CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number
NZ_CP047181	Rathayibacter festucae strain VKM Ac-2802 plasmid unnamed1, complete sequence	0 crisprs	csa3	0	0	5
NZ_CP047180	Rathayibacter festucae strain VKM Ac-2802 chromosome, complete genome	14 crisprs	csa3,cas3,WYL,DEDDh,PD-DExK,RT	1	2	0
NZ_CP047182	Rathayibacter festucae strain VKM Ac-2802 plasmid unnamed2, complete sequence	0 crisprs	NA	0	0	0

Results visualization

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CRISPR-Cas detection and classification

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

0 : 2314

Cronobacter_phage(100.0%)

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

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_104277457.1\|579_1029_+	translesion error-prone DNA polymerase V autoproteolytic subunit	F1C5A6	Cronobacter_phage	8.5e-26	50.0
WP_104353510.1\|1018_2314_+	Y-family DNA polymerase	F1C5A5	Cronobacter_phage	1.0e-71	39.4

DBSCAN-SWA_2

7128 : 8526

Mycobacterium_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_159424188.1\|7128_8526_+	ParB/RepB/Spo0J family partition protein	S5YZ97	Mycobacterium_phage	2.0e-57	36.7

DBSCAN-SWA_3

15722 : 19064

Mycobacterium_virus(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_104277746.1\|15722_15908_+	hypothetical protein	G1BQB2	Mycobacterium_virus	1.2e-07	57.7
WP_159424190.1\|15904_16171_+	hypothetical protein	NA	NA	NA	NA
WP_159424215.1\|16167_16398_+	glutaredoxin-like protein NrdH	A0A218MND6	uncultured_virus	1.0e-11	46.5
WP_159424191.1\|16394_17126_+	single-stranded DNA-binding protein	NA	NA	NA	NA
WP_159424192.1\|17135_17282_-	hypothetical protein	NA	NA	NA	NA
WP_104353531.1\|17414_17663_-	hypothetical protein	NA	NA	NA	NA
WP_104353530.1\|17726_18275_-	hypothetical protein	NA	NA	NA	NA
WP_159424193.1\|18467_19064_-	recombinase family protein	A0A219Y9V9	Aeromonas_phage	1.7e-34	46.7

DBSCAN-SWA_4

25607 : 30045

uncultured_virus(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_159424200.1\|25607_25958_+	metalloregulator ArsR/SmtB family transcription factor	A0A218MNF3	uncultured_virus	5.3e-07	38.5
WP_159424217.1\|25958_26627_-	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_159424201.1\|26676_27420_+	aquaporin family protein	NA	NA	NA	NA
WP_159424202.1\|27437_28823_+	FAD-dependent oxidoreductase	A0A2K5B2C5	Erysipelothrix_phage	8.8e-05	27.1
WP_159424203.1\|28819_29212_+	low molecular weight phosphatase family protein	NA	NA	NA	NA
WP_104305026.1\|29424_30045_+	recombinase family protein	A0A219Y9V9	Aeromonas_phage	1.3e-24	39.4

DBSCAN-SWA_5

45360 : 46500

Mycobacterium_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_159424211.1\|45360_46500_-	hypothetical protein	V5UQR9	Mycobacterium_phage	1.9e-13	39.3

Anti-CRISPR protein detection

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

2. NZ_CP047180

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP047180_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_1

4311-4397

Orphan

Consensus_repeat	Method
GGCGTATCGAGACCCGCTGTCGTCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_1

>merge|NZ_CP047180|1|4311-4397|CRISPRCasFinder
GGCGTATCGAGACCCGCTGTCGTCAGCACGGCCGGCTCATGCTGGTCGAGTAGCCCCGCAGGGGCGTATCGAGACCCGCCGTCGTCA

>NZ_CP047180|1|1|4311-4397|CRISPRCasFinder
GGCGTATCGAGACCCGCTGTCGTCA	GCACGGCCGGCTCATGCTGGTCGAGTAGCCCCGCAGG
GGCGTATCGAGACCCGCCGTCGTCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159421684.1\|4592_5948_+\|DNA-replication/repair-protein-RecF	unknown	unknown	gnl\|CDD\|234608
NZ_CP047180.1\|WP_123447255.1\|11516_11927_+\|DUF3566-domain-containing-protein	unknown	unknown	gnl\|CDD\|378809
NZ_CP047180.1\|WP_123447259.1\|3220_4108_+\|decarboxylating-6-phosphogluconate-dehydrogenase	unknown	unknown	gnl\|CDD\|236582
NZ_CP047180.1\|WP_159421688.1\|15156_15717_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_127887911.1\|8923_11524_+\|DNA-gyrase-subunit-A	unknown	unknown	gnl\|CDD\|235502
NZ_CP047180.1\|WP_159421687.1\|14641_15070_-\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|240040
NZ_CP047180.1\|WP_123447261.1\|0_1425_+\|chromosomal-replication-initiator-protein-DnaA	unknown	unknown	gnl\|CDD\|273037
NZ_CP047180.1\|WP_123447260.1\|1982_3134_+\|DNA-polymerase-III-subunit-beta	unknown	unknown	gnl\|CDD\|236089
NZ_CP047180.1\|WP_159421685.1\|12238_13462_-\|Fic-family-protein	unknown	unknown	gnl\|CDD\|225718
NZ_CP047180.1\|WP_123447257.1\|5940_6462_+\|DUF721-domain-containing-protein	unknown	unknown	gnl\|CDD\|179552
NZ_CP047180.1\|WP_159423947.1\|6762_8742_+\|DNA-topoisomerase-(ATP-hydrolyzing)-subunit-B	unknown	unknown	gnl\|CDD\|235542
NZ_CP047180.1\|WP_159421686.1\|14078_14405_-\|thioredoxin	unknown	unknown	gnl\|CDD\|239245
NZ_CP047180.1\|WP_133961335.1\|13549_14074_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_123447261.1\|0_1425_+\|chromosomal-replication-initiator-protein-DnaA	gnl\|CDD\|273037	TIGR00362, DnaA, chromosomal replication initiator protein DnaA. DnaA is involved in DNA biosynthesis; initiation of chromosome replication and can also be transcription regulator. The C-terminal of the family hits the pfam bacterial DnaA (bac_dnaA) domain family. For a review, see Kaguni (2006). [DNA metabolism, DNA replication, recombination, and repair].	0
NZ_CP047180.1\|WP_159421684.1\|4592_5948_+\|DNA-replication/repair-protein-RecF	gnl\|CDD\|234608	PRK00064, recF, recombination protein F; Reviewed.	2.50853e-131
NZ_CP047180.1\|WP_123447260.1\|1982_3134_+\|DNA-polymerase-III-subunit-beta	gnl\|CDD\|236089	PRK07761, PRK07761, DNA polymerase III subunit beta; Validated.	2.05742e-175
NZ_CP047180.1\|WP_159421685.1\|12238_13462_-\|Fic-family-protein	gnl\|CDD\|225718	COG3177, COG3177, Fic family protein [Function unknown].	2.35575e-26
NZ_CP047180.1\|WP_123447255.1\|11516_11927_+\|DUF3566-domain-containing-protein	gnl\|CDD\|378809	pfam12089, DUF3566, Transmembrane domain of unknown function (DUF3566). This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 136 to 304 amino acids in length. This region represents a transmembrane region found at the C-terminus of the proteins.	7.58962e-30
NZ_CP047180.1\|WP_123447257.1\|5940_6462_+\|DUF721-domain-containing-protein	gnl\|CDD\|179552	PRK03195, PRK03195, DUF721 family protein.	2.09751e-34
NZ_CP047180.1\|WP_123447259.1\|3220_4108_+\|decarboxylating-6-phosphogluconate-dehydrogenase	gnl\|CDD\|236582	PRK09599, PRK09599, NADP-dependent phosphogluconate dehydrogenase.	2.19033e-179
NZ_CP047180.1\|WP_159421687.1\|14641_15070_-\|NUDIX-domain-containing-protein	gnl\|CDD\|240040	cd04684, Nudix_Hydrolase_25, Contains a crystal structure of the Nudix hydrolase from Enterococcus faecalis, which has an unknown function. In general, members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity. They also contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of nudix hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.	6.85271e-36
NZ_CP047180.1\|WP_127887911.1\|8923_11524_+\|DNA-gyrase-subunit-A	gnl\|CDD\|235502	PRK05560, PRK05560, DNA gyrase subunit A; Validated.	0
NZ_CP047180.1\|WP_159423947.1\|6762_8742_+\|DNA-topoisomerase-(ATP-hydrolyzing)-subunit-B	gnl\|CDD\|235542	PRK05644, gyrB, DNA gyrase subunit B; Validated.	0
NZ_CP047180.1\|WP_159421686.1\|14078_14405_-\|thioredoxin	gnl\|CDD\|239245	cd02947, TRX_family, TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.	4.60421e-08

>NZ_CP047180.1|WP_123447259.1|3220_4108_+|decarboxylating-6-phosphogluconate-dehydrogenase
MHIGLVGLGKMGDNMRSRLREKGVEVTGYDRNPDVSDAASLDEMIAALPAPRVVWVMVPAGAITDAVVTDLSEKLSEGDLVIDGGNSRFTEDFKHDALLKPKGIHYIDAGVSGGVWGLENGYGLMVGGPKELVEYAMPVFDALRPEGPREEGFVHVGEVGAGHYAKMVHNGIEYALMQAFAEGYELLDTRKDIIKDVTGTFKAWQRGTVVRSWLLELLVRALEQDPEFEHIEGYVQDSGEGRWTIEEAINNAVPVPTISASIFARFVSRQEDSPAMKAVAALRNQFGGHSVKAVD
>NZ_CP047180.1|WP_123447260.1|1982_3134_+|DNA-polymerase-III-subunit-beta
MRFQANRDVFSEAVSFAVKLLPQRTTLPILSGILIEATAEGLTLSSFDYEVSAQTQIAADVEETGTVLVSGRLLADIANRLPNAPVRVATEESRVSVSAGSAHFTLLQMPVEEYPSIPEIDASTGLVPADAFSAAISQVAVAASRDDVTPVITGVQLEITENTIGLVATDRYRVAVREIDWDNGDNAAPSQPLTALVPARTLQEVGKTFSHSGTVSVAITQRDERELIAFTADRKTVTSLLIKGNFPPVKRLFPASVENYAVMATSDLIEATRRVSLVLEREAALRFSFSSDGLTLEAIGSEQAQASESIDAIVTGVDVVVSLKPQFLLDGLAAVHSEFVRIAFTKTENPNKPGPVLITAQTSREQPGSDSYRYLLQPNLLLR
>NZ_CP047180.1|WP_123447261.1|0_1425_+|chromosomal-replication-initiator-protein-DnaA
MPDDTSMIDAWNVIRGELSRDERITAPMYGFVSLVEPKGIMAGTFYLEVPNEFTRGMLEHRVRVPLLSAIGALDDSFGVSTFAFVVNPDIEHEPMSSPSSDSLNPFEPVTGSSATVAPPVRVVEELRTVPATDTRLNPKYSFDNFVIGGSNRFAHAAAVAVAEAPAKAYNPLFVYGDSGLGKTHLLHAIGHYAMSLYPGIRVRYVSSEEFTNDFINSIANNRGNAFHGRYRNVDILLIDDIQFLQGKAETQEAFFHTFNQLHDHNKQVVITSDLPPKALTGFEDRMRSRFEWGLITDVQAPDLETRIAILRKKAVSEKLLVPDDILEFMASKVSSNIRELEGTLIRVTAFASLNRTPVDMALVQTVLKDLITLDEDNVISPVDIINHTADYFKLTVDDLYGSSRSQAVATARQIAMYLCRELTNLSLPKIGQLFGNRDHTTVMYANKKISELMKERRSIYNQVTELTTRIKTNR
>NZ_CP047180.1|WP_159421684.1|4592_5948_+|DNA-replication/repair-protein-RecF
MQVTQLALSDFRNYASVDVALAPGPNLFVGRNGQGKTNLVESLGYLSTLGSHRVSTDQALIRAGQDSAVIRARLRNGDRDLLAEVQINRSSANRAQINRGGIKPRELPRFFSSVLFAPEDLLLIRGDPSARRRFLDQLVVIRSPRMSAVQADYERVLRQRNSLLKSARASGVRDPAKLGTLDIWDERLVALGTEIIQSRLTLVDELSGPVRAAYEAVAGADQRPVLRSRLSVEGAVDDDDEPVATAEASAAPAELTSTFSAALLSVRRRELDRGISLVGPHRDDVQFELNDLPAKGYASHGESWSFALALKLGAAELLRRDSPMGDPVLMLDDVFAELDARRRERLAAVVADYEQVLITAAVFDDVPAALAAHTVRIEAGRIVESDVVVVPETPLTAPEKAAEPEAGPEPEAGPEAESAPNAAPEPAPSAETEPVPEPSEEPEPTADPDRG
>NZ_CP047180.1|WP_123447257.1|5940_6462_+|DUF721-domain-containing-protein
MADSPRRGAPSPAPDSEAARVYQHLKEVFGGDAPRRVRKTVDRAEPKGDAAPFGGGRDPHDLGDVLSSLTVKLGWTAPLAQGDLMSSWTAIAGEETAKHSTPVGVVDGVLTVACESTAWSTQLRLMRIEIMNHIAVNHPDAGITAIRFQGPDVPNWKKGPRSIPGRGPRDTYG
>NZ_CP047180.1|WP_159423947.1|6762_8742_+|DNA-topoisomerase-(ATP-hydrolyzing)-subunit-B
MSTKSSGDYGANQIQVLEGLEAVRKRPGMYIGSTGPRGLHHLVYEIVDNAVDEALAGYCDNIEVVVRADGGLTVVDNGRGIPVDMHPTEGISTVELVLTVLHAGGKFGGGGYAVSGGLHGVGSSVVNALSTRLEVEVKRQGASYSMTFADGVPEAPLAKGGPSDETGTTITFWPNAEIFETVEFDYETLRARFQQMAFLNKGLRIALTDEKEIEFEGEGENETSGARSDVFLYEKGLVDYVEYINSLKKSDLVHSEIIDFESEDTERRISLEVAMQWTTAYTESVHTYANTINTHEGGTHEEGFRAALTTLVNKYARANNLLKDKDENLSGDDIREGLTAVVSIKLGEPQFEGQTKTKLGNTEAKAFVQRVAGEQLADWFDRNPNQAKDIIRKAIQAASARMAARKARETARRKGLLEGGGMPGKLKDCQSKDPSISEIFIVEGDSAGGSAVQGRNPETQAILPLRGKILNVEKARLDRALGNNEVQAMITAFGAGIGEDFNPDKARYHKIILMADADVDGQHITTLLLTLLFRYMRPLIDLGYVYLAQPPLYRLKWSNSPHEYVYSDRERDALLAHGAASNKRMPKENGIQRYKGLGEMDYKELWETTMDPATRTLLQVTLDDAAAADEIFSTLMGEDVESRRSFIQKNAKDVRFLDI
>NZ_CP047180.1|WP_127887911.1|8923_11524_+|DNA-gyrase-subunit-A
MADESDTPTGPDDGEDIVTETGVVIHGHDKIEPVDLQLEMQRSYLDYAMSVIVGRALPEVRDGLKPVHRRVIYAMYDGGYRPDKAFSKCSRVVGDVMGQFHPHGDSAIYDALVRLVQPWSLRYPLALGQGNFGSPGNDGAAAPRYTETKMAPLALEMVRDIDKNTVDFQDNYDGRTREPAILPARFPNLLVNGSVGIAVGMATNIPPHNLREVAAGAKWALENPEASREELLEALLQRIKGPDFPTGAQILGVRGIQDAYRTGRGSITMRAVVSIEEIQGRTCLVVTELPYQVNPDNLAIKIAELVKDGRVSGIADIRDETSGRTGQRLVVVLKRDAVAKVVLNNLYKHTPLQENFGANMLAIVDGIPRTLSLDGFIRAWVDHQVEVIVRRTQYLLDEAEARIHILRGYLKALDALDEVIALIRRSPTVEEARDGLMELLDIDEVQSRAILDMQLRRLAALERQKIIDEHDRIQAEIEDYKSILASPERQRTIISDELDEIVDRFGDDRRTEILFGFDGDMSVEDLIPEEEMVVTVTRGGYLKRTRSDSYRAQHRGGRGVRGAQLKADDIVEHFFVTTTHHWLLFFTNTGRVYRAKTYELQEVSRDAKGQHIANLLALEPGEQIAQILDIRDYEAARYLVLATRDGLVKKTALMEYDTNRSGGIIAIKLREGDELVSALLVDEDSDVLLVSRKGMSIRFTASDQALRPMGRSTSGVMGMSFRGDDRLLDANVVSDEGYVFVVTEGGYAKRTAVDQYRLQGRGGLGIKVAKLEEKRGDLVGAIITGEDDEVLVVLASGKVVRSAVAEVPAKGRDTMGVVFARFADDDRIIALAKNTERNLDAQDEDPDAAASAESEAVSEEDESVDE
>NZ_CP047180.1|WP_123447255.1|11516_11927_+|DUF3566-domain-containing-protein
MSSTVAEKLAKKSAKSPAAKQVRLKLVYVDFWSAVKLSFLLGLTLAIITIVVVYLVYTVLAQTGVFDEVNGLVQDIAGAEAFDLNTIISLPQIMGFAVVVAVLNTIVTTALGAIVALLYNLSVKITGGLLVGFTNQ
>NZ_CP047180.1|WP_159421685.1|12238_13462_-|Fic-family-protein
MTEDQSPPSQRSWPAVGFEQRPWQRSGDEVASRRLLRAAAGPYRAAVPPFVADLDVSLPSDLLAVSEDASRELTRFDAQVGSLTAPFASILLRTESASSSEVEHLTASAKQVALAELGDSTSTNAQLVVRNVAAMEAAIALSDELDADAVLTMHRVLLESTAPDIVGHWRDQQVWIGGGGVSPHGAVFVPPHHERVPALMLDVMEFARRVDVPVLAQVAIAHAQFETVHPFPDGNGRTGRALVQGMLRAAGVTENVTVPVSAGLLGDMKRYFDALTAYRSGDVRPIIETLADAAFAAVQNGRRLAADIAAIGARWDAGIRARSDSSVHALRQLLLRQPVVTVALVAAELGVSFPTAEASVQKLVDAGVLTQSQAGRRNRSFEAVEVLAALDDFAARARRPRYGTHSG
>NZ_CP047180.1|WP_133961335.1|13549_14074_-|hypothetical-protein
MPHRRRVASVAVVLAATASLALSGCATEPVSEATVGIGRGGQRAEVLGVVVVCSGAVDGLDLAVEDTAPLLIGDRARRITRWVAPEPVDDIGATDLAGRTVWPADREIERFPLGVDLTLGAYAVGGSVIGRPVVFTAEQFDTLSVGEIIVGDIRDGTSETLSVENFLGLACQPR
>NZ_CP047180.1|WP_159421686.1|14078_14405_-|thioredoxin
MSLPSRSSPGNRAVPPGVVVHVIVELYTSAFCGACNAARSVLERAAELVPAAEIREFDVAFAPEAAEAADIRSTPTVVVRDADGRAVFRAEGAPSLPQALSALALAVG
>NZ_CP047180.1|WP_159421687.1|14641_15070_-|NUDIX-domain-containing-protein
MDIRVAAYGVIIDGERMLLAHWSQGPWEAWTLPGGGIDEGESPADAAVREIFEETGYHAELEGLIGVDSHVIPAHRRSDPEAGPLHAIRVVYRARVTGGELTHEVDGSTDAAAWFPLAEVEGLERVELIDVALTMNEAWTLR
>NZ_CP047180.1|WP_159421688.1|15156_15717_-|hypothetical-protein
MGLSRKHKKDLKRLRKNAEAVWSEQQEVLAHAASVLEKSRRHATKYAKKEVVPAVKDAYSSRVKPVYDNGVSAVEGTYSSARDAYKHKVLPTFTAVGGTAAAAFEAAKDSKNRAKLAEISKARWEELTTPPKKKNKVGTVFAIGAALVAVGGIGYAVWQTFRADDELWVAEDEPASAAQSPASTAS

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

Crispr_ID: NZ_CP047180_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_2

302705-302935

Orphan

Consensus_repeat	Method
GACCCCCCGCCCTCCCCGCGAGATGCCACTTGCGTACGCCTCCCTCGG	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP047180_2

>merge|NZ_CP047180|2|302705-302935|PILER-CR
CCCTCCCTCCCCGCGAGATGCCACTTGGGTACGCCTCCCTCGGCGTGTCGCGTACCGAACCGGCATCTCGCGGACTGCCGCCGGGGCTCGGACCCCCGGTCGTCTCCGCGAGATGCCACTTATGAGCTTCCGCCTCGGCGTGTCGCCCTCATAAGTGGCATCTCGCGGACAGCCGCCGCACGCGCGCCCCTGCCCTCCCCGCGAGATGCCACTTGCGTACGCCTCTCTCGG

>NZ_CP047180|2|1|302705-302935|PILER-CR
CCCTCCCTCCCCGCGAGATGCCACTTGGGTACGCCTCCCTCGGCGTGT	CGCGTACCGAACCGGCATCTCGCGGACTGCCGCCGGGGCTCGGACCC
CCGGTCGTCTCCGCGAGATGCCACTTATGAGCTTCCGCCTCGGCGTGT	CGCCCTCATAAGTGGCATCTCGCGGACAGCCGCCGCACGCGCGCCCCTGCCCTCCCCGCGAG
ATGCCACTTGCGTACGCCTCTCTCGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159421833.1\|292186_293347_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|341042
NZ_CP047180.1\|WP_159421841.1\|306930_307926_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|366154
NZ_CP047180.1\|WP_159421835.1\|296711_297086_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_167306135.1\|303088_303646_+\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|239646
NZ_CP047180.1\|WP_159421844.1\|315108_315516_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|341028
NZ_CP047180.1\|WP_133960435.1\|297212_297521_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_127887736.1\|313976_314879_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223656
NZ_CP047180.1\|WP_159421839.1\|303695_304664_+\|DUF1731-domain-containing-protein	unknown	unknown	gnl\|CDD\|187553
NZ_CP047180.1\|WP_159421837.1\|300712_301552_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187613
NZ_CP047180.1\|WP_123448136.1\|298831_299473_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|180466
NZ_CP047180.1\|WP_123732480.1\|309313_310585_-\|phosphoribosylamine--glycine-ligase	unknown	unknown	gnl\|CDD\|234856
NZ_CP047180.1\|WP_123706287.1\|298479_298689_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_123448056.1\|310758_311136_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380033
NZ_CP047180.1\|WP_159421842.1\|307922_309182_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863
NZ_CP047180.1\|WP_159421843.1\|311271_313563_+\|bifunctional-metallophosphatase/5'-nucleotidase	unknown	unknown	gnl\|CDD\|223808
NZ_CP047180.1\|WP_159421836.1\|299532_300648_-\|type-III-polyketide-synthase	unknown	unknown	gnl\|CDD\|238427
NZ_CP047180.1\|WP_159421840.1\|304907_306854_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|269892
NZ_CP047180.1\|WP_159421834.1\|293442_296001_-\|ATP-dependent-DNA-ligase	unknown	unknown	gnl\|CDD\|236599
NZ_CP047180.1\|WP_159421838.1\|301921_302704_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_123448041.1\|296162_296648_+\|glutathione-peroxidase	unknown	unknown	gnl\|CDD\|223463

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_159421833.1\|292186_293347_+\|MFS-transporter	gnl\|CDD\|341042	cd17489, MFS_YfcJ_like, Escherichia coli YfcJ, YhhS, and similar transporters of the Major Facilitator Superfamily. This subfamily is composed of Escherichia coli membrane proteins, YfcJ and YhhS, Bacillus subtilis uncharacterized MFS-type transporter YwoG, and similar proteins. YfcJ and YhhS are putative arabinose efflux transporters. YhhS has been implicated glyphosate resistance. YfcJ-like arabinose efflux transporters belong to the bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.44732e-23
NZ_CP047180.1\|WP_159421841.1\|306930_307926_+\|glycosyltransferase	gnl\|CDD\|366154	pfam00535, Glycos_transf_2, Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.	5.45213e-36
NZ_CP047180.1\|WP_123448056.1\|310758_311136_+\|hypothetical-protein	gnl\|CDD\|380033	pfam17844, SCP_3, Bacterial SCP ortholog. This domain is found in MSMEG_5817 gene product from M. smegmatis. It has been shown to be vital for mycobacterial survival within host macrophages. Crystal structure revealed a Rossmann-like fold alpha/beta two-layer sandwich forming a highly hydrophobic interface cavity and with high structural homology to the SCP family. Hence, it has been suggested that this domain may be involved in the interaction of apolar ligands through its hydrophobic cavity. Alanine-scanning mutagenesis of the hydrophobic cavity of MSMEG_5817 protein demonstrated that the conserved Val82 residue plays an important role in ligand binding.	5.28841e-52
NZ_CP047180.1\|WP_167306135.1\|303088_303646_+\|NUDIX-domain-containing-protein	gnl\|CDD\|239646	cd03674, Nudix_Hydrolase_1, Members of the Nudix hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity. They also contain a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, U=I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of nudix hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance & "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.	3.36808e-26
NZ_CP047180.1\|WP_159421844.1\|315108_315516_+\|hypothetical-protein	gnl\|CDD\|341028	cd17475, MFS_MT3072_like, Mycobacterium tuberculosis uncharacterized MFS-type transporter MT3072 and similar transporters of the Major Facilitator Superfamily. This family includes the Mycobacterium tuberculosis uncharacterized MFS-type transporter MT3072. It belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	0.00121685
NZ_CP047180.1\|WP_123732480.1\|309313_310585_-\|phosphoribosylamine--glycine-ligase	gnl\|CDD\|234856	PRK00885, PRK00885, phosphoribosylamine--glycine ligase; Provisional.	0
NZ_CP047180.1\|WP_127887736.1\|313976_314879_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|223656	COG0583, LysR, Transcriptional regulator [Transcription].	2.9781e-32
NZ_CP047180.1\|WP_159421839.1\|303695_304664_+\|DUF1731-domain-containing-protein	gnl\|CDD\|187553	cd05242, SDR_a8, atypical (a) SDRs, subgroup 8. This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	9.22638e-99
NZ_CP047180.1\|WP_159421837.1\|300712_301552_-\|SDR-family-oxidoreductase	gnl\|CDD\|187613	cd05355, SDR_c1, classical (c) SDR, subgroup 1. These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	4.68826e-144
NZ_CP047180.1\|WP_123448136.1\|298831_299473_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|180466	PRK06202, PRK06202, hypothetical protein; Provisional.	5.59619e-88
NZ_CP047180.1\|WP_159421842.1\|307922_309182_+\|MFS-transporter	gnl\|CDD\|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.27826e-36
NZ_CP047180.1\|WP_159421843.1\|311271_313563_+\|bifunctional-metallophosphatase/5'-nucleotidase	gnl\|CDD\|223808	COG0737, UshA, 5'-nucleotidase/2',3'-cyclic phosphodiesterase and related esterases [Nucleotide transport and metabolism].	1.26914e-74
NZ_CP047180.1\|WP_159421836.1\|299532_300648_-\|type-III-polyketide-synthase	gnl\|CDD\|238427	cd00831, CHS_like, Chalcone and stilbene synthases; plant-specific polyketide synthases (PKS) and related enzymes, also called type III PKSs. PKS generate an array of different products, dependent on the nature of the starter molecule. They share a common chemical strategy, after the starter molecule is loaded onto the active site cysteine, a carboxylative condensation reation extends the polyketide chain. Plant-specific PKS are dimeric iterative PKSs, using coenzyme A esters to deliver substrate to the active site, but they differ in the choice of starter molecule and the number of condensation reactions.	4.77631e-112
NZ_CP047180.1\|WP_159421840.1\|304907_306854_+\|hypothetical-protein	gnl\|CDD\|269892	cd14791, GH36, glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.	2.34814e-27
NZ_CP047180.1\|WP_159421834.1\|293442_296001_-\|ATP-dependent-DNA-ligase	gnl\|CDD\|236599	PRK09632, PRK09632, ATP-dependent DNA ligase; Reviewed.	0
NZ_CP047180.1\|WP_123448041.1\|296162_296648_+\|glutathione-peroxidase	gnl\|CDD\|223463	COG0386, BtuE, Glutathione peroxidase [Posttranslational modification, protein turnover, chaperones].	5.52972e-71

