown	gnl|CDD|119339
CP029843.1|AWV06894.1|1474148_1474928_-|hypothetical-protein	unknown	unknown	gnl|CDD|143586
CP029843.1|AWV06898.1|1478669_1479746_+|GTPase-CgtA	unknown	unknown	gnl|CDD|237047
CP029843.1|AWV06903.1|1486337_1486856_+|peptidase-A8	unknown	unknown	gnl|CDD|234739
CP029843.1|AWV06891.1|1468658_1470221_-|hypothetical-protein	unknown	unknown	gnl|CDD|227628
CP029843.1|AWV06893.1|1471009_1473940_-|excinuclease-ABC-subunit-A	unknown	unknown	gnl|CDD|234734
CP029843.1|AWV06900.1|1480771_1482313_+|hypothetical-protein	unknown	unknown	gnl|CDD|240528
CP029843.1|AWV06892.1|1470338_1471013_-|thioesterase	unknown	unknown	gnl|CDD|223894
CP029843.1|AWV06902.1|1483495_1486330_+|isoleucyl-tRNA-synthetase	unknown	unknown	gnl|CDD|235588
CP029843.1|AWV06907.1|1490217_1490604_-|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV06896.1|1477967_1478237_+|50S-ribosomal-protein-L21	unknown	unknown	gnl|CDD|235510

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
CP029843.1|AWV06904.1|1486894_1487845_+|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase	gnl|CDD|234893	PRK01045, ispH, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Reviewed.	0
CP029843.1|AWV06899.1|1480215_1480485_-|30S-ribosomal-protein-S20	gnl|CDD|178943	PRK00239, rpsT, 30S ribosomal protein S20; Reviewed.	1.87184e-26
CP029843.1|AWV06901.1|1482529_1483489_+|riboflavin-kinase	gnl|CDD|235536	PRK05627, PRK05627, bifunctional riboflavin kinase/FAD synthetase.	2.29569e-140
CP029843.1|AWV06889.1|1466890_1467793_+|sulfurtransferase	gnl|CDD|225450	COG2897, SseA, Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism].	9.40079e-78
CP029843.1|AWV06897.1|1478249_1478510_+|50S-ribosomal-protein-L27	gnl|CDD|235464	PRK05435, rpmA, 50S ribosomal protein L27; Validated.	1.36685e-51
CP029843.1|AWV06906.1|1489561_1490164_-|hypothetical-protein	gnl|CDD|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	5.17933e-19
CP029843.1|AWV06895.1|1475186_1477265_-|peptidase-S8	gnl|CDD|173820	cd07496, Peptidases_S8_13, Peptidase S8 family domain, uncharacterized subfamily 13. 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.	1.62099e-114
CP029843.1|AWV06905.1|1488156_1488492_-|hypothetical-protein	gnl|CDD|367760	pfam03992, ABM, Antibiotic biosynthesis monooxygenase. This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.	0.00032273
CP029843.1|AWV06890.1|1467894_1468662_-|enoyl-CoA-hydratase	gnl|CDD|119339	cd06558, crotonase-like, Crotonase/Enoyl-Coenzyme A (CoA) hydratase superfamily. This superfamily contains a diverse set of enzymes including enoyl-CoA hydratase, napthoate synthase, methylmalonyl-CoA decarboxylase, 3-hydoxybutyryl-CoA dehydratase, and dienoyl-CoA isomerase. Many of these play important roles in fatty acid metabolism. In addition to a conserved structural core and the formation of trimers (or dimers of trimers), a common feature in this superfamily is the stabilization of an enolate anion intermediate derived from an acyl-CoA substrate. This is accomplished by two conserved backbone NH groups in active sites that form an oxyanion hole.	1.71689e-48
CP029843.1|AWV06894.1|1474148_1474928_-|hypothetical-protein	gnl|CDD|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	6.61266e-13
CP029843.1|AWV06898.1|1478669_1479746_+|GTPase-CgtA	gnl|CDD|237047	PRK12298, obgE, GTPase CgtA; Reviewed.	0
CP029843.1|AWV06903.1|1486337_1486856_+|peptidase-A8	gnl|CDD|234739	PRK00376, lspA, lipoprotein signal peptidase.	7.18821e-68
CP029843.1|AWV06891.1|1468658_1470221_-|hypothetical-protein	gnl|CDD|227628	COG5316, COG5316, Uncharacterized conserved protein [Function unknown].	3.76827e-32
CP029843.1|AWV06893.1|1471009_1473940_-|excinuclease-ABC-subunit-A	gnl|CDD|234734	PRK00349, uvrA, excinuclease ABC subunit UvrA.	0
CP029843.1|AWV06900.1|1480771_1482313_+|hypothetical-protein	gnl|CDD|240528	cd13123, MATE_MurJ_like, MurJ/MviN, a subfamily of the multidrug and toxic compound extrusion (MATE)-like proteins. Escherichia coli MurJ (MviN) has been identified as essential for murein biosynthesis. It has been suggested that MurJ functions as the peptidoglycan lipid II flippase which is involved in translocation of lipid-anchored peptidoglycan precursors across the cytoplasmic membrane, though results obtained in Bacillus subtilis seem to indicate that its MurJ homologs are not essential for growth. Some MviN family members (e.g. in Mycobacterium tuberculosis) possess an extended C-terminal region that contains an intracellular pseudo-kinase domain and an extracellular domain resembling carbohydrate-binding proteins. Proteins from the MATE family are involved in exporting metabolites across the cell membrane and are often responsible for multidrug resistance (MDR).	1.53735e-156
CP029843.1|AWV06892.1|1470338_1471013_-|thioesterase	gnl|CDD|223894	COG0824, FcbC, Predicted thioesterase [General function prediction only].	1.04881e-35
CP029843.1|AWV06902.1|1483495_1486330_+|isoleucyl-tRNA-synthetase	gnl|CDD|235588	PRK05743, ileS, isoleucyl-tRNA synthetase; Reviewed.	0
CP029843.1|AWV06896.1|1477967_1478237_+|50S-ribosomal-protein-L21	gnl|CDD|235510	PRK05573, rplU, 50S ribosomal protein L21; Validated.	2.47814e-37

Protein sequences

>CP029843.1|AWV06898.1|1478669_1479746_+|GTPase-CgtA
MKLVDEAEIQVIAGNGGNGCVGFRREKFIPLGGPDGGDGGDGGSVWLEASENLNTLVDFRHQKSFRAQRGENGMGRQMYGKAGEDTVITVPVGTVITNVETDEVIGDMTRHGDRLLVAKGGKGGLGNMHFKSSVNRAPRKALPGLPGEERVLKLELKLLADVGLLGFPNAGKSTLIRAVSAATPKVADYPFTTLYPNLGVVSVEAHRSFVIADIPGLIEGAADGAGLGAQFLRHLQRTRLLLHLVDMAPMEGGVEGVSPAEQVRAIEHELGKHDPELLNKPRWLILNKADLLLEEEQAEAAQAIIDELGWKGRWYKVSAISREGTWPVMLDVMAFFDRQAEEAAEAAAEAAAQGARAD
>CP029843.1|AWV06897.1|1478249_1478510_+|50S-ribosomal-protein-L27
MAHKKGVGSTRNGRDSNPKYLGVKIYGGQAIEAGNIIVRQRGTQFHPGSGVGLGRDHTLFALVDGKVEFSTKGPKKRRTVSVVAAE
>CP029843.1|AWV06896.1|1477967_1478237_+|50S-ribosomal-protein-L21
MQGETLRVELLEAEAGSEIKLDNVLMLGDGEGVKVGDEVKGATVTAKVVGHGRADKVRIVKFRRRKHHRKQMGHRQHYTEIEITGIAGK
>CP029843.1|AWV06895.1|1475186_1477265_-|peptidase-S8
MRWSALAIATAIVVAPAAYSGGKLNGFKPPSSAAAATATARAASESVDRFIVTYRQDPTLRASTTAASRVQGLATAARDAGIGIEPLRTLATGDAVIRTDRKLDRAASKALMIALMKDPNVLTVEPDRKLTRQFVPNDPAYPQQWHYQSGNGGINAEGAWDLSTGDGVVVAVLDTGSTPHVDLAGSYVAGYDFIDDLDTAVDGDGRDADPNDPGDWHSGECNIFGIPEDSSWHGTHVAGTIAAATDNGIGVAGVAHGAKVQPVRVLGKCGGYISDIADAITWASGGTVSGVPDNATPAEVINLSLGGGGACSAAMQSAIDGAVGRGTSVVVAAGNSSSDASGFTPANCDNVIAVAATGPDYQFASGYSNFGDTVDVAAPGGTGATPAEDNILSTLNSGATTQEDDVYAWYAGTSMAAPHVAGTVALMQAAAPMPKTPAEIEEILVNTAYAATGFPVGCSYSKSCGSGVIDAQYAVSVASGAEPLPDAPPPPPPPPPATPLENGVTVTDIEVEADGTVRYELQVPNGASNLLFAMYGGTGDADIYVRHGDEPTDTAYDCRPFSAGNNETCFFPAPEGGTWYVTIKGFSNAAGISLYPSFVDAGWPRALEAEAAQLNNHRTRVHLQWTHGAKYVDIYRNGAILKTVRNRRLSTTDTFRIIGSGTMSYKVCNNGTQECSDPVSIDYASQKRRSKQ
>CP029843.1|AWV06894.1|1474148_1474928_-|hypothetical-protein
MSDAVSAAAPAEAAFDSRLSIVDNNGMLRFDGTVDSDAARKTITEAIGAAYASDRVSGGVTVDGNARPAPWLHGLAPFLAGFKAPGAAISFRADTIELSGQVSADQRGRLETLARTHFPGLRLSGLFAGQDGDADPAIAALAALHPQSPAHGVESALNKMAIGFEQGSAKIAPASLAVIAQAGQTLASMPADRRVEIAGHAAASGDPDADALLSRRRAEAVKVQLIVNGVNPGMIETLASDGGAATGTQADQVTFRVLN
>CP029843.1|AWV06893.1|1471009_1473940_-|excinuclease-ABC-subunit-A
MDTIRIRGARTHNLKNIDLDLPRDKLIVITGLSGSGKSSLAFDTVYAEGQRRYVESLSAYARQFLSVMEKPDVDHIEGLSPAISIEQKSTSHNPRSTVGTITEIYDYLRLLYARVGTPRCPDHHYPLEAQTVSQMVDQVIALSARPDTAEQRYMLLAPVIRERKGEHAQVFEQLRAQGYVRVRVDGEVHEIDAVPTLALRQKHTIEAVVDRFRPREDMKQRLAESFETALKLGDGMASVMSLDQADAEPLLFSSRYSCPVCDYALPELEPRLFSFNSPVGACQHCDGLGVAQFFDPGRVVVHPELALSAGAVRGWDRRNAYYFQMIQSLARHYDFDVDTPWQALSEDVRQAVLYGSGEEQITFTYLTDGGSRNQRKHRFEGIIPNLERRYRETESAAVREELSKYISERPCPECGGARLNRAARNVFVDERPLPDIVVMPVDEALAFFQAMRLPGWRGEIAVKIVKEIADRLRFLVDVGLDYLTLERKADSLSGGEAQRIRLASQIGAGLVGVMYVLDEPSIGLHQRDNERLLGTLTRLRDLGNTVIVVEHDEDAIRLADHVVDIGPGAGVHGGEVVAQGQLDDVLKAPRSLTGQYLSGRKRIEVPSKRTRPNPKATLHLRGARGNNLKNVDLDIPAGLLTCVTGVSGSGKSTLINDTLYVIAANELNGASQTAAPYASVDNIDLFDKVVDIDQSPIGRTPRSNPATYTGLFTPLRELFAQVPESRARGYAAGRFSFNVRGGRCEACQGDGLIKVEMHFLPDVYVPCDVCGGKRYNRETLEILYKGYSIHDVLEMTVEDALGLFENIPAIARKLETLVDVGLSYIKLGQSATTLSGGEAQRVKLSKELSRRDTGRTLYILDEPTTGLHFHDIEHLLSVLHRLRDDGNTVVVIEHNLDVIKTADWIVDLGPEGGHRGGTILATGTPEDIAALEHSHTGRFLAPLLGKPAASSKGGKAGARKTAPRKTAAKKSKKANA
>CP029843.1|AWV06892.1|1470338_1471013_-|thioesterase
MSTQNKAGAASDADTGSAASPEAGDSARKPRKTAARKRTTAAKKRPAKKKTAPAPAPAQAADGGDGVGTAAPAADPAPAAPAATPTPADSPAETLLLNTPMTVRWRDLDAFNHVNNSKYLSYLEEARLRWMLGVPGQGLDDDVAPVVAAAHLNYKRPIEWPAEIAIELFVERLGNTSVSIGHRIAAAADRDTLYCDGYVVMVWIDRETGQAAPLPEAVREACSP
>CP029843.1|AWV06891.1|1468658_1470221_-|hypothetical-protein
MRHPLSLLAAACLLAACSPSGPAQDTAPRPSADADARGADNGRPDESEAAQGTRLTVYSGDYEALRSGVPSGPGMPGYALVERTLRYNLSVGGNDISATRIPPAMDVEAAVLRPESDGVSVGGQRYVAPLSGTGDVLTRAIGQRITVEHTSGGAKQTDSGILLAVGDGLSLGLADGRVKVIRDYDNFSIIAGNDTLPREAALHWAVEAEKAGETAFALSYPMGGMAWRAEYRATISPGDDCRLALDGAALVVNRSGVAFDSARLTLVAGEPARTGNAGGGANRYRMAPQADMAEISAAPPAPRRSGEYHAYELPSASRIGNGAVERLPLFAPRAAVACERTYVVGDDAPGWVPPSPQLSPGYGGRSGELPVTATVSFDNSSDAGLGQPLPAGRMRVFDGDDFLGESALGHSPEGREVRLRVGTAFDLSAERKATSLEVDRNGRRITESFELVLGNAGDDAVTIRAIESMMRWSDWEIVASSVPVADKDAQSAEFEVPVPAKGETTLTYTVRYQWPEGIRL
>CP029843.1|AWV06890.1|1467894_1468662_-|enoyl-CoA-hydratase
MSAHDLVESRRHGDIVELQLARAPVNALNPALCGALHGAIAAAVASQARGIVLSGGPKVFSAGLDVPHLLSLGEDKAALKAAWEAFFGAARALVECPVPVVAAIAGHAPAGGCVLALCCDYRVMASGPYRIGLNETRVGLVAPEGIQRLMRRVVGPYRAERLLVAGEMIESEQALAFGLVDELVGIDEVAQRARSWLEQLLALPTEAMLQTRAIARADMVAAMQPELIQLDRFIDAWYDAGTQRALNALVASLRK
>CP029843.1|AWV06889.1|1466890_1467793_+|sulfurtransferase
MTMQTPALTAAWNAWIDAERLARALGDDDLVVIDARFELADPEAGEAGWRQARIPGARYAHLDRDLSAPAESGAEAALHGQGRHPWPRAAEFAVRLRAWGVTPAHRVAVYDAAGGALAAARLWFLLRALGHEKVAVLDGGWQHWLAQGLPIDREPPAPTASAAAPYPGDFDAGLLLDAPQVQAHLRAGGLLVDVRAPERFRGDVEPIDRVGGHVPGAVNRPFADNLRDGLSKPPAELAAEFEGLLDGRAPRELVAMCGSGVSACHHLLAMAHAGLPGARLFTGSWSGWIEAPSRPIAIGA
>CP029843.1|AWV06899.1|1480215_1480485_-|30S-ribosomal-protein-S20
MANIKSAKKRAKQTVVRNARNASQRSMLRTYVKKVLKALGENDAAGAETAFKAAQPILDRYSSRGLIHKNKAARHKSRLNARIKALKAA
>CP029843.1|AWV06900.1|1480771_1482313_+|hypothetical-protein
MLRSTAVFSLMTFVSRIAGYVRDAVTASLFGAGPGMSAFVVAYRIPNYLRRIFAEGSFSSAFVPVLSELKEKGDQKALQEVLDHVAGALFAAVVVVSGLGMLAAPWVAQLFLALAPPGTETVPLAAQMLRITFPYLVFISMTALAGGVLNSFRHFGLPALTPVLHNLAMIAAMLLLAGRLEVPEASMAWGVLAAGILQVLVLWPAMGRLGLRPRLRFDFRHEGVRRVGRLMLPTVFSSSVAQINVLVGTMFAALLVPAAQSWLYYSDRLTELPLGLFGVAIGTVILPQLSRHHAAKDEAGYSKSLDWGLRIVLLIGIPAALGLALLAEPLTASLFQRRAFTAEDSRMVGIALTAMSVGIPTFMLSKVLLPAFYARQDTRTPMRAALITVVANVLLTVLLVTPLWMLGVAEAHVGIAAATALAGILNAALLWRYLRRQGLYTPEPGWGRWLGRIAAALLAMTVVVVAIREHVGAWGALPMGSRWLWLLATVAAGGGAYGATLLLLGLRPRHLRH
>CP029843.1|AWV06901.1|1482529_1483489_+|riboflavin-kinase
MVCIGAFDGLHLGHRALVRHAVARSRAIAGVGTTVGLQAVALSFEPLPREFFAPQAPPPRLLSPRAKVEGLLGLGADQVGLLRFNARLSGLDAESFVERVLVEHLRACEVWVGPGFRFGKARAGDIDLLHRLGRRHGFVAGEIEPVMLDGERVSSTRIRAALQDGAFDAAARMLGRPYAIGGRVVRGRQLGRTLGYPTANIRFGGRTPALSGIHATWVHGVGDAPMPSVSSLGTRPTVDGVEPLLEAHLFDFEGDLYGRRIEVEFVAKLRDEEKFDDLPALVAQMDRDAEQARAVLDRSPRNDPPRVPERTSHTEPSFE
>CP029843.1|AWV06902.1|1483495_1486330_+|isoleucyl-tRNA-synthetase
MSQDYKATLNLPATDFPMRGDLPRREPGTLERWESEGLYARLREHAAGRPRFVLHDGPPYANGAIHLGHAVNKILKDIIVKSKCMAGFDAPYVPGWDCHGLPIEIAIEKKHGKVGVKLDAVEFRQKCREYARSQIDVQRRDFKRLGVIGDWDNPYLTLDFHFEANEMRALARIIDNGHLTRGVKPVHWCFDCGSALAEAEIEYQDKVSPAIDVAYAARDPQAIARAFGVALPEGVEVAVPIWTTTPWTLPASLAVSVGPELEYALVEGPAHDGRRRWLVLADALAAAALARYGVDAPVVHGRVAGAALENLVLAHPFYATRDIPLILGDHVSAEDGTGAVHTAPGHGQEDYAAARRYGLIEKYDAAVLNPVDGRGVYLPGTPPAGDTELAGQHIWKANDAIVEALRASGALLAFARLEHSYPHCWRHKTPIAFRATPQWFISMEQANLRDDALAAIKNVGWFPKWGEARIAGMVEGRPDWTISRQRTWGVPIALFVHRQSGEPHPRSSELMRAVAERVEQGGVDVWYTLDAAELLGEEAADYEKITDILDVWFDSGVTHEAVLVERGFGKPADLYLEGSDQHRGWFQSSLLTGVAMDKAAPYRQCLTHGFTVDEKGRKMSKSLGNGIEPQDIMKTLGADILRLWIASADYSNEMSLSQEILKRNADAYRRIRNTARFLLSNLHGFEPARDLRALDDMVALDRWIVHRAWEVQEKIKAAYARYDFAEIVQALLNFCSVDLGSVYLDITKDRLYTMQEDSRGRRSAQSAMFRIIEAFVRWIAPVLSFTADELWGYLPTPADGARLDNVLFATWYEGLAPMPADAPLSAARFDRLLELREQVSAVLEPMRAAGEIGAALDAEVTLAVGDDEQAWLAPLADELRFLFISGDVSVVAGGNGVKAAATDKPKCVRCWHHRADVGSDPAHPQLCGRCVSNIDGSGEQRQWF
>CP029843.1|AWV06903.1|1486337_1486856_+|peptidase-A8
MPMTASRPSPNALAWLLVSVLVIALDQLTKWWVLTSLPEYTAIPVIDGFWNWYRTYNTGAAFSFLSDAGGWQKYFFLVLAVAISGLLGWWLSHTPRRDWRTALPYALVIGGAIGNVIDRLMHGHVVDFIQWYWRDWYWPAFNIADSAIVAGAVGIALMGVFGHKAREAAGEG
>CP029843.1|AWV06904.1|1486894_1487845_+|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase
MDVLLANPRGFCAGVDRAIEIVKRALETLGAPIYVRHEVVHNRFVVDDLRHRGAIFVEELDEVPDGATVIFSAHGVSQAVRTEAERRDLKVFDATCPLVTKVHFEVARHCRAGRDVVLIGHAGHPEVEGTMGQWQREAGEGRIYLVEDIEDVAALQVGQPENLAYTTQTTLSVDDTKVVIEALRRRFPAIQGPKNDDICYATQNRQDAVRELAARCDLVLVVGSVNSSNSNRLRELAEREGTRAYLIDGAIEIDPEWVRGCERIGVTAGASAPEVLVRGVIERLRELGAGHVNELDGEPESMVFALPKELRLQLVD
>CP029843.1|AWV06905.1|1488156_1488492_-|hypothetical-protein
MTNPQLAFCALYRWRLHPGTEASFVRAWSRVTQLLKAERGSLGSRLHRGPDDIWYSYTQWPSAEAKAEGLAQPSVDPEAWQQMRDAIAERLPEIILEPVADYLAPLPNDGD
>CP029843.1|AWV06906.1|1489561_1490164_-|hypothetical-protein
MTPSQTAATYDRIAQHWDHAGFDHSNGMAQHERALAFVSARGSALDVGCGSSGRIVSLLLQKGFRVEALDLSPEMLRRAKRHHPDVTFHRADICTWEIDEPFDFISAWDSIWHVPLGHQAAVVDKLCRGLSSGGVLIFSSGGVYAPDEVTGTCFGQALYHASPGIPALLRTIEDAGCHCRHLEFDAGPDDKHVYFIVQRP
>CP029843.1|AWV06907.1|1490217_1490604_-|hypothetical-protein
MSPEITAGLFGIIGVLVGGLVAWWLQKDRSSTDFRIALEAIKTEHMAETTARHFLSHQGYTDRSFELLSERLGGFEEDELRRILVRAGAIRYIRKDGSEFWRLLSREPEAIARARARSESSEPFDDDI
>CP029843.1|AWV06908.1|1491046_1491430_-|membrane-protein
MLKARIIVLLSGLVLPYAARLPRGSEWLHQYTDQAPMAWLFLGACNAVAWSAILAVSFLYRRPSSLLAPSLPGFGFLAWAHYSLDLAADAQAAIALIFIPVFALAPILVGAAIGYLIDRRAGSQGVA

Crispr_ID: CP029843_2

• CRISPR_ID: CP029843_2
• CRISPR_location: 2426187-2426327
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of CP029843_2

Consensus_repeat	Method
GCGGCTTACGCCGCTCCTACGAAAGCCGATCGCTTGTCCTGCTCCT	CRISPRCasFinder

spacers of CP029843_2

>2.1|2426233|49|CP029843|CRISPRCasFinder
GTAGGAGCGGCATGAGCCGCGACCCGAAGTATCTGGAGGCAGGCCCATC

CRISPR arrays and Neighbor proteins around CP029843_2

CRISPR arrays

The CRISPR arrays of CP029843_2

>merge|CP029843|2|2426187-2426327|CRISPRCasFinder
GCGGCTTACGCCGCTCCTACGAAAGCCGATCGCTTGTCCTGCTCCTGTAGGAGCGGCATGAGCCGCGACCCGAAGTATCTGGAGGCAGGCCCATCGCGGCTTACGCCGCTCCTACGAAAGCCGATCGCCTGTCCTGCTCCT

>CP029843|2|2|2426187-2426327|CRISPRCasFinder
GCGGCTTACGCCGCTCCTACGAAAGCCGATCGCTTGTCCTGCTCCT	GTAGGAGCGGCATGAGCCGCGACCCGAAGTATCTGGAGGCAGGCCCATC
GCGGCTTACGCCGCTCCTACGAAAGCCGATCGCCTGTCCTGCTCCT

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
CP029843.1|AWV07644.1|2429609_2430704_+|ribonuclease-D	unknown	unknown	gnl|CDD|130455
CP029843.1|AWV07635.1|2417601_2418168_-|elongation-factor-P	unknown	unknown	gnl|CDD|234788
CP029843.1|AWV07641.1|2425518_2426019_+|polyhydroxyalkanoate-synthesis-repressor-PhaR	unknown	unknown	gnl|CDD|130907
CP029843.1|AWV07642.1|2426441_2427338_-|peptidase	unknown	unknown	gnl|CDD|320690
CP029843.1|AWV07636.1|2418610_2419435_+|lysine-2,-3-aminomutase	unknown	unknown	gnl|CDD|163533
CP029843.1|AWV07639.1|2423411_2424329_+|glutamyl-Q-tRNA(Asp)-ligase	unknown	unknown	gnl|CDD|235573
CP029843.1|AWV07651.1|2449643_2450891_-|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV07638.1|2422421_2423333_-|protease-HtpX	unknown	unknown	gnl|CDD|235478
CP029843.1|AWV07640.1|2424403_2425144_+|3-ketoacyl-ACP-reductase	unknown	unknown	gnl|CDD|273823
CP029843.1|AWV07649.1|2447076_2448714_-|hypothetical-protein	unknown	unknown	gnl|CDD|372323
CP029843.1|AWV07645.1|2431675_2435287_-|type-IV-secretion-protein-Rhs	unknown	unknown	gnl|CDD|225750
CP029843.1|AWV07647.1|2437683_2438544_-|hypothetical-protein	unknown	unknown	gnl|CDD|274305
CP029843.1|AWV07633.1|2415162_2415744_-|bifunctional-2-polyprenyl-6-hydroxyphenol-methylase/3-demethylubiquinol-3-O-methyltransferase-UbiG	unknown	unknown	gnl|CDD|235350
CP029843.1|AWV07643.1|2427412_2429323_-|hypothetical-protein	unknown	unknown	gnl|CDD|335469
CP029843.1|AWV07632.1|2414452_2415166_-|phosphoglycolate-phosphatase	unknown	unknown	gnl|CDD|237311
CP029843.1|AWV07648.1|2445125_2445809_-|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV07650.1|2448715_2449630_-|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV07637.1|2419589_2421665_+|membrane-protein	unknown	unknown	gnl|CDD|376350
CP029843.1|AWV07634.1|2416098_2417442_-|N-ethylammeline-chlorohydrolase	unknown	unknown	gnl|CDD|236366
CP029843.1|AWV07646.1|2436439_2437468_-|hypothetical-protein	unknown	unknown	gnl|CDD|379396

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
CP029843.1|AWV07644.1|2429609_2430704_+|ribonuclease-D	gnl|CDD|130455	TIGR01388, Ribonuclease_D, ribonuclease D. This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA both in vitro and when overexpressed in vivo. Trusted members of this family are restricted to the Proteobacteria; Aquifex, Mycobacterial, and eukaryotic homologs are not full-length homologs. Ribonuclease D is not essential in E. coli and is deleterious when overexpressed. Its precise biological role is still unknown. [Transcription, RNA processing].	7.1924e-100
CP029843.1|AWV07635.1|2417601_2418168_-|elongation-factor-P	gnl|CDD|234788	PRK00529, PRK00529, elongation factor P; Validated.	1.83588e-105
CP029843.1|AWV07641.1|2425518_2426019_+|polyhydroxyalkanoate-synthesis-repressor-PhaR	gnl|CDD|130907	TIGR01848, Uncharacterized_protein_Alvin_0064, polyhydroxyalkanoate synthesis repressor PhaR. Poly-B-hydroxyalkanoates are lipidlike carbon/energy storage polymers found in granular inclusions. PhaR is a regulatory protein found in general near other proteins associated with polyhydroxyalkanoate (PHA) granule biosynthesis and utilization. It is found to be a DNA-binding homotetramer that is also capable of binding short chain hydroxyalkanoic acids and PHA granules. PhaR may regulate the expression of itself, of the phasins that coat granules, and of enzymes that direct carbon flux into polymers stored in granules. The C-terminal region is poorly conserved in this family and is not part of this model.//GO terms added 12/6/04 [SS] [Fatty acid and phospholipid metabolism, Biosynthesis, Regulatory functions, DNA interactions].	5.22068e-59
CP029843.1|AWV07642.1|2426441_2427338_-|peptidase	gnl|CDD|320690	cd07331, M48C_Oma1_like, Peptidase M48C, integral membrane endopeptidase. This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.	2.73657e-85
CP029843.1|AWV07636.1|2418610_2419435_+|lysine-2,-3-aminomutase	gnl|CDD|163533	TIGR03821, EFP_modif_epmB, EF-P beta-lysylation protein EpmB. Members of this radical SAM protein subfamily, including yjeK in E. coli, form a distinctive clade, homologous to lysine-2,3-aminomutase of Bacillus, Clostridium, and methanogenic archaea. Members of this family are found in E. coli, Buchnera, Yersinia, etc. The gene symbol is now reassigned as EpmB (Elongation factor P Modification B). [Protein fate, Protein modification and repair].	1.78024e-148
CP029843.1|AWV07639.1|2423411_2424329_+|glutamyl-Q-tRNA(Asp)-ligase	gnl|CDD|235573	PRK05710, PRK05710, tRNA glutamyl-Q(34) synthetase GluQRS.	4.27378e-127
CP029843.1|AWV07638.1|2422421_2423333_-|protease-HtpX	gnl|CDD|235478	PRK05457, PRK05457, protease HtpX.	2.99161e-176
CP029843.1|AWV07640.1|2424403_2425144_+|3-ketoacyl-ACP-reductase	gnl|CDD|273823	TIGR01829, Acetoacetyl-CoA_reductase, acetoacetyl-CoA reductase. This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.	3.23064e-138
CP029843.1|AWV07649.1|2447076_2448714_-|hypothetical-protein	gnl|CDD|372323	pfam12810, Gly_rich, Glycine rich protein. This family of proteins is greatly expanded in Trichomonas vaginalis. The proteins are composed of several glycine rich motifs interspersed through the sequence. Although many proteins have been annotated by similarity in the family these annotations given the biased composition of the sequences these are unlikely to be functionally relevant.	2.86089e-12
CP029843.1|AWV07645.1|2431675_2435287_-|type-IV-secretion-protein-Rhs	gnl|CDD|225750	COG3209, RhsA, Rhs family protein [Cell envelope biogenesis, outer membrane].	2.94609e-26
CP029843.1|AWV07647.1|2437683_2438544_-|hypothetical-protein	gnl|CDD|274305	TIGR02800, Protein_TolB, tol-pal system beta propeller repeat protein TolB. Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear. [Transport and binding proteins, Other, Cellular processes, Pathogenesis].	1.13124e-29
CP029843.1|AWV07633.1|2415162_2415744_-|bifunctional-2-polyprenyl-6-hydroxyphenol-methylase/3-demethylubiquinol-3-O-methyltransferase-UbiG	gnl|CDD|235350	PRK05134, PRK05134, bifunctional 2-polyprenyl-6-hydroxyphenol methylase/3-demethylubiquinol 3-O-methyltransferase UbiG.	4.33965e-114
CP029843.1|AWV07643.1|2427412_2429323_-|hypothetical-protein	gnl|CDD|335469	pfam03781, FGE-sulfatase, Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.	4.38405e-68
CP029843.1|AWV07632.1|2414452_2415166_-|phosphoglycolate-phosphatase	gnl|CDD|237311	PRK13226, PRK13226, phosphoglycolate phosphatase; Provisional.	1.64898e-104
CP029843.1|AWV07637.1|2419589_2421665_+|membrane-protein	gnl|CDD|376350	pfam00563, EAL, EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.	4.59137e-52
CP029843.1|AWV07634.1|2416098_2417442_-|N-ethylammeline-chlorohydrolase	gnl|CDD|236366	PRK09045, PRK09045, TRZ/ATZ family hydrolase.	0
CP029843.1|AWV07646.1|2436439_2437468_-|hypothetical-protein	gnl|CDD|379396	pfam13861, FLgD_tudor, FlgD Tudor-like domain. This domain has a tudor domain-like beta barrel fold. It is found in the FlgD protein the flagellar hook capping protein. The structure for this domain shows that it contains a nested Ig-like domain within it. However in some firmicute proteins this inserted domain is absent such as Q67K21.	1.04543e-08