>NZ_CP047180.1|WP_159421838.1|301921_302704_+|hypothetical-protein
MSTPTDRGPGSDSSDPTRSDRDATTRSDTTSTASTTPGTGATATGATASTAPDDQPAAHRAPVDPDSAEAAKARTAARKDIHQREKDRFGGLKIGCAFFGWLAATGLAVILTALVTAIGAAVVGTQDVTADLAADPAAFGWVGAIALLVILLVAYYSGGYVAGRMARFSGAKQGVAVWAWAVVVAIVVGIVSALTGGSQILSAVSGFPQIPLDAGDATVTAIVTVLAALVVSLIGAVLGGLAGMRFHRRVDREGLSGLAV
>NZ_CP047180.1|WP_159421837.1|300712_301552_-|SDR-family-oxidoreductase
MTPESPEQTPPGTEAELTPKADHGETSYRGSDRLRGKVALVTGADSGIGKAVAIAFAREGADVAISYLNEHEDAEDTAKWVREAGREALLLPGDLQDPAHCRSVVAETVEKLGHLEVLVSNAAFQMSREEVTDIPDEEWDRTIATNISAYFHLVKSALPHLTSGASIIATSSVQSDQPSYQLLPYAATKAAMLSMTASLAQALGEKGIRANAVAPGPIWTPLIPATMPPEAVASFGEQVPLGRPGQPAEVAHAYVLLASDDASYMSGSTIAVTGGKPIL
>NZ_CP047180.1|WP_159421836.1|299532_300648_-|type-III-polyketide-synthase
MSVHIRSIETAVPPTVLHQPALRDLFAAQPAVTRLGSRLIGAAFNASGIDTRHTVIDELDGEERDGESTFYDARSGLLLDPGTAARNAVYTARAPELFAQAARRALEAAGFAPDEVTHVVTVSCTGFYAPGPDYQLVRALGLRVSTQRFHLGFMGCYGAFPGLRAARAFCEADPSAVVLVVTAELCSIHLTSSSDAEQIVATSVFADGAAAAVVTARAPEPGTAVLDIDELDTTLTPEGEDEMAWTIGDHGFTMRLSTYVPSIIGTNITAALEPMLGLGGVGAADVQRWAVHPGGRSILDRVQSAIGLSDEQMRPSREVLRTVGNMSSATVLFILRRLLHGEAADGERIGAMAFGPGLTVEMALLTKRGGA
>NZ_CP047180.1|WP_123448136.1|298831_299473_-|methyltransferase-domain-containing-protein
MDDPSCDRALLDATYARFGTVNRLVSGWRRLYRTRLRPLFRSEEPLRLLDIGSGGGDIARSLADWAHADGLRLAITAIDPDERAFAFATSTPAPAGLEFRRASSAELVAEGAQYDIVTSNHLLHHLPAEALRALLEDSERLAPRALHNDIERSRLAYTAYAAATRPIAAGSFLHYDGSLSVRRSYTAPELRVLAPEGWRVERAAPYRLLLARG
>NZ_CP047180.1|WP_123706287.1|298479_298689_+|hypothetical-protein
MKTRVIFYLIGGVLLLGAGISSLGDGVSVPDIITVLCGVLILALAGWQYRRSHGPDERTPGDDVERPHR
>NZ_CP047180.1|WP_133960435.1|297212_297521_-|hypothetical-protein
MTYGPQNLEIEFEERVLAHLKVAVLSKLRRNEAFSLSWTEDASTGHGRSSVWLHPSVPLHFRFAETHQPKLNRAWIEQMLSVASMHGELSVLPEPEETRQGS
>NZ_CP047180.1|WP_159421835.1|296711_297086_-|hypothetical-protein
MTETARAVAAPTLTGTGGSLRKDEPIAVRHAPDSASTDSQPVLGCRIDVSGRIFTVELEMAGVFLRQVRRTLRDGDSALVLLRHVDGIEMIPFTRATPFEVSDIVCPEGVEPAEARIAEGLRAR
>NZ_CP047180.1|WP_123448041.1|296162_296648_+|glutathione-peroxidase
MPETITDIPLTTIDGSSSTLADYAPVKLIVNVASRCGLAPQYEKLEALQKQYGDRGFTVLGFPSNQFLQELSDSDKIKEYCSTTWGVTFPMFEKVKVNGRSAHPLYAELTKTEDEAGKAGKVKWNFEKFLITADGTVHRFRPTVEPDDPRIVQLIEASLPA
>NZ_CP047180.1|WP_159421834.1|293442_296001_-|ATP-dependent-DNA-ligase
MTPSSQQLVSVGGRRLRLTNLDKVVYPEAEFTKADVLSYYASVASAMLPHLARRPVTRKRWVDGVGTAEHPGEVFFEKNLPSSAPYWLSRTKLAHSSRDVEYPLVDDVAGLTWLAQQAALELHVPQWRVGSDGERRPPDRLVLDLDPGEGAGLAECAEVAFLARDLLEGMGLEPFPVTSGSKGIHLYCPLDASASSDQISSVAHELAKVLESDHRDLVVSDMKKTLREGKVLVDWSQNSAAKTTIAPYSLRGRLLPRVAAPRTWEEIGAADLRHLAPDEVVERLRNDGDLLRLVLAARGAGLEPSPERMAGFAATDASADRLAAYRSMRDASKTPEPVPSPGAGIATSGDTFVVQEHHARRLHYDFRLEHDGVLVSWAVPKGPPLDGDPNRLAVQTEDHPLEYATFEGTIPAGEYGGGEVRIWDEGTYALEKWREGEEVIAVLTGRPDGGLGGEPRRYALLHTGAKGGKGDEKNWLLHLMAPGAAAHGEKAHGRGVGVRKGGGPGGSSGAGASGSGAAGSGATGSGATTPSSSPIAEAAAFRPMLATAGRAADIPGDSAIEMKWDGYRALVRVAGGAVTLTSRNGNDLTAAFPDLLDPIAEAAAVDCVLDGEIVALDDRGRPDFGRLQTRGGLTKPREIEAAARATPVHLMLFDLLAIDGTDAIGRPYDERRAALEQLATENERVHVPSVFDGDLEEAMSTSLALGLEGVVAKRRDAAYRPGVRSGDWVKLTHHRVQEVVIVGWREGEGGLVGSVGSLLTALPGDDGLVYSGRVGSGFSDRERRGLVARLAEHATDEPAVSVPPAESRGVHWVEPVLVGEVRYRERTAGGTLRQPVWRGWRADKSAAEVRLE
>NZ_CP047180.1|WP_159421833.1|292186_293347_+|MFS-transporter
MPDRQALSTGALLTHAVLIQAVAFLLRPAAVYQAIQLDVPAWALGALGASFAVVPLLIALPVGGLVDRVGARFVMACGSLLTIAAAGLLLLAGGGLVGLLCGTALLGAGHLGCVVGQQAVVAGGAAGTRLDSRFGYYTFAASLGQAIGPAFIPVFAGSAVRPDPAPLFLVGGALAVLLLAVTTAIARPAPRATAAAPSEGSTLGLLRIPGLARALLTSATVVAAVDLTVVYLPALGAERGLPAGVVGALLTVRALASMASRLLLGATTSRFGRTRVMIAGIVVSAVCLVLTALPAPTALLFVAVALLGLGLGIGQPITMSWLIERTPADRHGRALSLRLAGNRMGLIALPTLLGTIAAAAGAGGVLIGTGVAVGSTLVLLRGVRLD
>NZ_CP047180.1|WP_167306135.1|303088_303646_+|NUDIX-domain-containing-protein
MENARAGRLSSELAGWAAPAALAGLRDEYLAFLAEHGDAALERDGGPEHVTASCFVLSPALDRVLLCYHRKGRFWVQLGGHVEQADASVPAAAEREAREESGLPALTLLGDVPLDLDRHGLGGGFGRCSTHWDIGYGAIADPAQPFAVSDESDALAWWPVDALPEDVPPGFPERLAGALAAARRL
>NZ_CP047180.1|WP_159421839.1|303695_304664_+|DUF1731-domain-containing-protein
MPDPARPVVVLAGASGFLGTDLARRFEADGWTVRRIGRSGPDARWGDTAAITRALDGTRLLVNLAGKSVDCRYTPANRAEILRSRIDTTQELHRAVAAAATPPPVWMNASTATIYRHEEERANTEQDGVLGEGFSVDVARAWEEAFFAGETPGVRRLALRMTIVLGDGPATGILLKLARLGLGGPQFDGRWPATRARRAAGVHHEYRPTHGRQHFSWIHVEDVYRSIRFLEEQPLDGPVNLAAPNPSDNTELSRLLRAAVGRRIGLPAPRFVLEPATFALRTESELLLKSRWVVPGRLEEAGFTFAHPDLGEALRDIVATAR
>NZ_CP047180.1|WP_159421840.1|304907_306854_+|hypothetical-protein
MGSSDSTARRTAAGSVEVRARRVDGTTVGFRAVLIATGDGRLVVADSTPVPTGWRFTGAADELLEVRLPARPELRDVSVVYTTTLDNLDHVVVPDTGRWHMNSSHPISAWRFSGDLQVRANSLKTPVYVFERLGGGVHGVGVIAAPTEMDITLHEPASNRALNVHFRRLRVEFTLLHLADTAEAGDDGEAVHRFWIAVLPASQHADWRSVLRRFSACERLALDVRYSTRPEALEPYWCTWVDWSSEHVTQELVLRNARLAAELGIPNIVIDDGWFGRGLDSSYDVPMDIGDWTPDPVKYPDLPWLIESIHALGSRVIIWCAPHAVGPASAAFGRVGDLLVQDVLGAPILNPTMFYSLCFRSERARRVMVDVVRDLFRRHPFDGVKYDLFNWLPSEECESPEHAHDLGSTIVGLHRVLAECAAITEAQPRPVVVEMKQDYATAAIAGLGSVVRGGDSPYASRTNLVRMDYIQARGMPGLNDYQTFPRSASPAEVCVIALRMVAGGVPAWGRDLTALDPSQRVCLLRVHRWYRALLHHGAGAHRESDRDGVLLLRTDVGVVLICTEPGRVVTVPADCCQIVNATLSTELVLRSEQKRTVLGSRSILAEVCVPRLRSLPSGVHRLDLGTGTVLTLAVELRPHPTDADGGTR
>NZ_CP047180.1|WP_159421841.1|306930_307926_+|glycosyltransferase
MPQNLSIVVPAYNVEAYLLECLASLADRDDVGEVVVVDDGSTDGTLALARAFAASQPRVTVLSEEHRGLSATRNTGVAAAQGEFLAFCDADDRVPPGAYDHLLRALGASGSDFASGDVRRFDSARVWAHPRYRDVFAATRLGTHLTRDPALILDRMSWNKVFRRSFWDRSGLAFQLAEYEDGPVMIEAHLRAASVDVVSEVVYHWRVRESGPHSITQRLHEPANAAARMTMAVETALVLQRLAPELLPELALDIVHGDMRVVANAVQRGTGDAIGVAVARACDFLDLLPPGLLEELSEEDALMVGRFRRSDLAAIRSDAPGHDPTGRTPPR
>NZ_CP047180.1|WP_159421842.1|307922_309182_+|MFS-transporter
MTAARESVRRILRANPDYRRVFLAQIVSQGGDWFTMIPLIVLLQRLTGDGALGALLLAAETAVIAVLSLWAGGLVDRTSRRTVLVVAQAGSALAVLPLFLLQSAGTAWLAVLTFGLLAAGKAFFTPAVNAIVPQIVPRESLLVASTGLNSVWGVMLALGASLGGIASALVSPHFCFAITAGAYGFSALLLLGLPAARGAERGAGRGAGREAGRRGGLARFARDVREVAAFCRSDRRIPALLLAKPGSHLGNGAIALFPALALTMAADPAVAASLLFAARGVGAVIGPRVARFTAERSPDLRGGFIAAVLLFGLAYALVSISTSLVLAITLVLIAHIGGSMNASLSGYGLQSITANDLRGRVFAVDTMIAMLAIALSQALVSLGILLLEPRTVMALCSAAVLGCAALWWSATRRTPLRTS
>NZ_CP047180.1|WP_123732480.1|309313_310585_-|phosphoribosylamine--glycine-ligase
MKILVLGSGAREHAIITALLAEEEAHEIIAAPGNAGIARDVEVIHFDTNSPRLVSDFAVEQGIELVVIGPEAPLVAGVADALRRRRIPTFGPDRAAAALEGSKTFAKRVMDMARVPTGRATRVSTLVDATRVIDEFGAPYVVKADGLAAGKGVLVTESRTAAVAHAEFWLQSGDVLIEEFLAGQEVSLFLLSDGHDVVPLSPAQDYKRLADGDEGPNTGGMGAYSPLPWLADRWESERAFVDEVIDTVAIPTIRQLERERTPFVGLLYCGLIVTDAGIRVIEFNARFGDPETQVVLPRLVSPLSALLFAAATGALASVPWPAFSEDVAVTVVLASEGYPENAATGRVLGGLEAAAEVPGVTLAHAATQLVDGRFVATGGRVLNVVARGADFAEARERAYRALDLITLDGGQYRRDIALRVAGR
>NZ_CP047180.1|WP_123448056.1|310758_311136_+|hypothetical-protein
MAKGKIDEATGQDAVRAALAGGADRNTTATAVRFLLQIIETNVPGRSVEVRVPPFGAAQCVEGPGHTRGTPPNVIEMDAATWLPLATGSLPWSEGLASGRIHASGVRADLSPFLPLLHVRRPSAN
>NZ_CP047180.1|WP_159421843.1|311271_313563_+|bifunctional-metallophosphatase/5'-nucleotidase
MRSTTTGRRRGLLRTLSATAIGAVAGAALLGAAPAMAADGKVIDIYTMNDFHGRLEASAAGTVDGSTPGAASLASAYATLKAENPDNSILISAGDNIGASTFTSYVQQDTPTIDALGLMGVSASAIGNHEFDQGRADLDDRVIPRAEFEYFSSNLLEKGTDDHAYASSYVQDFDGVTVGFIGATTASLPSLVSPAGIASLDIAPVVDSVNAEAARLQDGVDDSADSSVSAEDKNLEADVLVAVIHEGAESATVDLTDANTVFGAIVDGIGGGLDAIVSAHTHQAYASEVTVDGNTLPVVQAGQYGNRLGHIELTIDPETKEVTNSAQNLVDTLVPAQVTNPTTGVVSTVFQPAYAADSTPEGVAVAALVADAVAVAEVQGAVPVGSITADIRRGVQSNGSENRGAESTMGNLVADAQLWATQEDLGTQIAFMNPGGVRNDLLFASSGAGDADGQVSYKEAAAVQLFANTLVTETLTGAQIKTVLEQQWQPGQSRPELHLGISKDLTYTYDPTAEVGSHVTGVFFQGEPMADEETFKIVTNSFLASGGDNFTELANGTGKADSGRVDLTAFTDYIAAFSPVTPDAASRSIGIVDTSVEGAETLSYELSSLDVNNSTVRDDEVQVLIDGVQVATAPIDHTVVDTTDEQGRASVGFSVAELSAGDHELEFALPVTGVSVVSTLTVTEAAGPGTTPTPTPTPEPTDTVIPTTPATTAPAVPGASGGSTGHLAATGVDATPAFAAGAAALLLGLGMTVARLRRRTAAK
>NZ_CP047180.1|WP_127887736.1|313976_314879_+|LysR-family-transcriptional-regulator
MDVRRLELLRELSMRRSITAVAAATHRTPSAVSQQLKVLEREAGVPLIERSGRGVVLTAAGRELARSATEIATALERADAVWQTFKNNPIGEVTIATFPTAGQMLLPDALVALRSVEGLVVHCEDADPGTDEFLDLTADFDIVLAHSPNGRSAWAGHGLAMAELMVEPLDIALPLGHRLADRATVTAGDLVGETWIGVPDGFPFERIMQEIETTSGEPVRVEQRFASTRVTEAFVAAGLGIAVVPRYTAGTAGIVVKPLRGVNSVRHIVALMRPDRAERLSVRTVVRELRAQAGRLLHSM
>NZ_CP047180.1|WP_159421844.1|315108_315516_+|hypothetical-protein
MTDPLDSSPRPDDVEITREEVDVRRSPRVWRILALGAGLGAIVAFVLTFALPETEGFSQAQVFGFSLLLFVTIFGGLAALVVVILDRVVGRRVVRTTAERTVAREVDRDDEPADELDDAPDENEAPGTEPDASTR

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Crispr_ID: NZ_CP047180_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_3

331715-331817

Orphan

Consensus_repeat	Method
GCGCGCTGTGCTTCCGGGTCTCGATACGCCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_3

>merge|NZ_CP047180|3|331715-331817|CRISPRCasFinder
GCGCGCTGTGCTTCCGGGTCTCGATACGCCGCGTGCCGCGGCTACTCGACCAGCATGGAAGGGCGCGCGATGCGCGCTGTGCTTCCGGGTCTCGATACGCCGC

>NZ_CP047180|3|2|331715-331817|CRISPRCasFinder
GCGCGCTGTGCTTCCGGGTCTCGATACGCCGC	GTGCCGCGGCTACTCGACCAGCATGGAAGGGCGCGCGAT
GCGCGCTGTGCTTCCGGGTCTCGATACGCCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159421852.1\|331926_332763_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_CP047180.1\|WP_123741054.1\|332882_333548_-\|AhpC/TSA-family-protein	unknown	unknown	gnl\|CDD\|239268
NZ_CP047180.1\|WP_127887731.1\|321656_322610_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197666
NZ_CP047180.1\|WP_159423968.1\|342736_343171_-\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP047180.1\|WP_123448078.1\|333745_334027_-\|oligoribonuclease	unknown	unknown	unknown
NZ_CP047180.1\|WP_123706320.1\|330782_331697_+\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_CP047180.1\|WP_159421847.1\|320811_321360_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159421849.1\|325124_327212_-\|amylo-alpha-1,6-glucosidase	unknown	unknown	gnl\|CDD\|225942
NZ_CP047180.1\|WP_159421850.1\|327308_328346_+\|LacI-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224525
NZ_CP047180.1\|WP_159421851.1\|328419_329661_+\|extracellular-solute-binding-protein	unknown	unknown	gnl\|CDD\|270451
NZ_CP047180.1\|WP_159421853.1\|334116_335586_+\|NAD(P)-binding-protein	unknown	unknown	gnl\|CDD\|366721
NZ_CP047180.1\|WP_123448069.1\|323341_323539_-\|DUF3073-domain-containing-protein	unknown	unknown	gnl\|CDD\|378620
NZ_CP047180.1\|WP_159421856.1\|343237_343471_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_123706324.1\|335557_336256_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159421855.1\|340351_342124_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|173803
NZ_CP047180.1\|WP_159423967.1\|322665_323253_-\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|239516
NZ_CP047180.1\|WP_127887723.1\|336404_337193_+\|DUF4184-family-protein	unknown	unknown	gnl\|CDD\|379379
NZ_CP047180.1\|WP_123448074.1\|329676_330786_+\|sugar-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224096
NZ_CP047180.1\|WP_159421854.1\|337772_340076_-\|amino-acid-permease	unknown	unknown	gnl\|CDD\|223605
NZ_CP047180.1\|WP_159421848.1\|323693_324797_+\|NAD(P)-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|224983

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_159421852.1\|331926_332763_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	3.59471e-39
NZ_CP047180.1\|WP_123741054.1\|332882_333548_-\|AhpC/TSA-family-protein	gnl\|CDD\|239268	cd02970, PRX_like2, Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.	2.92867e-34
NZ_CP047180.1\|WP_127887731.1\|321656_322610_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|197666	smart00342, HTH_ARAC, helix_turn_helix, arabinose operon control protein.	4.2002e-16
NZ_CP047180.1\|WP_159423968.1\|342736_343171_-\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	4.04522e-21
NZ_CP047180.1\|WP_123706320.1\|330782_331697_+\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	1.65368e-79
NZ_CP047180.1\|WP_159421849.1\|325124_327212_-\|amylo-alpha-1,6-glucosidase	gnl\|CDD\|225942	COG3408, GDB1, Glycogen debranching enzyme [Carbohydrate transport and metabolism].	6.6838e-73
NZ_CP047180.1\|WP_159421850.1\|327308_328346_+\|LacI-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	8.74778e-72
NZ_CP047180.1\|WP_159421851.1\|328419_329661_+\|extracellular-solute-binding-protein	gnl\|CDD\|270451	cd14748, PBP2_UgpB, The periplasmic-binding component of ABC transport system specific for sn-glycerol-3-phosphate; possesses type 2 periplasmic binding fold. This group includes the periplasmic component of an ABC transport system specific for sn-glycerol-3-phosphate (G3P) and closely related proteins from archaea and bacteria. Under phophate starvation conditions, Escherichia coli can utilize G3P as phosphate source when exclusively imported by an ATP-binding cassette (ABC) transporter composed of the periplasmic binding protein, UgpB, the transmembrane subunits, UgpA and UgpE, and a homodimer of the nucleotide binding subunit, UgpC. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	3.23877e-62
NZ_CP047180.1\|WP_159421853.1\|334116_335586_+\|NAD(P)-binding-protein	gnl\|CDD\|366721	pfam01593, Amino_oxidase, Flavin containing amine oxidoreductase. This family consists of various amine oxidases, including maze polyamine oxidase (PAO) and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.	2.73675e-38
NZ_CP047180.1\|WP_123448069.1\|323341_323539_-\|DUF3073-domain-containing-protein	gnl\|CDD\|378620	pfam11273, DUF3073, Protein of unknown function (DUF3073). This family of proteins with unknown function appears to be restricted to Actinobacteria.	3.9816e-16
NZ_CP047180.1\|WP_159421855.1\|340351_342124_+\|hypothetical-protein	gnl\|CDD\|173803	cd07477, Peptidases_S8_Subtilisin_subset, Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. 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. The S53 family contains a catalytic triad Glu/Asp/Ser. 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. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	1.06869e-35
NZ_CP047180.1\|WP_159423967.1\|322665_323253_-\|NUDIX-domain-containing-protein	gnl\|CDD\|239516	cd03424, ADPRase_NUDT5, ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. Like other members of the Nudix hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue Nudix motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the Nudix motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer.	3.63865e-31
NZ_CP047180.1\|WP_127887723.1\|336404_337193_+\|DUF4184-family-protein	gnl\|CDD\|379379	pfam13803, DUF4184, Domain of unknown function (DUF4184). This domain of unknown function contains several highly conserved histidines.	5.68587e-32
NZ_CP047180.1\|WP_123448074.1\|329676_330786_+\|sugar-ABC-transporter-permease	gnl\|CDD\|224096	COG1175, UgpA, ABC-type sugar transport systems, permease components [Carbohydrate transport and metabolism].	1.14399e-71
NZ_CP047180.1\|WP_159421854.1\|337772_340076_-\|amino-acid-permease	gnl\|CDD\|223605	COG0531, PotE, Amino acid transporters [Amino acid transport and metabolism].	3.26725e-32
NZ_CP047180.1\|WP_159421848.1\|323693_324797_+\|NAD(P)-binding-domain-containing-protein	gnl\|CDD\|224983	COG2072, TrkA, Predicted flavoprotein involved in K+ transport [Inorganic ion transport and metabolism].	1.85862e-31