Protein sequences

>CP029843.1|AWV07641.1|2425518_2426019_+|polyhydroxyalkanoate-synthesis-repressor-PhaR
MAATRVIKKYPNRRLYDTEISSYITIEDVRQLIVDGESFEVRDARSGEDLTRQVLLQIIAEQEQDGEPVLSTQLLSQIIRFYGDSLQGFMGNYLERSMQLFLDQQQQFRKQMGGLMGETPWAMMNQLTERNLAMWKEFQQNLSGSVGQTPTSPRPGNKNEGGKRGR
>CP029843.1|AWV07640.1|2424403_2425144_+|3-ketoacyl-ACP-reductase
MQSRVALVTGGTGGIGTSIIKRLAAAGHKVATNYRDEGRARAWQEKMKAEGVDVAMAQGDVTSPEQAEAMVRDIERQLGPIEILVNNAGITRDTTFHRMKPDQWNDVICTNLNSVYNVTRPVIEGMRERKWGRIIQISSINGLKGQYGQANYAAAKAGMHGFTISLARENARLGITVNTISPGYVATDMVMAVPEEVRAKIVADIPTGRLGEPDEIAYAVAFLTDDQAGWITGSNLDINGGHHMGW
>CP029843.1|AWV07639.1|2423411_2424329_+|glutamyl-Q-tRNA(Asp)-ligase
MPAPASDRPAPDPANRANPPYRGRFAPSPTGDLHAGSLLAAFGSWLLARHAGGEWWLRVEDLDPPREVAGAAQRQLTALREFGFVPDAPVVFQSRRHDLYRNALERLLDSGAAFECHCSRSDLAASGGIHRRCVARRRRPQPAVRLRVADGSIVAFEDAIQGRHVQDVAATVGDFVLRRADGLWAYQLAVVVDDAAQAITDVVRGADLLDSTPRQILLQRALDLPTPGYAHLPLVTDVHGRKLSKSDAAWPLDAADPLPALRRAWAALGQPGDALAGADLPASLLATARTAFQPHLIPPTLSATD
>CP029843.1|AWV07638.1|2422421_2423333_-|protease-HtpX
MFKRVALFLATNLAVLALISIVLAVLEKFFGINIGTGSNTGLLVFALLFGFGGSFISLMTSKWMAKRGTGAHVIEQPRNEAEQWLVNTVRRQAEAAGIKMPEVAIYDAPEINAFATGPSRNNSLVAVSTGLLRAMSRDEAEAVLGHEVSHVANGDMVTMALIQGVLNTFVIVLARVVGRVIDGYLSGGRDGPGIGYYVIVFVLDMVFGLFASMIAMWFSRYREFRADAGGARLAGRDKMVAALERLSVTYGESTLPKQVAAFGISGGVAHGLRQLLMSHPPLAERIQALRNAPAEPVGGRVAG
>CP029843.1|AWV07637.1|2419589_2421665_+|membrane-protein
MQFGKDLPLRLLVVDDSVEAAEAIVSMLRNSGIAVRPSRPENADALAQMLTAQPFDIVLVAHDAASVPLEEVMQRVDASGKDLPVLILHDDIDTARLLRAASLGARGVVLRSQPDLLRQQVMREWSDLEARRSLRKLENHVRETERRCDALIESSRDPIAYIHEGMHIRANAAYLETFGFDDFEEIEGMSLLDMVAPQHVDDFKQLLKKLSRGEPPPPRYELEARGLDGSAFPAVMEFTAATYEGEACQQVVLRRQELDPELAREVEELRQRDQVTGLLNRPTFLRALEDTVADAGEKASQHALLLVEPDHYTRLLQDIGLDEADALVAACARRLRDVLGPDDVAARFGEHQFAVLRRNCDYADSMALAEQIRAAFAAAVLDTGSRSLNATVSIGGVQIGQKIANVSSVLGKANQGVLSAVGVGGNRIELFDPSAADRAEEARVQAWVDRIRDAIDHDRFIMHFQPLVGLHGPPDQIYEAYLRLLNEHGELVQPMTFLQIAEEHGLLWEIDRWVVGHAIAVVGERRKAGHDTTVLVKITEVSLQDDSLLKHMAEQLARHGVEGRQLVVQLPESKVFTHLRAAQTFQEGAARLGVRVGLEQFGLGLNSFQLLSHFNAGLVKLDRSFMDDLPNNQEHQERIREITNRTRENGRLTIAEFVQDASSMSILFGAGIDYAQGQFLAPAGPEMNYEF
>CP029843.1|AWV07636.1|2418610_2419435_+|lysine-2,-3-aminomutase
MRPGDPHDPLLRQVLPLDAEMRPMPGFALDAVGDTAAKAGDGVIRKYRGRALLVATGSCAVHCRYCFRRHFPYAEEAAAAAGWRHTVELIRDDPGIDEVILSGGDPWSLATHKLAELTDALSAIAHLKRLRVHTRLPVVLPERVDAPLLDWLAALPWPVTVVVHANHANEFDASVDAAMARLRGAGATLLNQAVLLRGVNDDIQALCELSERGFQAGVLPYYLHQLDRVQGAAHFEVDDARARQLHAAMAARLSGYLVPKLVREVAGDTGKRPL
>CP029843.1|AWV07635.1|2417601_2418168_-|elongation-factor-P
MASYGMNDVKNGMKILVNNEPCIITDTEYVKPGKGQAFTRVKYRFIKSGRVVELTMKATDSLEAADVVDTDMQFLYADGEYWHFMNPENFEQVQADEAGIGDARKFLKGEEECVVTLWNGTPIAVQPPNFVELKITETDPGVRGDTSGGGGKPATLETGAVVRVPLFVNQDEVIKVDTRSGEYVGRVK
>CP029843.1|AWV07634.1|2416098_2417442_-|N-ethylammeline-chlorohydrolase
MSIENAPQPCDLLIEAGWVVPVVPHGVVLEQHAVAISDGAIVAVLPIREARERFAAAQVVSRPQSALIPGLVNAHTHNPMTLLRGVADDLPLMEWLQGHIWPVEGAVIGPEFVADGIELAIAEMLRGGTTCANENYFFPDVQAAVYKREGFRARVGLPVIDFPTAWAKTDDEYFDRAIEVHDQWRDDPFIATSFVPHAPYTVSDASFERIRMLSDQLDMPVHLHTHETAQEIDESRQKHGQRPLARLDRLGLVSDRLVAVHMTQLTDAEIAMCAERGVCVVHCPESNLKLASGFCPIGRLEKAGVTIAIGTDGCASNNDLDMFGETRTAALLAKAVADDAAAFDAASALRAATLGGARAVGFEDLIGSIEPGKQADLACVDLARIETQPLHHVISQLVYAAGRHQVSDVWIAGHAKLRDGVLVDMDADALIARAREWRKRIAAIRIS
>CP029843.1|AWV07633.1|2415162_2415744_-|bifunctional-2-polyprenyl-6-hydroxyphenol-methylase/3-demethylubiquinol-3-O-methyltransferase-UbiG
MAERASLAGAQALDVGCGGGLLSEALAGEGAEVTAIDLAPELVKVARLHRLETGLSVDYRLQSVEALAAEMPARFDVITCMEMLEHVPDPAAIVNACATLLKPGGRLFLSTLNRTAAAFALAIVGAEYVARVLPKGTHQYRDFIKPSELAAWLRAAGLQLEDVSGLAYEPWRNSARVIGRTDVNYLACAVKPE
>CP029843.1|AWV07632.1|2414452_2415166_-|phosphoglycolate-phosphatase
MSMVGEHRSTRVAAATAGFPKAVLFDLDGTLADSAHDLLAAANAMRAARGRPPMSLPEFRPSVSRGARAMLLAAFPDLPETERESWVPELLDQYQRQIGAHQGVFDGVEAMLGALEAAGTIWGIVTNKPEYLARELLPHLGWDSRSAVLIGGDTLPVRKPDPLPLTVAADRIGVAASDCVYVGDDERDIVAARAAGMRSVVALWGYRLAGDDPAGWGGDIMVEHPAELADPARWPRS
>CP029843.1|AWV07642.1|2426441_2427338_-|peptidase
MGRGGRGGGRRGGKFRWWILLLFAGYAAWQWFGSAEVDPYTGETAHYGASADEEVQLGAQAFRQVLGDANAQGALLPADAQLTQQIRSIAQRLVAKVPQVTADLAAMHNQAVPTSHQGFLWDVAVIQSDEANAFCLPGGKMAVYTGLIPVAQNENAVAVVMGHEIAHALLRHGSQRMAQQKLVQMGQVATGMAVGDMAPQQQQAIMAALGAGAQYGLILPYGRNHETQADRVGLMLAAAACYDPAEAVPLWQRMGQLGGGQRPPEFASTHPDPANRIAELQALMPQAEAFRQKYCGGQ
>CP029843.1|AWV07643.1|2427412_2429323_-|hypothetical-protein
MLLLAVLAGCSREPAQEDAGTTSAAAGEQAAPSVTVSADQALETMPDWQAPAVSLTDENIEALLAQADEALQAGRLYEDDESAIPIYLALKAGAEQASEAADGTEPTEATETAQAVDAAERSDTETAEKAEAGLQRALTALLAQGDAALESIDDAPEALQRAQQIGAVARAVAADADPVVAYLERVELMERVQQANVAGERALAAGRIDSGKDAALPHFRHALELREADARALQGLAASESALIREAEQAAEAYDYDKAEAGLARAAKVRSGDDTVAHARERIAAMRVERIGDLRDQGIAALSREDGLDTAREHLAELLRIAPKGDPAAIELRERIELATHYGLFRPGQVFTDALKNGGRGPQMVVVPHGAFTMGAADDEAGASDSERPTRNIRFDRGLAFARTEVTVAEFRRYLEATGNEPRAVRRGYSTAYDERSGNLVRRSGADPDDGYTGERADDDMPVIHVSAADAAAYARWLSEQTGHVYRLPSEAEFEYALRAGSQDRFPWGEGTPPAGSGNFTGGEDVSPSGRRWRNAFEGYGDGAWGPAAVASYRANAFGLHDMAGNVSEWVADCWHDNYRRAPRDAHAWVNPGCREKVVRGGSWASSPEQTRSAWRLSVRGDTTNARVGFRVVREI
>CP029843.1|AWV07644.1|2429609_2430704_+|ribonuclease-D
MPAPITDPAALQARLSPRPRRIGLDTEFIRERTYWPQLALVQISIETEDGLEVVLADPLAPGIAETLAPILADPAILKIMHSPSEDLVAFKHACNTVPAPLFDTQLAAALAGIGSGLGYQKLVEQLTGVTLAKGETRSDWLRRPLSAAQLEYAADDVRHLFELHDVLDHRLGELGRRDWLAEDATRTVTQADSDTPERWPHLAMRSAQFLDLDAQRRLLRLLRWRETHARQSDRPKSWILDNELAGTLARNPPIDLAGLQREFDSHPKAPRKLAATVWEVLNAPLDDEAEIPDASVAERRDRNRLRKLQAAVAARSAELGLPDGVLASRRWLEALLDHGRWPDALAGWRREALEPSLAPLLAES
>CP029843.1|AWV07645.1|2431675_2435287_-|type-IV-secretion-protein-Rhs
MVVAYQPRLTRIQERSADGVLTGYWIAFEYSESTGRLTRAVASDGRQVTYGHDEFEGATRGNLRTVAGLDDYVQGFAYTDPVDPHRLTAIVKNEGAAPVVNTYNAAGQVIRQVEGGSTFELDYSTPGRNVTTEIVTDASGAELQRRVRTREFDEAGYLTRKVDAAGHEERYIYNAGKDRIRTETWEKQADGSLVLLKAVDNTYNGQAQKLTESVTLASGEVVTATWTYDHGWIASEQKASTASPQVFRTEYEFVRDAQGVPINIAAVKRRNDDGSFATTSYSYCSASEAAAPGSTCPDTALLKTVDGPRTDVSDLTTYVYYGTTDVSGCGSASGPCQRRGDLKQVTNALGQSMDYLRYDGAGRAVQVRDANGVITDMVYHPRGWLLEQAVRGPDDAVTTDDAITSYQYDSRGNVISQTRPDGSFLEFEYDDRDRLTVTRDPDGNEVRYTLDSIGNRWKEETFAADGTRVRTLSREFDMLDRIARQLDAQNHTTVLVYDGRGRQTQITDALGRRAEQSYDALDRLKQSITDADGLQVGTSFHYDAAGNLRQVVDPKGLATSYQYDALGQLLQLDSPDTGTTIYTYDPAGNHNSQTDARGETSTYGHDALNRLSSVSYSDSSLDAAYAYDSVQPGCATGETFAIGRLSRMSDGSGHTDYCYDRFGQLVRKIQVTNGQSFTLRYAYTQAGQLSLMTYPDGTEVDYVRDGQGRTSEIGVTAPGGSREVLLSNASWYPSGPVGAWTFGNGRTLSRTLDLDYRPQSILSTDTGSPTSGGGLDLGFRFDAVGNLTSLHGADRADPPRVRLDYDALSRLTAFRDGPTDTAIESYGYDATGNRTSFTNAGGTQAYSYPTDSHRLGAVAGVARGYDAVGNTTAIGGTKEYVYSAANRLSAVKQGGAVTMHYGYNGSGERVHRHLGSDVTYSVYDEAGHWVGDYDASGAPKQQAIWLDDLPVGLLNGIAATANRLHYIEPDHLGTPRAVIEPQRDVAVWTWDIASEAFGNSAPNQDPDGDSTAFTLDMRFPGQRYDAASGLNYNYFRDYEAGTGRYSQSDPIGLLGGIGTYNYALAQPVQVHDRLGLNPATIGTAVVLGAIQGCAGGCAGAIVGDYTSCVIEKRRAGGKNLGQCSDECTPNPCDALRSCVSGCIAGAVLGGVTAGQGVALSPVAGYLLRNYFRFLFSPDFCQKYGIPAPPDPIPLPLPDWLRNL
>CP029843.1|AWV07646.1|2436439_2437468_-|hypothetical-protein
MRFDPERGETATVHFRIDVPAEVTLVIYDGRDRRVREVEGGRLEAGEHSLAWDGQDGRGRQVPAEAYVYTLEAIADSGAPVIHDLTDLTGGEALEVADVEWDPEAGLVRYRTDKPARVNIRLGLQNGGPYLRTLIDWVPRAAGKQAESWDGQDASGVLSLSRHPRLSVGVMAYGLPDNTLLVGAAPDRVSFADLPEEASRPRQTPKGPKRMYHHADQPLETRGDVSASLTLDGITRRDAQGRWIVSGSVPVRLNVADEDRELVLTRRFEPVFFVDGIYAFENEVGFLPMTWHWDTSSVNEGEHFVTVNVRGYDGNFGTATLKVWVDRPGAGSAPAGQEQTRE
>CP029843.1|AWV07647.1|2437683_2438544_-|hypothetical-protein
MTLAGLCLALMSGCRSEAPESIAFLAVSDGYWEVWVTDDEGRSPRKLSDFKADVSRISWFPDGNTLLVNLHDGRMFRLDADSGEASAVQAPMPGILDAVVSPDGRQATFSLSTADSIDNNDIWTFDLSTGGLNKLTSMARLQHEPTWSSDGAQVYFLSGRGGQTHDIWRADVATRETEQLTVNALYHFDLAARPDGALAYSGNQTGNYDLWIRHPDGRAEQLTDDPELDARPTWSPDGKALAFESTRDGNIDIWRYDLGSSELKRLTEMPEGARHPVWSPVHGGER
>CP029843.1|AWV07648.1|2445125_2445809_-|hypothetical-protein
MVFAAVLLAPVVVWLVSVGNPLDYLDHTLPPGQALYVTSKFAALLALSCFWAQCLLALARRTPVLNGIPPAPLKLHRRLGCATLVLVLAHVGLFFVAASLRGGVPAWSLLLPNFGQGYYNAFVSLGLLAFWCLLLVAYAGWRVSRGRQRWKLVHMLWFVVFTLVFLHAYAIGSESRFGAMRYVLLFVATSLVAASWSRLRVAMKGRRPAIEQPAGVALEQVRERERV
>CP029843.1|AWV07649.1|2447076_2448714_-|hypothetical-protein
MAALAAPPVRARASAAPVLLAGGQGRPPAPWIRSAVREVLERAPNYRHLSADDRRTLAGAMVRVSALAAELIDEEGQAQQAIERQGGDSTPVGVSQGPRRPAPLARAQSQPGFAAAADRVAGTTQAVLNAVSFPRFVTDLINGVFRAMLDSSTQQMQQYVQLLNAVSASAEGFERTQFGLAQVRQWVADHFPESVEYETPDPDFDDPEDPVETRLRLRDGASMPEEEAIRATLGMEPGESVDAGNPEQLVPLARRYLARQRQQMLATMVMMGMHRIVIDSGRINAAMRFHVDTRSAASEDRGSQFSLQNRVRAAGRFGAGPWGVSAEVENNIGYVSTQRNQSTEEMNTDLELNSSVELNFRSDYLPLNRMAAQAQADRIRNASINPVAESDPIAARTERLQAQHESERARREAMDTAIGEAGQTSMADSPLEVPEPNSGSGRSGSGGSGSGGSSSGGSSSGGSSSGGSSSGGSSSGGSSSGGSGSGGSGSGGSGSGGSGSGGSGSGGSGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGSGG
>CP029843.1|AWV07650.1|2448715_2449630_-|hypothetical-protein
MRLAPPPADVCLYPGHEHAGLLRSLSLAMSVLGERKALALALSGTGFDELGAIDLPPGPAGGLDRVRLRAAAPLYFAAKLEDAGLLPTAELIAGLFASGAITQPIGPVARMINDFWRARRERLSADERAAIYARAVEPPYFDRLMAALCEAIVAQADGSDIRERVVLETAIDALVEFLSQRVDPMAAMAARDIVENINQALGFMRDRMLQAAFGVQSLWSLVAIAGDARGQGAGPVQRHVDLGRAGQTVLLWLAEHAGTSAPLLDPGDFELIGAAQRWLSGRIESGTATAPMDMPVLPALPAVA
>CP029843.1|AWV07651.1|2449643_2450891_-|hypothetical-protein
MSEPVPRATHNPAWLDDETLAAVRPQVRRLLQSSPGFRELPVAEQQELARNMVRVASYMSNPDGLAKQELTPGRGVLAKDEAPQGGLARALAGEVDAAKRKASEKVGTFAGSDFEAGSVEQGATNFRKYIGAVDFPAFVGGLIQNVFQAIVDASIQQMRAYGELLKSVSQTVDQFASDNISLNNARDWLVDRFAGDFRIETASDGFDEGGGPRVALVNEDNAQEVMGRVNQEMQMAKPITDLSDPEQEGRLAQAARMQMARSRQQLLSSMVILGINRIVITDGAINAKVVFDFRASDQAQRSAAASLYDRDTSYNRNTTVAGAHFGWGGAATANTNVQTHMTTVSSSVDEESESKQEMKAKLTGEVRVNFKSDYFPMEKLASPAMIAAIQGNSTPVDPNYIPSTRNAAGAGGSGG

Crispr_ID: CP029843_3

• CRISPR_ID: CP029843_3
• CRISPR_location: 2439850-2439942
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of CP029843_3

Consensus_repeat	Method
CGCACGTAGATGCCGTAGTTGTTG	CRISPRCasFinder

spacers of CP029843_3

>3.1|2439874|45|CP029843|CRISPRCasFinder
GCCGTGATCTCGTTGCCGTTGGTGATCTGCGGCGAACTGCCTGCA

CRISPR arrays and Neighbor proteins around CP029843_3

CRISPR arrays

The CRISPR arrays of CP029843_3

>merge|CP029843|3|2439850-2439942|CRISPRCasFinder
CGCACGTAGATGCCGTAGTTGTTGGCCGTGATCTCGTTGCCGTTGGTGATCTGCGGCGAACTGCCTGCACGCACGTAGATGCCGTAGGTGTTG

>CP029843|3|3|2439850-2439942|CRISPRCasFinder
CGCACGTAGATGCCGTAGTTGTTG	GCCGTGATCTCGTTGCCGTTGGTGATCTGCGGCGAACTGCCTGCA
CGCACGTAGATGCCGTAGGTGTTG

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
CP029843.1|AWV07655.1|2455831_2457298_-|hypothetical-protein	unknown	unknown	gnl|CDD|173810
CP029843.1|AWV07656.1|2457294_2458068_-|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV07644.1|2429609_2430704_+|ribonuclease-D	unknown	unknown	gnl|CDD|130455
CP029843.1|AWV07645.1|2431675_2435287_-|type-IV-secretion-protein-Rhs	unknown	unknown	gnl|CDD|225750
CP029843.1|AWV07649.1|2447076_2448714_-|hypothetical-protein	unknown	unknown	gnl|CDD|372323
CP029843.1|AWV07642.1|2426441_2427338_-|peptidase	unknown	unknown	gnl|CDD|320690
CP029843.1|AWV07654.1|2453532_2455647_-|hypothetical-protein	unknown	unknown	gnl|CDD|237110
CP029843.1|AWV07639.1|2423411_2424329_+|glutamyl-Q-tRNA(Asp)-ligase	unknown	unknown	gnl|CDD|235573
CP029843.1|AWV07646.1|2436439_2437468_-|hypothetical-protein	unknown	unknown	gnl|CDD|379396
CP029843.1|AWV07640.1|2424403_2425144_+|3-ketoacyl-ACP-reductase	unknown	unknown	gnl|CDD|273823
CP029843.1|AWV07653.1|2452430_2453486_-|hypothetical-protein	unknown	unknown	gnl|CDD|274575
CP029843.1|AWV07647.1|2437683_2438544_-|hypothetical-protein	unknown	unknown	gnl|CDD|274305
CP029843.1|AWV07641.1|2425518_2426019_+|polyhydroxyalkanoate-synthesis-repressor-PhaR	unknown	unknown	gnl|CDD|130907
CP029843.1|AWV07652.1|2450929_2452237_-|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV07643.1|2427412_2429323_-|hypothetical-protein	unknown	unknown	gnl|CDD|335469
CP029843.1|AWV07650.1|2448715_2449630_-|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV07638.1|2422421_2423333_-|protease-HtpX	unknown	unknown	gnl|CDD|235478
CP029843.1|AWV07651.1|2449643_2450891_-|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV07648.1|2445125_2445809_-|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV07657.1|2458064_2458355_-|hypothetical-protein	unknown	unknown	unknown

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
CP029843.1|AWV07655.1|2455831_2457298_-|hypothetical-protein	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.	7.91178e-44
CP029843.1|AWV07644.1|2429609_2430704_+|ribonuclease-D	gnl|CDD|130455	TIGR01388, Ribonuclease_D, ribonuclease D. This model describes ribonuclease D, a 3'-exonuclease shown to act on tRNA both in vitro and when overexpressed in vivo. Trusted members of this family are restricted to the Proteobacteria; Aquifex, Mycobacterial, and eukaryotic homologs are not full-length homologs. Ribonuclease D is not essential in E. coli and is deleterious when overexpressed. Its precise biological role is still unknown. [Transcription, RNA processing].	7.1924e-100
CP029843.1|AWV07645.1|2431675_2435287_-|type-IV-secretion-protein-Rhs	gnl|CDD|225750	COG3209, RhsA, Rhs family protein [Cell envelope biogenesis, outer membrane].	2.94609e-26
CP029843.1|AWV07641.1|2425518_2426019_+|polyhydroxyalkanoate-synthesis-repressor-PhaR	gnl|CDD|130907	TIGR01848, Uncharacterized_protein_Alvin_0064, polyhydroxyalkanoate synthesis repressor PhaR. Poly-B-hydroxyalkanoates are lipidlike carbon/energy storage polymers found in granular inclusions. PhaR is a regulatory protein found in general near other proteins associated with polyhydroxyalkanoate (PHA) granule biosynthesis and utilization. It is found to be a DNA-binding homotetramer that is also capable of binding short chain hydroxyalkanoic acids and PHA granules. PhaR may regulate the expression of itself, of the phasins that coat granules, and of enzymes that direct carbon flux into polymers stored in granules. The C-terminal region is poorly conserved in this family and is not part of this model.//GO terms added 12/6/04 [SS] [Fatty acid and phospholipid metabolism, Biosynthesis, Regulatory functions, DNA interactions].	5.22068e-59
CP029843.1|AWV07642.1|2426441_2427338_-|peptidase	gnl|CDD|320690	cd07331, M48C_Oma1_like, Peptidase M48C, integral membrane endopeptidase. This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.	2.73657e-85
CP029843.1|AWV07639.1|2423411_2424329_+|glutamyl-Q-tRNA(Asp)-ligase	gnl|CDD|235573	PRK05710, PRK05710, tRNA glutamyl-Q(34) synthetase GluQRS.	4.27378e-127
CP029843.1|AWV07638.1|2422421_2423333_-|protease-HtpX	gnl|CDD|235478	PRK05457, PRK05457, protease HtpX.	2.99161e-176
CP029843.1|AWV07640.1|2424403_2425144_+|3-ketoacyl-ACP-reductase	gnl|CDD|273823	TIGR01829, Acetoacetyl-CoA_reductase, acetoacetyl-CoA reductase. This model represent acetoacetyl-CoA reductase, a member of the family short-chain-alcohol dehydrogenases. Note that, despite the precision implied by the enzyme name, the reaction of EC 1.1.1.36 is defined more generally as (R)-3-hydroxyacyl-CoA + NADP+ = 3-oxoacyl-CoA + NADPH. Members of this family may act in the biosynthesis of poly-beta-hydroxybutyrate (e.g. Rhizobium meliloti) and related poly-beta-hydroxyalkanoates. Note that the member of this family from Azospirillum brasilense, designated NodG, appears to lack acetoacetyl-CoA reductase activity and to act instead in the production of nodulation factor. This family is downgraded to subfamily for this NodG. Other proteins designated NodG, as from Rhizobium, belong to related but distinct protein families.	3.23064e-138
CP029843.1|AWV07653.1|2452430_2453486_-|hypothetical-protein	gnl|CDD|274575	TIGR03429, Tryptophan_dimethylallyltransferase_2, aromatic prenyltransferase, DMATS type. Members of this protein family are mostly fungal enzymes of secondary metabolite production. Characterized or partially characterized members include several examples of dimethylallyltryptophan synthase, a brevianamide F prenyltransferase, LtxC from lyngbyatoxin biosynthesis, and a probable dimethylallyl tyrosine synthase.	0.000128646
CP029843.1|AWV07647.1|2437683_2438544_-|hypothetical-protein	gnl|CDD|274305	TIGR02800, Protein_TolB, tol-pal system beta propeller repeat protein TolB. Members of this protein family are the TolB periplasmic protein of Gram-negative bacteria. TolB is part of the Tol-Pal (peptidoglycan-associated lipoprotein) multiprotein complex, comprising five envelope proteins, TolQ, TolR, TolA, TolB and Pal, which form two complexes. The TolQ, TolR and TolA inner-membrane proteins interact via their transmembrane domains. The {beta}-propeller domain of the periplasmic protein TolB is responsible for its interaction with Pal. TolB also interacts with the outer-membrane peptidoglycan-associated proteins Lpp and OmpA. TolA undergoes a conformational change in response to changes in the proton-motive force, and interacts with Pal in an energy-dependent manner. The C-terminal periplasmic domain of TolA also interacts with the N-terminal domain of TolB. The Tol-PAL system is required for bacterial outer membrane integrity. E. coli TolB is involved in the tonB-independent uptake of group A colicins (colicins A, E1, E2, E3 and K), and is necessary for the colicins to reach their respective targets after initial binding to the bacteria. It is also involved in uptake of filamentous DNA. Study of its structure suggest that the TolB protein might be involved in the recycling of peptidoglycan or in its covalent linking with lipoproteins. The Tol-Pal system is also implicated in pathogenesis of E. coli, Haemophilus ducreyi , Salmonella enterica and Vibrio cholerae, but the mechanism(s) is unclear. [Transport and binding proteins, Other, Cellular processes, Pathogenesis].	1.13124e-29
CP029843.1|AWV07649.1|2447076_2448714_-|hypothetical-protein	gnl|CDD|372323	pfam12810, Gly_rich, Glycine rich protein. This family of proteins is greatly expanded in Trichomonas vaginalis. The proteins are composed of several glycine rich motifs interspersed through the sequence. Although many proteins have been annotated by similarity in the family these annotations given the biased composition of the sequences these are unlikely to be functionally relevant.	2.86089e-12
CP029843.1|AWV07654.1|2453532_2455647_-|hypothetical-protein	gnl|CDD|237110	PRK12472, PRK12472, hypothetical protein; Provisional.	1.45284e-07
CP029843.1|AWV07643.1|2427412_2429323_-|hypothetical-protein	gnl|CDD|335469	pfam03781, FGE-sulfatase, Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.	4.38405e-68
CP029843.1|AWV07646.1|2436439_2437468_-|hypothetical-protein	gnl|CDD|379396	pfam13861, FLgD_tudor, FlgD Tudor-like domain. This domain has a tudor domain-like beta barrel fold. It is found in the FlgD protein the flagellar hook capping protein. The structure for this domain shows that it contains a nested Ig-like domain within it. However in some firmicute proteins this inserted domain is absent such as Q67K21.	1.04543e-08