>NZ_CP047180.1|WP_123706320.1|330782_331697_+|carbohydrate-ABC-transporter-permease
MSTLVDSEPRTEAEPPPQAPLPHRRVQLGARGRASLIGGYLLLIGLALVYIYPFLISVASSFKTDADATSNPLSLLPATWSFASYERLFTDVPLPLWTLNSVIVTVFVTVGRVFFDSLAGYALSRLRFRGRGLLFALFIGVMSVPAVVLLIPRFLILKQLGLYDSYAGMIVPLIVDAAGIFIMKQFFDSIPLSIEEAARIDGAGVFRTFRSIVVPMARPAIVTLFILSFQGSWNEFSHFVVSRQSPELNTLTTGVASLVSGQLGTGNQYPLQLAAAVLMSIPVAVLFFVFQRRIMNTTEGAEKG
>NZ_CP047180.1|WP_123448074.1|329676_330786_+|sugar-ABC-transporter-permease
MSTATASRSRRSGIRGNEARYGWLFTLPAILVVGVFLVVPIALALWVSVSNWNGLGSPLGPTAQFVGTDNYRAVLLDSGLAQKDFGTAIRNNVYYVLLVVPLQTALALFLAVQVNRRVLRGRGFFRTAFYFPSVTSSIAITVIFLFLFSASGVVNAVLGWFGADGPTWMADPTGVLHSLLGLVGVDGAWFAGGAPLGLTWWDWLSGPSVAMCVLITMAIFTTSGTFMLLFLAALQNIGAEIDEAALMDGAGPLRKFFSVTLPMLKPTLFTVLTLGLIGTWQVFDQIYLTGGGAPGKTLLTPAYLAYESSFTDLRWGQGAAIAFILFFIIVVLTLLQRAILREKGEPSARRTRRAARADAATTLTTGGVR
>NZ_CP047180.1|WP_159421851.1|328419_329661_+|extracellular-solute-binding-protein
MTHSTRTARWGAAVLAGGLALSLGACSSGGGGSDDSAGLTVMIGSSGDAETTAVTDAVNSWGEANDTAVDVVAASDLTQQLGQGFSGGNPPDLFYMSWDQFQTYASNRYLEPYAQDADDADAFYPALRDAFTYDDQFYCEPKDFSTLGLVINTDLWAAAGLTDADVPTDWASLQSAAQKLTANGVTGLSFGPEYARIGTFMNQAGGSLLSEDGTTVTADTPENVAGLTEVKTLLSDGVLKFPADLDSGWSGEAFGKGAAAMVIEGPWINGALEADYPDVNYTVAELPAGPGGKSTFTFSNCWGIPAGSTTADQAESLVASLTSDEQQLAFSDAFGVIPSTESGAAEYASKYPENAAFVTGNDYAVSPVAFAGAATVITDFNSALEGLASGDPEAILADLQTNLQDALDTANAK
>NZ_CP047180.1|WP_159421850.1|327308_328346_+|LacI-family-DNA-binding-transcriptional-regulator
MALPTVEDVARAAGVSRQTVSNVLNSPQIVRESTRERVEKAIGDLNYRPHASARRLRTRKSGTIGVRMDRVLDGVSGSLLDRFLHAVTEQADARGMRILLYTAASPEEEIERIGKLRDGADVDAFVLTSTFYGDQRTAWLIEQGVPFVTFGRPWGLDDQGDPQHLWVDVDGAAGVAQATAHLADEGCSRIAFFGWPDGSATGDDRRNGWERVMAERFAGVPLLVAEAEDDVQRARSAAIAFLEAHPEVDGLVCVSDSLALGASMAAVAVGRPSLAIVGFDNTPVAGAVGLSSVEQDLGAVAAGALELLLGEQGDDVVHRPLAPGEAHRLITPHLVVRTPLHHSES
>NZ_CP047180.1|WP_159421849.1|325124_327212_-|amylo-alpha-1,6-glucosidase
MLPAATALSTGRTLQYRRSSEESTVTTDHDDRPRPPRQPLLNDAVVLLRAPTQLWSDDAGELGALPAHGLYHGDVRVLAGLRLLVGGEPLESIAVGRDGASSARFTALARHLDDDAADPRLRVVRLRTVTAGGLEERIRLESALPDAVATTVELALDPDFSLVHVVKAGLRDETAVATAVDDSSLVWTHAGARAEVRAEGAAVSPGGTLSWDVVVPARGSVEVAWSIAMTDSAAVVGAAPGPAEWADAVVEAGDSRLASWCRAALDDLDALRMVTLERPDAPFLAAGAPWFFTLFGRDSIWAARMLLPLGTELAASTLRVLAGLQGTEHVAETAEQPGKIMHELRSTTLEIPGEGVSLPPLYFGTVDATALWVCLLHDAWRWGLADEEVEALLPALEAALRWLRDEGDSDGDGFLEYVDTTGHGLANQGWKDSGDSIQWRDGSLADGPIALCEVQAYAHEAAVGGAALLEHFGRDGAEWRAYAAALKDRFTGAFWIDDADGGHPAIALDAAKRPVDTVTSNIGHLLGTGILQPEQAARVAQLLGSPELDSGYGLRTLSTDSGGYWPLSYHGGSVWAHDTAIAVAGLAREGFGAEATALSRGLLAAAEGFGYRMPELHSGDAAAEVAAPVPYPAACRPQAWSAAASIAVLSAALGLAPGGSTLVVAPITPPLADSIRVDGIRYRGSVVPIDWRDAH
>NZ_CP047180.1|WP_159421848.1|323693_324797_+|NAD(P)-binding-domain-containing-protein
MGSTVDSALDPRPVVVVGAGQAGLSVAYYLRRLGLRPGVDFVVLDRGPRAGGAWQFRWEALRLGSAHRVHDLPGMDRLGLSFATADRRRPARDVVTEYYEAYESAYELAVRRPVAVRGVSSATIGDRTAPLVVETDAGSERARILVNATGTWGSPFLPYYPGRDGFEGVQIDTTEYLRAADFAGQQVIVVGGGTSAIGFLLELERVARSLTWATRRPVVYRDGEQLALESAVEAVAEQDRAARAGRALPSIVGGTGVQRTRRVVAGIERGVLHERGMFSSIEPHGVRWPDGSYTRADAIIWATGFRPELRHLAPLGLREREGGVAVEDGASLTDPRVFFAGYGPTASTIGANRSGRRIARAVVARLS
>NZ_CP047180.1|WP_123448069.1|323341_323539_-|DUF3073-domain-containing-protein
MGRGRQKAKNTKIARELKSFSPTVDYSALERELSHPDEPDYSKWIDDEDEGDDTDLVEEQHQKRA
>NZ_CP047180.1|WP_159423967.1|322665_323253_-|NUDIX-domain-containing-protein
MPEQPAFPEHSGQHGRVEQLSTRIAYETPWIRVREDEVRWPGGVEGVYSVVERADYALIIPRERDGFWLVEQYRYPIGRRTWEFPSGGWPHDSPGGDAEALARAELREETGLRAGRLRPLGRLSEADGFVAQSFDVFLAEDLEHGEPEREETEQDMRQQWFPDAEVAAMVRSGAIVGTSDVAALGLFWLDRGLGS
>NZ_CP047180.1|WP_127887731.1|321656_322610_-|helix-turn-helix-transcriptional-regulator
MKPASAPSPVWHSETRGRDLDEARAFYSRGYNGSGFRAEHTRIPFAYRYASTGPGPVSLHAASFLGSVRGTVEPTGVYVVLWLNDGRASLDLGRDENRLVAGRPAMFPSGRPFGFETSEYRDALVHFDSAYLERAAAERHGTAPGPIRFAPLAHSPAPWWAAVRVLRDTLTGVKAPSSLQRESASQVAAAAVLQAFAHRVVPLPSAPHSVSARRLRRAVEFVHANADLPLGVADIADAAGLTVRGVQLAFQRAYSMTPRQYLRGVRLDLAHDELVAGGPQTLVVGDVAAHWGFISGGRFAQHYTQRFGELPSETLRR
>NZ_CP047180.1|WP_159421847.1|320811_321360_-|hypothetical-protein
MFEPEGSARPVARIMSVTAALLIGAVLVGGAVGAAVALALYLPSALAAGALDPSALVGFGMLMGVASGAGLGAVGGLGAIAGMVTVRAMSRRSGAFIAGTSVGAAFGVLVLAANLLVSRDAATWITALLATAAAFLLCAWGSWLLTRREHSWERAHAPERRRPPAQSAAPGAPSPASRHRPA
>NZ_CP047180.1|WP_159421852.1|331926_332763_-|alpha/beta-fold-hydrolase
MAEITAHHGLFKDTDLHVDDTGGSGRPVVLIHGWPLSGESWSEQVPAFAAAGFRVITYDRRGFGRSDKPLTGYTYDTLTEDLHTLLTELDLQDVTLVGFSMGGGEVARYFSKYGTERLHSVVFASAVPPYLMKTDDNPDGPLEKSAGAEMTAGLTKDEDSFYEQFTTEFFSVNGELKVTEAQRQDALALAKQSSKHAALACMAAFAGTDFREDLPKVTVPTLVIHGDGDGTVPFEGSGARTHAAIPGSELHVVAGAPHGVNVSHAEEWNRVVLEFLKK
>NZ_CP047180.1|WP_123741054.1|332882_333548_-|AhpC/TSA-family-protein
MPTEQTTATIGAQTADFTTGFNETIGDELATVFASEQADLVENGVPAGAVAAGERLPSATVVTEGGESVALSSLLGDGPAVLVFYRGAWCPYCNITLRHYDATLAPELASRGIAFVAVSPETPDASATLGGELGFTVVTDPGNALATELGIVTAPSDAAIEAHTALGFAVKDSNADDTPAIPFPTVLVLDAEGVVRFADVHVDYTTRTETEAILAAVDALS
>NZ_CP047180.1|WP_123448078.1|333745_334027_-|oligoribonuclease
MSNDIRELSEGESYLAFFQGGPFDGQTETRVSTEGGYEKSVDVYAAVDGQETHLVYTSVSAKEVGESVHVTYALDAPDSDPVEDPEDRGGGFQ
>NZ_CP047180.1|WP_159421853.1|334116_335586_+|NAD(P)-binding-protein
MTIGRRLFLSGAASGAGLLVLAGCTPPRPTPTRSVTEAPVPTPSTTAVPTPAAFVRSGWAEDPYALGAVSYLAVGATPEHRDDLAGNVLDRLFFAGEATDSEEPGTLQGAWNSGVRAAGEIAAIAEEGERIAIIGAGLAGAVAARRLLDAGYDVALVEARDRVGGRIATSTPDGWPIAVDSGAWALVGAGPALRESVLDAGITTSAVDLATVLSSTEDGDRPDVGDTAAKALTRALEWAAEQPTDLPLADAFAGSGAPDPAAVEPGSGDGDAARVAAFLAGGPVLRTGAAPAELSAWYGLGDASAASTAEDVADSSDEAAAVLTDGLAPLVETLLTDVEISLRAAVSGIGYSDTGASIRLATGESFTADRVLVTVPIGVLQSDAIAFDPPLPFAHRTAIAAIGSGVVETLWLRFDEPFWDTDPALPARWSLVGSAAGITEWLNLEPTTGEAVLVGLVGADQALSLQSLSDDELLVVAQSALTPFAVAAG
>NZ_CP047180.1|WP_123706324.1|335557_336256_-|hypothetical-protein
MRKAFAILRLALAGLGAVGLVGDFLYTLGFRLFQIDNFFAYFTTQSNMAGVVVLGLSGIVALAREREPRWLSTLRALVLTYMVVSGIVFGLIAVEANNRGVRVDVPWSSALLHFVIPTLALLDWLLAPGRRPVAWRGTLTVLGFPIVWGVITLVRGALIGWYPYFFLDPAQVDGPVMFVVYDVIVLGLISGIAAFMLALSRVRPLGAARATEWRGPLARLRERLSRQRRRTA
>NZ_CP047180.1|WP_127887723.1|336404_337193_+|DUF4184-family-protein
MPFTPSHAVVALAFTNSRIPAAAVAIGAMAPDIGLYLPLRWARDATHSMLGIVTVDLAVGAVGLVLWLVLLQPAWRDLAPWIVRVRLRPPPAPPSTARARTTAIVLAMVGIVIGAASHVLWDAFTHDGGPFVAALPFLREELGPFAGYKWAQYASGVLGLVGLGIGALVWYVARRPHHVAVDHRGPARVAAWTAVLAAAVVPAGVVLSGSGLDPFEEAYRSYVVDAAVLVVVWTTAALLAVAVLWHLALGVAPRQGADADPS
>NZ_CP047180.1|WP_159421854.1|337772_340076_-|amino-acid-permease
MGTSLEPLARQLRKCPVTARVQPSRGGRPGGLTAPGHGVVSSLVTHEGPPSGAKASPTGADDADANELRTAKHFFIGEPLSSDKLEGQLLQKRLALPIFASDPLSSVAYAPQELLMILLLGGLSFLTFAPWVAGCVVVLLVVVVLSYRQLIKAYPSGGGDYEVARTNLGETAGLTVAAALLVDYVLTVAVSVASGVDNIISAIPALAPLRVELAILFVILLAAVNLRGVSESSKAFAVPTYLFVASVFVMVVVGLGRAAFGDAPIAESAGYTVQGEQLTQAAIVLLLLRSFASGCAALTGVEAISNGVPAFRVPKVKNAQRTLVAMGTIAIVLFVGLTALALLANVHYAENACHLVGFTDCATTPQRSVIAQVAAATFGNNTILFFVIQAATAAVLLLAANTAFNGFPLLGSVLARDGYAPKSLNTRGDRLIYSNGVIILALVAAIILLVYQASLTSLVQLYIIGVFVSFTLGQSGMVKHWIRMIKNGEGSRTVKTSLAINLFGATLTFAVLVVVTITKFTHGAWLVYLVMPILGVLMAGVYRYYRDVEKEIEVDPTTTFGANGDHAVVLVGRMNKPTLKALDYAIAARHESLEAVHSSIDDAQTAQLKADWARMDIEVPLRCIASPYRDISYPLIKYIKAHRLEHGSEIITVYMPQYIVGHWWEGFLHNHKSRRIRQKLLLVHGVTVALVPWLLDSSELIYGRRSRPIPGQSRRGEPVRPVTRRPIPPASVLPKGAAGEGAPRSGSRTAAATRPKKPAGKGGGKRR
>NZ_CP047180.1|WP_159421855.1|340351_342124_+|hypothetical-protein
MSTSRTAAPPARSRLWRAAGLATALAVTAGIALAGSAPAQAATTGQYLVSVDSSSISEQVVRALGVADDVQFEGGVAGFTAPLTERQKAVLEADSRVLGITPADQVVDGQAQTVPSHVLTAEADKAPVRAGDGVTNYSGPAVAVIDSGVSSHPDYNLKEQINCFGSGTAADANGHGTGVSGYMAALDNGSGSVGVAPGAPIYSVRALDANNRGNTGTLMCALDWVSANAAKYNIKVVNMSLATYGTDDGNCGRSNGDVIHQAICDLEAKGIVSVGSAGNTSEDLAGWIPAAYDEVLAVTNMANYDGKPGGLGTAPCGVQTKDDAVSTNSNFAVTAADQKHTIAAPGMCPYTTKKGGSYAYIQSGTSMAAAGTSGVVLDCMSSGGSCAGKSPAQVRAQVIAQAKAATERGRTFQGDPTRPVAGRYFGYAVSTIPVGTVPTPDPTPTATPTPTATPTATPTATPTSTPKPTATPTSTPKPTATPTPTATPTTPPAADTQKPTVSITSPATNTTVVGSIRLVASASDNVGVTAVAFYASGTKLGNGVKQSDGTWALTASSSAYPNAAYQVTAKAQDKAGNVTTSSAITLRVAN
>NZ_CP047180.1|WP_159423968.1|342736_343171_-|MarR-family-transcriptional-regulator
MDTDPLALQNQVCFSLAVAARTVIGLYRPVLDPLGLTHPQYLVMLALWERAPRSLADLGAALHLEPATLSPLVKRLESAGCVTRARSTEDERRLDVALTPSGAALRERALQVPPQIVERLDLPLDELTAVRDALTRLIGAATRP
>NZ_CP047180.1|WP_159421856.1|343237_343471_+|hypothetical-protein
MPKPTRSLYQRFNARLFPWLGPPPLGPYDQPEPEAPAGRACPLCGRLMSEHVIDRSGPRTQLYCPGTDPAADPGAAA

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Crispr_ID: NZ_CP047180_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_4

394916-395007

Orphan

Consensus_repeat	Method
GCCCCGGAGGGGCGTATCGAGACCCG	CRISPRCasFinder

1 spacers

csa3

The CRISPR arrays of NZ_CP047180_4

>merge|NZ_CP047180|4|394916-395007|CRISPRCasFinder
GCCCCGGAGGGGCGTATCGAGACCCGACGTCAGCATGATCGGCTGCCCTCCCCTGCTGGTCGAGTCGCCCCGAAGGGGCGTATCGAGACCCG

>NZ_CP047180|4|3|394916-395007|CRISPRCasFinder
GCCCCGGAGGGGCGTATCGAGACCCG	ACGTCAGCATGATCGGCTGCCCTCCCCTGCTGGTCGAGTC
GCCCCGAAGGGGCGTATCGAGACCCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159421886.1\|393876_394611_+\|RES-domain-containing-protein	unknown	unknown	gnl\|CDD\|378053
NZ_CP047180.1\|WP_159421882.1\|390125_390962_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|375319
NZ_CP047180.1\|WP_123446985.1\|402977_403100_+\|50S-ribosomal-protein-L36	unknown	unknown	gnl\|CDD\|179138
NZ_CP047180.1\|WP_159421892.1\|401868_402930_-\|cobalamin-biosynthesis-protein-CobW	unknown	unknown	gnl\|CDD\|214844
NZ_CP047180.1\|WP_159421887.1\|396545_397355_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213260
NZ_CP047180.1\|WP_159421878.1\|386221_387337_+\|ROK-family-protein	unknown	unknown	gnl\|CDD\|224851
NZ_CP047180.1\|WP_123447078.1\|385435_386194_+\|carbohydrate-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223472
NZ_CP047180.1\|WP_123446984.1\|403133_403415_-\|helix-turn-helix-transcriptional-regulator	csa3	COG0640_csa3_CAS-I-A	gnl\|CDD\|238042
NZ_CP047180.1\|WP_159421890.1\|400243_400651_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|100004
NZ_CP047180.1\|WP_159421883.1\|390930_391887_-\|EamA-family-transporter	unknown	unknown	gnl\|CDD\|273359
NZ_CP047180.1\|WP_159421891.1\|400719_401700_+\|adenosine-deaminase	unknown	unknown	gnl\|CDD\|238645
NZ_CP047180.1\|WP_159421885.1\|393484_393880_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159421881.1\|389342_390023_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|187585
NZ_CP047180.1\|WP_159421888.1\|398166_399027_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223673
NZ_CP047180.1\|WP_159421889.1\|399035_400247_+\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|238624
NZ_CP047180.1\|WP_159421880.1\|387998_389255_-\|FAD-binding-protein	unknown	unknown	gnl\|CDD\|273751
NZ_CP047180.1\|WP_159421884.1\|391977_392868_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176102
NZ_CP047180.1\|WP_159421893.1\|403752_404415_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224046
NZ_CP047180.1\|WP_132436735.1\|395409_396474_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|378117
NZ_CP047180.1\|WP_159421879.1\|387477_387876_-\|cation-transport-regulator-ChaB	unknown	unknown	gnl\|CDD\|377614

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_159421886.1\|393876_394611_+\|RES-domain-containing-protein	gnl\|CDD\|378053	pfam08808, RES, RES domain. This presumed domain contains 3 highly conserved polar groups that could form an active site. These are an arginine, glutamate and serine, hence the RES domain. The domain is found widely distributed in bacteria. The domain is about 150 residues in length.	0.00172095
NZ_CP047180.1\|WP_159421882.1\|390125_390962_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|375319	pfam17765, MLTR_LBD, MmyB-like transcription regulator ligand binding domain. This domain is found in a family of actinobacterial transcription factors. The structure shows it has a PAS domain like fold and it is bound to Myristic acid.	9.38947e-41
NZ_CP047180.1\|WP_123446985.1\|402977_403100_+\|50S-ribosomal-protein-L36	gnl\|CDD\|179138	PRK00831, rpmJ, 50S ribosomal protein L36; Validated.	3.69265e-11
NZ_CP047180.1\|WP_159421892.1\|401868_402930_-\|cobalamin-biosynthesis-protein-CobW	gnl\|CDD\|214844	smart00833, CobW_C, Cobalamin synthesis protein cobW C-terminal domain. CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.	7.55368e-17
NZ_CP047180.1\|WP_159421887.1\|396545_397355_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213260	cd03293, ABC_NrtD_SsuB_transporters, ATP-binding cassette domain of the nitrate and sulfonate transporters. NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.	1.43144e-107
NZ_CP047180.1\|WP_123447078.1\|385435_386194_+\|carbohydrate-ABC-transporter-permease	gnl\|CDD\|223472	COG0395, UgpE, ABC-type sugar transport system, permease component [Carbohydrate transport and metabolism].	2.22595e-78
NZ_CP047180.1\|WP_123446984.1\|403133_403415_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238042	cd00090, HTH_ARSR, Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.	3.83435e-15
NZ_CP047180.1\|WP_159421890.1\|400243_400651_+\|hypothetical-protein	gnl\|CDD\|100004	cd00448, YjgF_YER057c_UK114_family, YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.	4.2921e-19
NZ_CP047180.1\|WP_159421883.1\|390930_391887_-\|EamA-family-transporter	gnl\|CDD\|273359	TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter. [Transport and binding proteins, Amino acids, peptides and amines].	3.56609e-12
NZ_CP047180.1\|WP_159421891.1\|400719_401700_+\|adenosine-deaminase	gnl\|CDD\|238645	cd01320, ADA, Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.	2.6644e-125
NZ_CP047180.1\|WP_159421878.1\|386221_387337_+\|ROK-family-protein	gnl\|CDD\|224851	COG1940, NagC, Transcriptional regulator/sugar kinase [Transcription / Carbohydrate transport and metabolism].	2.44039e-42
NZ_CP047180.1\|WP_159421881.1\|389342_390023_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|187585	cd05324, carb_red_PTCR-like_SDR_c, Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs. PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	1.90004e-62
NZ_CP047180.1\|WP_159421888.1\|398166_399027_+\|ABC-transporter-permease-subunit	gnl\|CDD\|223673	COG0600, TauC, ABC-type nitrate/sulfonate/bicarbonate transport system, permease component [Inorganic ion transport and metabolism].	2.70932e-35
NZ_CP047180.1\|WP_159421889.1\|399035_400247_+\|amidohydrolase-family-protein	gnl\|CDD\|238624	cd01299, Met_dep_hydrolase_A, Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.	6.58896e-68
NZ_CP047180.1\|WP_159421880.1\|387998_389255_-\|FAD-binding-protein	gnl\|CDD\|273751	TIGR01678, D-arabinono-14-lactone_oxidase, sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.	1.10586e-42
NZ_CP047180.1\|WP_159421884.1\|391977_392868_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176102	cd05466, PBP2_LTTR_substrate, The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the type 2 periplasmic binding fold protein superfamily. This model and hierarchy represent the the substrate-binding domain of the LysR-type transcriptional regulators that form the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, oxidative stress responses, nodule formation of nitrogen-fixing bacteria, synthesis of virulence factors, toxin production, attachment and secretion, to name a few. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	1.1404e-25
NZ_CP047180.1\|WP_159421893.1\|403752_404415_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224046	COG1121, ZnuC, ABC-type Mn/Zn transport systems, ATPase component [Inorganic ion transport and metabolism].	2.52463e-66
NZ_CP047180.1\|WP_132436735.1\|395409_396474_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|378117	pfam09084, NMT1, NMT1/THI5 like. This family contains the NMT1 and THI5 proteins. These proteins are proposed to be required for the biosynthesis of the pyrimidine moiety of thiamine. They are regulated by thiamine. The protein adopts a fold related to the periplasmic binding protein (PBP) family. Both pyridoxal-5'-phosphate (PLP) and an iron atom are bound to the protein suggesting numerous residues of the active site necessary for HMP-P biosynthesis. The yeast protein is a dimer and, although exceptionally using PLP as a substrate, has notable similarities with enzymes dependent on this molecule as a cofactor.	4.91053e-39
NZ_CP047180.1\|WP_159421879.1\|387477_387876_-\|cation-transport-regulator-ChaB	gnl\|CDD\|377614	pfam06150, ChaB, ChaB. This family of proteins contain a conserved 60 residue region. This protein is known as ChaB in E. coli and is found next to ChaA which is a cation transporter protein. ChaB may be regulate ChaA function in some way.	1.74242e-15

>NZ_CP047180.1|WP_159421886.1|393876_394611_+|RES-domain-containing-protein
MTPQLVVARDPGEVWRVGYRPRPWDWADWRYATDHGRFNGRWDDQLAEFRTLYTGESLEACLFEVLAHFRPEPGIDSELDEIVDADGWVELFPDAAAGTVGRGWAADRMVGTARQTGSYCFITHSESLGAVQASFPFERFGLTPCLLDASVVKNPDHRDLTRSIARWLFDEPGPDGRDAALDGVAFRSRFGDELRLWAVFERPEDAEEGASHCLLGRSEAPLDVEAPELSRVFAVHGIRWADDS
>NZ_CP047180.1|WP_159421885.1|393484_393880_+|hypothetical-protein
MSAVAGTQKPGLRAHQEATRASVPELVTGLREIVGVRLVAYLGNVKSTRAVAEWADGARKPGETDVDRLRLAYQVAILLREQNEAVTVQSWFKGMNPALGDVSPARVLREGAPDAVGPDVMGAAKAFAFVG
>NZ_CP047180.1|WP_159421884.1|391977_392868_+|LysR-family-transcriptional-regulator
MDPARLRLLRELGDRGSVAAVAAALGVSPSAVSQQLAALQAGVPVPLTVKEGRRLVLTEAGEALAVAGTRVEEALAEAANTIGSFLRHDDRAVRVSAFHSAGLAFFGPLLAALADGPRVALADADVAQSRFAGLTADHDLVVAHRLPQDPEWPRARLVVTPLLVEPLDIALPAAHPLAAQSSIRPEQLADEQWVSTHEGFPLTGVLEHLGALIGRAPRVAHRINEFSVAAQVVRSGAAIAILPRITAAPLAVDGMVLRPLEGAGLVRHVDVLARPDALARTAVRTVLAALRRVAAA
>NZ_CP047180.1|WP_159421883.1|390930_391887_-|EamA-family-transporter
MPLRSRPDLAVDLLLLAVAAVWGASFVAAKDVAADIGVPSTVALRFLTAAAALALLCLARRERLPHGRGLAVAALLGASQAAIIGLETWGVHLTSATNAGLLISLALVLTPALEGLASRSWLPRSFFVTAVAAVVGVALLVSDGGLRTPTWGDALVLAAAVVRAVHVTASARLVRGRAEGSLGVVLVQLVVCAAVFSLLAGPDLPAAARALDAGGWAGVLFLGLLCSVFAFVVQLWAVRRTSAARASILMGTEPVWALLVGVVVAGEAIGPLGAVGAALIVAAGYAGQAIERRHRLGASTPADRSADPVSAPRAPAAP
>NZ_CP047180.1|WP_159421882.1|390125_390962_+|helix-turn-helix-domain-containing-protein
MSEFADVLRSWRERVTPAEVGLPAGPSRRTAGLRREELAALAGVSVDYIVRLEQGRAVHPSAQLLGALACALRVTEAERDHLYRVAGVAPPTATQVPQHITPGVQRIVDRCGDVPLAVFSAAHDILLWNPLWAALNGDPSRHTGLDRNLVWRYFTQGHEGTEFDDQHAEDFANDLAADLRAAVGRYPDDAALAHLVARLRATSPDFERRWAVARVAEHRSSRKTVTSTPVGPITIDCDVLAVPGGDLRIVIYTATPGSTDQTRLDLLRVTGLQELVAR
>NZ_CP047180.1|WP_159421881.1|389342_390023_-|SDR-family-NAD(P)-dependent-oxidoreductase
MTTTLITGANKSLGLETARRLIEAGHTVYAGMRDPAKGDAVRALGAQVVQLDVTDQSSVDAALASLPALDVLVNNAGILGTSFGVDDLSAEAMASVLETNVVGIVRVTQAALPLLRRSAAPVVVNVSSGVGWPRALVTPGRDEFGVPAIPYAASKAAVITLTVQYAKNLPEFRINASDPGYTATDFNGHSGHQTVTEGTDATVALALLGPDGPTGEFHDRHGRIEY
>NZ_CP047180.1|WP_159421880.1|387998_389255_-|FAD-binding-protein
MTQRSNWAGTYEYRAADILEPESIDEVQNLVRENERVRALGTRHSFNALPDTPGALLHLGRIAPDPVIDADASTVTVGGATRYGIVASHLHSNGYALHNMGSLPHISVAGAISTGTHGSGDRNANLSSAVSALELVTADGSLRTIRRGEPGFEGVVVGLGAFGVVTRVTLDIQPTFDVRQDAFVDLPWDRVLDDFDAITSSAYSVSLMTHWSSPTVEQLWLKTKVAQGSVADVDATHLGAVAASASLFAVSEGVDSNLNPFGGSVGPWSERLPHFRLDREPSAGDEIQSEYMVPRENIREALVALRAIGERIDEVLLITELRTMAGDDQWLSPASGRDSVGIHFTFKKDRAGVDAVLPAVEGALLPLGARPHWGKHFLATAADIAPLYPHLDEWRTLRSAWDATDRFASAFVQDRLLG
>NZ_CP047180.1|WP_159421879.1|387477_387876_-|cation-transport-regulator-ChaB
MPAKEEIPSTIERSDEHAQKLWSAAHDSAVDSYGEGERAHRTAFAALKHEYEKVGDHWERKAESGPSDDRAAQRGPDGDGDTAGGVDANASKAHLLDLAKRLDVSGRSRMTKAELVDALQRANAKQTRRARD
>NZ_CP047180.1|WP_159421878.1|386221_387337_+|ROK-family-protein
MGQLRVTEKALPSHNRRHNRSLVLQRLFHDGEMSRADLARISGLTAVTISDLVGELHSEGLLLDLGPRVDARVGKPALVIAFDHGARSIVGLDLSAEAQCTGALVSLRGEIREHRRLARDGASGADAVELALGLAAELIASSQAPVLGIGIGSPGVVDHGGVVREAPNLGWRGLDLRRVFAERFGLPVHVANDANTAALAVHTFHRGGGANLLLVLLGDGVGAGLIIGGSLVEGDQFTGGEIGHVVIDEDGEQCSCGRRGCLESAVSVAHLGPRLAAASAPEQERLLRRAGRSLGIALAPIVAVLGIDAVVLAGPERFVEGVLLEEARATIARRTLPAVTRELRMESRTDPGELVLQGAAALVLSHELGIS
>NZ_CP047180.1|WP_123447078.1|385435_386194_+|carbohydrate-ABC-transporter-permease
MVNTAFKPQSEMLSSTPHFLPESPTLDNFVRALTQGDFLRHLQNSVVVVGAAVVFAMVLGLFAAAALARFRFRGRRAILVLLLVVQMLPATALLLPQFLLLNAVDLIGTSAGLALAYVAGVLPFSIWVMRGFFLALPVELDEAARLDGASTWQLLTRVLFPLVMPGIVSSSVFAFIAGWNDYIVAYTFLKDQARYTLPVWLASFSTASGGQVGTDYGGQMAGAVLFSLPVVVFFLIIQRNLVSGMSAGAVKG
>NZ_CP047180.1|WP_132436735.1|395409_396474_+|ABC-transporter-substrate-binding-protein
MPRTAPSRSRLRSVLGVLAVAVVAGTTLAACSNGSDAAESGDAGSFGEATMQLSWVPHVEFAGEYLADANGYFADAGFDSVTLTPGGTGATGAETAIASGSAFAGVSSPLITGPAISEGAEMKIVGATYQKNPFAIVSLTDAPIETPEDMVGKTIGVSDSNDLVWRAFLAANEIDEDDVTRVPLTDSTLLTTGQVDGYIGYATAGANTLNQRGFSAQQFLLADTGLPMVGETIVVAQESIDDDREKVKALLYAVARGWQDAVADPDATAATVVADYAADQNYKVEEQAQVMVTQTELISTPDTDANGLLTITPQLQDESVASLALTGIELDADELFDTTLIDEVYEEHPELLEG
>NZ_CP047180.1|WP_159421887.1|396545_397355_+|ATP-binding-cassette-domain-containing-protein
MTEQATTTENEGIRLSGLSKRFDLGSRSVQALAEVDLVTPRGSFLSLLGPSGCGKSTILRMLAGLEKPTTGSVSIHGTPVLGTKRSAELGIAFQDSALLPWRSVRSNVRLPLELTRQAAKRDSIPDLLDLVGLTGFEDAYPSQLSGGMRQRASIARALVVQPDLLLLDEPFGALDDMTRQRLNLELQRIWTARPATTLMVTHGIAEAILLSDTVAVMSPRPGRIVEVIDIDLPRPRTVEMLRSPEFHAIEDRITDILFSQHGVAMEDEA
>NZ_CP047180.1|WP_159421888.1|398166_399027_+|ABC-transporter-permease-subunit
MSTATRTPSSSSSTRAARRPSDLTGRMVLRIVRGELVPLAVAAVLALAFWYAFLAITDISPLLGKTPTDVAEYLFVEADAAENRAIVFGNLGVTAVDALVGYVAGLLVALAIAVLFVLIRSLEATVMPIAMLLKSMPLIVVTPLVTLAIGNGIGAVATVGAIAVFFPALVTVGFGLRSLSRESFELVSVYGGSPLDVLLKVALPTAVPAIFAAAKVAVPSALSGAMLAEWLATGQGLGGAVQRASAGFRYDELWASLAVITALGVVAYAVVAIGERLAAVRFGGQN
>NZ_CP047180.1|WP_159421889.1|399035_400247_+|amidohydrolase-family-protein
MSTTTSITGAVWDGTRALGTATLAWSGDAIASVEPADGPSVERGSGEFSIIPGLVDTHVHLGAYSGAGTADFASWPLVTPREERVFHIANNARKAARAGVTTLRDLGADELQMTVARMFEQGIAEGPRIVTHGAVGMTAGHGDLFVPPHYPHRDRVADSPDECRRLVRTWARAGADGIKIYTSGGVLSMGDKVGWRNQTDEEIAATIDEAHALGMPVAAHTHSEVGLDRALALGVDSIEHGTAIGPQHWATLVERNLPVAPTLFINDVIAAGRAPSSPEASLKAQDVVAVRDAGFLAAGQAGVRFVLGTDANGVYVDWGEQLDEVRRMRESFGWSSERALVAATSDAAAVVGLGAKVGRLAPGFGADFVVLRGRPWESIDDLRAESIVAVVSRGRVVSGELPR
>NZ_CP047180.1|WP_159421890.1|400243_400651_+|hypothetical-protein
MTATATRRFVTAEALGAPRGAYSHAVEAHGVVYGSAIGPFAPGDGSVPEGTLPEGISAQTGAALDNIERLLATEFGLGLGDVVRVTMILSDFERDFAAASEVYGARFAVDPPARTVIGAVLPGPLVALDFIAARP
>NZ_CP047180.1|WP_159421891.1|400719_401700_+|adenosine-deaminase
MTSDSFLLGLPKVELHVHLEGTLEPELRAQLAERNGLPVPAALAYDFDSLASFLAVYYPAMDVLREEQDFYDLATAYFRRAAADGVVRVEAFFDPQAHTSRGVPFEAVIGGYHRAAQDAAQLGVDAALILCFLRDLSAESAAETLERALPFADRLIGVGLDSDERGNPPAKFREVFARAREAGLRLTMHCDVDQPNGVEHLRQVLEEIGVDRIDHGTNLVEAPELIDVLVERGLALTCCPLSNSFVSSDSKAAEMRALLERGVRVTVNSDDPAYFGGYIADNYAALADMGFTRDELVQLARNSVLGSWASETSKAELLARIDAYAG
>NZ_CP047180.1|WP_159421892.1|401868_402930_-|cobalamin-biosynthesis-protein-CobW
METPSPLPRPPVLAVTLVSATDAAHSARIARQLSGGVTSVESFAVDLPDSDSAEFAAELADELARQADDGENGITVISLDPVADPMEVALVLEHLCVRRHPGDTRIGVLDVVAVTSVDEVTRVLLGEGAEQGSEQEPPQWDRAERLATRLEFAGLIVLTDGDGAGASPAVDLLRALSPGAEILTERDLDRYRQRRAVLAPQRAHRLASDLGWQRALRGVPGDAGSVTTFVFRDPLPFHPGRLNTAVADDFVAHRVGRILRSRGLVRLASRADRIASWSIAGDVLSLDPTAIRSWSTDAPVGQEIVFLGRDLDVDELTRVLHGCLLTPRELLAGPDLWRTLADPFPRWEDEHQH
>NZ_CP047180.1|WP_123446985.1|402977_403100_+|50S-ribosomal-protein-L36
MKVRNSLKSMKSMPGSQVVRRRGRVFVINKLNPRFKARQG
>NZ_CP047180.1|WP_123446984.1|403133_403415_-|helix-turn-helix-transcriptional-regulator
MTEDLEPAAELFKVLSSSSRLRLLRALASERSTVGHLAETTGLSQPLVSQHLRTLRAAGLVAVERIGREAHYSVADTHVSHIVDDAVRHALEG
>NZ_CP047180.1|WP_159421893.1|403752_404415_-|ATP-binding-cassette-domain-containing-protein
MSSSQQPSSRVSLRGVGVDFGERVALDDVDLDLPPGTLTVVGGPNGAGKSTLLEVIAGTRRPSRGVRTVSSAIAFVPQRTAVSDRLPVTVRDVVTVGVWGRTGRWRRVGPDLRAVVAAAMERLEISGLAAEPFAVLSGGQRQRTLLAQGLARGADLLLLDEPTTGLDAASAERIREILRAEAERGVAVVCVSHDPAVIALADRVVQLADGRLRGEGALAR

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Crispr_ID: NZ_CP047180_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_5

649842-649936

Orphan

Consensus_repeat	Method
GCGCGGGCTACTCGATCAGCATG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_5

>merge|NZ_CP047180|5|649842-649936|CRISPRCasFinder
GCGCGGGCTACTCGATCAGCATGGATGCGACCCTGCCCTGCGCGGCCGCTCAGCATGGCTGCCGCCCTGTCCGCGCGGGCTACTCGATCAGCATG

>NZ_CP047180|5|4|649842-649936|CRISPRCasFinder
GCGCGGGCTACTCGATCAGCATG	GATGCGACCCTGCCCTGCGCGGCCGCTCAGCATGGCTGCCGCCCTGTCC
GCGCGGGCTACTCGATCAGCATG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159422011.1\|643158_643458_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423989.1\|655142_656447_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340883
NZ_CP047180.1\|WP_159422008.1\|637644_639000_-\|DNA-repair-protein-RadA	unknown	unknown	gnl\|CDD\|236994
NZ_CP047180.1\|WP_159422016.1\|649993_651061_-\|FUSC-family-protein	unknown	unknown	gnl\|CDD\|379231
NZ_CP047180.1\|WP_127888573.1\|648123_649518_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350143
NZ_CP047180.1\|WP_159422022.1\|658797_659358_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|182015
NZ_CP047180.1\|WP_159422013.1\|644492_644804_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159422018.1\|651717_652758_+\|FUSC-family-protein	unknown	unknown	gnl\|CDD\|226614
NZ_CP047180.1\|WP_159422017.1\|651142_651685_+\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP047180.1\|WP_159422015.1\|646643_648074_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|373145
NZ_CP047180.1\|WP_159422019.1\|652771_653905_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|366166
NZ_CP047180.1\|WP_159422014.1\|645033_645906_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159422010.1\|642340_643060_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159422012.1\|643485_644007_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159422007.1\|636131_637607_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379450
NZ_CP047180.1\|WP_159422009.1\|639264_640161_+\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_CP047180.1\|WP_159422020.1\|656532_657360_+\|TIM-barrel-protein	unknown	unknown	gnl\|CDD\|224007
NZ_CP047180.1\|WP_159422021.1\|657356_658487_+\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP047180.1\|WP_123446774.1\|653983_654511_-\|MOSC-domain-containing-protein	unknown	unknown	gnl\|CDD\|377051
NZ_CP047180.1\|WP_159422023.1\|659380_659614_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_159422008.1\|637644_639000_-\|DNA-repair-protein-RadA	gnl\|CDD\|236994	PRK11823, PRK11823, DNA repair protein RadA; Provisional.	0
NZ_CP047180.1\|WP_127888573.1\|648123_649518_+\|family-43-glycosylhydrolase	gnl\|CDD\|350143	cd18822, GH43_CtGH43-like, Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	1.01675e-130
NZ_CP047180.1\|WP_159422022.1\|658797_659358_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|182015	PRK09646, PRK09646, ECF RNA polymerase sigma factor SigK.	4.66213e-38
NZ_CP047180.1\|WP_159422019.1\|652771_653905_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|366166	pfam00561, Abhydrolase_1, alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes.	1.61583e-21
NZ_CP047180.1\|WP_159422018.1\|651717_652758_+\|FUSC-family-protein	gnl\|CDD\|226614	COG4129, COG4129, Predicted membrane protein [Function unknown].	3.18816e-15
NZ_CP047180.1\|WP_159422017.1\|651142_651685_+\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	8.50934e-15
NZ_CP047180.1\|WP_159422015.1\|646643_648074_+\|hypothetical-protein	gnl\|CDD\|373145	pfam14587, Glyco_hydr_30_2, O-Glycosyl hydrolase family 30.	9.10589e-33
NZ_CP047180.1\|WP_159422016.1\|649993_651061_-\|FUSC-family-protein	gnl\|CDD\|379231	pfam13515, FUSC_2, Fusaric acid resistance protein-like.	1.82735e-17
NZ_CP047180.1\|WP_159423989.1\|655142_656447_+\|MFS-transporter	gnl\|CDD\|340883	cd17325, MFS_MdtG_SLC18_like, bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters. This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	3.82866e-26
NZ_CP047180.1\|WP_159422007.1\|636131_637607_-\|hypothetical-protein	gnl\|CDD\|379450	pfam14067, LssY_C, LssY C-terminus. This domain is found at the C-terminus of Legionella LssY proteins, which may be a part of the type I secretion system. This domain is functionally uncharacterized. This domain is found in bacteria, and is typically between 182 and 195 amino acids in length. It is often found in association with pfam09335 and PF01569. There are two completely conserved residues (P and W) that may be functionally important.	2.29512e-86
NZ_CP047180.1\|WP_159422009.1\|639264_640161_+\|alpha/beta-fold-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	6.12625e-16
NZ_CP047180.1\|WP_159422020.1\|656532_657360_+\|TIM-barrel-protein	gnl\|CDD\|224007	COG1082, IolE, Sugar phosphate isomerases/epimerases [Carbohydrate transport and metabolism].	5.57164e-21
NZ_CP047180.1\|WP_159422021.1\|657356_658487_+\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	1.44167e-51
NZ_CP047180.1\|WP_123446774.1\|653983_654511_-\|MOSC-domain-containing-protein	gnl\|CDD\|377051	pfam03473, MOSC, MOSC domain. The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich domains identified in the molybdenum cofactor sulfurase and several other proteins from both prokaryotes and eukaryotes. These MOSC domains contain an absolutely conserved cysteine and occur either as stand-alone forms or fused to other domains such as NifS-like catalytic domain in Molybdenum cofactor sulfurase. The MOSC domain is predicted to be a sulfur-carrier domain that receives sulfur abstracted by the pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulfur-metal clusters.	9.38955e-06

>NZ_CP047180.1|WP_127888573.1|648123_649518_+|family-43-glycosylhydrolase
MALATAALVAVTGLAPATAAPQTVTNGTQFLTTQGQPIHGHGAGLLKVGQYYYWVGQSTDADNRFISVPLYRSTDFKNWEFRGDILTRNSSPDLNVSTIERPKLVYNAATQKYVLWMHWENGRDYTQGRVAVATSSTVDGSYAYQGSFRPQGYESRDMTVYQDDDGSAYLFSSTAIPTTNASTAIFKLNASYTNVESFQGLHWENQSREAPTIFKRNGVYFALSSGTTGWSPNQNKYSTATKITGPWSTPTDFGGPTGNRSQPTYVATISGSAGTSYLYMGDRWAGANNGAVNDSSYVWQPLQFPSNTSVAMPEVDGVVIDTAAGTVNAAPALPRSTIKSASSGLCVNVADDSTATGSKVVQWTCGNGSNAVFARASAGGYVQFQTQHSGLCLAQSGSSGSGGALVQAPCTSGSTAQWQVSGQTIVNRASGACLDVPDESTTAGRQLGTWSCNGGNHQKWSFVA
>NZ_CP047180.1|WP_159422015.1|646643_648074_+|hypothetical-protein
MTMDRRGLLALAGTAALTGAVTAVAGPGTRPAHAATGTAVVDPAQRGPVWEGFGTALCWFAHRIGGTAAVRDTYADLLFDRDKGLGLNIVRYNIGGGENPAYPGHMDLRARIPGYLASASAAYDWSADPNQRWFLQAAKSRIPASEFLAESFANSPPWWMTISGSVTGGRNAAENLRPDSYEVFARYLVTVNERFRTTWGVPFRTLSPVNEPSAAYWTFGNRQEGNRMLPANQATMLRALADELARQGSPTRIAASEETSIDVGRDTVNSWSAQTRALVGQYNVHSYQGSDRTGFKTAARGTRIWDSEHGNGDASGSTLSQNILWDVKWLGASAFAYWQAVDSGGWGMLDTDLNNASADLSSYTRNKKFWAMAQWSRYVRRGYRVIGVSDNDTVAFHDEAGRRVVLVTVNTTSTPATVTYDLSRFAPATATASGVRTGASEDLAALPPAALAGNRFTASAPAMSTTTWVVPSMTLN
>NZ_CP047180.1|WP_159422014.1|645033_645906_-|hypothetical-protein
MNDALHNDPGTAAVVDAVNRSHRSHAWIARRIGMSESTIHRQLTCKSPMTVAEADRIRRTLGTSFLAETSWSGAPEQRHRTSSGSEPTSHAPLNVGGRPLPNPTALLLNGQLHHHARHMPEARSTNASTIITDGIHFPHGGDWEAISNDRKDTRWSAELMGIILALVGDNEIAYSTGAVFPSLNSDSAKIEITILTPASVILADFTAGSSTNDRTSWRLLRHDVRAHPRSAISSIHVEPAPIAQSTGRSEPGQVAVTVVVAGASRRLPASVEADYDPRLTALLTNLNRSW
>NZ_CP047180.1|WP_159422013.1|644492_644804_-|hypothetical-protein
MDGGLPASFYNLQELLDIQREAPGVEAGRSQAESLMEAIAPGWKAHTADLDSRIDQSMAETIDRRLSSIERYGHGEMKPKLVAHWLKLGGATPAPVRAFDWPS
>NZ_CP047180.1|WP_159422012.1|643485_644007_-|hypothetical-protein
MPTPLDAPAVLKAVSDGLEGGGLTVGLDVGSYAGIGLTILIALLGSRVLGTWLGGMIENGRLERGFSREDANAAIAALTKLHVAYSKWSAKGRLSTKEEAARDLEVENLAALCLGACALTGVKNLNSASSYRSLGDQWVSLDPDASRDDLDDRYLKLLRALSVHSYRAKARHD
>NZ_CP047180.1|WP_159422011.1|643158_643458_+|hypothetical-protein
MLSITLPRLAGTREAADRLVDEQAQGAAAFDTVCVFARDLSVSSTSFTDEFFKKLSEGGAAEVLIFGGPETFISAAEKVLERRKLTTKVRRASAAELPA
>NZ_CP047180.1|WP_159422010.1|642340_643060_+|hypothetical-protein
MIDLSYLRFAEPSGLVLICSEAERLAAQGHVDFTSPRNSEVANYLARMRLHEVLNELGISHGLPRVRENGVGLGLLEIRRFSSTDAASKLAEHVHANLVSQNGDIAAAVYVGICEAGENVFRHSESSRGYAVAQTTHQGRSLRFAVADAGVGVLATLRNRGAETDSDALELAMQEGISSYDDAGSGYGLSNLAGSLAKVRGGLTLLSGGASRRHVGSQIHRGASMASIPGAILEGSALL
>NZ_CP047180.1|WP_159422009.1|639264_640161_+|alpha/beta-fold-hydrolase
MTSTVHTLKSGRALGVAWSGPEDAEHVVVLAHPAPGAAGLDPDPAATARHGVRLLSFDRPGYGASELLNDVDPAGAGAGASPEQAAADIAEYLATAGIASVTAAGWSAGGRVALALSANYPGLVERVAVLGTPAPDDAVPWVGEQNRAMLEQLRELPVDEAVRSLAAALDTAFGPSPAPESLLGVLGGDAADEDVLEAPGVRERLLAMLERAVAQGNLGQAADIVGYTLQEWGFAVETVDAPALLLYGGEDATVGRQHGEWYAARLPDSRLEVVPGRGHLLAVSEWERVLAFLLPEPA
>NZ_CP047180.1|WP_159422008.1|637644_639000_-|DNA-repair-protein-RadA
MASSKTRTAAYRCSECGWTTAKWVGRCGECQQWGSVIESTERTGLVRAVAAVAPTAARLAKPITQIETTSAAHRPTGVGELDRVLGGGIVNGAVVLLSGEPGVGKSTLLLEVASRAAAEGQRVLYVSAEESAAQVRMRAERTGAMHHSLFLAAETDLATVLGQIDEVRPDLLIVDSVQTVASDTVDGLPGGPSQVREVAATLIRVCKERALPLVLVGHVTKDGSIAGPRLLEHLVDVVCHFEGDRQTALRFVRSLKNRFGPTDEVGCFEMTAEGIAEIPDPSGLFLSRTRFPTPGICVTVAMEGRRALPVEIQALVIANDGDHPRRVTNGVDASRVAMILAVLERQAGIPLRRCDVYVSTVGGVKLMEPAADLAIAVAIASAHAYTPLRPGIAAFGEISLSGDIRPASGAKQRANEATRLGHPSHLDSSAFTLSSAITHALVPVPTRIPVG
>NZ_CP047180.1|WP_159422007.1|636131_637607_-|hypothetical-protein
MSSDTERGGTDQDRPATDGDSAPAPVPAVRRRRFPIPALLDQAFFVLGGVAATLLAVVLVTDGVRSGWAQIGFYVAVWVLVAYLVLPRLHRILTRLYVPDYFIGRARTSDGLLGDPVNLAFQGSDAQLVHAMTSSGWTRADEVTVRSSRRIITATLTRRSYHRAPVSPLFVFGRQQDVAFQQEVAGNPGKRHHVRFWRCPENWFLPGGFPVEWVAAGTFDRSVGLSLFTLQVTHKISPDTDQERDHIVASLREHHPEVTVDVIQDFSTGYHSRNGGGDSIVTDGDLPVVDLRAIPLPSGAAEHDAIAPVAATELAGALGTSSATVLRRPVTTHVGALMLVARGLAYALQAVLLLAGAASLDDLTWLDGGTATAGGSTLDEASTRPIAAALLGAATLLWLLLGALVLRGSGTARLLALSSSLLSTITAFAAVLQGGAAISLQTNLGSVAFDILVLLALSSRSSRDYAAAKSRLRADRRAESRSRRAARGRTG
>NZ_CP047180.1|WP_159422016.1|649993_651061_-|FUSC-family-protein
MPATPSLRSALPHPRELVAFGPHDGAHRVALRAGISMAVPLLLLWVFGRTDLALYATFGAFTALYGRRHTHRPRLLMQASAAAYLVAMVTIGTTVALSPQRDWLIIPVVTLAAVGAAYLSDALHWHPPGPLFPVFAVTACASVPVEATRIPEAFALAAASAAFSLLIGVSGIAAPRARLLPATPWRPSFRAAAVRSTTRAGMLRFGAVVLIAGAIPTATGLGHPYWAMVSAVAAVSGADATARLVRAGHRMLGTVIGVAIAAALLALPLSPLATIGVVVLLQMLAELVVGRNYGLTLALITPLAILMVELAHHTDEFVLLRDRALETAIGVAVGVAATLLSHAIASRTSRPTPEG
>NZ_CP047180.1|WP_159422017.1|651142_651685_+|MarR-family-transcriptional-regulator
MNHLLSSDSSHPDPDATPDAVDEIRAGWRRLRPELDTSAVDVAGRLIRASALLVRATEERLAAFELTRGEFDVLTTLRRLAAPQSPTTLRTIGLASAPAVTKRLHALERRGLVLRTANPADGRGALIALTTEGIALVDAAFPEVLEVERELLAAVPDALRDDAARGLRAVLASIEAAPRQ
>NZ_CP047180.1|WP_159422018.1|651717_652758_+|FUSC-family-protein
MRLTSSFTVDTRPPVLQLVKTAAATVVTWIIAALIFPGTLPVFGAIAALLVVAPSVNQSFSKALERSVGVIIGVVVGSLIGTLFGDDSAIVLGAIVAAIAVGWAVRLTPASAVQIPISAMLVLSVGSVTPNYAVDRILETLIGAAVGIVVNALIVPPITLAPAERAVGDLTAQLAAALDDLADVLETKVGRERLSELLINARLLQTVQTKAEEAIATGEESLRLNPRRSAHRDRLLALDSVTPRLARIVTRVRGMTRTVHDLYDQDLVGEPTIGDIAVQLHRAAHDLRLLVQSSVAVPEPEPITDELPALTAPLVIVTPHPEHWILLGALAEDLRRIREEIVGEES
>NZ_CP047180.1|WP_159422019.1|652771_653905_-|alpha/beta-fold-hydrolase
MPYPGRPLRALASSVRHGLRDVFSTTRSRRRDPRRRYKNTDVSVLRVHRRDVYARVNTVGHTGERTFVLVPGIGVAATYFERLAPALNEFGPVHALDLPGFGGVPHPPNARHMTIGDYAELVGAVIDDLGLDDPVVLGHSMGTQVVAELAARRPELTTIVLLGPVMNPHERRIPVAAWRFLQSSVREPVQVAVLAAAAYLLCGPRWFSRVLPEMMQYRIEDVLPRIRASTLVIRGEFDRLVPREWAEEVAEAIPHARAWEIPDASHSVMHAHAEEVARLCVEHARAPQPDRDEAELRRFPDDEIDRSQEDAPIDDPLGAIRGRVTELAGILVDDDSLIAEGKTQHAEATDPAALQESDTDAGDGDSGPGLFDAPAAR
>NZ_CP047180.1|WP_123446774.1|653983_654511_-|MOSC-domain-containing-protein
MEAAAIELVRFVVSPLHRFEGRPADGPIPSEGNEQPERIEIRAGLGIVGDRYFAQRAHRTAAVTLFAIESLEHVAAELGRAAFDPADTRRNIIVRGADIDALAGRTFAVEQGGERIEFQGGRPANPCAWMDVSLAPGAFKAMRRRGGVRCAPLTNGLLHIGPARLILHRSEDMLI
>NZ_CP047180.1|WP_159423989.1|655142_656447_+|MFS-transporter
MPSGMTTATATVRGHHAFSEPTEPATKGYVFWLLAAQLIFFVALLGPAVVGIGLKIQSLVESGEIAQDGATGAAAVLGGFGALFATIANVVVGRLSDRTTSRFGRRRIWIVTGTVLMTVAFAIMALAPTLLVATVGWSLAQLGANMTLAPFTATLADQVPKFQRGKITAALGIAQNVGILGGTYVAQAFAGQLVVMFVAPSILAIVAMVVFAVVLPDKRLPQAPPRATLRDWAETFWVSPVKNPDYALAWWSRFLIIFASFGFTTFRFFYLLNHIGVEEGSIPAVITTSVLIYTVTLVGASYFAGWLSDRIGRRKVFVWSSTALFAVGTFALIFVQDIGAFYVLEAVLGLAYGIYVGVDLALVVDVLPNPDDSGKDLGVFNIANALPQTLAPLVGGILVYVSDPTGNNYGLWFTVCALAAVVGALVILPIKKVR
>NZ_CP047180.1|WP_159422020.1|656532_657360_+|TIM-barrel-protein
MTLPLASIQLYTLAKEFSEDPNGSLEKLAAIGLKNVEAFDFVRRPAEIRAALDATGLASPTGHAPLLSDELWTPDGSIPTPAPEVVFEAAAQIGIQTVIDPFVSAERWLTEDGVADIADRLNKAAEVAATFGLKVGYHNHAQEFIASFDGRTAYERFVATTDERVEIELDLFWALTGGQDGPALVSKLGSRLVAVHVKDGIAPAENPFAPGAAAFGSDTLDQRRPGEGDVPLVEALKAGEGAIKYAVIEYDNAPGDVFADIQASYDFLVKGGYAA
>NZ_CP047180.1|WP_159422021.1|657356_658487_+|Gfo/Idh/MocA-family-oxidoreductase
MSGPIGIGVIGVGVISDTYLENLASFPDVEVLIVGDLLLDRARSQAEKHGVPAWGSAEDVLAHAGVQVVVNLTIPAAHVEVSAAAIAAGKHVWSEKPLGLDRAGTAQLLKDAAAKGLRVGSAPDTLLGPGFQTAKRAIADGVIGEPMFASTVFQTVGPDLWHPSPAFLFAQGAGPLLDMGPYYFTGLVSLFGSVQRVAALGRKKLEDRVIRSGPDAGTTFPVEVPTSLQVLTSFAAGPQASSLLSFDSALERHGVFEIHGTEGSIVIPDPNQFEGRTAYVKARTSIADGQWGEQEWTEIEQKGTVVGRGLGLLDMVRAIAEDRPHVATGELGFHVLDVMLSAQESAERGEFVAIDSTLSAPVPAVPVDFDPFAQTL
>NZ_CP047180.1|WP_159422022.1|658797_659358_-|sigma-70-family-RNA-polymerase-sigma-factor
MTDGAPSAQDALVPPLADGDHAAFRRLYERTVRRVRSITVGILQDHAQAEEVAQETYFELWRSAARHAVLEEQQHLVAVIARRRAIDRVRAAQSSRERDHRYAIHSYLREIDEAESHGEIAGEFRRAAAEIRRLAPKHRDLLFLAYVRGLTHAEIATELGLPIGTVKTRLRDTLARLRRELTPPPP
>NZ_CP047180.1|WP_159422023.1|659380_659614_-|hypothetical-protein
MSFNSRRWQVRTIVARVQATAALSTSTLDTAGRADRKLEILRIADGVDAGRVSNDEAVTAFERLAQDVGRTPEARLG