Protein sequences

>CP029843.1|AWV07647.1|2437683_2438544_-|hypothetical-protein
MTLAGLCLALMSGCRSEAPESIAFLAVSDGYWEVWVTDDEGRSPRKLSDFKADVSRISWFPDGNTLLVNLHDGRMFRLDADSGEASAVQAPMPGILDAVVSPDGRQATFSLSTADSIDNNDIWTFDLSTGGLNKLTSMARLQHEPTWSSDGAQVYFLSGRGGQTHDIWRADVATRETEQLTVNALYHFDLAARPDGALAYSGNQTGNYDLWIRHPDGRAEQLTDDPELDARPTWSPDGKALAFESTRDGNIDIWRYDLGSSELKRLTEMPEGARHPVWSPVHGGER
>CP029843.1|AWV07646.1|2436439_2437468_-|hypothetical-protein
MRFDPERGETATVHFRIDVPAEVTLVIYDGRDRRVREVEGGRLEAGEHSLAWDGQDGRGRQVPAEAYVYTLEAIADSGAPVIHDLTDLTGGEALEVADVEWDPEAGLVRYRTDKPARVNIRLGLQNGGPYLRTLIDWVPRAAGKQAESWDGQDASGVLSLSRHPRLSVGVMAYGLPDNTLLVGAAPDRVSFADLPEEASRPRQTPKGPKRMYHHADQPLETRGDVSASLTLDGITRRDAQGRWIVSGSVPVRLNVADEDRELVLTRRFEPVFFVDGIYAFENEVGFLPMTWHWDTSSVNEGEHFVTVNVRGYDGNFGTATLKVWVDRPGAGSAPAGQEQTRE
>CP029843.1|AWV07645.1|2431675_2435287_-|type-IV-secretion-protein-Rhs
MVVAYQPRLTRIQERSADGVLTGYWIAFEYSESTGRLTRAVASDGRQVTYGHDEFEGATRGNLRTVAGLDDYVQGFAYTDPVDPHRLTAIVKNEGAAPVVNTYNAAGQVIRQVEGGSTFELDYSTPGRNVTTEIVTDASGAELQRRVRTREFDEAGYLTRKVDAAGHEERYIYNAGKDRIRTETWEKQADGSLVLLKAVDNTYNGQAQKLTESVTLASGEVVTATWTYDHGWIASEQKASTASPQVFRTEYEFVRDAQGVPINIAAVKRRNDDGSFATTSYSYCSASEAAAPGSTCPDTALLKTVDGPRTDVSDLTTYVYYGTTDVSGCGSASGPCQRRGDLKQVTNALGQSMDYLRYDGAGRAVQVRDANGVITDMVYHPRGWLLEQAVRGPDDAVTTDDAITSYQYDSRGNVISQTRPDGSFLEFEYDDRDRLTVTRDPDGNEVRYTLDSIGNRWKEETFAADGTRVRTLSREFDMLDRIARQLDAQNHTTVLVYDGRGRQTQITDALGRRAEQSYDALDRLKQSITDADGLQVGTSFHYDAAGNLRQVVDPKGLATSYQYDALGQLLQLDSPDTGTTIYTYDPAGNHNSQTDARGETSTYGHDALNRLSSVSYSDSSLDAAYAYDSVQPGCATGETFAIGRLSRMSDGSGHTDYCYDRFGQLVRKIQVTNGQSFTLRYAYTQAGQLSLMTYPDGTEVDYVRDGQGRTSEIGVTAPGGSREVLLSNASWYPSGPVGAWTFGNGRTLSRTLDLDYRPQSILSTDTGSPTSGGGLDLGFRFDAVGNLTSLHGADRADPPRVRLDYDALSRLTAFRDGPTDTAIESYGYDATGNRTSFTNAGGTQAYSYPTDSHRLGAVAGVARGYDAVGNTTAIGGTKEYVYSAANRLSAVKQGGAVTMHYGYNGSGERVHRHLGSDVTYSVYDEAGHWVGDYDASGAPKQQAIWLDDLPVGLLNGIAATANRLHYIEPDHLGTPRAVIEPQRDVAVWTWDIASEAFGNSAPNQDPDGDSTAFTLDMRFPGQRYDAASGLNYNYFRDYEAGTGRYSQSDPIGLLGGIGTYNYALAQPVQVHDRLGLNPATIGTAVVLGAIQGCAGGCAGAIVGDYTSCVIEKRRAGGKNLGQCSDECTPNPCDALRSCVSGCIAGAVLGGVTAGQGVALSPVAGYLLRNYFRFLFSPDFCQKYGIPAPPDPIPLPLPDWLRNL
>CP029843.1|AWV07644.1|2429609_2430704_+|ribonuclease-D
MPAPITDPAALQARLSPRPRRIGLDTEFIRERTYWPQLALVQISIETEDGLEVVLADPLAPGIAETLAPILADPAILKIMHSPSEDLVAFKHACNTVPAPLFDTQLAAALAGIGSGLGYQKLVEQLTGVTLAKGETRSDWLRRPLSAAQLEYAADDVRHLFELHDVLDHRLGELGRRDWLAEDATRTVTQADSDTPERWPHLAMRSAQFLDLDAQRRLLRLLRWRETHARQSDRPKSWILDNELAGTLARNPPIDLAGLQREFDSHPKAPRKLAATVWEVLNAPLDDEAEIPDASVAERRDRNRLRKLQAAVAARSAELGLPDGVLASRRWLEALLDHGRWPDALAGWRREALEPSLAPLLAES
>CP029843.1|AWV07643.1|2427412_2429323_-|hypothetical-protein
MLLLAVLAGCSREPAQEDAGTTSAAAGEQAAPSVTVSADQALETMPDWQAPAVSLTDENIEALLAQADEALQAGRLYEDDESAIPIYLALKAGAEQASEAADGTEPTEATETAQAVDAAERSDTETAEKAEAGLQRALTALLAQGDAALESIDDAPEALQRAQQIGAVARAVAADADPVVAYLERVELMERVQQANVAGERALAAGRIDSGKDAALPHFRHALELREADARALQGLAASESALIREAEQAAEAYDYDKAEAGLARAAKVRSGDDTVAHARERIAAMRVERIGDLRDQGIAALSREDGLDTAREHLAELLRIAPKGDPAAIELRERIELATHYGLFRPGQVFTDALKNGGRGPQMVVVPHGAFTMGAADDEAGASDSERPTRNIRFDRGLAFARTEVTVAEFRRYLEATGNEPRAVRRGYSTAYDERSGNLVRRSGADPDDGYTGERADDDMPVIHVSAADAAAYARWLSEQTGHVYRLPSEAEFEYALRAGSQDRFPWGEGTPPAGSGNFTGGEDVSPSGRRWRNAFEGYGDGAWGPAAVASYRANAFGLHDMAGNVSEWVADCWHDNYRRAPRDAHAWVNPGCREKVVRGGSWASSPEQTRSAWRLSVRGDTTNARVGFRVVREI
>CP029843.1|AWV07642.1|2426441_2427338_-|peptidase
MGRGGRGGGRRGGKFRWWILLLFAGYAAWQWFGSAEVDPYTGETAHYGASADEEVQLGAQAFRQVLGDANAQGALLPADAQLTQQIRSIAQRLVAKVPQVTADLAAMHNQAVPTSHQGFLWDVAVIQSDEANAFCLPGGKMAVYTGLIPVAQNENAVAVVMGHEIAHALLRHGSQRMAQQKLVQMGQVATGMAVGDMAPQQQQAIMAALGAGAQYGLILPYGRNHETQADRVGLMLAAAACYDPAEAVPLWQRMGQLGGGQRPPEFASTHPDPANRIAELQALMPQAEAFRQKYCGGQ
>CP029843.1|AWV07641.1|2425518_2426019_+|polyhydroxyalkanoate-synthesis-repressor-PhaR
MAATRVIKKYPNRRLYDTEISSYITIEDVRQLIVDGESFEVRDARSGEDLTRQVLLQIIAEQEQDGEPVLSTQLLSQIIRFYGDSLQGFMGNYLERSMQLFLDQQQQFRKQMGGLMGETPWAMMNQLTERNLAMWKEFQQNLSGSVGQTPTSPRPGNKNEGGKRGR
>CP029843.1|AWV07640.1|2424403_2425144_+|3-ketoacyl-ACP-reductase
MQSRVALVTGGTGGIGTSIIKRLAAAGHKVATNYRDEGRARAWQEKMKAEGVDVAMAQGDVTSPEQAEAMVRDIERQLGPIEILVNNAGITRDTTFHRMKPDQWNDVICTNLNSVYNVTRPVIEGMRERKWGRIIQISSINGLKGQYGQANYAAAKAGMHGFTISLARENARLGITVNTISPGYVATDMVMAVPEEVRAKIVADIPTGRLGEPDEIAYAVAFLTDDQAGWITGSNLDINGGHHMGW
>CP029843.1|AWV07639.1|2423411_2424329_+|glutamyl-Q-tRNA(Asp)-ligase
MPAPASDRPAPDPANRANPPYRGRFAPSPTGDLHAGSLLAAFGSWLLARHAGGEWWLRVEDLDPPREVAGAAQRQLTALREFGFVPDAPVVFQSRRHDLYRNALERLLDSGAAFECHCSRSDLAASGGIHRRCVARRRRPQPAVRLRVADGSIVAFEDAIQGRHVQDVAATVGDFVLRRADGLWAYQLAVVVDDAAQAITDVVRGADLLDSTPRQILLQRALDLPTPGYAHLPLVTDVHGRKLSKSDAAWPLDAADPLPALRRAWAALGQPGDALAGADLPASLLATARTAFQPHLIPPTLSATD
>CP029843.1|AWV07638.1|2422421_2423333_-|protease-HtpX
MFKRVALFLATNLAVLALISIVLAVLEKFFGINIGTGSNTGLLVFALLFGFGGSFISLMTSKWMAKRGTGAHVIEQPRNEAEQWLVNTVRRQAEAAGIKMPEVAIYDAPEINAFATGPSRNNSLVAVSTGLLRAMSRDEAEAVLGHEVSHVANGDMVTMALIQGVLNTFVIVLARVVGRVIDGYLSGGRDGPGIGYYVIVFVLDMVFGLFASMIAMWFSRYREFRADAGGARLAGRDKMVAALERLSVTYGESTLPKQVAAFGISGGVAHGLRQLLMSHPPLAERIQALRNAPAEPVGGRVAG
>CP029843.1|AWV07648.1|2445125_2445809_-|hypothetical-protein
MVFAAVLLAPVVVWLVSVGNPLDYLDHTLPPGQALYVTSKFAALLALSCFWAQCLLALARRTPVLNGIPPAPLKLHRRLGCATLVLVLAHVGLFFVAASLRGGVPAWSLLLPNFGQGYYNAFVSLGLLAFWCLLLVAYAGWRVSRGRQRWKLVHMLWFVVFTLVFLHAYAIGSESRFGAMRYVLLFVATSLVAASWSRLRVAMKGRRPAIEQPAGVALEQVRERERV
>CP029843.1|AWV07649.1|2447076_2448714_-|hypothetical-protein
MAALAAPPVRARASAAPVLLAGGQGRPPAPWIRSAVREVLERAPNYRHLSADDRRTLAGAMVRVSALAAELIDEEGQAQQAIERQGGDSTPVGVSQGPRRPAPLARAQSQPGFAAAADRVAGTTQAVLNAVSFPRFVTDLINGVFRAMLDSSTQQMQQYVQLLNAVSASAEGFERTQFGLAQVRQWVADHFPESVEYETPDPDFDDPEDPVETRLRLRDGASMPEEEAIRATLGMEPGESVDAGNPEQLVPLARRYLARQRQQMLATMVMMGMHRIVIDSGRINAAMRFHVDTRSAASEDRGSQFSLQNRVRAAGRFGAGPWGVSAEVENNIGYVSTQRNQSTEEMNTDLELNSSVELNFRSDYLPLNRMAAQAQADRIRNASINPVAESDPIAARTERLQAQHESERARREAMDTAIGEAGQTSMADSPLEVPEPNSGSGRSGSGGSGSGGSSSGGSSSGGSSSGGSSSGGSSSGGSSSGGSGSGGSGSGGSGSGGSGSGGSGSGGSGSGGGGSGGGGSGGGGSGGGGSGGGGSGGGGSGGSGG
>CP029843.1|AWV07650.1|2448715_2449630_-|hypothetical-protein
MRLAPPPADVCLYPGHEHAGLLRSLSLAMSVLGERKALALALSGTGFDELGAIDLPPGPAGGLDRVRLRAAAPLYFAAKLEDAGLLPTAELIAGLFASGAITQPIGPVARMINDFWRARRERLSADERAAIYARAVEPPYFDRLMAALCEAIVAQADGSDIRERVVLETAIDALVEFLSQRVDPMAAMAARDIVENINQALGFMRDRMLQAAFGVQSLWSLVAIAGDARGQGAGPVQRHVDLGRAGQTVLLWLAEHAGTSAPLLDPGDFELIGAAQRWLSGRIESGTATAPMDMPVLPALPAVA
>CP029843.1|AWV07651.1|2449643_2450891_-|hypothetical-protein
MSEPVPRATHNPAWLDDETLAAVRPQVRRLLQSSPGFRELPVAEQQELARNMVRVASYMSNPDGLAKQELTPGRGVLAKDEAPQGGLARALAGEVDAAKRKASEKVGTFAGSDFEAGSVEQGATNFRKYIGAVDFPAFVGGLIQNVFQAIVDASIQQMRAYGELLKSVSQTVDQFASDNISLNNARDWLVDRFAGDFRIETASDGFDEGGGPRVALVNEDNAQEVMGRVNQEMQMAKPITDLSDPEQEGRLAQAARMQMARSRQQLLSSMVILGINRIVITDGAINAKVVFDFRASDQAQRSAAASLYDRDTSYNRNTTVAGAHFGWGGAATANTNVQTHMTTVSSSVDEESESKQEMKAKLTGEVRVNFKSDYFPMEKLASPAMIAAIQGNSTPVDPNYIPSTRNAAGAGGSGG
>CP029843.1|AWV07652.1|2450929_2452237_-|hypothetical-protein
MAAPAGAAAAAPGASRETTDAVRRKVRQMLEQAQSFQDLAPDKREALAKGLVQIGSYLAEPDGIRLKPHQQSPQVRALAGDDSEPLPASDQPEFGTALKTGVQQAGALMQAVNFPEFVTGLIDGVFNSIVTSSIQQMEAYAKLVADVSKSLNQFRDDNTTQNQGRDHLVEQFPDIFQLQMGAGDWGDFGTFGDEQPSNEPRVVVRQDVDERRAIDRLNQSLPLDKPITRLDDELVEALLVPAARTQIATGRQQLLATLVMLGINRIVVTDGRISAKVMYDFQARDNLKYRHSATKMDHQRDAYGNIAKTRGYEGEYDRKYEGGSGSGEDRQDASWYSKGNYKYTEQPIIKMMSTSQLQNDASLQARASLAGQVEVNFKSDYLPLEKMANPEAIAAIQMNAQPGMVKTMAGRPQPTPPGTAPATGEAPANTPAATP
>CP029843.1|AWV07653.1|2452430_2453486_-|hypothetical-protein
MNKPISHIGKRPMAAHVKRSLSSAARALGTRDPLPYLDSLIDRTFSLPEDDVAYTRNALTPGAVPYEPSFSEAEPGTLRFTIEPLGPEASPVARRDEATREMRRLVCPVFGRDALRWFDSRSEEWRGFGGLGWMSYGAWFGSAFDEDGLYATKIYYELLPSQIDALAAPLARLTRQAMNEMPSLMPIFTSIGCNREAGSQRVTFLHRGPLVVAALGPLMNRLGIGHQLPSLMRIVGVALGGRFELPSGGVLIGMRNTPGGVEMKLEILLASLPDLPSRFLDLLKLGLAERPRQLAALARWLEAFGMDAGEHGHFSVLSIRVTPNSPARISLYVRPIEFEMREQLEEARALQ
>CP029843.1|AWV07654.1|2453532_2455647_-|hypothetical-protein
MKRILLVDLGERELKKRQELRARQQVLETIDKTAETSGGLSSKQLEELTRIRKQLGSDVVIDPFYRLVAATHQQRDWSELRRDNSFVHEYGLLGSQRMIGNLLDPLEKNEREIASICGLLQIDGYTDAARPDFVQKISSAQGEYRRHRALFDAVFAHLGQRYEVSLKSQIDAGLVDPAIVGCVDPGGDPQSRTEMLDHATAKRAAINAAQGAATRAADAERAAQAAKESAQALARVVKEKQAELDAAQAAHPRGGKEVTAAKRALTVATKAADTAAEQAKAAAIVAKEALATAKEAKAEASDASVAASIRASLAAFEPSPAETICALSGRNVAAVVRRLATEKVSANDAWLASRIQNAYDMDTGVVAGAPPSSMEIMLPDLDESTDVEIVRENLHAVQAIYFSWMLEEMHLPQVVERIVELFRAGLLPLGRGKAGDYLFNYYKRAVDRITEGERRDLYMRVFGAPGGDPNGNQPNREFNDLWLRFVSAVSSFARQLTVDRLLRSNIPVAVSQEQVRKAGRDLAANLSLHGYGIAYFAATELQSMIREYLEKLNDPELRTAFGARDIWQVIDQVNANYLGGPRNTHRYRTQAHAGAVIIRWLANHHQRLGGRFGEVISLAALTNPQLRGSDRPTVEPNDWDLVQACEQWLAVGGVQDDHVEQFAQPVESPVITSKPIEMPAFAREALDSLTGGIGDSLNGALPPL
>CP029843.1|AWV07655.1|2455831_2457298_-|hypothetical-protein
MNMRRAMPAVRGRLLLTLRLGEVPEHVPGLRAVIGYGTDKAEHIDGGVIDRLLRHHGGAFRVTRLHSARKRRVERPVPGARRFDDVEQISGVARVLRIEVRDPDAVPALLQALAEVPVVERVCADHLCHGPFAADGGGGDNPVDPHTVSDPLWARELIRLPEALAYEPGDPATVIGLADTGVALEHQELQARLRAGFDSVDLDPELVGGLTLVGDYRHRGEQPQDEVGHGTGCAGILAARGRDIPPGGAGACGLTPVRVLGAALGPGERRFGVGALDNIDAGMKRLIDLNVKVINMSFGTPESALATDAPRPHEEVIRYALARGVILVAASGNSGLEERYYPAAHEGVIAVGAVDRQRRPAGFSTRGGHVAVCAPGNGILTCGLHGYQAATGTSFAAPFAAAACALLASRAQRRAWPLDSDDARELLVESATPFGRAGVGGCGRGVLDAAAALRLLDRRIDRDIAAEAASADDDLEPVSEPRTAPVAA
>CP029843.1|AWV07656.1|2457294_2458068_-|hypothetical-protein
MSAQIPPLVRDSGIPFDLFIQALTEQLDKAQAAMAIKARVGKLPLTFAVKEVSMDLRAFVQMVDEDVFLRPAGPGESEASTIKLALTTITKPMIEENAVDFKAEDPKFSLREALGDRITEDEQRRLERIGVRTVTQLNELKKTAGADVIARLSRMPVNRLQQALLSAAAPRVTRVEPGANGQATRRVHLSTPGLRGGRLPLVRAAGEAVPVVESGDDAIVLAPLAHQLGCEAELDFGEGEVARVELSEGRLGQWEAP
>CP029843.1|AWV07657.1|2458064_2458355_-|hypothetical-protein
MLRELSQLLEELHDGLLAVETRGGVQLAGAEMTLPLELRPVLQDGGCVLLADVPRSRGSGDWLIAPSRLRLAWGDAAADAEDEATGNVQVSTEAWP

Crispr_ID: CP029843_4

• CRISPR_ID: CP029843_4
• CRISPR_location: 3712291-3712457
• CRISPR_type: Orphan
• Repeat_type: NA
• Spacer_info: 1 spacers

Consensus repeat of CP029843_4

Consensus_repeat	Method
CCCGGGCTTTCCCATGAAGGCCCCATCGCGGCTTACGCCGCTCCTACGAAAGGCA	CRISPRCasFinder

spacers of CP029843_4

>4.1|3712346|57|CP029843|CRISPRCasFinder
TCAGCGCACGCATCGGCATGCCGCAGGATTGACTTGTAGGAGCTGCGTGAGCTGCGA

CRISPR arrays and Neighbor proteins around CP029843_4

CRISPR arrays

The CRISPR arrays of CP029843_4

>merge|CP029843|4|3712291-3712457|CRISPRCasFinder
CCCGGGCTTTCCCATGAAGGCCCCATCGCGGCTTACGCCGCTCCTACGAAAGGCATCAGCGCACGCATCGGCATGCCGCAGGATTGACTTGTAGGAGCTGCGTGAGCTGCGACCCGGGCTCTCCCATGAAGGCCCCATCGCGGCTTACGCCGCTCCTACGAAAGGCA

>CP029843|4|4|3712291-3712457|CRISPRCasFinder
CCCGGGCTTTCCCATGAAGGCCCCATCGCGGCTTACGCCGCTCCTACGAAAGGCA	TCAGCGCACGCATCGGCATGCCGCAGGATTGACTTGTAGGAGCTGCGTGAGCTGCGA
CCCGGGCTCTCCCATGAAGGCCCCATCGCGGCTTACGCCGCTCCTACGAAAGGCA

Neighbor Proteins Overview

Protein	Signature genes	Signature genes Name	Protein_function
CP029843.1|AWV08646.1|3725796_3726486_+|methyltransferase	unknown	unknown	gnl|CDD|379312
CP029843.1|AWV08631.1|3704529_3707235_-|pyruvate-dehydrogenase	unknown	unknown	gnl|CDD|236500
CP029843.1|AWV08640.1|3717736_3718339_+|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV08643.1|3722382_3723582_-|GTPase-RsgA	unknown	unknown	gnl|CDD|234988
CP029843.1|AWV08629.1|3699504_3699822_+|putative-transcriptional-repressor-protein	unknown	unknown	gnl|CDD|238045
CP029843.1|AWV08634.1|3710330_3710720_+|anti-sigma-F-factor-antagonist	unknown	unknown	gnl|CDD|132914
CP029843.1|AWV08642.1|3719510_3722045_-|hypothetical-protein	unknown	unknown	gnl|CDD|366183
CP029843.1|AWV08638.1|3714944_3716348_+|hypothetical-protein	unknown	unknown	unknown
CP029843.1|AWV08630.1|3699927_3700866_+|hypothetical-protein	unknown	unknown	gnl|CDD|379157
CP029843.1|AWV08639.1|3716344_3717616_-|hypothetical-protein	unknown	unknown	gnl|CDD|369651
CP029843.1|AWV08627.1|3696949_3698062_-|addiction-module-protein	unknown	unknown	gnl|CDD|225718
CP029843.1|AWV08645.1|3725022_3725787_+|lysophospholipase	unknown	unknown	gnl|CDD|238870
CP029843.1|AWV08633.1|3709899_3710331_+|hypothetical-protein	unknown	unknown	gnl|CDD|379279
CP029843.1|AWV08637.1|3712474_3714769_-|malic-enzyme	unknown	unknown	gnl|CDD|235976
CP029843.1|AWV08636.1|3711883_3712246_+|transposase	unknown	unknown	gnl|CDD|224854
CP029843.1|AWV08635.1|3710749_3711148_+|hypothetical-protein	unknown	unknown	gnl|CDD|132914
CP029843.1|AWV08641.1|3718354_3719509_-|cytochrome-C-peroxidase	unknown	unknown	gnl|CDD|224771
CP029843.1|AWV08644.1|3723794_3725054_+|aminotransferase	unknown	unknown	gnl|CDD|181738
CP029843.1|AWV08628.1|3699119_3699419_-|DUF2339-domain-containing-protein	unknown	unknown	unknown
CP029843.1|AWV08632.1|3708013_3709906_+|hypothetical-protein	unknown	unknown	gnl|CDD|369272

rpsblast for functional proteins

Protein	Function_ID	Function_description	E-value
CP029843.1|AWV08646.1|3725796_3726486_+|methyltransferase	gnl|CDD|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	3.27452e-08
CP029843.1|AWV08631.1|3704529_3707235_-|pyruvate-dehydrogenase	gnl|CDD|236500	PRK09405, aceE, pyruvate dehydrogenase subunit E1; Reviewed.	0
CP029843.1|AWV08643.1|3722382_3723582_-|GTPase-RsgA	gnl|CDD|234988	PRK01889, PRK01889, GTPase RsgA; Reviewed.	2.04608e-153
CP029843.1|AWV08629.1|3699504_3699822_+|putative-transcriptional-repressor-protein	gnl|CDD|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	3.85039e-14
CP029843.1|AWV08634.1|3710330_3710720_+|anti-sigma-F-factor-antagonist	gnl|CDD|132914	cd07043, STAS_anti-anti-sigma_factors, Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation. Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.	1.64634e-21
CP029843.1|AWV08645.1|3725022_3725787_+|lysophospholipase	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.	1.95831e-31
CP029843.1|AWV08630.1|3699927_3700866_+|hypothetical-protein	gnl|CDD|379157	pfam13391, HNH_2, HNH endonuclease.	7.75454e-12
CP029843.1|AWV08639.1|3716344_3717616_-|hypothetical-protein	gnl|CDD|369651	pfam08014, DUF1704, Domain of unknown function (DUF1704). This family contains many hypothetical proteins.	1.82084e-143
CP029843.1|AWV08627.1|3696949_3698062_-|addiction-module-protein	gnl|CDD|225718	COG3177, COG3177, Fic family protein [Function unknown].	1.1138e-52
CP029843.1|AWV08633.1|3709899_3710331_+|hypothetical-protein	gnl|CDD|379279	pfam13581, HATPase_c_2, Histidine kinase-like ATPase domain.	1.43298e-25
CP029843.1|AWV08637.1|3712474_3714769_-|malic-enzyme	gnl|CDD|235976	PRK07232, PRK07232, bifunctional malic enzyme oxidoreductase/phosphotransacetylase; Reviewed.	0
CP029843.1|AWV08636.1|3711883_3712246_+|transposase	gnl|CDD|224854	COG1943, COG1943, Transposase and inactivated derivatives [DNA replication, recombination, and repair].	1.81368e-12
CP029843.1|AWV08635.1|3710749_3711148_+|hypothetical-protein	gnl|CDD|132914	cd07043, STAS_anti-anti-sigma_factors, Sulphate Transporter and Anti-Sigma factor antagonist) domain of anti-anti-sigma factors, key regulators of anti-sigma factors by phosphorylation. Anti-anti-sigma factors play an important role in the regulation of several sigma factors and their corresponding anti-sigma factors. Upon dephosphorylation they bind the anti-sigma factor and induce the release of the sigma factor from the anti-sigma factor. In a feedback mechanism the anti-anti-sigma factor can be inactivated via phosphorylation by the anti-sigma factor. Well studied examples from Bacillus subtilis are SpoIIAA (regulating sigmaF and sigmaC which play an important role in sporulation) and RsbV (regulating sigmaB involved in the general stress response). The STAS domain is also found in the C- terminal region of sulphate transporters and stressosomes.	8.59011e-24
CP029843.1|AWV08641.1|3718354_3719509_-|cytochrome-C-peroxidase	gnl|CDD|224771	COG1858, MauG, Cytochrome c peroxidase [Inorganic ion transport and metabolism].	8.14746e-80
CP029843.1|AWV08644.1|3723794_3725054_+|aminotransferase	gnl|CDD|181738	PRK09265, PRK09265, aminotransferase AlaT; Validated.	0
CP029843.1|AWV08642.1|3719510_3722045_-|hypothetical-protein	gnl|CDD|366183	pfam00593, TonB_dep_Rec, TonB dependent receptor. This model now only covers the conserved part of the barrel structure.	1.59551e-09
CP029843.1|AWV08632.1|3708013_3709906_+|hypothetical-protein	gnl|CDD|369272	pfam07228, SpoIIE, Stage II sporulation protein E (SpoIIE). This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.	6.37171e-47