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Crispr_ID: NZ_CP047180_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_6

811318-811459

Orphan

Consensus_repeat	Method
CATGCTGGTCGAGTAGCCCGCGCAGCGGGCGTATCGAGACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_6

>merge|NZ_CP047180|6|811318-811459|CRISPRCasFinder
CATGCTGGTCGAGTAGCCCGCGCAGCGGGCGTATCGAGACCCACGTCCTCCCGCAGTTGCGGCAGCACGCACCCCTCGCTCCGCCTCGCACTTCACGCGAACATGCTGGTCGAGCAGCCCGCGCAGCGGGCGTATCGAGACC

>NZ_CP047180|6|5|811318-811459|CRISPRCasFinder
CATGCTGGTCGAGTAGCCCGCGCAGCGGGCGTATCGAGACC	CACGTCCTCCCGCAGTTGCGGCAGCACGCACCCCTCGCTCCGCCTCGCACTTCACGCGAA
CATGCTGGTCGAGCAGCCCGCGCAGCGGGCGTATCGAGACC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159422105.1\|806258_807101_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|153097
NZ_CP047180.1\|WP_159423998.1\|808176_809472_+\|transcriptional-regulator	unknown	unknown	gnl\|CDD\|225822
NZ_CP047180.1\|WP_123447035.1\|809597_811172_+\|aldehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|143434
NZ_CP047180.1\|WP_159422110.1\|821083_822553_-\|deoxyribodipyrimidine-photo-lyase	unknown	unknown	gnl\|CDD\|223492
NZ_CP047180.1\|WP_159422100.1\|797638_798466_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|374030
NZ_CP047180.1\|WP_159422104.1\|805208_806210_+\|substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|224525
NZ_CP047180.1\|WP_159423999.1\|811980_812463_+\|DUF4396-domain-containing-protein	unknown	unknown	gnl\|CDD\|379568
NZ_CP047180.1\|WP_123446633.1\|811493_811892_+\|DUF779-domain-containing-protein	unknown	unknown	gnl\|CDD\|377532
NZ_CP047180.1\|WP_123446641.1\|798566_799409_+\|ROK-family-protein	unknown	unknown	gnl\|CDD\|224851
NZ_CP047180.1\|WP_159422108.1\|814044_816387_-\|PASTA-domain-containing-protein	unknown	unknown	gnl\|CDD\|223815
NZ_CP047180.1\|WP_127887446.1\|822638_823229_-\|winged-helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224759
NZ_CP047180.1\|WP_159422106.1\|807219_808173_+\|EamA-family-transporter	unknown	unknown	gnl\|CDD\|273359
NZ_CP047180.1\|WP_159422107.1\|812541_813357_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236940
NZ_CP047180.1\|WP_159422101.1\|799723_800848_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|132490
NZ_CP047180.1\|WP_159422103.1\|804412_804973_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|99750
NZ_CP047180.1\|WP_123446628.1\|819485_820421_+\|cysteine-synthase-A	unknown	unknown	gnl\|CDD\|273463
NZ_CP047180.1\|WP_159422109.1\|816689_819101_-\|PASTA-domain-containing-protein	unknown	unknown	gnl\|CDD\|223815
NZ_CP047180.1\|WP_123447033.1\|820417_821038_+\|serine-O-acetyltransferase	unknown	unknown	gnl\|CDD\|223975
NZ_CP047180.1\|WP_159422102.1\|800967_804387_+\|helicase	unknown	unknown	gnl\|CDD\|223627
NZ_CP047180.1\|WP_123446632.1\|813353_813950_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274357

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_159422105.1\|806258_807101_-\|hypothetical-protein	gnl\|CDD\|153097	cd00657, Ferritin_like, Ferritin-like superfamily of diiron-containing four-helix-bundle proteins. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).	0.000139452
NZ_CP047180.1\|WP_159423998.1\|808176_809472_+\|transcriptional-regulator	gnl\|CDD\|225822	COG3284, AcoR, Transcriptional activator of acetoin/glycerol metabolism [Secondary metabolites biosynthesis, transport, and catabolism / Transcription].	4.09788e-24
NZ_CP047180.1\|WP_123447035.1\|809597_811172_+\|aldehyde-dehydrogenase	gnl\|CDD\|143434	cd07116, ALDH_ACDHII-AcoD, Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like. Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.	0
NZ_CP047180.1\|WP_159422110.1\|821083_822553_-\|deoxyribodipyrimidine-photo-lyase	gnl\|CDD\|223492	COG0415, PhrB, Deoxyribodipyrimidine photolyase [DNA replication, recombination, and repair].	3.39961e-175
NZ_CP047180.1\|WP_159422100.1\|797638_798466_+\|hypothetical-protein	gnl\|CDD\|374030	pfam15698, Phosphatase, Phosphatase. Members of this family have phosphatase activity.	5.10896e-82
NZ_CP047180.1\|WP_159422104.1\|805208_806210_+\|substrate-binding-domain-containing-protein	gnl\|CDD\|224525	COG1609, PurR, Transcriptional regulators [Transcription].	1.43213e-79
NZ_CP047180.1\|WP_159423999.1\|811980_812463_+\|DUF4396-domain-containing-protein	gnl\|CDD\|379568	pfam14342, DUF4396, Domain of unknown function (DUF4396). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 167 and 310 amino acids in length.	6.20489e-41
NZ_CP047180.1\|WP_123446633.1\|811493_811892_+\|DUF779-domain-containing-protein	gnl\|CDD\|377532	pfam05610, DUF779, Protein of unknown function (DUF779). This family consists of several bacterial proteins of unknown function.	2.00687e-58
NZ_CP047180.1\|WP_123446641.1\|798566_799409_+\|ROK-family-protein	gnl\|CDD\|224851	COG1940, NagC, Transcriptional regulator/sugar kinase [Transcription / Carbohydrate transport and metabolism].	2.74591e-26
NZ_CP047180.1\|WP_159422108.1\|814044_816387_-\|PASTA-domain-containing-protein	gnl\|CDD\|223815	COG0744, MrcB, Membrane carboxypeptidase (penicillin-binding protein) [Cell envelope biogenesis, outer membrane].	9.30337e-91
NZ_CP047180.1\|WP_127887446.1\|822638_823229_-\|winged-helix-turn-helix-transcriptional-regulator	gnl\|CDD\|224759	COG1846, MarR, Transcriptional regulators [Transcription].	2.85924e-10
NZ_CP047180.1\|WP_159422106.1\|807219_808173_+\|EamA-family-transporter	gnl\|CDD\|273359	TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter. [Transport and binding proteins, Amino acids, peptides and amines].	1.77271e-20
NZ_CP047180.1\|WP_159422107.1\|812541_813357_-\|hypothetical-protein	gnl\|CDD\|236940	PRK11633, PRK11633, cell division protein DedD; Provisional.	5.55972e-05
NZ_CP047180.1\|WP_159422101.1\|799723_800848_-\|glycosyltransferase	gnl\|CDD\|132490	TIGR03449, mycothiol_MshA, D-inositol-3-phosphate glycosyltransferase. Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species.	1.48179e-86
NZ_CP047180.1\|WP_159422103.1\|804412_804973_-\|hypothetical-protein	gnl\|CDD\|99750	cd06259, YdcF-like, YdcF-like. YdcF-like is a large family of mainly bacterial proteins, with a few members found in fungi, plants, and archaea. Escherichia coli YdcF has been shown to bind S-adenosyl-L-methionine (AdoMet), but a biochemical function has not been idenitified. The family also includes Escherichia coli sanA and Salmonella typhimurium sfiX, which are involved in vancomycin resistance; sfiX may also be involved in murein synthesis.	1.60191e-07
NZ_CP047180.1\|WP_123446628.1\|819485_820421_+\|cysteine-synthase-A	gnl\|CDD\|273463	TIGR01136, Cysteine_synthase, cysteine synthase. This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family].	1.54534e-162
NZ_CP047180.1\|WP_159422109.1\|816689_819101_-\|PASTA-domain-containing-protein	gnl\|CDD\|223815	COG0744, MrcB, Membrane carboxypeptidase (penicillin-binding protein) [Cell envelope biogenesis, outer membrane].	2.52338e-99
NZ_CP047180.1\|WP_123447033.1\|820417_821038_+\|serine-O-acetyltransferase	gnl\|CDD\|223975	COG1045, CysE, Serine acetyltransferase [Amino acid transport and metabolism].	1.87117e-77
NZ_CP047180.1\|WP_159422102.1\|800967_804387_+\|helicase	gnl\|CDD\|223627	COG0553, HepA, Superfamily II DNA/RNA helicases, SNF2 family [Transcription / DNA replication, recombination, and repair].	2.1717e-99
NZ_CP047180.1\|WP_123446632.1\|813353_813950_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274357	TIGR02937, RNA_polymerase_sigma_factor, RNA polymerase sigma factor, sigma-70 family. This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.	1.39473e-27

>NZ_CP047180.1|WP_123447035.1|809597_811172_+|aldehyde-dehydrogenase
MTLYADPVADQAPKEPESTVYANPGTEGSVASFRSRYDHFIGGEYVAPAKGQYFENITPITGKPFCEIARGTAEDIDRAVEAGWKAFPSWGKTSPAERSNVLLRIADRMEANLELLAVAETWENGKPVRETLAADIPLAIDHFRYFAGALRAQEGGVSEIDHDTIAYHFHEPLGVVGQIIPWNFPILMAVWKLAPALAAGNCIVLKPAEQTPASIHVLMDLIHDLLPAGVLNIVNGFGIEAGAPLASHPRIRKIAFTGETTTGRLIMQYASENLIPVTLELGGKSPNVFFADVAAERDSFYEKALEGFSFFALNQGEVCTCPSRALVQKSIYDDFVGDGLERVGRIKQGNPLDVSTMIGAQASNDQLEKILSYMDIGKQEGAKLLIGGDRADLGGELSGGYYVNPTVFEGRNSMRIFQEEIFGPVLALTSFEDFDDGIAIANDTLYGLGAGVWSRNGAQLYRAGRAIEAGRVWSNTYHQYPAHAAFGGYKQSGIGRENHKMMLDHYQQTKNLLVSYAEGPMGFF
>NZ_CP047180.1|WP_159423998.1|808176_809472_+|transcriptional-regulator
MPCRGARAPHDRRRGADEMTNPWLALPGSGRRRPLVEASWERARRHRLDPERLTAPLSFSSDELRDYRMGHPLASVLPVIRRLLVRDADEDSGVLVAVGDALGRLLWIDGDQALKSSAERMLFVEGAAWAEPDVGTSAPGTALVLDHGVQIHGAEHFASLVHPWSCTAVPIHDPETHEILGVIDITGGAEVVAPQTLPLMEATAAAVESQLMVQRLQRPRRAQPRRSPPRPAAARAPSLRVLGRETGVVTADGVELELSTRHAEILTLLAWHRAGLSAEALAQLLYGREDAVVTVRAEMVRLRRILEPRLPRLVPLSRPYRLASPVDLDARQVVGLLDRGAHRLALDAYAGAPLPGSEAPGVRAIADELRARVRATVLTSAAAETLLAYAHGPDGHDDAEVWAELLRILPRRSPRRAGIVAHLEELEAEQR
>NZ_CP047180.1|WP_159422106.1|807219_808173_+|EamA-family-transporter
MGSRGSAVAAILLAAVCFGTTGTAQSLGAEGVDPLLLGAARIVLGGALLAALLGVETARAPRRAARRPRVSTVLLVLLGAAGVAAYQPAFFTGTAENGVAVGTIVALGSAPAFTGLLEWLLLRSAPSPRWFVSTALAAVGVVLLAGLLTGGAAGGVSVLGLAGSAGAGAAYALYAVCGKLLLERGFSPAAAMGAQFGTAALLALPVLLAGDPGRLAGSLPAVLWLGVVTVAVAYTFFARGLRLLPAATVSTLTLVEPATATLLGVALLGERLTPDAVAGIAVLVLAVLLLAVPARRGSARRRRPEVVAPEAPSSLAE
>NZ_CP047180.1|WP_159422105.1|806258_807101_-|hypothetical-protein
MGIAEPFDVESYRRSAHGSLHDHFSIREFEEAPLDREAIVASAYLRALEHAAVVRVLPLARAHPDPRVRSFATTWAAERHRIADALGEVLAASPRIRGVETGSAEPVVRSRVLRDRSSRLLAGPVALTLAVDAQIALHAYRRLARLSLHPEMERLAETVAAILERHADFFGELAADTIGRPLRRRIVAAAVLASVRLPVGEAALPEELAREGRELVFGRDDGGLDGIDAGVVALFALPCTAARRLLRPHRTLPLRAAVQAGRVGADVVAGVRELRSLVAD
>NZ_CP047180.1|WP_159422104.1|805208_806210_+|substrate-binding-domain-containing-protein
MAEPTLVDVARIAGVSRATAARVLAGRTNVDAGMTAAVERAAKQLGYEANGAARLLRGGRAGSIALIVAFEDLDRLPGTILTAVLKGAAASLHAQGVQPVLLPADYDDRGRVARLLRTRAVDGAIVILQNEMTQVTQELADSPAPIAWVGRPRVALADDALVIDADNYGGGRLAARVLAESGRRRLGIITGPHDMKPARERLRGWRDELEHLGIDYAPLAHGAFTVESGVTAMVRLLQRYPDLDGIFASSDLMAHGAIHVLRAAGRRVPTDVSVVGFDDVVIATTTDPPITTIRQPLAEMGRIAAETVVAVLQGREVDRQRILPVSLVQRESA
>NZ_CP047180.1|WP_159422103.1|804412_804973_-|hypothetical-protein
MHGGRRLARRLGVGALAALVLVVGAGIPVYVLPATDPVPEHADAVLVLGPPTRARTELGRDLIEAGVADTLVISVWASDLAAAPGENDVVACDEPDMDVICFTAEPGTTQGEARALADDARADHWDSVVVITQTPHIARARLLLGRCFDGELSMVSSGEPYTLGDWAYEYVYQTGAFVKALADPAC
>NZ_CP047180.1|WP_159422102.1|800967_804387_+|helicase
MARQSPPEEVLPPSAAPGAEGREPFSEQDIRGLVGTAALDKGVAYADEGRVAELQWFGGRTRLFGQVRGSGRSPYAVSVQLRDEGDHSILLGGACSCPVKHECKHVAAVLIEALRREREGALSGPFPGEAAVDAVPEWRSALAPLLAGAERSHSGIPLGLQFELLPGEPVRRPPGRYNSYRPPPEPRPRLGVRPVRMGDRDRWVRTGTSWRDLGYLHYSHDYDERQIDVVREMQGLLSGHSASSYYSPDTWLYLDQCRSEAIWAALHGAVRAGIGLVMGDRDQTPLKILDTTATASIDVTRTAAGLELRSLVAIGDHPAPEHFGFIGDPAVGLYTWDEGDELRGKAVTLVPFAAPLVSSARTFLWSNEPIRIPEQEESAFLTEHYQRLHRLFDIVSRDGSFEAPPVPEPRLGLTLEHTEGAGLRGSWWWRYGIEGGRGTEAERLPLRLDDESGYRDAEAEQRILDSLGGAGIDPESTPALVSPSSRRLRPTFDLRGMQTVGFLTGEVERLRELGTVEIEEIGQRVEYREAETAPVVAVQTVAQPDSRDWFNLEISVTVNEEAVPLAEIFLALARGDEYMVLPSGVYFALDDERFGRLRELIAEARELSDDPSETLRISRFQSSLWDELVELGVVEAQAAAWRRSVEGLSGFTATGALESRALPEGFAVELRPYQQLGYDWLSFLYDNQLGGVLADDMGLGKTVQSLALVTRVMQEQRAAAASAGTSPRPFLVVAPTSVVPNWVGEAKRFAPDLRVVGIDETSKKKRKALSTMIGEAELVVTSYALFRLDYESYAGIQWSGFLLDEAQFVKNRQSATHQLARRLDVPFKLAITGTPMENNVMELWSLLSIVAPGLFPSPAGFAEYYQKPIERDADTERLSQLRRRIRPLMLRRTKELVATELPPKQEQTIEVELGTRQRKVYDTYLARERQRVLGLIGDFEKNRFAIFRALTVLRQVALDAALVDEAHATVPSTKLDLLDELLADALAEGHRVLVFSQFTRFLGRVRGRLDAAGVEYAYLDGATKKRDEVIDRFRSGEAGVFLISLKAGGFGLNLTEADYCILLDPWWNPATESQAVDRAHRIGQTRSVMVYRLVAKDTIEEKVMALKEAKAALFAAVMSDDGAAATGGITAEDVRELLG
>NZ_CP047180.1|WP_159422101.1|799723_800848_-|glycosyltransferase
MPRLSIVSAHTSPLEQPSTGDAGGMNVYLAGVLPELAALGWEVTVLTRGEGVRRLAPGVSVVGVPVEAADKYALAASAPAFAAAAEGADVVHSHYWVSGLAGALTGAPHVHSMHSNSLAKNVRLVPGDVREPEERIRAERSVLGSADAVVVAGASERSDVVDGYGVDPARVLVVPPGVDARFSPGAGERAREIVLLGRVQPLKGQLLAVQALARIPADERPLLRLAGGPAPGREGYLEEVRAAARELGVDEWVRFEGVADRETAAALLRGARLALVPSAAETFGLIALEAAASATPVLARRTTGLVDAVRDGESGVLIDSGDPGEWAAEIRRLLADDAERARLGRGGVEWAAAHSWAAAAARLDALYRRLLRTR
>NZ_CP047180.1|WP_123446641.1|798566_799409_+|ROK-family-protein
MTQPQDGLLPRFAVGVDIGGTSIKASLVDVTTGERAARRFAVANPVGKEPEDFAAAIAGIVRDVSPIAGTPVGVGFPGIVRGGIVRQTTHVSQRWVGIDAQALLSEATGVDVVVVNDADAAGVAEREFGAMRDREGLCLLTTLGTGIGTALVYEGEVIPNSELGHVHIDGPDFEPRVGFSAVRREGITLEEWAGRLNVYYRHLEMLLSPQLFVIGGAAAHVFDEFARFLDLGTEIVSARFGNDAGFTGAAMVAVSPDRLAPWYRSTRGAHFDPGTPAIAD
>NZ_CP047180.1|WP_159422100.1|797638_798466_+|hypothetical-protein
MPLSAAALAALLDESLLTGAVLTGRASNLGNLRRLAAREPAHLYGVDVAEHWDVESLLALMGERVGISTDPAFEHGQDRIDAALTVAALDTYRDRFARAVREGALILFATAHPATLLDVYRRLAAAATAAGARVIDVNTLPFARPDGIRVSLADEHQRLWCTGGVTCAYRGGSLQHTHSAEPMNALLDELEALGIRPDLVVADHGWAGASGRRGLATIAIADCNDPAVFVAEAQGSIEVVVPIDDGLAVHLYEPVIAYLLDGLDATSEPARTSGS
>NZ_CP047180.1|WP_123446633.1|811493_811892_+|DUF779-domain-containing-protein
MDSTRVDVTEAAAGMLQRMSELHGPLMFHQSGGCCDGSSPMCFPVGMFRTGASDVLVETLHVDGLAPIEFYMSRTQFEYWKHTHLTVDLVDGRGSGFSVEAPEGKRFMIRSRLLTDAELVEFGLLPAAAVQL
>NZ_CP047180.1|WP_159423999.1|811980_812463_+|DUF4396-domain-containing-protein
MTDAAHDHSTHTSSATTSWRTAATATLHCLTGCAIGEVLGMVLGTALGLHNLGTVLLSIVLAFAFGYALTMRGVLRAGVSWRAAVGIALAADTVSIAVMEVIDNTAMLAIPGAMDAGLATGLFWGSLAGSLALAFVVTTPVNRWLIGRGRGHAVVHRFHH
>NZ_CP047180.1|WP_159422107.1|812541_813357_-|hypothetical-protein
MNDKPVIDPERDRAFRRMIVENARADRARRPLRHRASFLVGLVTAAVLLSGGGVAVALTGAFDPPEPAPVETATPEPVPTPTPSATPTATAAAAPVPAPTPVPTETAATADLSAWVIGFDGIGPIAFGGSSESASAALDTTALVPYDFGIEECRSDRRGSAENPQAWIMAVSDEPGRVTLLNVFGYGVDATRAAAAFPRTAEGIGIGSTEQELLAAYPGITPADPVAGDALYALSDGSGRTLWFRIAADQGTVVDITLNEQPVLTIGGCGA
>NZ_CP047180.1|WP_123446632.1|813353_813950_-|sigma-70-family-RNA-polymerase-sigma-factor
MTASSPPREAGVSWATALSGDPDDFGRLYDAFRQRVFWHALRHTRALHDAEDVTALVFLEAWRRRASVRLVDGSPLPWLLATTNNVARNAGRSARRHRLALGRLPEPEHQDDFSGDSDRRIDDEPRREAIRLAFGALGLRDQDVLSLCVIAEMPVADAAAVLGVPEGTVKSRLSRAKGKLAGLISDLTADAATDGGAR
>NZ_CP047180.1|WP_159422108.1|814044_816387_-|PASTA-domain-containing-protein
MIVSVLAGLLATVVVAPAFALTGAATSSTISAFQSLPSYLEVGELMQKTDVYAGDPDDPTLLASFYDQNRIEVTADQIAAPVFDALVSSEDPRYYEHGGIDLQGTLRAVASTYLLDAAPQGGSSITQQYVKNVLVQKAESISDESERDAAYTEATATTPERKLKEMRLAIGVEKEYSKDEILLGYLNIALFGGTVYGIEAAAEYYYGVHAADLSVGQSAALLAIVNNPEKFRFDRPDDPDNGDANGYALTTSRRDYILDRMLEYGKIDAATHDSAQAAPIEPVITPPSTGCQTAGSAAYFCDYVSHVLRDDPALGDTADERYAALKRGGLKVYTTIDLGLQETAQALMDEQIPASDPRFDVGATAVAVQTGTGKVLTMVQNKRYSQDPDVIASGPEYSAINLNVDADMGGGNGFQPGSGYKVFTLAEWLRSGHTLLEQFDSKRKNWTGFTDSCEGRQDYASYNPKNAGDGGYSDTQTALNSTIWSLNTGYTGMSHLLDLCRIRTTAESFGIHRADGGELVQSAASVIGTNEVAPMTMAVAYAAIADDGRRCTPVVITEITGPDGVSIPPSESECTRAVSSSVARAMQYAMLRVTAEGTGTQADPKDGVQHITKTGTSDNSADTWALGASSSVSLAVWVGSIKAQDSGSRVNLESIDFASGWAPSARHRIWKPLMTEIDSLYGGSDFAAADPKMIAAPQVVVPDLSGRSSDSATRTLTDAGFTVGSITQVDSTQPQGAVAGTVPAAGTTVDKGSLVGVTLSTGTPPPDASPPPASPAPATG
>NZ_CP047180.1|WP_159422109.1|816689_819101_-|PASTA-domain-containing-protein
MSLRAVLGFIGMSAVAGVLITVGVTPALALTGLATSNTIGMFQNLPGYLDAGQLMQRTNIYAGDGTTLLASVYNQNRVEVGWDEVAQTAKDAAVAGEDPRFYEHGGIDLQGTLRALAVTLTGDDLQGGSSITQQYVKNVLVQKAESITDEAERDAAYKLATDPTPERKLKEMRLAIGLEKETSKDDILLGYLNIALFGGTVYGIEAAANYYYGIPASQLSTSQAASLLAIVNNPSKFRFDDPTDEANGAANGYAATKERRDYILTEELKYSKISQEVYDAAIAEPITPNITEPSTGCATAGDAAYFCEYVLNVLRNDEAFGADDDERYQRIRQGGFDIVTTLDLDIQQVSQAAINAYIPSYDSRFQVGATAASIQAGTGRVLSMVQNTKYSQDEEFLAANPGFSAINLNVDVAMGGTAGVQTGSTYKVFTLAQWLQAGHTLNESFPSPTSGFRAYPQKCNVANDGLFTERFAPRNDVASEDASSMTAVQATANSINTGFMGMANQLDLCDIRTTAESFGIHRANGNELENGAASVLGTNEIAPLTVANAYAGIANDGSTCAAIVIDRITDSTGAAVAPPTSSCTQSVTPEVARGMQYAMQRVITSGTATASDPRDGIEHIGKTGTTDEAADVWTAGASRAASLAVWVGSIKGFDDGSKQNLRTTRLTGEKGTIRAADARHAIWKPIMTALDQKYGGDDFIDPPASMLASSPRSATLTEVPDVTGLTVAAATATLTAAGFSVGVTEPVDSARIPEGSVVSTTPSADETVLRGAVIPLQVSTGKAPKNPSDISDVNGTLLATASE
>NZ_CP047180.1|WP_123446628.1|819485_820421_+|cysteine-synthase-A
MARIHDDVTQLVGRTPLVRINRLDGADSAVVLAKLEFYNPANSVKDRIGVAIVDAAEASGELPPGGTIVEGTSGNTGIALAMVGAARGYKVILTMPETMSTERRVLLRAYGAEIVLTPGSEGMRGAVERAQAIVAETPGAVLARQFENAANPEVHRRTTAEEVWEDTDGEVDVFVAGIGTGGTITGVGQVLKERKPGVQIIGVEPIDSPLLTQGTAGPHKIQGIGANFVPANLDRDVYDEIIDVTLDDSVRVAREMAAQEGILGGISSGSIMWAALEVAKRPENAGKTIVAIVCDFGERYISTVLYEDLRS
>NZ_CP047180.1|WP_123447033.1|820417_821038_+|serine-O-acetyltransferase
MSAAGPHRGAAGRLTAFARLREDVAAARLRDPAARSAAEVVLAYPGLHAVWVHRLAHRWWRRGARLPARLLAQAARAATGVEIHPGATIGRRLFIDHGMGVVIGETARIGDDCMLYHSVTLGGKSAKRERRHPTLGDRVVVGAGAVILGPIVLGSDVSVGANAVVVKDAPDGAVLVGIPARDLRALGRAEDALADPAFWIDPAMYI
>NZ_CP047180.1|WP_159422110.1|821083_822553_-|deoxyribodipyrimidine-photo-lyase
MSSSSSTLVWLRDDLRLADNPALRAAIDRGGPVAVCYVLDEESDGIRPLGGAARWWLHGSLLALAGDLEEVGASLILRRGPAEAVVLQLAEELDAGAVHWNRRYGKAERTVDAAIKEALRDRDVEAESHQGSLLFEPWTVQTGGGTPYSVYTPFARACRNRDTPRAPLPRPREIDGIAAEAASDDLDDWQLLPTSPDWAGGLRERWVPGEKAAAKRLRAFLAEQLDDYADDRNLPARDATSNLSPHLRWGEISPFQVWHALEEAHAKGQHRGEGSDRFLAEVLWREFCYHLLFHWPDLAIANFDSRFDSFPWGHPGEDRIDAWHQGRTGFPLVDAGMRELWKTGYMHNRVRMVTASFLIKNLLVDWRVGEDWFWDTLVDADPASNAANWQWVAGSGADASPFFRVFNPVTQSKKFDPEGGYLREYVPELAELDRTVIHEPWTLGDTLTPEADGYPAPILDLKETRAHALDAFAVIKSAKRDISRPDDDD
>NZ_CP047180.1|WP_127887446.1|822638_823229_-|winged-helix-turn-helix-transcriptional-regulator
MKAGRSPQRPAFCRSRTEHRLRATAAGRPRAPGAGRPSRRRILNGTQGGCVSSRRAVAAWESLFRAQVHVMRALSTDFPSKEISLNEYDVLFNLTLQPERRARLRDLNKHVLLTQPSVSRLIDRLVARGCVTKSEDPTDARGTVIQITDEGYALFRRVAMTHMQTISDHVGAALDDDELDQLTALCDKLRERVASA