Protein sequences

>CP029843.1|AWV08636.1|3711883_3712246_+|transposase
MFADPARAMTAARALVDPRCWTRSHLLAWVLMPDHWHGLVALGEDDALPALIRRIKTSTARCVRRDQRHAGPVWARAYHDHALRKEEDLLGAARYLVMNPVRAGLVRRCGWYPYWDAVWL
>CP029843.1|AWV08635.1|3710749_3711148_+|hypothetical-protein
MLQIETYPPVNGNQYLRLSGRLDTHTHVELETALAPLLDAGPRALVLDIAHLEYISSAGIRTLLRARKALAPEGGQVLLLHPPPQIRKVIDLARAVPLEAVFDTRHEADAYLDRIQQGVLDGDLDMPDDGTP
>CP029843.1|AWV08634.1|3710330_3710720_+|anti-sigma-F-factor-antagonist
MSLNIDIQPAAASQRVALGGRLDTHTHAELDAALTPLLADPSITTLVLDLSGLEYISSAGIRSVFRARKALATRSGKVLVANPQPQIKKVFDMVKAVPMNSIFASVEEADAYLDAMQRKVLQGADEDED
>CP029843.1|AWV08633.1|3709899_3710331_+|hypothetical-protein
MLIRLIVPGELARVEDLNASLEAVLKLHGIDAELCADVRLIVEELASNVIKYGGDPEGVPRHELSVHIAIAGELLRLEFRDTGAPFDPTQAPPPDLDGDILERDVGGLGVHLIRSLAESVSYRREEPYNLLDLSLRMNQKESA
>CP029843.1|AWV08632.1|3708013_3709906_+|hypothetical-protein
MVSVTVVVLMTAAMAGYTHWRIDQEARLTTLANGQQMAEHLDTMMDTVAVTAGALSELAADSPLDPRDLTETLRALVEATPGCAGGLLALEADGGREAYTRYVSLDRPDRDFIADGYDYRTRAWFQRTLSERAGWWSEPYFNETAGGVWMVTYNAPLRRRGRSGEALGMVSLDLPLTALTDPLQTLAHLPGWQVWLVAPEGTVAMGPDASADAGQRSLDVHVADTGRGDLAPLAAAAGEHRHLLLSHTNQRSGEDLLSVIGPVGDSGWSVLVSQSHALIEARLNQALALLAAGGLVLALLCTLLVGRLARRIAQPVQRLSDSAARLADGDYTTPVPDLHRGDEVGVMARTLEHARSSIQRQLVEIEEMGAARQKLESELSIARDIQLAMLPPGRVIDRADHHLEAYAQLEPAKAVGGDFYSFVELGNNDLWFAIGDVSDKGVPAALFMARTTTVLEAAARGGGDPSQVLAAASRRLVEGNDTCMFATVLCGRINVRSGDCVLASAGHDPPVCLHPDGRIETLPVETGGPLGFEPAEAFPLWRCRLEPGMTLLAYTDGVTEAFDAGNVAFGMEGLIASVRAHRDARGQCERLIAEVHAFAQPAAQDDITVLAIRLRLDPTPETPMEASNAC
>CP029843.1|AWV08631.1|3704529_3707235_-|pyruvate-dehydrogenase
MTQTYESPFADLLQNDPDPAETQEWVESVQAVIAHDGAERAHQLLQGMVEVTRRAGAHLPFSPTTEYINTIPPHLEPKTPGDQTMEWRIRSLIRWNAMAMVVRANRKPGDLGGHIASFASAATLYDVGFNHFWRGPEGDHPGDLIGVQGHSSPGIYARSFLEGRISESQLDHFRMEVDGRGISSYPHPWLMPDYWQLPTVSMGLGPIASIYQARNWKYLEGRGLIPKSDRKVWCFMGDGECDEPESLGAISVAGREGLDNLVFVINCNLQRLDGPVRGNGKIIQELEGQFRGAGWNVIKTIWGSYWDPLLARDTSGKLRQLMMETVDGEYQNCKAFGGAYTREHFFGKYPETARLVANLSDEDIWRLNRGGHDPHKVYAAYDAATKMKGMPTVILAKTVKGYGMGSAGESLNPTHQTKKLDDEAVRAFRDRFNIPVTDKQLADGQVPFFHPGKDSEEVQYMLERRKSLGGFLPQRRRQASQSLEVPKLEAYERLLKATGDREISTTMAFVQTLNITLRDKQVGPRCVPIVADEARTFGMEGLFRQLGIYAPQGQKYKPVDRDQLMYYREDAAGQVLEEGITEAGAFASWMAAATSYSTNDLQMLPFYIFYSMFGFQRIGDSAWQAADMRARGFLLGATAGRTTLNGEGLQHEDGHSHLLAGAVPNCRSYDPTFGYEVTVIVQHGMQRMLAEQRDEYYYITLMNENYTHPEMPEGSADGIIKGMYLLKDAGKPKKGELRVQLMGSGTILREAIAAAELLDKDFGVTADIWSCPSFNELRRDGVDAERWNRLNPEAKTPRKPYVTELLDGRQGPAIAATDYVRAFADQIREYVPMRYTVLGTDGFGRSDTRANLRRHFEVDRFHIAHAAIAALAADGKMSAKDVTRAIKEYKIDVEKPNPIGV
>CP029843.1|AWV08630.1|3699927_3700866_+|hypothetical-protein
MAFWWVNHKQTRDHEVRGGYLWSPKRNANGAFNQTYENMRLVRPGDIVFSYANGQIGAIGQVIETVSASPKPSEFGHVGDYWSDEGWLVSVYFNDAPKPLRPKAHIERIAPLLPTKYSPIQKTGDGNQGCYLAGISDALGHILLALLGVEAPPVFSPMLAVAEPNAEVLEDLHLVESDTTIPETQRLQLTKARIGQGLFRNRVMSLDPRCRVTGVEDSRLLVASHIKPWRDSSNAERINGFNGIMLSPHIDALFDERLITFEDDGRMRMHPSLSKDVLERWSISPSTKVDRFGPEQAAFLSHHRKAFAARLG
>CP029843.1|AWV08629.1|3699504_3699822_+|putative-transcriptional-repressor-protein
MATKPPTPRETFARRLRAERLKAGLSQRELGRRIGLSEDVVSSRITRYEKGTSEPDFETARQLADALGVPLAYLLADSDTLAEIVRAAAGLSLAKQRKLLADIKT
>CP029843.1|AWV08628.1|3699119_3699419_-|DUF2339-domain-containing-protein
MKMRAALSDHEEFIASGAEVDPTAPATGYLLPEDAYRTLEQARDRLDLLARLAAPRDPQDDAPEAELPLRIAALAQCFEELADQLDRGLRAARWSKSLP
>CP029843.1|AWV08627.1|3696949_3698062_-|addiction-module-protein
MSFDPRRPYNTLPELPPAAEIESKPVLKACIEARAALAELKAVGGLIPSQAVLINTIPLLEAQASSEIENIVTTSDALFRFSQMEERADDRATKEALRYRGALHRGFQSIRERPLNTNTAVMVCSWIKGGDMQIRRVSGTALSNAATGEVIYTPPEGEALLREKLANWERFIHEATTVDPLVRMAVAHYQFEAIHPFLDGNGRTGRVLNLLMLVELGLLDQPVLYLSRHILRNRPEYYARLQAVTRDGAWEAWIGFMLAAVTDTARWTTAKVRAIRQLQAEATAFVKARAGKIHSRELVDVLFEQPYCRIQNLVEAGVAKRQTASVYLKQLVDIGMLREVRMGREKLFIHPGFVRLLTSDEHPVSAYGQD
>CP029843.1|AWV08637.1|3712474_3714769_-|malic-enzyme
MSDNDAFKQAALDYHRLSPAGKIKVTATKPMVTQRDLALAYSPGVAYACEAIAVDPNTARDYTARGNLVAVVSNGTAVLGLGDIGALAGKPVMEGKGVLFQKFAGIDVFDIEVDERDPDKLVDIIASLEPTFGGINLEDIKAPECFIVERKLRERMKIPVFHDDQHGTAIIVGAAVLNALEVAGKDIENVRVATTGAGAAGIACLDMLVALGVKKEHITAFDREGVIYSGRPNLDPDKARYASDTDKRSLEEIVEGADLFLGLSAGGILKPEMVAKMADKPIILALANPYPEILPEDAKKVRPDCIIATGRSDYPNQVNNALCFPYIFRGALDVGATVINEDMKLACVRAIARLARMEAGDLGSAYGGDVPTFGAEYLIPRPFDPRLLVMLAPAVALAAMKSGVATRPLDDVEAYVEQLGQFIHRTGLVMKPVYDRARSDRKRVVYAEGEEETVLRAVQTVVDERLAYPVLIGRPEVIQARIERLGLRMREGADYELTNINDDPRFNDYWQQYHALTERRGVTPAAAKNLLRSRPTLIASLMVERGEADAMICGLVGRFHKKLGYLRSVFDFERGVTGTAAMTGVINDKGVWFFLDTHVQVDPPAEQIAEATLQATYRLKLFGVEPRVALLSHSNFGSHDNPSAAKMRKVREILAQRMPKLVVDGEMMADTAWDEDLRKRIFPNTTLEGRPNLFVMPNLDAANITYNMIRMMTEGVALGPILMGLDKPAHILTPNSTSRRVVNMTAIAAVDAQIRAAREAGHKA
>CP029843.1|AWV08638.1|3714944_3716348_+|hypothetical-protein
MARPPTSTPPIPAWLLPAAALLAFLAQWPLVANPGYFSHDELQWAARAWSADGGPLPWMAWTDPGVFQYRPLTFNLWLWLSRHLFDTPMAFHAVLVAMGALNTALLAGLLRRLGAAPAMALIGALGFALGPYATYVHGWVGTIGDLLWVAMALACGWVCSTSSSTLPGARRPRQAAVAIGCALLTAIGLLAKEAALSIPALLAVAALLDRERPGWRWGLLGSALPAAAYLALRIGVLGAAGEGSGAYAWSIERIPVRALEYFVFLPQFGAFETLSALVRGFADPSVWVAIALWLVVLAALARTGWRAPAALVGGGLAALGPVLVLPTAYNQYGYGFAAVVAGVFALAWPRLPRWGRAATGLLAVLVLWHGIHVMRWMHRVGEVQAVFTPALVEAVRDRDPARPLRLRVAADAKAWMFMRLTHEIPHVRGEPIGGRVVLVDGDVEGDAAADAVVRADGRIEPLPAPDR
>CP029843.1|AWV08639.1|3716344_3717616_-|hypothetical-protein
MKGTSADDLAIAHHAALDARMVQAARGIRLLTLTSWPAGQEQRFLEEHATGRLALPRIEYPRHDFAEVRAELEAVAAEADPDHPLGQYLRESAHSWGIAAQLLESLGTPAVTAHSVRLFGRPDEALPGDGPSAREAAQHFISIADELDRELMAPAEHITVSATALQLQLQRELDNFFGERVIEVELDPELISKAAAGATRIRLRSNAAFSDYDRDQLLQHEAFVHSLTAINGRQQPVLPSLGLSSPRSTETQEGLATFAEQITGSIDIGRMKRISLRIEAVDMALGGADFVEVFRYFLDAGQAAEESFASAQRVFRGVPVSGGCAFTKDTVYLRGLVSVHTFFRWALREQKLQLCRWLFAGKMTLADVQRFEPLFVDGVLEPARWMPHWITRANGLAGMLAFSLFANRIRLDAIAGGDEPLEL
>CP029843.1|AWV08640.1|3717736_3718339_+|hypothetical-protein
MTEPATPQPPLRSSSRLFEIVIGIGVLVISVVSVFVAVNANRTQERILAASVWPSLMFGTSNASTEGAPQITLDLLNRGTGPARVRWAELLYKDAPVRDSDTLLSLCCGVPANAADDPTLLSSGIQRRVIAPGEWINLVRYPQPDPVTPAWEALDRERHNVRLRACYCSVLDECWLLDSNRDDPEPVNQCPRTPGVLWGS
>CP029843.1|AWV08641.1|3718354_3719509_-|cytochrome-C-peroxidase
MRRVARSGSAAALLLLAGLAPVAVADADNAVQEGGDVCRQRIAPSAPSIDFACLREIYSRPIGEWPAPQVAEGAVWQELAPLPRRVPEPPDNPGTPEKVALGKALFEDPRLSGSGQIACASCHDRQLGWGDGRSVSFGHDRQAGRRNAMSVAMAAYAAPLFWDGRAGSLEAQALHPIQDRVEMAASLADVERRLNRDGAYRERFRQVFGERRIGIHRVAQALAAYQRSLVPRSNRFDRFLEGRRDLLSDRQLWGLHLFRTHGRCMSCHSGPALTDNRFHNLGLHFYGRSRQDLGRYEVTGDPADSGKFRTPSLRNVRRTGPYMHNGIFRDLRGVMNMYNAGMPRPRPRPGQEDDPLFPRPDPMLEPLDLHRSELEAITEFLQTL
>CP029843.1|AWV08642.1|3719510_3722045_-|hypothetical-protein
MAAGAHAAERVDDGAPASSESATDTSASRYLADPPTLDTITVVGQRLFPYQEGMVLNEGYIDDQVRGNGDIGTLLRINPNVQFDDSAAASSNRMGEIRPSDISINGGLYYQNLFRFDGATFNNDLDPSSDNPHHVADVPSSTQGIALDTELIGRLTVYDSNVPAGFGGFNGGVVDAQSRKAKDGFGGKVSLRMSRSAWNEMILPEGDEDSAGLSSRYTTQPNYDKYRLAAMLEGRTSRGLGWIANVQRTRSDIPLRGYSSGNVSPDDAFIKEQRRQNTSASLRLDWTGERVDLAASLTYAPTDERYFTQNAKNSYFDLKQGGPIASVRMSSGHGAWTLAQTLSHSDMESSRRVEPAVDYWKSWARSSEFDWGVNNSSFEGNWGNVDQRNRTSGYGLTLSREPMRWGGSEHALQLGLQYRDRLGTYHRLNDHYSYLSPSATTTCTTASGTVDTEACSLAPVYASTSGGLVAGQGQYFRTMNVYRAGHFEARVKEWSVFVEDDIRLGRWSLRAGLRVDGDDLMDKTTVAPRLALSWDMFGDRRTLLTAGANRYYGRSFFSYKLREGRENLQTTHTRTADTLEWTPSRQYTANNRFETLDIPYSDELNGGINQRWRGLDINLKYVRRDGHDEVLRQRVASDDDSGYYSSNVYQYVNAGRSRSDTYTLSIGPEKPWAWRGAATHWQFAFDHTDVRRNYSDYESSYTDGSYNRWVRYEGTLIRAYELPQSSYNRPWTARLSSQTRIARWGLLWSNFFRYRAGHTGLATVDTEPYQGEEIDVIRRYELPRTFTWDSTVEYTLPLAGDSEAYVRVEAQNVTNRRNPLSGAPGGVSYYEPGRSYWLELGYRF
>CP029843.1|AWV08643.1|3722382_3723582_-|GTPase-RsgA
MTATIADLQSIGWPVNGLRTGIDAATDAALPPGWARLLDAHPAARPARIVEQHRSGYMVAESPDTGDAPGNSYRAESLPEWTRPAQYRKGEVAPEERPAVGDWVLVEGEGGSARIVALLPRWSAIKRGAAGEHYRQQLIAANVDTVFVVSGLDDDFNPRRIERYLLLVSGTGDAAERSALEPVIVLTKADLAEAAEPGAVAAATQALRALGDPGLAVCALNARDRDAVATLSPWLRPGRTVVLVGSSGAGKSTLTNSLLGIERMKTGEVRGSDSRGRHTTTHRALIPLPSGACLIDTPGMRELKPTGEEDVAESFTDIEALAEQCRFRDCAHAREPGCAVRAAIEAGTLDAQRFANYLKLRDEVAGAAGKLADRLAQKAQTRVQSKAVNKRQTDKYGKR
>CP029843.1|AWV08644.1|3723794_3725054_+|aminotransferase
MPPSSLKTRERLSEVRYEIRGELARRARELEAQGRTLIKLNIGNPGAFGFRAPAHLQRAIVDGIDQTDPYTHQQGLPAAREAVAAHYRKRGTPNATPERVFLGNGVSELIDLSLRALLNPGDEVLLPSPDYPLWSAATILNDGRPVYYRCLPENGFLPDPDEIEALVSSRTRAIVLINPNNPTGANYPRELIERIVAVAARHGLLLLCDEIYDSILYDGAGFQPIAPLAGDVPCLSFGGLSKVHRACGWRVGWAVLSGDPLAIGEFHHAMDLLGALRLCANVPGQFAVEAALHGDNTIDALCAPDGRLYEARRAVIDSVAASRHLQLVAPAGALYAFPAVAGAAAEGFDDHRFALELLETENVLVVPGSSFNVPYRNHFRVTLLPQPDELREVFQRIERVLDRRADRDADGGSARAALG
>CP029843.1|AWV08645.1|3725022_3725787_+|lysophospholipase
MADRHVRRWAETALATARRAFGAGHPLVAALVTTALLAACAGPTRPKEPTMTPTPYLALGDSYTIGEAVAEDDRWPVRLAAALRDEGVALADPRIIATTGWTTDELAEALDAAEPLGEWGFVSLLIGVNNQYRGRSLDNYRSEFDALLVRAIGYAGGRADRVMVLSIPDWGVTPFGERDDRGVDAIGAEIDAFNAAARELCAARGVVFVDITPVSREHGAEPAMVAEDGLHPSASMYAEWTRVALPVARGLLAD
>CP029843.1|AWV08646.1|3725796_3726486_+|methyltransferase
MSDDARPLPSATARAIARAYRPAHPLGSYWDYFYVRGKLSSDPLYPGIVDALRGTSAPVLDLGCGLGLLAHALRDAGLALPYRGVDIDAGKIARAARAADRAGLDAGFARLDLAGGLPAHRGSVAVLDVLQFVPRQAHDGILDGAIAMLAPGAKLVIRTGFDDGGSRARVTRAVDVFSRVLGWMNAAPRHYPEREALCARLADAGLRVEVDSLSGDTPFNNWRVVAHAP

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NC_010335	Caulobacter sp. K31 plasmid pCAUL01, complete sequence	8545-8575	4	0.871
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NC_013857	Azospirillum sp. B510 plasmid pAB510c, complete sequence	319473-319503	6	0.806
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP029831	Azospirillum ramasamyi strain M2T2B2 plasmid unnamed7, complete sequence	472601-472631	6	0.806
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NZ_CP054620	Azospirillum oryzae strain KACC 14407 plasmid unnamed5, complete sequence	11430-11463	6	0.824
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP015867	Streptomyces parvulus strain 2297 plasmid pSPA1, complete sequence	96833-96863	7	0.774
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP024891	Rhodococcus ruber strain YYL plasmid pYYL1.2, complete sequence	16616-16646	7	0.774
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP024891	Rhodococcus ruber strain YYL plasmid pYYL1.2, complete sequence	47953-47983	7	0.774
CP029843_5	5.2|3839758|31|CP029843|CRISPRCasFinder	3839758-3839788	31	NZ_CP016620	Microvirga ossetica strain V5/3m plasmid unnamed4, complete sequence	363496-363526	7	0.774
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NZ_CP032322	Azospirillum brasilense strain MTCC4035 plasmid p1, complete sequence	140537-140570	7	0.794
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NZ_CP022367	Azospirillum sp. TSH58 plasmid TSH58_p02, complete sequence	1672511-1672544	7	0.794
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NC_013859	Azospirillum sp. B510 plasmid pAB510e, complete sequence	486591-486624	7	0.794
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NZ_CP032340	Azospirillum brasilense strain MTCC4038 plasmid p1, complete sequence	941346-941379	7	0.794
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NZ_CP032346	Azospirillum brasilense strain MTCC4039 plasmid p1, complete sequence	131982-132015	7	0.794
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NZ_CP012915	Azospirillum brasilense strain Sp 7 plasmid ABSP7_p1, complete sequence	1191027-1191060	7	0.794
CP029843_5	5.6|3839704|36|CP029843|CRT	3839704-3839739	36	NC_010335	Caulobacter sp. K31 plasmid pCAUL01, complete sequence	8540-8575	7	0.806
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP010990	Pseudonocardia sp. EC080625-04 plasmid pFRP1-1, complete sequence	139716-139746	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP012477	Arthrobacter sp. ERGS1:01 isolate water plasmid unnamed2, complete sequence	214931-214961	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP012182	Pseudonocardia sp. EC080610-09 plasmid pBCI2-1, complete sequence	584043-584073	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP013855	Pseudonocardia sp. HH130630-07 plasmid pLS2-1, complete sequence	121419-121449	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP012185	Pseudonocardia sp. EC080619-01 plasmid pBCI1-2, complete sequence	463366-463396	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP012186	Pseudonocardia sp. EC080619-01 plasmid pBCI1-1, complete sequence	44858-44888	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP022666	Rhizobium leguminosarum bv. viciae strain BIHB 1217 plasmid pPR1, complete sequence	72652-72682	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NC_013513	Paracoccus aminophilus strain JCM 7686 plasmid pAMI3, complete sequence	4945-4975	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP011667	Streptomyces sp. Mg1 plasmid pSMg1-3, complete sequence	153921-153951	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP015043	Rhodovulum sp. P5 plasmid pRGUI04, complete sequence	20288-20318	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	MG962366	Rhodococcus phage Finch, complete genome	14550-14580	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NC_011366	Rhizobium leguminosarum bv. trifolii WSM2304 plasmid pRLG202, complete sequence	24657-24687	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP007516	Rubrobacter radiotolerans strain RSPS-4 plasmid 2, complete sequence	128196-128226	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP033583	Streptomyces sp. ADI95-16 plasmid pADI95-16b, complete sequence	84886-84916	8	0.742
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	MH834603	Arthrobacter phage Bridgette, complete genome	12094-12124	8	0.742
CP029843_5	5.2|3839758|31|CP029843|CRISPRCasFinder	3839758-3839788	31	NZ_LN831789	Streptomyces leeuwenhoekii strain type strain (C34 = DSM 42122 = NRRL B-24963) plasmid pSLE2	1579-1609	8	0.742
CP029843_5	5.2|3839758|31|CP029843|CRISPRCasFinder	3839758-3839788	31	NZ_CP018075	Streptomyces venezuelae strain NRRL B-65442 plasmid, complete sequence	3428-3458	8	0.742
CP029843_5	5.2|3839758|31|CP029843|CRISPRCasFinder	3839758-3839788	31	NC_010851	Streptomyces sp. FR1 plasmid pFRL1, complete sequence	52501-52531	8	0.742
CP029843_5	5.3|3839812|31|CP029843|CRISPRCasFinder	3839812-3839842	31	NZ_AP022593	Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence	5382703-5382733	8	0.742
CP029843_5	5.4|3839866|34|CP029843|CRISPRCasFinder	3839866-3839899	34	NZ_LR134451	Tsukamurella tyrosinosolvens strain NCTC13231 plasmid 9, complete sequence	361119-361152	8	0.765
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NZ_CP034811	Paracoccus sp. Arc7-R13 plasmid unnamed1, complete sequence	70629-70662	8	0.765
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NZ_CP017076	Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence	1022249-1022282	8	0.765
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP049794	Ralstonia solanacearum strain 204 plasmid unnamed, complete sequence	1279998-1280028	9	0.71
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP049792	Ralstonia solanacearum strain 203 plasmid unnamed, complete sequence	1061474-1061504	9	0.71
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP052069	Ralstonia solanacearum strain FJAT91.F50 plasmid Plas1, complete sequence	631865-631895	9	0.71
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP016613	Ralstonia solanacearum FJAT-91 plasmid unnamed1, complete sequence	1999049-1999079	9	0.71
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP049790	Ralstonia solanacearum strain 202 plasmid unnamed, complete sequence	1391850-1391880	9	0.71
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP044425	Paracoccus pantotrophus strain DSM 2944 plasmid pPAN2, complete sequence	73766-73796	9	0.71
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP016915	Ralstonia solanacearum strain CQPS-1 plasmid unnamed, complete sequence	1988519-1988549	9	0.71
CP029843_5	5.1|3839704|31|CP029843|CRISPRCasFinder	3839704-3839734	31	NZ_CP017244	Rhizobium etli 8C-3 plasmid pRsp8C3c, complete sequence	1155626-1155656	9	0.71
CP029843_5	5.3|3839812|31|CP029843|CRISPRCasFinder	3839812-3839842	31	CP021131	Meiothermus taiwanensis strain WR-220 plasmid pMtWR-220, complete sequence	177521-177551	9	0.71
CP029843_5	5.5|3839923|34|CP029843|CRISPRCasFinder	3839923-3839956	34	NZ_CP014690	Gluconobacter albidus strain TMW2.1191 plasmid pGS1191_1, complete sequence	219221-219254	9	0.735
CP029843_5	5.3|3839812|31|CP029843|CRISPRCasFinder	3839812-3839842	31	NC_012520	Rhodococcus opacus B4 plasmid pROB01, complete sequence	525025-525055	10	0.677
CP029843_5	5.4|3839866|34|CP029843|CRISPRCasFinder	3839866-3839899	34	NZ_LR026982	Rhodoplanes piscinae isolate Rhod_plasmid plasmid 1, complete sequence	32389-32422	10	0.706
CP029843_5	5.6|3839704|36|CP029843|CRT	3839704-3839739	36	NZ_CP029831	Azospirillum ramasamyi strain M2T2B2 plasmid unnamed7, complete sequence	472596-472631	10	0.722
CP029843_5	5.6|3839704|36|CP029843|CRT	3839704-3839739	36	NC_013857	Azospirillum sp. B510 plasmid pAB510c, complete sequence	319473-319508	10	0.722

1. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NC_010335 (Caulobacter sp. K31 plasmid pCAUL01, complete sequence) position: , mismatch: 4, identity: 0.871

-accgccgaggccggccagcagtacggcgacc	CRISPR spacer
gatcggc-aggccggccagcagtacggcaacc	Protospacer
 *.** * ********************.***

2. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NC_013857 (Azospirillum sp. B510 plasmid pAB510c, complete sequence) position: , mismatch: 6, identity: 0.806

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cacgccgaggccggccagcagggcggcgccg	Protospacer
  ******************* .***** * 

3. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP029831 (Azospirillum ramasamyi strain M2T2B2 plasmid unnamed7, complete sequence) position: , mismatch: 6, identity: 0.806

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cacgccgaggccggccagcagggcggcgccg	Protospacer
  ******************* .***** * 

4. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NZ_CP054620 (Azospirillum oryzae strain KACC 14407 plasmid unnamed5, complete sequence) position: , mismatch: 6, identity: 0.824

-ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
ccgcgtc-gccgccagcgccgggtcgccggcgacc	Protospacer
 . **** ******** ******** ******** 

5. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP015867 (Streptomyces parvulus strain 2297 plasmid pSPA1, complete sequence) position: , mismatch: 7, identity: 0.774

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cgcggagaggccggccagccgtgcggcgaac	Protospacer
  **  ************* **.****** *

6. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP024891 (Rhodococcus ruber strain YYL plasmid pYYL1.2, complete sequence) position: , mismatch: 7, identity: 0.774

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
accgtcgaggccggccagctgtagcgccgct	Protospacer
****.************** ***  ** .*.

7. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP024891 (Rhodococcus ruber strain YYL plasmid pYYL1.2, complete sequence) position: , mismatch: 7, identity: 0.774

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
accgtcgaggccggccagctgtagcgccgct	Protospacer
****.************** ***  ** .*.

8. spacer 5.2|3839758|31|CP029843|CRISPRCasFinder matches to NZ_CP016620 (Microvirga ossetica strain V5/3m plasmid unnamed4, complete sequence) position: , mismatch: 7, identity: 0.774

cggatccacgagaacgcccgggtccgcgatg	CRISPR spacer
ggcaagcccgtgaacgcccgggtcggcgatg	Protospacer
 * *  * ** ************* ******

9. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NZ_CP032322 (Azospirillum brasilense strain MTCC4035 plasmid p1, complete sequence) position: , mismatch: 7, identity: 0.794

ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
ttcgtcggcagccagggccgcgtcgtcgaggccg	Protospacer
********* ********** *** .**. * **

10. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NZ_CP022367 (Azospirillum sp. TSH58 plasmid TSH58_p02, complete sequence) position: , mismatch: 7, identity: 0.794

ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
ttcgtcggcagccagggccgcgtcgtcgaggccg	Protospacer
********* ********** *** .**. * **

11. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NC_013859 (Azospirillum sp. B510 plasmid pAB510e, complete sequence) position: , mismatch: 7, identity: 0.794

-ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
ccgcgtctg-cgccagcgccgggtcgccggcgacc	Protospacer
 . **** * ****** ******** ******** 

12. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NZ_CP032340 (Azospirillum brasilense strain MTCC4038 plasmid p1, complete sequence) position: , mismatch: 7, identity: 0.794

ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
ttcgtcggcagccagggccgcgtcgtcgaggccg	Protospacer
********* ********** *** .**. * **

13. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NZ_CP032346 (Azospirillum brasilense strain MTCC4039 plasmid p1, complete sequence) position: , mismatch: 7, identity: 0.794

ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
ttcgtcggcagccagggccgcgtcgtcgaggccg	Protospacer
********* ********** *** .**. * **

14. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NZ_CP012915 (Azospirillum brasilense strain Sp 7 plasmid ABSP7_p1, complete sequence) position: , mismatch: 7, identity: 0.794

ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
ttcgtcggcagccagggccgcgtcgtcgaggccg	Protospacer
********* ********** *** .**. * **

15. spacer 5.6|3839704|36|CP029843|CRT matches to NC_010335 (Caulobacter sp. K31 plasmid pCAUL01, complete sequence) position: , mismatch: 7, identity: 0.806

-accgccgaggccggccagcagtacggcgacctggag	CRISPR spacer
gatcggc-aggccggccagcagtacggcaacccgggc	Protospacer
 *.** * ********************.***.**. 

16. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP010990 (Pseudonocardia sp. EC080625-04 plasmid pFRP1-1, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cggggcgagaccggccagcaggacggcgagg	Protospacer
   * ****.*********** *******  

17. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP012477 (Arthrobacter sp. ERGS1:01 isolate water plasmid unnamed2, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
gttgaagagcccggccagcagcacggcgacg	Protospacer
...*  *** ***********.******** 

18. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP012182 (Pseudonocardia sp. EC080610-09 plasmid pBCI2-1, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cggggcgagaccggccagcaggacggcgagg	Protospacer
   * ****.*********** *******  

19. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP013855 (Pseudonocardia sp. HH130630-07 plasmid pLS2-1, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
tacgccgagaccggcctgcagtacgggcccg	Protospacer
  *******.****** *********   * 

20. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP012185 (Pseudonocardia sp. EC080619-01 plasmid pBCI1-2, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cggggcgagaccggccagcaggacggcgagg	Protospacer
   * ****.*********** *******  

21. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP012186 (Pseudonocardia sp. EC080619-01 plasmid pBCI1-1, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cggggcgagaccggccagcaggacggcgagg	Protospacer
   * ****.*********** *******  

22. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP022666 (Rhizobium leguminosarum bv. viciae strain BIHB 1217 plasmid pPR1, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
tgttccgaggccggcgagcagtaaggcgggc	Protospacer
  . *********** ******* ****. *

23. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NC_013513 (Paracoccus aminophilus strain JCM 7686 plasmid pAMI3, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
ggcatcgaggtcggccagcagtccggcgatt	Protospacer
. *..*****.*********** ******..

24. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP011667 (Streptomyces sp. Mg1 plasmid pSMg1-3, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
gtcctccaggccggccagcagggcggcgacg	Protospacer
..* .* ************** .******* 

25. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP015043 (Rhodovulum sp. P5 plasmid pRGUI04, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
gatgtcgaggccggcccgcaggacggcggct	Protospacer
. .*.*********** **** ******.*.

26. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to MG962366 (Rhodococcus phage Finch, complete genome) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
gtcaccgaggacggcgagcagtacggcttca	Protospacer
..*.****** **** ***********  * 

27. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NC_011366 (Rhizobium leguminosarum bv. trifolii WSM2304 plasmid pRLG202, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
aaaatcgcggccggccagcagtccggcggca	Protospacer
*  ..** ************** *****.* 

28. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP007516 (Rubrobacter radiotolerans strain RSPS-4 plasmid 2, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
gccttcgaggccggccagcgggacggcgtga	Protospacer
.** .**************.* ******   

29. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP033583 (Streptomyces sp. ADI95-16 plasmid pADI95-16b, complete sequence) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
gtcctccaggccggccagcagggcggcgacg	Protospacer
..* .* ************** .******* 

30. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to MH834603 (Arthrobacter phage Bridgette, complete genome) position: , mismatch: 8, identity: 0.742

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
gatgccgaggcccgcctgcagtacgggttcc	Protospacer
. .********* *** *********   **

31. spacer 5.2|3839758|31|CP029843|CRISPRCasFinder matches to NZ_LN831789 (Streptomyces leeuwenhoekii strain type strain (C34 = DSM 42122 = NRRL B-24963) plasmid pSLE2) position: , mismatch: 8, identity: 0.742

cggatccacgagaacgcccgggtccgcgatg	CRISPR spacer
gcgatccacgacaacgcccggatcccggcgg	Protospacer
  ********* *********.***  *  *

32. spacer 5.2|3839758|31|CP029843|CRISPRCasFinder matches to NZ_CP018075 (Streptomyces venezuelae strain NRRL B-65442 plasmid, complete sequence) position: , mismatch: 8, identity: 0.742

cggatccacgagaacgcccgggtccgcgatg	CRISPR spacer
gcgatccacgacaacgcccggatcccggcag	Protospacer
  ********* *********.***  *  *

33. spacer 5.2|3839758|31|CP029843|CRISPRCasFinder matches to NC_010851 (Streptomyces sp. FR1 plasmid pFRL1, complete sequence) position: , mismatch: 8, identity: 0.742

cggatccacgagaacgcccgggtccgcgatg	CRISPR spacer
gcgatccacgacaacgcccggatcccggcgg	Protospacer
  ********* *********.***  *  *

34. spacer 5.3|3839812|31|CP029843|CRISPRCasFinder matches to NZ_AP022593 (Mycolicibacterium arabiense strain JCM 18538 plasmid pJCM18538, complete sequence) position: , mismatch: 8, identity: 0.742

aaggtcgccgcgtcggcgcataccggcgctc	CRISPR spacer
gagacggccgccacggcgcataccggcgcga	Protospacer
.**.. *****  ****************  

35. spacer 5.4|3839866|34|CP029843|CRISPRCasFinder matches to NZ_LR134451 (Tsukamurella tyrosinosolvens strain NCTC13231 plasmid 9, complete sequence) position: , mismatch: 8, identity: 0.765

cgcctggaagagacggtgaccgtcgacggcagca	CRISPR spacer
cggaccggcgagacggtgcccggcgacggcagca	Protospacer
**  . *. ********* *** ***********

36. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NZ_CP034811 (Paracoccus sp. Arc7-R13 plasmid unnamed1, complete sequence) position: , mismatch: 8, identity: 0.765

ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
gacatgggcggccagggccgggtctgcggcgatc	Protospacer
  *.* *** *************** ******. 

37. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NZ_CP017076 (Novosphingobium resinovorum strain SA1 plasmid pSA1, complete sequence) position: , mismatch: 8, identity: 0.765

ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
attgttctccgccagcgccgggtctgcggcgagg	Protospacer
 *.**.  ******* ********* ****** *

38. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP049794 (Ralstonia solanacearum strain 204 plasmid unnamed, complete sequence) position: , mismatch: 9, identity: 0.71

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cgcgcccaggccggccagcagttcgaggttg	Protospacer
  **** *************** **. * . 

39. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP049792 (Ralstonia solanacearum strain 203 plasmid unnamed, complete sequence) position: , mismatch: 9, identity: 0.71

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cgcgcccaggccggccagcagttcgaggttg	Protospacer
  **** *************** **. * . 

40. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP052069 (Ralstonia solanacearum strain FJAT91.F50 plasmid Plas1, complete sequence) position: , mismatch: 9, identity: 0.71

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cgcgcccaggccggccagcagttcgaggttg	Protospacer
  **** *************** **. * . 

41. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP016613 (Ralstonia solanacearum FJAT-91 plasmid unnamed1, complete sequence) position: , mismatch: 9, identity: 0.71

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cgcgcccaggccggccagcagttcgaggttg	Protospacer
  **** *************** **. * . 

42. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP049790 (Ralstonia solanacearum strain 202 plasmid unnamed, complete sequence) position: , mismatch: 9, identity: 0.71

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cgcgcccaggccggccagcagttcgaggttg	Protospacer
  **** *************** **. * . 

43. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP044425 (Paracoccus pantotrophus strain DSM 2944 plasmid pPAN2, complete sequence) position: , mismatch: 9, identity: 0.71

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
ctgaacgaggccggcctgcaggacggcgccg	Protospacer
 . . *********** **** ****** * 

44. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP016915 (Ralstonia solanacearum strain CQPS-1 plasmid unnamed, complete sequence) position: , mismatch: 9, identity: 0.71

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cgcgcccaggccggccagcagttcgaggttg	Protospacer
  **** *************** **. * . 

45. spacer 5.1|3839704|31|CP029843|CRISPRCasFinder matches to NZ_CP017244 (Rhizobium etli 8C-3 plasmid pRsp8C3c, complete sequence) position: , mismatch: 9, identity: 0.71

accgccgaggccggccagcagtacggcgacc	CRISPR spacer
cgcgccgagaccggccagcagtgcgcccgga	Protospacer
  *******.************.** * .  

46. spacer 5.3|3839812|31|CP029843|CRISPRCasFinder matches to CP021131 (Meiothermus taiwanensis strain WR-220 plasmid pMtWR-220, complete sequence) position: , mismatch: 9, identity: 0.71

aaggtcgccgcgtcggcgcataccggcgctc	CRISPR spacer
acccccgccgcgccggcgcctaccggcgtgg	Protospacer
*   .*******.****** ********.  

47. spacer 5.5|3839923|34|CP029843|CRISPRCasFinder matches to NZ_CP014690 (Gluconobacter albidus strain TMW2.1191 plasmid pGS1191_1, complete sequence) position: , mismatch: 9, identity: 0.735

ttcgtcggccgccagggccgggtctccggcgacg	CRISPR spacer
ttcgtcagccgtcagggccgggtcggccggaaga	Protospacer
******.****.************  * * .* .

48. spacer 5.3|3839812|31|CP029843|CRISPRCasFinder matches to NC_012520 (Rhodococcus opacus B4 plasmid pROB01, complete sequence) position: , mismatch: 10, identity: 0.677

aaggtcgccgcgtcggcgcataccggcgctc	CRISPR spacer
ggcatcgccgcggccgcgcataccggcagca	Protospacer
.. .******** * ************. . 

49. spacer 5.4|3839866|34|CP029843|CRISPRCasFinder matches to NZ_LR026982 (Rhodoplanes piscinae isolate Rhod_plasmid plasmid 1, complete sequence) position: , mismatch: 10, identity: 0.706

-----cgcctggaagagacggtgaccgtcgacggcagca	CRISPR spacer
atgaccctccagaa-----ggtgaccgtcgacggcatca	Protospacer
     * .*..***     ***************** **

50. spacer 5.6|3839704|36|CP029843|CRT matches to NZ_CP029831 (Azospirillum ramasamyi strain M2T2B2 plasmid unnamed7, complete sequence) position: , mismatch: 10, identity: 0.722

accgccgaggccggccagcagtacggcgacctggag	CRISPR spacer
cacgccgaggccggccagcagggcggcgccgaacgg	Protospacer
  ******************* .***** *  . .*

51. spacer 5.6|3839704|36|CP029843|CRT matches to NC_013857 (Azospirillum sp. B510 plasmid pAB510c, complete sequence) position: , mismatch: 10, identity: 0.722

accgccgaggccggccagcagtacggcgacctggag	CRISPR spacer
cacgccgaggccggccagcagggcggcgccgaacgg	Protospacer
  ******************* .***** *  . .*