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Crispr_ID: NZ_CP047180_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_7

1792294-1792373

Orphan

Consensus_repeat	Method
CTCATGCTGATCGAGTAGCCCGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_7

>merge|NZ_CP047180|7|1792294-1792373|CRISPRCasFinder
CTCATGCTGATCGAGTAGCCCGCGGAGCGCGCGTATCGAGATACACCAGCATGTGACTCATGCTGATCGAGTAGCGCGCG

>NZ_CP047180|7|6|1792294-1792373|CRISPRCasFinder
CTCATGCTGATCGAGTAGCCCGCG	GAGCGCGCGTATCGAGATACACCAGCATGTGA
CTCATGCTGATCGAGTAGCGCGCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_123446284.1\|1789364_1789697_+\|metal-sulfur-cluster-assembly-factor	unknown	unknown	gnl\|CDD\|225062
NZ_CP047180.1\|WP_123446293.1\|1797003_1798263_-\|glucose-1-phosphate-adenylyltransferase	unknown	unknown	gnl\|CDD\|234846
NZ_CP047180.1\|WP_123446570.1\|1793372_1793603_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_123704299.1\|1784941_1785196_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_123446285.1\|1789781_1790387_-\|biotin-transporter-BioY	unknown	unknown	gnl\|CDD\|224187
NZ_CP047180.1\|WP_159422577.1\|1783092_1784025_+\|protoheme-IX-farnesyltransferase	unknown	unknown	gnl\|CDD\|235293
NZ_CP047180.1\|WP_123735783.1\|1792515_1793376_-\|SURF1-family-protein	unknown	unknown	gnl\|CDD\|119401
NZ_CP047180.1\|WP_127886865.1\|1793602_1793953_-\|DUF3099-domain-containing-protein	unknown	unknown	gnl\|CDD\|378630
NZ_CP047180.1\|WP_123446282.1\|1788270_1788600_+\|non-heme-iron-oxygenase-ferredoxin-subunit	unknown	unknown	gnl\|CDD\|239604
NZ_CP047180.1\|WP_123733093.1\|1790560_1792159_+\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|223562
NZ_CP047180.1\|WP_159422580.1\|1794847_1795489_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|339675
NZ_CP047180.1\|WP_123446295.1\|1799564_1800347_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224044
NZ_CP047180.1\|WP_159422578.1\|1784024_1784984_+\|heme-A-synthase	unknown	unknown	gnl\|CDD\|224528
NZ_CP047180.1\|WP_159422583.1\|1798350_1799532_+\|glycogen-synthase	unknown	unknown	gnl\|CDD\|273997
NZ_CP047180.1\|WP_127886864.1\|1794084_1794795_+\|beta-ketoacyl-ACP-reductase	unknown	unknown	gnl\|CDD\|187594
NZ_CP047180.1\|WP_123446280.1\|1785546_1786965_+\|Fe-S-cluster-assembly-protein-SufB	unknown	unknown	gnl\|CDD\|131035
NZ_CP047180.1\|WP_123446283.1\|1788600_1789362_+\|Fe-S-cluster-assembly-ATPase-SufC	unknown	unknown	gnl\|CDD\|223473
NZ_CP047180.1\|WP_159422582.1\|1796265_1796925_-\|phosphoserine-phosphatase-SerB	unknown	unknown	gnl\|CDD\|319803
NZ_CP047180.1\|WP_159422579.1\|1787035_1788274_+\|Fe-S-cluster-assembly-protein-SufD	unknown	unknown	gnl\|CDD\|376550
NZ_CP047180.1\|WP_159422581.1\|1795482_1796250_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_123446284.1\|1789364_1789697_+\|metal-sulfur-cluster-assembly-factor	gnl\|CDD\|225062	COG2151, PaaD, Predicted metal-sulfur cluster biosynthetic enzyme [General function prediction only].	4.92973e-31
NZ_CP047180.1\|WP_123446295.1\|1799564_1800347_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224044	COG1119, ModF, ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion transport and metabolism].	4.89923e-87
NZ_CP047180.1\|WP_159422583.1\|1798350_1799532_+\|glycogen-synthase	gnl\|CDD\|273997	TIGR02149, glgA_Coryne, glycogen synthase, Corynebacterium family. This model describes Corynebacterium glutamicum GlgA and closely related proteins in several other species. This enzyme is required for glycogen biosynthesis and appears to replace the distantly related TIGR02095 family of ADP-glucose type glycogen synthase in Corynebacterium glutamicum, Mycobacterium tuberculosis, Bifidobacterium longum, and Streptomyces coelicolor. [Energy metabolism, Biosynthesis and degradation of polysaccharides].	0
NZ_CP047180.1\|WP_159422580.1\|1794847_1795489_+\|hypothetical-protein	gnl\|CDD\|339675	pfam16264, SatD, SatD family (SatD). This family consists of uncharacterized proteins around 220 residues in length and is mainly found in various Streptococcus species. The function of this family is involved in acid resistance.	5.87215e-13
NZ_CP047180.1\|WP_123446285.1\|1789781_1790387_-\|biotin-transporter-BioY	gnl\|CDD\|224187	COG1268, BioY, Uncharacterized conserved protein [General function prediction only].	1.6563e-36
NZ_CP047180.1\|WP_159422577.1\|1783092_1784025_+\|protoheme-IX-farnesyltransferase	gnl\|CDD\|235293	PRK04375, PRK04375, protoheme IX farnesyltransferase; Provisional.	9.95975e-140
NZ_CP047180.1\|WP_123735783.1\|1792515_1793376_-\|SURF1-family-protein	gnl\|CDD\|119401	cd06662, SURF1, SURF1 superfamily. Surf1/Shy1 has been implicated in the posttranslational steps of the biogenesis of the mitochondrially-encoded Cox1 subunit of cytochrome c oxidase (complex IV). Cytochrome c oxidase (complex IV), the terminal electron-transferring complex of the respiratory chain, is an assemblage of nuclear and mitochondrially-encoded subunits. Its assembly is mediated by nuclear encoded assembly factors, one of which is Surf1/Shy1. Mutations in human Surf1 are a major cause of Leigh syndrome, a severe neurodegenerative disorder.	1.68219e-46
NZ_CP047180.1\|WP_127886865.1\|1793602_1793953_-\|DUF3099-domain-containing-protein	gnl\|CDD\|378630	pfam11298, DUF3099, Protein of unknown function (DUF3099). Some members in this family of proteins are annotated as membrane proteins however this cannot be confirmed. Currently no function is known.	7.42254e-16
NZ_CP047180.1\|WP_123446282.1\|1788270_1788600_+\|non-heme-iron-oxygenase-ferredoxin-subunit	gnl\|CDD\|239604	cd03528, Rieske_RO_ferredoxin, Rieske non-heme iron oxygenase (RO) family, Rieske ferredoxin component; composed of the Rieske ferredoxin component of some three-component RO systems including biphenyl dioxygenase (BPDO) and carbazole 1,9a-dioxygenase (CARDO). The RO family comprise a large class of aromatic ring-hydroxylating dioxygenases found predominantly in microorganisms. These enzymes enable microorganisms to tolerate and even exclusively utilize aromatic compounds for growth. ROs consist of two or three components: reductase, oxygenase, and ferredoxin (in some cases) components. The ferredoxin component contains either a plant-type or Rieske-type [2Fe-2S] cluster. The Rieske ferredoxin component in this family carries an electron from the RO reductase component to the terminal RO oxygenase component. BPDO degrades biphenyls and polychlorinated biphenyls. BPDO ferredoxin (BphF) has structural features consistent with a minimal and perhaps archetypical Rieske protein in that the insertions that give other Rieske proteins unique structural features are missing. CARDO catalyzes dihydroxylation at the C1 and C9a positions of carbazole. Rieske ferredoxins are found as subunits of membrane oxidase complexes, cis-dihydrodiol-forming aromatic dioxygenases, bacterial assimilatory nitrite reductases, and arsenite oxidase. Rieske ferredoxins are also found as soluble electron carriers in bacterial dioxygenase and monooxygenase complexes.	1.29558e-39
NZ_CP047180.1\|WP_123733093.1\|1790560_1792159_+\|ABC-F-family-ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|223562	COG0488, Uup, ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only].	6.64235e-171
NZ_CP047180.1\|WP_159422578.1\|1784024_1784984_+\|heme-A-synthase	gnl\|CDD\|224528	COG1612, CtaA, Uncharacterized protein required for cytochrome oxidase assembly [Posttranslational modification, protein turnover, chaperones].	2.82774e-26
NZ_CP047180.1\|WP_127886864.1\|1794084_1794795_+\|beta-ketoacyl-ACP-reductase	gnl\|CDD\|187594	cd05333, BKR_SDR_c, beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs. This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	8.16763e-109
NZ_CP047180.1\|WP_123446280.1\|1785546_1786965_+\|Fe-S-cluster-assembly-protein-SufB	gnl\|CDD\|131035	TIGR01980, UPF0051_protein_slr0074, FeS assembly protein SufB. This protein, SufB, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	0
NZ_CP047180.1\|WP_123446283.1\|1788600_1789362_+\|Fe-S-cluster-assembly-ATPase-SufC	gnl\|CDD\|223473	COG0396, sufC, Cysteine desulfurase activator ATPase [Posttranslational modification, protein turnover, chaperones].	1.4885e-137
NZ_CP047180.1\|WP_159422582.1\|1796265_1796925_-\|phosphoserine-phosphatase-SerB	gnl\|CDD\|319803	cd07500, HAD_PSP, phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p. This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	1.69713e-76
NZ_CP047180.1\|WP_159422579.1\|1787035_1788274_+\|Fe-S-cluster-assembly-protein-SufD	gnl\|CDD\|376550	pfam01458, UPF0051, Uncharacterized protein family (UPF0051).	5.31836e-85
NZ_CP047180.1\|WP_123446293.1\|1797003_1798263_-\|glucose-1-phosphate-adenylyltransferase	gnl\|CDD\|234846	PRK00844, glgC, glucose-1-phosphate adenylyltransferase; Provisional.	0

>NZ_CP047180.1|WP_123733093.1|1790560_1792159_+|ABC-F-family-ATP-binding-cassette-domain-containing-protein
MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIAAKGSVDRGGEIGYLPQDPRSGDPEELARTRILDARGLGQLVLGMQEATVAMSSSDTAVSEAGMKKYGNLTDRFLSLGGYAAEAEAASIASNLNLPDRILDQPLKTLSGGQRRRIELARILFSDAQTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANRQVIDVYNMNWKNYLRQRAADEERRKKERVNVEKKAGALQLQAARFGAKASKAAAAHQMVARAERMLSGLEEVRAVDRVAKLRFPTPSACGRTPLQAQNLSKSYGSLEIFTSVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDAPDTGVIEAGHGLRIGYYAQEHETIDVKRSVLENMVSSSPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEGAVVLVSHDEGAVEALNPERVLIMPEGTEDHWTADYLDLIMLA
>NZ_CP047180.1|WP_123446285.1|1789781_1790387_-|biotin-transporter-BioY
MSSYSLAPSRPVLADRLLTRSLVTDLVLVLAAAAFTAGMAQLYIPMWPVPITGQTFAVLLVGTTLGALRGALSMGVYALVGALGAPIFTEGSSGWAVLAGPTGGYIVGFVLASIVTGWLAQRQWDRRVVGTVVTFLAGTATIYLVGLPWLATALGSMGYPADLGSVLTAGLVPFLVGDTLKILLAAALLPTTWALLGRRKG
>NZ_CP047180.1|WP_123446284.1|1789364_1789697_+|metal-sulfur-cluster-assembly-factor
MAVTTLDPKLFDQVEEALKDVMDPELGVNVVDLGLIYDLGWDDENDALVIHMTLTSAGCPLTDVLEEQTAESLDGVVEAFRINWVWMPPWGPDRITEDGRDMMRALGFSI
>NZ_CP047180.1|WP_123446283.1|1788600_1789362_+|Fe-S-cluster-assembly-ATPase-SufC
MSVLQISDLHVSVETEQGTKQILRGVDLTINQGEIHAVMGPNGSGKSTLAYTIAGHPKYHVDGGSITLDGVEVLDMTVDERARAGLFLAMQYPVEIPGVTNTNFLRTAKTAIAGEAPAIRTWTKDVKKAMADLRMDPSFAARNVNEGFSGGEKKRNEILQLELLAPQFAVLDETDSGLDVDALKIVSEGVNRAHASTGLGVLLITHYTRILRYIQPDFVHVFVAGRIAEQGGKELATRLEDEGYDRFLAPATA
>NZ_CP047180.1|WP_123446282.1|1788270_1788600_+|non-heme-iron-oxygenase-ferredoxin-subunit
MSDAARICAASELIPNQAVRYVVDGIAIAIVQDTAGEIHAIGDTCTHGEVSLAEGFVEDDTLECWAHGSAFSLRTGAPLNLPAFEPVPVFVVEVIDGDVYIDPTVTKEV
>NZ_CP047180.1|WP_159422579.1|1787035_1788274_+|Fe-S-cluster-assembly-protein-SufD
MTVPTSAPTSPAIDGADAAARLGIAAHSDGAFTPVQTRSERFASTDVDAFETVTGREIAWKLTPVARLGDLIDGPLDGSPTPLEWAAVEGVDVSWVGRDDARIGTAGLPEDRAAANAWSQFEQALSIRVTGEDEKVATLVRTGLGSAPRAAHTIIEAAPYARGVVVLQNEGEATLAENVEVLVGEGAQLTIVTLQEWADDARHLANHFLRVGRDAKVKHIVVTLGGSIVRVNPSAHLVERGADGELLGLYFADGGQHLEQQVYVDHDAPDTRSRVTYKGALQGQGARTVWIGDVLIRQSANGTDSYEQNRNLVLSDGTRADSIPNLEIETGDIAGAGHASATGRFDDEQLFYLQSRGIREDEARRLVVRGFLSEIVQQIGVTELEDRLQLAIEAELAGSAGQTGAYSPEVSA
>NZ_CP047180.1|WP_123446280.1|1785546_1786965_+|Fe-S-cluster-assembly-protein-SufB
MSDILIDRPELASLGVYEFGWSDSDSAGASARRGISPEVVSDISALKNEPAWMRERRMKALALFERKPMPTWGADLSDIDFDNIKYFVRSTEKQAQTWEDLPDDIKNTYEKLGIPEAERQRLVGGVAAQYESEVVYHQIREDLEEQGVIFMDTDTALREHPEIFEEYFGTVIPAGDNKFAALNTAVWSGGSFVYVPKGVRVDIPLQAYFRINTENMGQFERTLIIADEGSYVHYIEGCTAPIYKSDSLHSAVVEIIVKKNARVRYTTIQNWSNNVYNLVTKRAIAHEGATMEWIDGNIGSKVTMKYPSIFLVGEHAKGETLSVAFAGPGQHQDAGAKMIHMAPYTQSSIVSKSIARGGGRAGYRGEVRVDANAHHSANTVRCDALLVDTISRSDTYPAIDIRVDDVQLGHEATVSKVSEEQLFYLMSRGMPEDEAMAMIVRGFIEPIARELPMEYALELNKLIEMGMEGSVG
>NZ_CP047180.1|WP_123704299.1|1784941_1785196_-|hypothetical-protein
MTNDDSIPTLPRLLLALARTGLEPRPARDFGALAEPLARSLPLPRLALALVRLRRHLRSGGKGLRAGHRPSQSAGASSSTACRR
>NZ_CP047180.1|WP_159422578.1|1784024_1784984_+|heme-A-synthase
MVTPFSFLAERVTLSPRALRWGTTAALVASILIIFFGGVVRLTGSGLGCPTWPACDAGSLTSTPELGIHGFIEFTNRAFTGVLIVAVGWAITAARLQKPRDRTMTRLAWSQFWLVVANALAGGATVHSGLNPYIVAGHFMLAIALLTTTALTWHRAHRSQSVAFEPDALTRGVSIALVAVTLAVIAVGTLVTGTGPHAGDSAEVPRMRFHWESVTVVHGVLGTATLVLGLALLVLLARVPGSELARRRVITFLVVVGMQALVGVAQSLLALPEALVAVHLLGSAFVWVGALRVLLDVNPRLFTVRAQRRQAVEELAPAL
>NZ_CP047180.1|WP_159422577.1|1783092_1784025_+|protoheme-IX-farnesyltransferase
MDVVAETTAIERGGPVRSPLSRKVRAYVALTKPRVIELLLVVTAPTMILAQGGIPNLLLVLNVLIGGALSAGSAGAFNCYIDRDIDRVMKRTRNRPLVTGEVSDREALVFATTIGVLSIVWLGLTANWLAASLSLAAILIYVLFYTLFLKRRTPQNIVWGGIAGCMPVLIGWAAVANSLDWAPIILFSVIFLWTPPHYWPLSMKYREDYRAAGVPMLAVVRGRSIVGLQVILYAWATVACSLLLIPVAGMGVVYTVVALASGVWFIAETHRLYSLAIRHEHVSPMRVFHGSIGYLTLLFLAVGIDPLLPF
>NZ_CP047180.1|WP_123735783.1|1792515_1793376_-|SURF1-family-protein
MSATATRPSWRFAFSRRWFGYLALTIVFAVACVLLSRWQVARLDEAASTNRLVTANWNADPVALDGLLPEGASWDDALEYRPVEVSGVYETDGETLVRNRPYNGNPGFEILTPLRLADGSVFVVDRGWVPVGSTQDSPDVVPAPPEGEVTVTARLKPGEGRIEGRGAPAGQIATIQLDDLSAQLDEPLRTAGYGLLVQEDPAPIEERPLAAIKPVADEGLHISYAIQWVLFAIMGFGGLAWAIRHEYRIRNADDPEVIAAEERREQRRLRRGRTDAEIEDELLDAR
>NZ_CP047180.1|WP_123446570.1|1793372_1793603_-|hypothetical-protein
MPLGGVPDQHACSRAGCALTATWAIEWRNPRIHTADRRKTWLACGEHLDYLREFLAAREFPLEVKPLLTVDRGAAL
>NZ_CP047180.1|WP_127886865.1|1793602_1793953_-|DUF3099-domain-containing-protein
MKSRESLTSLPPSPSAARRSRAIKYSIAMGIRMVCVICLIFAQGWWLLFFALGAIVLPYFAVVLANVGSAGESGTVERPGAIVLSRPVPPYVPPTADDAAPSADAPEGGDPSEGRR
>NZ_CP047180.1|WP_127886864.1|1794084_1794795_+|beta-ketoacyl-ACP-reductase
MTTPRTVLVTGGNRGIGYAIAEEFVAAGHRVAVTARSGSGPEGSFTVVADVTDSASIDAAFSQIEAELGPVEVVVANAGITRDMLLLRMSEEDFTSVVDTNLTGAFRVVKRASKAMLKQRFGRIVLISSVVGLYGGPGQINYSSSKAALVGFARSLTRELGARNITANVVAPGFIETDMTAELPAEQQAEYRKSIPLARYGTAAEVAKVTRWLASDEADYISGAVIPVDGGLGMGH
>NZ_CP047180.1|WP_159422580.1|1794847_1795489_+|hypothetical-protein
MTEPPVVAVLLDLVDSREITARSSVQRAIERGFAAVDAAVPALEPLHPTVGDEFQAVYASVSAALGATLQARLALPPGVDCRVGLGRGEVRVVGSGVAGDLQDGPGWWRARAAIERAHALEDGAVPTARGWFIASDAPDAQEAAVNAYLLARDALVGEMSDRDRRLVLGTARGLPQKILAEQESITQSAVSQALRRAGAGALLTGARLLADAC
>NZ_CP047180.1|WP_159422581.1|1795482_1796250_+|hypothetical-protein
MLTALLLALVGLADLARTHLGRPVAAGAVVVLWVGAVLSAVLGLGAPPLGVATVAVLAGVWLLLTTTAAGSRPPGGLRPAVGLVVAVLVLSLLDRATGPAAGPLVDAYAGLGRSGPIPPIAQALLAGGAALFLLESANVVVRAALYRELPQPVAARSRFSLRDRFARSAPQEVRVPDLRGGRAIGPLERLLVAGLTLAGAIGLAGAVFAAKGIVRFPEISRDGEGGSKAEYFLVGSLVSWALALGAAALVATAGG
>NZ_CP047180.1|WP_159422582.1|1796265_1796925_-|phosphoserine-phosphatase-SerB
MSEPLRTPARFLVVVDADSTLLQDEVIELLAAHAGSEERVAAITERAMHGEIDFGESLRERVATLAGVLDDVCAGVSARVRVTPGVEELIAGIHSAGGRIGVVSGGFHEVLDPVAGALGLDFVRANRLGSRDGRLTGAVEGPVIDAAAKAAALCEWAAESGVPLRRAIAVGDGANDLEMMRVAGLSVAFNAKPVVRERADLVVDGLDLSQLLPVLGLRG
>NZ_CP047180.1|WP_123446293.1|1797003_1798263_-|glucose-1-phosphate-adenylyltransferase
MQSKKIFGIVLAGGEGKRLMPLTADRAKPAVPFGGQYRLIDFALSNLINSGLTQIVVLTQYKSHSLDRHVSQTWTLSGLLNSYVASVPAQQRLGKRWFSGSADAILQSLNLIRDEKPDIVVVVGADHVYRMDFSQMIEAHIKSGAKATVAAIRQPIELADQFGVIQLAGDEAGDGIVPTKIAEFLEKPKDAVGLADSPHEVLASMGNYVFDADALIDAVIRDGELSTSDHDMGGDIIPDFVARGEAGVYDLKLNEVPGSTDRDRYYWRDVGTIDSFFEAHQDLISALPVFNLYNQQWPIFSSQLNSPPAKIVRDGKGNLGTTVDSVVSLGTVISGAHIERSVVGPWAVIESNATVSDSVVFDKVRIGPDAVVARAILDKDVVVEPGARVGVDHDHDRERGFTVTESGITVVGKGVVVRP
>NZ_CP047180.1|WP_159422583.1|1798350_1799532_+|glycogen-synthase
MRVDLLTKEYPPEVYGGAGVHVAELTKALRHDIEVVVRCFGAPRDEEGAFAYPVPAELSQANGALQTLGVDLQIAQDAAGADLVHSHTWYANAAGHLAQLLHGIPHVVSAHSLEPLRPWKAEQLGGGYRVSSWIEREAYESADAVIAVSGGMRNDILRSYPALDPAKVHVVYNGIDLDAWHPVEDEAVLAELGIDPSRPSVVFVGRITRQKGLPYLLRAAAMLPPEVQLVLCAGAPDTPEIMAEVTALVRGLQQERTGVVWIDRHLPRHQLSAVLTAATTFVCPSIYEPLGIVNLEAMACGAAVVGTATGGIPEVVVDGVTGRLVPIEQVTDGTGTPVDPDRYVADLAAAMAEVVADPAAAKRMGEAGRLRAQSDFSWTQIARDTRAIYDSLV
>NZ_CP047180.1|WP_123446295.1|1799564_1800347_+|ABC-transporter-ATP-binding-protein
MPSVVSFVDVSFVRNGKRILDHVDWTVSEEERWVILGSNGAGKTSILQIAAAQNYPSTGSAHLLEETLGRVDVFELRPRIGYASTAMARRLPAGETVLDVVMTAAYAVTGRWNEGYDEIDERRARRVLVEWKLDHLADRTFGTLSDGEQKRVQIARAIMTDPELLLLDEPAGSLDLGAREELVQLLGGFAQDPASPAIVMVTHHVEEIPAGFTHALLLRDGAVVAAGPLAEALTEATLADAFGLDIALTHENGRYSARAR

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Crispr_ID: NZ_CP047180_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_8

2657822-2657933

Orphan

Consensus_repeat	Method
GCTGGTCGAGCAGCCCCGCAGGAGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_8

>merge|NZ_CP047180|8|2657822-2657933|CRISPRCasFinder
GCTGGTCGAGCAGCCCCGCAGGAGCGTCTCCTTCGCCACCGTGCTCCGGTGCGTGGGTCTCCTTGGAAGAGACGCCCGCAGACCATGCTGGTCGAGCAGCCCCGCAGGGGCG

>NZ_CP047180|8|7|2657822-2657933|CRISPRCasFinder
GCTGGTCGAGCAGCCCCGCAGGAGCG	TCTCCTTCGCCACCGTGCTCCGGTGCGTGGGTCTCCTTGGAAGAGACGCCCGCAGACCAT
GCTGGTCGAGCAGCCCCGCAGGGGCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_164874434.1\|2659756_2661079_-\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	unknown	unknown	gnl\|CDD\|236486
NZ_CP047180.1\|WP_123445564.1\|2661152_2661749_-\|3-isopropylmalate-dehydratase-small-subunit	unknown	unknown	gnl\|CDD\|179314
NZ_CP047180.1\|WP_123445992.1\|2652317_2652902_+\|16S-rRNA-(guanine(966)-N(2))-methyltransferase-RsmD	unknown	unknown	gnl\|CDD\|223813
NZ_CP047180.1\|WP_159423117.1\|2666921_2668220_-\|trypsin-like-serine-protease	unknown	unknown	gnl\|CDD\|214473
NZ_CP047180.1\|WP_159424105.1\|2645412_2647587_-\|DEAD/DEAH-box-helicase	unknown	unknown	gnl\|CDD\|236794
NZ_CP047180.1\|WP_159424107.1\|2661751_2663167_-\|3-isopropylmalate-dehydratase-large-subunit	unknown	unknown	gnl\|CDD\|235490
NZ_CP047180.1\|WP_159423113.1\|2653981_2654485_+\|DUF3515-family-protein	unknown	unknown	gnl\|CDD\|378794
NZ_CP047180.1\|WP_123445569.1\|2655866_2657021_-\|NAD(P)-dependent-glycerol-3-phosphate-dehydrogenase	unknown	unknown	gnl\|CDD\|234629
NZ_CP047180.1\|WP_159423114.1\|2658075_2658759_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159424108.1\|2664111_2664873_-\|serine/threonine-protein-phosphatase	unknown	unknown	gnl\|CDD\|223704
NZ_CP047180.1\|WP_127886247.1\|2654492_2654867_-\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224639
NZ_CP047180.1\|WP_123445574.1\|2651185_2652229_-\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
NZ_CP047180.1\|WP_159423112.1\|2652924_2653956_-\|thiamine-phosphate-kinase	unknown	unknown	gnl\|CDD\|100030
NZ_CP047180.1\|WP_159423111.1\|2649840_2651196_-\|DUF58-domain-containing-protein	unknown	unknown	gnl\|CDD\|224635
NZ_CP047180.1\|WP_123445570.1\|2654863_2655970_-\|D-alanine--D-alanine-ligase	unknown	unknown	gnl\|CDD\|234993
NZ_CP047180.1\|WP_159423115.1\|2658930_2659518_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_123445562.1\|2663446_2664013_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423116.1\|2666257_2666896_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293802
NZ_CP047180.1\|WP_159423110.1\|2647597_2649844_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376628
NZ_CP047180.1\|WP_123445561.1\|2664910_2665954_-\|TerC-family-protein	unknown	unknown	gnl\|CDD\|274743

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_164874434.1\|2659756_2661079_-\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	gnl\|CDD\|236486	PRK09369, PRK09369, UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated.	0
NZ_CP047180.1\|WP_123445564.1\|2661152_2661749_-\|3-isopropylmalate-dehydratase-small-subunit	gnl\|CDD\|179314	PRK01641, leuD, 3-isopropylmalate dehydratase small subunit.	7.03672e-121
NZ_CP047180.1\|WP_123445992.1\|2652317_2652902_+\|16S-rRNA-(guanine(966)-N(2))-methyltransferase-RsmD	gnl\|CDD\|223813	COG0742, COG0742, N6-adenine-specific methylase [DNA replication, recombination, and repair].	1.33332e-51
NZ_CP047180.1\|WP_159423117.1\|2666921_2668220_-\|trypsin-like-serine-protease	gnl\|CDD\|214473	smart00020, Tryp_SPc, Trypsin-like serine protease. Many of these are synthesised as inactive precursor zymogens that are cleaved during limited proteolysis to generate their active forms. A few, however, are active as single chain molecules, and others are inactive due to substitutions of the catalytic triad residues.	4.69496e-06
NZ_CP047180.1\|WP_159424105.1\|2645412_2647587_-\|DEAD/DEAH-box-helicase	gnl\|CDD\|236794	PRK10917, PRK10917, ATP-dependent DNA helicase RecG; Provisional.	0
NZ_CP047180.1\|WP_159423113.1\|2653981_2654485_+\|DUF3515-family-protein	gnl\|CDD\|378794	pfam12028, DUF3515, Protein of unknown function (DUF3515). This family of proteins is functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 166 to 214 amino acids in length. This protein has a conserved RCG sequence motif.	2.5634e-14
NZ_CP047180.1\|WP_123445569.1\|2655866_2657021_-\|NAD(P)-dependent-glycerol-3-phosphate-dehydrogenase	gnl\|CDD\|234629	PRK00094, gpsA, NAD(P)H-dependent glycerol-3-phosphate dehydrogenase.	5.85039e-152
NZ_CP047180.1\|WP_159424108.1\|2664111_2664873_-\|serine/threonine-protein-phosphatase	gnl\|CDD\|223704	COG0631, PTC1, Serine/threonine protein phosphatase [Signal transduction mechanisms].	5.48236e-53
NZ_CP047180.1\|WP_127886247.1\|2654492_2654867_-\|GntR-family-transcriptional-regulator	gnl\|CDD\|224639	COG1725, COG1725, Predicted transcriptional regulators [Transcription].	3.40504e-23
NZ_CP047180.1\|WP_123445574.1\|2651185_2652229_-\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	2.45712e-93
NZ_CP047180.1\|WP_159423112.1\|2652924_2653956_-\|thiamine-phosphate-kinase	gnl\|CDD\|100030	cd02194, ThiL, ThiL (Thiamine-monophosphate kinase) plays a dual role in de novo biosynthesis and in salvage of exogenous thiamine. Thiamine salvage occurs in two steps, with thiamine kinase catalyzing the formation of thiamine phosphate, and ThiL catalyzing the conversion of this intermediate to thiamine pyrophosphate. The N-terminal domain of ThiL binds ATP and is related to the ATP-binding domains of hydrogen expression/formation protein HypE, the AIR synthases, FGAM synthase and selenophosphate synthetase (SelD).	2.48275e-90
NZ_CP047180.1\|WP_159423111.1\|2649840_2651196_-\|DUF58-domain-containing-protein	gnl\|CDD\|224635	COG1721, COG1721, Uncharacterized conserved protein (some members contain a von Willebrand factor type A (vWA) domain) [General function prediction only].	6.10736e-19
NZ_CP047180.1\|WP_123445570.1\|2654863_2655970_-\|D-alanine--D-alanine-ligase	gnl\|CDD\|234993	PRK01966, ddl, D-alanine--D-alanine ligase.	1.6135e-168
NZ_CP047180.1\|WP_159424107.1\|2661751_2663167_-\|3-isopropylmalate-dehydratase-large-subunit	gnl\|CDD\|235490	PRK05478, PRK05478, 3-isopropylmalate dehydratase large subunit.	0
NZ_CP047180.1\|WP_159423116.1\|2666257_2666896_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293802	cd07716, RNaseZ_short-form-like_MBL-fold, uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain. The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.	4.33623e-16
NZ_CP047180.1\|WP_159423110.1\|2647597_2649844_-\|hypothetical-protein	gnl\|CDD\|376628	pfam01841, Transglut_core, Transglutaminase-like superfamily. This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.	1.45584e-22
NZ_CP047180.1\|WP_123445561.1\|2664910_2665954_-\|TerC-family-protein	gnl\|CDD\|274743	TIGR03718, R_switched_Alx, integral membrane protein, TerC family. Rfam model RF00080 describes a structured RNA element called the yybP-ykoY leader, or SraF, which may precede one or several genes in a genome. Members of this highly hydrophobic protein family often are preceded by a yybP-ykoY leader, which may serve as a riboswitch. From the larger group of TerC homologs (pfam03741), this subfamily contains TerC itself from Alcaligenes sp. plasmid IncHI2 pMER610 and from Proteus mirabilis. It also contains the alkaline-inducible E. coli protein Alx, which unlike the two TerC examples is preceded by a yybP-ykoY leader.	7.98746e-137

>NZ_CP047180.1|WP_123445569.1|2655866_2657021_-|NAD(P)-dependent-glycerol-3-phosphate-dehydrogenase
MSRGSRAEKAPIPVPRRVAVLGAGSWGTTFAKILADGGSDVVMWARRAELAREITEAKRNSDYLPGINLPRNIRATPRIEEALEGADHVYLSIPSQTLRGNLEAITPFLTERTVLVSLMKGVEKGTGQRMSEVISQVLPIDPSRIAVASGPNLALEIAKEQPTAAVIASESLVTAQEVALAATNRYFRSYVNTDVIGTEFGGVLKNLIAVAIGIVDGVGYGENTKASIITRGLAEMTDFAVAYGGRPETMSGLAGLGDLIATSSSSLSRNNTAGRLLGQGYSFGDVVKSMQQTAEGLSSVAPILELARARGVDMPIVEQVSQVLAGTLDPKDIAPHLTTDSDEPQGERNLDDQQARSGRSVRGAFKRALDQLRNGGGGAAGDRS
>NZ_CP047180.1|WP_123445570.1|2654863_2655970_-|D-alanine--D-alanine-ligase
MTSKLAVAVLFGGRSSEHSISCATAAGVLRAIDRDRFDVIPVGITADGAFVLEEDRPEKFALDASALPRVEDNGTRVRWPESALSRELTVTAADGSVRSLGDVDVVLPILHGPWGEDGTVQGMLELVGLPYVGSGVLASALGMDKHFTKTVFRAAGIAVAPWYTVTEAEWREDPSDASSALDELGLPAFVKPARAGSSVGVSRVDERSQLDAALEEAFSHDSRVLIESAIVGREVEIGVLGARRGESPRASVAGEVVVSGGGFYDFEAKYLGMKGVELVCPAELTEDELAEMRALAVSAFTAIGAEGLARVDFFLTADGFVINEINTMPGFTPISMFPRMWGASGVDYPDLISELLDLALERVPAAVR
>NZ_CP047180.1|WP_127886247.1|2654492_2654867_-|GntR-family-transcriptional-regulator
MTEAGLGLRLEPGPRAPFEQIREGITAQVAAGSLLVGTRLPAVRTLAEELGVAPGTVARAYKELEAAGIVETRGRAGTVVSGGVDSVEHELQLAAGAYAARARALGATPERALEVAAAALGTAV
>NZ_CP047180.1|WP_159423113.1|2653981_2654485_+|DUF3515-family-protein
MSYRLLRTPLVAAAAVLLLSGCSAAVALQPAADATNEGCAEVSVRLPDVVAELPERETNAQGTAAWGTPAAVILHCGVTPPGPTTELCVSVNGVDWIIDESQAADDVYTLTTYGRDPAVEITVDQSRASGTSAVVDLANAVSYLPQERACTNVSDTDTLDPPSTPAG
>NZ_CP047180.1|WP_159423112.1|2652924_2653956_-|thiamine-phosphate-kinase
MAPDPSPTLAELSEGEVLARILPRLGGGAETLVGPGDDSAVLRAPDGRFVVTTDMMVHGPDFRLAWSSPFDLGWKAAASNLSDVAAMGARPTGLVVAIAAPQRLGVDVLEGIADGLAAGCAAMAPGCGVVGGDLSASATLTLAITAFGSLDGRPPVLRSGARPGDVIATAGPLGVSGLGLRLLFERARTAGEPDAAVARALRAEHPEVLDAQLRPTPPIAAGIAAGGVATAMMDVSDGVVLDARRMARASGVVLDLDPDAVDAHAAPLTAVAGIDAALARALVLGGGEDHAMLACFPPGTALPPGFTALGTVREGASEVRLGGVALDERGGWDPYLGWDGAAG
>NZ_CP047180.1|WP_123445992.1|2652317_2652902_+|16S-rRNA-(guanine(966)-N(2))-methyltransferase-RsmD
MTRIIAGFAGSLTLRVPRAGTRPTSDRVREAIFSALEARDALDGATVIDLYAGSGALGLESASRGAASVLLVERDPKAAKTAGENARAIATAAASNKRPKPRIEVVIASVRSFLDGSPAVNADTVFLDPPYDLPEDELAADLAGVLPLLAEHSVVVVERSSRSPEPRWPAGLERDRRKDYGETTIWWASPAAGE
>NZ_CP047180.1|WP_123445574.1|2651185_2652229_-|MoxR-family-ATPase
MTSLDETRSAVGTASDRGAAPGSAMTREEFSAHCAAILKNLCSVIDGKDAEVSMALTVFLAGGHLLMEDVPGTGKTVLAKSLAASVGGTVSRIQFTPDLLPSDVTGVSVFNQATRDFEFKPGPVFANVVIGDEINRASPKTQSALLECMEERQVSVDGVTHILPRPFAVVATQNPVEMEGTYSLPEAQRDRFMARLSLGYPDERAELEMIRTRDAASPLEELRQVVGHDQLARMMDYVQSIYVAPPVQEYVVAIMQATRIDPELRLGGSPRATLQLIAAAKALAAINDRDFVVPDDIDVLAVPVLGHRLLPATRLPGRSGTGASHSVTEIVQRIVAATPVPFSGRAD
>NZ_CP047180.1|WP_159423111.1|2649840_2651196_-|DUF58-domain-containing-protein
MPTEPRGPRSGAPRSREPQRRGAERPARRIGALPAVRGVALTLRGWALVVLGALGIVVAPVIEFRELLFVGIVLLGLPVAAVLALLAVTPVLQVQRRFAPQVVAVGDVVDVDVVLDNRGAALRAGARAEDRLDRVERGLVSGRTVARGAFTLPAVAQRGSGSSRVRARYRLPAGRRGIHRIGPLRLLRGDLFGLAVRETIAGAAQPFVVTPRAVPLQSDVLDAHGAGGSSPVAHATAGAGTDDVIPRDYRPGDAMRRVHWRASARSGELKVRQDEQNTDPHAWILLETRAARILDERGGDDRLEWAVSMTASLAVHLLERGFETHLIETGAPDQPVRSEDEREAAHDVLLRLAELAPAAESVEAVGRIAAEMRDAGGSRPVFAVLSRLHEEDLAALASLAAHARPAVAFLVGGTPEEEAALASLGWYPVPVTPRTAVEEAWAQALALRVVA
>NZ_CP047180.1|WP_159423110.1|2647597_2649844_-|hypothetical-protein
MSRRGRDARSGSVLLSVLLWLSLVTASSGIGRLLEGIGWLVQLAVAVGVVLAVPAAARAVRAHPVVPPILGTLAAVGVLTAMFVPGRALLFLVPTPGAIADAQTLAQAGFTSIAEQGLPAVADNGIAFLLVGGVVVLAWAADLFAFSVRLPALAGLFPATLLAVPAIIDPADVSWPSLLLTALVYLGILAVSARPERRAPRGGSLGTAVPSIAMAGVVVIAAGLVAGSAGGFTRVSTPSGVSGTLFNGSIDPVVALGADLRRPNPVTVLRYSTDSDLPVYLRVLTVSDFEGEDWAPSDTEETADIAAPIAPAGLGEAVPRETEEVDVSVETLRSRWLPVPYPVSELSGVGDGWLQDVQDGSIRGDATTRAGDEYQVQALRLEPDPQQLLDAPVPTGFERYLSLPEDVPEIVRSTATEVTADEVTAYDRARALQTFFRSSEFRYSEDTPAEEGYDGDGVGVLASFLEVREGYCVHFASAMAVMARELGIPSRLAIGYQPGSVVPSPGTELTSYRVQSSDLHAWPELYFEGVGWLPFEPTPSRGAPASYTLPSATTSAPSTTPGAAASAAPGAEPGETATPTPTASTATAAPGALGGSTTSTAPVVTLWSLLVLLLLVPWLLRVVQRAVRRRRAADGSLEPAWAELVASARDLGIPVEDGESPRAQEALIADALGEDEGARSALRELRQGVERVRYAPVLAEQSAGWRAATTVVAGLRSSAGTGRRLSAAVAPRSVLPGLARVRRPRSDL
>NZ_CP047180.1|WP_159424105.1|2645412_2647587_-|DEAD/DEAH-box-helicase
MPDPLDASLAPLIGPRTAKPIEKAFGYRTVGELLGHYPRRYAKRGELTDVSRLPVGENVTIVAEVREVRSREMKNRRGGLLEVIISDGTGTLSLTFFGQPWRAAQLRRGVRGIFAGTVSMFRDTKQLTHPDYRLFEDEEVTAHGPIAKSALTKDWTERPIPIYPATSTIASWQLQAAIDVVLDDLKYVQDPIPAEVRANRKLLDLGAALELIHRPQREGEEIPARDTLRFHEAFLLQLALLERRAAARSTPGTRRVAEPGGLLERFDAALPFTLTDDQRTVGREIAGDLAAESPMSRLVQGEVGSGKTLVALRAMLATAESGGQSALLAPTEVLAGQHLRSIVRTLGPELAAELSPTLLTGGLGAAARRAALLRIVSGTAKIVVGTHALLGDKVSFYDLGLVVIDEQHRFGVDQRDALRRKGAQPPHVLVLTATPIPRTVAMTVFGDLDVSTIRELPAGRPGITSHVVPLADHPAWIARAWERAEEEIRKGHQVYLVCPAIEPGEAAEGPLAGEDEPAATPLSTVSETIEGVRGHALLGKRRSAALHGRMTAEEKDAVMRAFAAGEIDVLVSTTVIEVGVDVPNASMMIVLDAERFGVSQLHQLRGRIGRGGVPGVCLFVTAAEAGTTARERVETVAATLDGFELAEADLELRREGDVLGDSQSGGRSSLRLLRVVQDSWMILEARVLAERLLETDPVLATHDRLRAALERRVQERDREFLGKS
>NZ_CP047180.1|WP_159423114.1|2658075_2658759_+|hypothetical-protein
MSERRENPVSAALHRLTDSVTALPTLAFVLLLGFVAVYSIGTRSPELLAQLLAWAGLVAVGVALATGLVLVVVRSVARAVAGPLAHVEAEASDGEVVLSRGDLVDVLRWVEPRLPRRISRPYAVVVPAARGLSVSFRSHVVIVPWSRVRAVRRRRIRRGLRRHDAVVVDLSRAGGGRTRSLTLVPVEQPGLLGQSPASEQTLVLLHRRIAAALPPGEPAPAWGSPDG
>NZ_CP047180.1|WP_159423115.1|2658930_2659518_+|hypothetical-protein
MLAAASESPALLVAAATAAVTIVLLVVLVAARLVTAPRALVQASAIGGVVVVGGPAVSRLLRFGDPTLPTPDLHPYLVLDPAEEALVVLAGDRRVEILWDEIRALERRTVGLGSRTAIGVTVSRGFRPRSADLRLVEEPGLLGLRPASAESVDRFHGRLRAQVEAAGPASPDSRRARRRSGTRASARPAGIDREG
>NZ_CP047180.1|WP_164874434.1|2659756_2661079_-|UDP-N-acetylglucosamine-1-carboxyvinyltransferase
MTTERITIHGGRPLKGRIELKGAKNLVTKAMVAALLGETASTLRDVPDISDVRVVKGLLEVHGVKVKQGPEVGELILDPSNVESAHFADIDAHAGSSRIPILFCGPLLHRLGEAFIPDLGGCRIGDRPIDYHLEVLRNFGAIVEKLPSGIRMSAPEGLHGAKVSLPYPSVGATEQVLLTAVRASGITELSGAAIEPEIMDLINILQKMGAIISVDTDRVIRIEGVDRLEGYTHRALFDRNEAASWAAAALATDGDIFVGGARQQEMTTFLNVFRKVGGAFEIAEDGIRFYHPGGELKPVIIETDVHPGFMTDWQQPLVVALTKAKGVSIVHETVYEQRFGFVDALVEMGATIQIHRECLGGQACRFGQRNFMHSAVISGPSKLHGADIVVPDLRGGFSHLIAALSAEGTSSVSNVGIISRGYENFLTKLELLGADFSLDA
>NZ_CP047180.1|WP_123445564.1|2661152_2661749_-|3-isopropylmalate-dehydratase-small-subunit
MEKFETVTGIAAPLKRSNVDTDQIIPAVFLKRVTKTGFEDALFHGWRQDPEFVLNQPAFQGAQILVAGPDFGTGSSREHAVWALRDFGFRVVLSSRFGDIFRGNSGKQGLLAAALAESDIDRLWELIDATPGIEATVDLVGRTVTAGGETFPFEVDDYTRWRLIEGLDDIGLTLRDEALISEFETRRASWRPKTLPVK
>NZ_CP047180.1|WP_159424107.1|2661751_2663167_-|3-isopropylmalate-dehydratase-large-subunit
MAEKVWDDHLVAKGEDGTPDLIYIDLHLVHEVTSPQAFDGLRQAGRPVRRPDLTIATEDHNTPTVGIDKPIADLTSRTQIETLRRNAAEFGVRLHSLGDIEQGIVHVVGPQLGLTMPGITVVCGDSHTSTHGAFGAMAFGIGTSEVEHVMATQTLPLKPFKTMAITVEGELREGVTAKDIILAVIAKIGTGGGQGYVLEYRGSAIRALSMEGRMTICNMSIEAGARAGMVAPDETTFAYLKGRPHAPEGQDWDDAVAYWRTLPSDEGAVFDAEVVLDADALEPFVTWGTNPGQGVSLSQAVPDPDAIADPNERSNARRALEYMDLEAGTPMKEIPVDAVFMGSCTNSRIEDLRAFASIIAGRTKAPGVRVMVVPGSARVRIEAEAEGLDKVITAFGAEWRFAGCSMCLGMNPDQLAPGERCASTSNRNFEGRQGKGGRTHLVSPLVAAATAVRGTLSSPSDLEPVRELVEA
>NZ_CP047180.1|WP_123445562.1|2663446_2664013_-|hypothetical-protein
MDTVEALDRAKMRFAEGDVRGAVSLLERCVEADPTWIDPRVLLSELYRRSGDLIEAGRWGYLIENCAAPEERRAFERALVRTDEDPFEFAERALVRPLELAAESKHAAMMLAALPARIDEAERFERESPDPLDGDWFEHEALPVKRRSGFVGMVGAAVAAVFVVGGVVVGAAALLVVPAVLIAMLVAP
>NZ_CP047180.1|WP_159424108.1|2664111_2664873_-|serine/threonine-protein-phosphatase
MELPQGVLHLTVSSSTDVGAVRRVNEDALLVAPTLVAVADGMGGHARGDLASSTAVESLRASATEAIGPVSDVFAVVETANAAVRDLDVGGALCGTTLTGLTLVRPEDGGPASWALFNVGDSRVYRWDGAGIQQLTVDHSAVQELVSAGLLSREAAESHPDRNIVTRALGADDEVETDVWTLPIVPRATYLLCSDGLTKELSDARIAELFARRDAGDLHGADVAEELVRAAVDAGGRDNVTVVVVEAVLVPRA
>NZ_CP047180.1|WP_123445561.1|2664910_2665954_-|TerC-family-protein
MQELPVWFVTGSFVVLSLILAADLLLVYKRPHVPSLKESGLWVGFYVTLALIFALVMLLLGGGEVAGQFVAGWLTEYSLSIDNLFVFVIIMGRFAVPPKYQQEVLMVGIIIALIFRGVFILLGAQLIESFSWIFYLFGAFLVYTAWNQAFGKEDENEGTDNLLIRLLRKRVKISDEFDGSKIRTVKDGKKYFTPMLIVFLAIGSTDLLFALDSIPAIFGITESPFIVFTANIFALMGLRQLYFLLGGLIDKLEYLKYGIAFILAFIGVKLVLHALHENDLPFLNGGEPLPVWDIDTITSLAVIVVSMTVATVASLIKMRREHSHIELHDGHPEVVADADGQDRAEKK
>NZ_CP047180.1|WP_159423116.1|2666257_2666896_+|MBL-fold-metallo-hydrolase
MRLTKLEHATVLVEEAGSRLVLDPGSFTRLLEGTADTVAVVITHEHADHWTAEQLERLRAANPALRILGPAGVTAAAEGFEVETVAEGDVVEIGPFELRFFGSRHAVIHSSIPVIDNVGVLVNGRFYYAGDSFTVPAGVDVEVLGAPSGAPWMKIAESIDYVLELAPRHAFATHERVLSEAGQRLGHDRLGWATREGGGEYHALEPGDVLEL
>NZ_CP047180.1|WP_159423117.1|2666921_2668220_-|trypsin-like-serine-protease
MRTRFLRRTAAALVVLATVLGIGALTTAPAVALTSGTKSNEPWVVQVYDKIVGIQTNTCTGTAIAADWVLTVDHCPASHVYYRYAPSPTEDEVTEAVPVAESISLAPVDLKLLHLSRPHALPHYPRLVPGGYRVGSVGDVYGLGPDMFPTQRTEKVWIRKVGRMPNGALGMYSTATTGSTEQIGDTGDSGGPLIVNGNLVGVFYGTTLLGDPVQMMGYTDVRPALEKLKELQGHDRSPREAASDPTVGITDVSVVRGYVEATMSEALVRSGKRVVVWVNGRYAGDYNEGRGWYAWKYDVPGGTKIVPTTPVKDGDLVQVGVLASGVDVAAADLLFQSTLDGIDSVQRTGDRVAVTMSRALVNSGKRVVVWVDGVYRAEVLDDVSLYASKSNIDGASIITPDGTVPEGALVQIGVLPAGTDHDQAEILDARVL

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Crispr_ID: NZ_CP047180_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_9

2844564-2844671

Orphan

Consensus_repeat	Method
AGTCGAGCGCGAGTACCGCGACTTC	CRISPRCasFinder

1 spacers

DEDDh

The CRISPR arrays of NZ_CP047180_9

>merge|NZ_CP047180|9|2844564-2844671|CRISPRCasFinder
AGTCGAGCGCGAGTACCGCGACTTCCGCGGACTCGGAGGTGCCTCCGCCTCCCGGCCTCGCTCCACTCCCCGAGAGTTGCGGCAGTCGAGCGCGACTACCGCGACTTC

>NZ_CP047180|9|8|2844564-2844671|CRISPRCasFinder
AGTCGAGCGCGAGTACCGCGACTTC	CGCGGACTCGGAGGTGCCTCCGCCTCCCGGCCTCGCTCCACTCCCCGAGAGTTGCGGC
AGTCGAGCGCGACTACCGCGACTTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159423206.1\|2831773_2832895_+\|aminotransferase-class-V-fold-PLP-dependent-enzyme	unknown	unknown	gnl\|CDD\|224029
NZ_CP047180.1\|WP_127886151.1\|2833300_2833735_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423207.1\|2835754_2839687_+\|amino-acid-adenylation-domain-containing-protein	unknown	unknown	gnl\|CDD\|274093
NZ_CP047180.1\|WP_123445426.1\|2847962_2848550_+\|DNA-polymerase-III-subunit-epsilon	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|99834
NZ_CP047180.1\|WP_159423210.1\|2843534_2844209_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|223377
NZ_CP047180.1\|WP_159423212.1\|2848583_2849480_-\|hemagglutinin	unknown	unknown	unknown
NZ_CP047180.1\|WP_127886142.1\|2853396_2853957_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423209.1\|2842926_2843418_-\|DUF1877-domain-containing-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423213.1\|2849669_2850902_+\|DNA-recombination-protein-RmuC	unknown	unknown	gnl\|CDD\|376878
NZ_CP047180.1\|WP_127886145.1\|2846807_2847881_-\|redox-regulated-ATPase-YchF	unknown	unknown	gnl\|CDD\|236583
NZ_CP047180.1\|WP_127886150.1\|2834103_2835630_+\|multidrug-efflux-MFS-transporter	unknown	unknown	gnl\|CDD\|129794
NZ_CP047180.1\|WP_123702777.1\|2846275_2846479_-\|CopG-family-transcriptional-regulator	unknown	unknown	unknown
NZ_CP047180.1\|WP_123445422.1\|2854033_2855080_-\|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase	unknown	unknown	gnl\|CDD\|234893
NZ_CP047180.1\|WP_159423208.1\|2841021_2841765_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225002
NZ_CP047180.1\|WP_159423211.1\|2845881_2846271_-\|type-II-toxin-antitoxin-system-death-on-curing-family-toxin	unknown	unknown	gnl\|CDD\|226180
NZ_CP047180.1\|WP_123704712.1\|2851177_2852110_-\|class-II-fructose-bisphosphatase	unknown	unknown	gnl\|CDD\|236536
NZ_CP047180.1\|WP_123445978.1\|2841814_2842747_-\|polyphosphate-kinase-2	unknown	unknown	gnl\|CDD\|213852
NZ_CP047180.1\|WP_159424112.1\|2839704_2841039_+\|M1-family-peptidase	unknown	unknown	gnl\|CDD\|341066
NZ_CP047180.1\|WP_123445428.1\|2844284_2844497_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_123445424.1\|2852359_2853385_+\|class-II-fructose-bisphosphate-aldolase	unknown	unknown	gnl\|CDD\|236406

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_159423206.1\|2831773_2832895_+\|aminotransferase-class-V-fold-PLP-dependent-enzyme	gnl\|CDD\|224029	COG1104, NifS, Cysteine sulfinate desulfinase/cysteine desulfurase and related enzymes [Amino acid transport and metabolism].	1.87286e-157
NZ_CP047180.1\|WP_123445422.1\|2854033_2855080_-\|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase	gnl\|CDD\|234893	PRK01045, ispH, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Reviewed.	8.18234e-178
NZ_CP047180.1\|WP_159423207.1\|2835754_2839687_+\|amino-acid-adenylation-domain-containing-protein	gnl\|CDD\|274093	TIGR02353, NON-RIBOSOMAL_PEPTIDE_SYNTHETASE, non-ribosomal peptide synthetase terminal domain of unknown function. This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.	0
NZ_CP047180.1\|WP_123445426.1\|2847962_2848550_+\|DNA-polymerase-III-subunit-epsilon	gnl\|CDD\|99834	cd06130, DNA_pol_III_epsilon_like, an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with similarity to the epsilon subunit of DNA polymerase III. This subfamily is composed of uncharacterized bacterial proteins with similarity to the epsilon subunit of DNA polymerase III (Pol III), a multisubunit polymerase which is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. The Pol III holoenzyme is a complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.	9.52739e-67
NZ_CP047180.1\|WP_159423210.1\|2843534_2844209_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|223377	COG0300, DltE, Short-chain dehydrogenases of various substrate specificities [General function prediction only].	4.8917e-30
NZ_CP047180.1\|WP_159423213.1\|2849669_2850902_+\|DNA-recombination-protein-RmuC	gnl\|CDD\|376878	pfam02646, RmuC, RmuC family. This family contains several bacterial RmuC DNA recombination proteins. The function of the RMUC protein is unknown but it is suspected that it is either a structural protein that protects DNA against nuclease action, or is itself involved in DNA cleavage at the regions of DNA secondary structures.	1.57755e-97
NZ_CP047180.1\|WP_127886145.1\|2846807_2847881_-\|redox-regulated-ATPase-YchF	gnl\|CDD\|236583	PRK09601, PRK09601, redox-regulated ATPase YchF.	0
NZ_CP047180.1\|WP_127886150.1\|2834103_2835630_+\|multidrug-efflux-MFS-transporter	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	4.0217e-85
NZ_CP047180.1\|WP_159423208.1\|2841021_2841765_-\|hypothetical-protein	gnl\|CDD\|225002	COG2091, Sfp, Phosphopantetheinyl transferase [Coenzyme metabolism].	6.11467e-15
NZ_CP047180.1\|WP_159423211.1\|2845881_2846271_-\|type-II-toxin-antitoxin-system-death-on-curing-family-toxin	gnl\|CDD\|226180	COG3654, Doc, Prophage maintenance system killer protein [General function prediction only].	1.35603e-22
NZ_CP047180.1\|WP_123704712.1\|2851177_2852110_-\|class-II-fructose-bisphosphatase	gnl\|CDD\|236536	PRK09479, glpX, fructose 1,6-bisphosphatase II; Reviewed.	1.30278e-169
NZ_CP047180.1\|WP_123445978.1\|2841814_2842747_-\|polyphosphate-kinase-2	gnl\|CDD\|213852	TIGR03707, PPK2_P_aer, polyphosphate kinase 2, PA0141 family. Members of this protein family are designated polyphosphate kinase 2 (PPK2) after the characterized protein in Pseudomonas aeruginosa. This family comprises one of three well-separated clades in the larger family described by pfam03976. PA0141 from this family has been shown capable of operating in reverse, with GDP preferred (over ADP) as a substrate, producing GTP (or ATP) by transfer of a phosphate residue from polyphosphate. Most species with a member of this family also encode a polyphosphate kinase 1 (PPK1). [Central intermediary metabolism, Phosphorus compounds].	1.04966e-155
NZ_CP047180.1\|WP_159424112.1\|2839704_2841039_+\|M1-family-peptidase	gnl\|CDD\|341066	cd09603, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains mostly bacterial and some archaeal M1 peptidases with smilarity to the catalytic domain of aminopeptidase N (APN; CD13; alanyl aminopeptidase; EC 3.4.11.2), a type II integral membrane protease belonging to the M1 gluzincin family. APN preferentially cleaves neutral amino acids from the N-terminus of oligopeptides and, in higher eukaryotes, is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation, thus considered a marker of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs. APNs are also present in many pathogenic bacteria and represent potential drug targets. Some APNs have been used commercially, such as one from Lactococcus lactis used in the food industry. APN also serves as a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection. APNs have also been extensively studied as putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established.	3.06095e-166
NZ_CP047180.1\|WP_123445424.1\|2852359_2853385_+\|class-II-fructose-bisphosphate-aldolase	gnl\|CDD\|236406	PRK09197, PRK09197, fructose-bisphosphate aldolase; Provisional.	0

>NZ_CP047180.1|WP_123445428.1|2844284_2844497_+|hypothetical-protein
MSRPDTCAVLHRLVEVLEDPAPINPGHARHVSGLLAGALDSAPALRDCAGAPAQLVAFATEDPADENPAL
>NZ_CP047180.1|WP_159423210.1|2843534_2844209_-|SDR-family-NAD(P)-dependent-oxidoreductase
MTRFEGSIVLVLGASGGLGRLIADELEQRGATVVRSGRRAADLGDAPLVADLLGEDAPQRLVDEVLRRHGRLDGVVVAAGVVAFGPSAELDPAVLEELVDVNALAPIRVLTASFAALSASGNRPFAVTISGVVAEAPTAGLAAYSASKAALYSFVRASAREYRKAGVLLLDARPGHTETALSQHPLAGTAPRFGAGHSPESVAARIVCAVEDGETDLPPAAFDA
>NZ_CP047180.1|WP_159423209.1|2842926_2843418_-|DUF1877-domain-containing-protein
MGIRYYAYAFDADLTERALAYPRSVIGETALAGAWGMPHGAAIEAADLPQPVPEDDMLCLDRAWSGLQALTAPRSPGQPPRPAHRMLEGRVSLRGMCWDPWTRAVLPGEVPEIADDLLALRQELEEGLSQHPEGEQLGQYLDRAVDFASRIARSGRGFVYLIG
>NZ_CP047180.1|WP_123445978.1|2841814_2842747_-|polyphosphate-kinase-2
MPTPELLRSLTPEDARDLVVLDEDDDDPVLLRRDGTQIDTWREGYPYDERMSREEYEAGKRLLQIELLKLQNWIKKHGRRLVVVFEGRDAAGKGGTIKRFTEHLNPRGARVVALEKPTEREGTQWYFQRYVSHLPAAGEIVLFDRSWYNRAGVERVMGFCTPEQYDEFVRQTPLFESMLVGEGIDLVKLWFSVSAEEQRTRFTIRMIDPVRQWKLSPMDLASLDKWDDYTAAKEAMMAATDTADAPWTIVKSNDKKRARLEAMRYVLSLYDYDGRDDEVVSPLGPDPLIVGSAADVYERGEHAATARAAE
>NZ_CP047180.1|WP_159423208.1|2841021_2841765_-|hypothetical-protein
MRNDDGVRDLPGVHLRWLALDEQRLDAERLLPLLGTAERERYRATGSAAVAERFVFGRVLLRMLAGELLGLSASMVRVTARCSRCGGPHGRPWIEGAEHLSVSIAHCPGAVVVAASSAGVVGVDVEPVAGPPERGVAITRIAGAPFATGGFRAADPILHWTRIEAALKADGRGLDVDPRRVRIHESRFTAEARIDASRFRLAEPHLDPSLRVSVALGDSVGGAGPIIGWRREHGDALEDSLVSAGGR
>NZ_CP047180.1|WP_159424112.1|2839704_2841039_+|M1-family-peptidase
METAGDPYLPGIGNTGYRVESYDLDLDYRVSSNRLAGRATLRIVALQPLRRFSLDLSRLRATRVRVAGRKARSDQASHKLRITPAEPLEAGASAVVEIEYGGHPGPRASHWGELGWEELTDGVLVASQPSGASTWYPCNDDVADKATYRIRVSAEEGYSVLANGVLLETSERSGRRTWLYEQLEPTASYLASVQIGRYVLEDRLLSGVAVTLARPAALATRVARDFAPLSAMLAFFSRVFGPYPFRQYTVVVTADELEIPLEAQGMAVFGANHVDGRGGSERLIAHELAHQWFGNSVGLARWRHIWLNEGFACYAEWLWSEESGGLSADAQARRHHALLRFQRQDLVLGDPGPVDLFDDRVYKRGALTLHALRLRLGDGAFFRLLRTWTARHASSAASENDFRALCAEVAGGSAIAGGTAAAAVESLLDAWLVDVRLPPLPAAR
>NZ_CP047180.1|WP_159423207.1|2835754_2839687_+|amino-acid-adenylation-domain-containing-protein
MSTDAHPQNLLDAGALAPAPRTLIDVLRDTAERHPDASALEDPAGALSYRELLARVVSAAAELTAAGVRRGDRVGVRMASGSRELYLAILSILAAGAAYVPVDADDPEERARLVFGEAAVRGVVTGSGRFERTDAEPARLFTGSAPHPSTASVPLLQPPTLEDDAWIIFTSGSTGTPKGVAVSHRSAAAFVDAEARVFLQAEPLGPGDRVLAGLSVAFDASCEEMWLAWRHGACLVPAPRSLVRSGMDLGPWLTTHGITVVSTVPTLAALWPAESLENVRLLIFGGEACPPELGQRLAVDGREVWNTYGPTEATVVACAAPLGGPGPVRIGLPLDGWRLAVVDPEGRRVGEGEVGELIIGGVGLARYLDPAKDAEKYAPAPTLGWERAYRSGDLVRFESAGLVFQGRADDQVKLGGRRIELGEVEAALQGLPGVSGAAAAVRTTGAGIQVLVGYLALAGGRELDRDAALTRLREELPAALVPLLAVVDELPTRVSGKVDRAALPWPLPESTAADPGLDAGTAWLAGLWREVLGVPVDERANFFDLGGGSLAAAQLVARIREQDPEFTVADVYAHPRLAAMSAEIASRATGAGEVSSHRIAPVPRRMQVLQTLLGAPLLVLSGARWTTVVLTVCALLDLLPGFGWLPTVPLPGLVVAFALFCTPFGRMGLTVLAARALLRGVRAGDHPRGGGVHLRLWLAERIAHQLGAVSLAGAPWVAHYARALGARIADDVDLHSLPPLTGMLTLGRGAAIEPEVDLSGYWIDGDVLRVGAVRVGAGSTVGARSTLLPGTRIGKNAQIEPGSAVFGRVPAGQRWGGSPAQRLGKASAGFPAERPPRATPWVWAYAVSAVGLAAVPVVSFAAGLGVLALAVQGAADLAEALPRAVAALVPAVAVTGVVLAGLVVVLVRLLGRGVEAGTHPVRGRIGWQVWSTERLLDHARALLFPLYSGLFTPVWLRLLGAKVGRDVEASTVLLLPAMTTIRDGAFLADDTLVASYALGGGWMRLARAEIGERAFLGNSGMAAPGHTVPAGGLVAVLSSAPRKSKAGSSWLGSPPVRLRRTVVEAESARTFRPAMRLRAARIVWELLRFVPVVVSMAIGLGVVAALLALVPVIGAIATAVAGGIVLLAAGAVAAGVSTGAKWLLIQRVRPSEQPLWSSFVWRSELADTFTEMVAAPWFAHAAAGTPALVWWLRSLGARIGRGVWCDSYWLPEADLVDLGDGATVNRGCVVQTHLFHDRIMSMDLVSLDAGATLGPHSVILPAATIAAHGTVGPASLVMRGELVPAGSRWSGNPIGPWREVRVGDYHAPVA
>NZ_CP047180.1|WP_127886150.1|2834103_2835630_+|multidrug-efflux-MFS-transporter
MRPLTTIPFTTGDAPVTERTLPETRPAAATDTPSTALDPRSRLVISLLLVSAFVVILNETIMSVALPDLMRDFGVEAHVGQWLSTAFMLTMAVVIPITGYLIQRLHTRTLFAAAMTLFSLGTLSAALAPTFEVLLAARVVQAGGTAIMMPLLMTTVMTLVPPAIRGRMMGNISIVISVAPAVGPTISGVILNFLSWRWMFWIVLPIAVGALILGLRKVENVTEPRKIPIDSLSVVLSVFGFGGLVYGLSSLGEGGEAIVAPWVPFVVAGVALAAFIVRQLLLQKTDRALLDLRTFSSGNFTVVIVMMAVSMSALFGTLILLPLYTQNVLGLTPLETGLLLLPGGLLMGLLAPFVGRGYDRFGPRVLLVPGSIIVAGALWGYTTLDENSVSWFILSLHVVLSLGLALVFTPLFTAGLGSVRPALYSHGSAIIGTVQQLGGAAGTALFVTVLSVQSAALAREGVDEVVATAGGIHSAFVWGASIATAAIVAAFFVKRPAETDGPRPVVAH
>NZ_CP047180.1|WP_127886151.1|2833300_2833735_+|hypothetical-protein
MTAVLSGCALGLPPIDGSAPPSPAPSAVPSVDGPGPAVPLDLEEFDAINSATVASIGDPSGADLTRALIAGGVDRAGLEVTADITTADKRADAVFVAVRVGDSCLVGQYRHKASGEDGDRRYLGAVVAPLATGRCLIGDPAPGE
>NZ_CP047180.1|WP_159423206.1|2831773_2832895_+|aminotransferase-class-V-fold-PLP-dependent-enzyme
MIYLDHAATSPVRREVLEAMWPFLTGEYGNPSSSHALGASAARALEEARRHVARFLGGRGSEVLFTSGGTESINTAVKGIALGGLAAGRGRHVVISAIEHEATVESADHLRRLHGFEVSVAPVDGAGRLDLAALAALLRPDTALVSVLAASNEIGTLQDVPAIAALCRPHRIPLHVDAVQAAGWIDLAGLGADAVSISGHKLGAPKGVGALLLRSRVPIEPLVHGGGQERARRSGTENVAFAVALGAAVQLVDPARGARVSAVRDAFAARVAAEVPRAVPLGSAEHRLPSIASFVVPGRSGESILLALEERGVVVSSGSACAAGRDEPSPTLLALGLEPAVAQTAVRFSFGAESTPADADAAADAFAAVLARA
>NZ_CP047180.1|WP_159423211.1|2845881_2846271_-|type-II-toxin-antitoxin-system-death-on-curing-family-toxin
MRDARRVRYLRLEDLLALADDLGVPHVRDLGLLDSAAHRPQSSLFGREAYPDVPQKAAVLLESLVRNHPLVDGNKRLGWLSVVVFLGLNGLELDAPEDDAYDLVIGVATGSVEVAETAGLLESWTRAVE
>NZ_CP047180.1|WP_123702777.1|2846275_2846479_-|CopG-family-transcriptional-regulator
MAMTLRLTDEQESALTALAEAQGISKQEATVRAILEAADRRVHREDVAALSARGRERYAALLDRLAQ
>NZ_CP047180.1|WP_127886145.1|2846807_2847881_-|redox-regulated-ATPase-YchF
MALTIAIVGLPNVGKSTLFNALTKNTVLAANYPFATIEPNVGVVNLPDSRLEVLAGIFGSERILPAPVSFVDIAGIVRGASEGEGLGNKFLANIREADAIAQVIRGFEDADVVHVDGKVDAASDMETINTELVLADLQTLEKAEARYEKELKGKKIEPIVLETAKKAREFLDTGKPLSASSIELEPIRELGLLTAKPFIYVFNVDEAVLTDEARKAELAALVAPAHAIFLDAKIESELIDLDEADAAEMLESTGQTESGLNQLASIGFDTLGLQTYLTAGPKETRAWTIGKGWTAPQAAGVIHTDFQKGFIKAEIISFDDLVETGSIAEARAKGKARIEGKDYVMQDGDVVEFRFNV
>NZ_CP047180.1|WP_123445426.1|2847962_2848550_+|DNA-polymerase-III-subunit-epsilon
MPIDFTAIDFETANSHGASACSVGLVKVRDGRVVDRAGWLIRPPYGYDDFLEWNTRIHGIRKHDVHGAASWVEQFADLVAFAGEDVFVAHNAGFDMSVIRAACAATALELPAYDYLCSLQLARRTYQLESYRLPSVAFAAGYDDFRHHDASADAEACAAIVVHAARRHGAGSLAELGELAGVSVKRLRPKAPVAA
>NZ_CP047180.1|WP_159423212.1|2848583_2849480_-|hemagglutinin
MSPADPSPAAASPSAVRRRRGGTAALAALAVALLLTGASDLSAAAAPATEVPGIRMWTDLAGGVDESGFDPGDIVSDEVFFDGGALGPLTVQAFLNARVPSCAGTDVPCLRDYAEDTGDVAADEQCDAYLGGQDVSAAEIVSAVAGACDVSPAVLLTLLQKEQSLVTDSAPSERQFRSATGYGCPDTADCDSDYFGFFGQVYGAAWQFQRYRNPDSSFDWYPVGETSEIQYSPDAACGTAPVRIENAATAGLYYYTPYQPNAAALANLYGSGDACSAYGNRNFWRIFSNWFGDPRAGE
>NZ_CP047180.1|WP_159423213.1|2849669_2850902_+|DNA-recombination-protein-RmuC
MELSFVLGLAVGALLAAVVAVLLARARTPDTALALELATAQARAEGLEERHESVVEQHREHLGSARDQIRELQEQLRVVAERERHDARILQTLSPVAESLRGMQESVRRLESERAAQFGAITEQLEGQRLAGERLRSTTETLASALRSSASRGAWGETQLRNVVEAAGLTQRVDFDVQFGLEGEGGRGRADMVVRLPGGKAIAVDAKVPFDAYLEASAIPAGAGAEEEARRAGLLRAHVRALRGHIDALAGRAYWTGLPASPEFVIAFIPSEPLLASALDADPTLLEYAFRKRVALASPVTLWSVLKTVAYTWQQDVLTDDAKRLLDLGKTLYARLATLADHAEGLRRSIEKTVDSYNAFAGSLETRVLVTARQFDTLDESRVIAPAAGVTVSPRRLTAVELLAPDERTA
>NZ_CP047180.1|WP_123704712.1|2851177_2852110_-|class-II-fructose-bisphosphatase
MELVRATEAAAIRAVPFIGKGDKNAADGAAVDAMRTFLGTVNFDGVVVIGEGEKDNAPMLYNGEHVGNGSGPAADIAVDPIDGTSLTAAGRQNALSMIAVADRGAMFDPSAVFYMEKIVTGPEGVGIIDIQRPIGENIRALARAKRKPVDEMRIAVLDRPRHAQLIDDIRAAGAGTRLLLDGDVAGGINAARHDSRVDMCVGTGGTPEGIITACAIRALGGVIQGILRPKDDDERQRAIDAGHDLDRVLHANDLVRSDNTYFVATGVTNGGLVKGVRKEGHIITTESIVLRSRSGTIRRVTAQHLAEKWV
>NZ_CP047180.1|WP_123445424.1|2852359_2853385_+|class-II-fructose-bisphosphate-aldolase
MPVATPDQYAEMLDKAKKGGFAYPAFNVSSSQTINSVLQGLSEAGSDGIIQVTTGGADYFAGHTVKNRAAGAIAFAKFATEVAKNYPVTVALHTDHCPQNALEGFVYPLIAASEEEVKAGREPLFQSHMWDGSAVPLDENLKIAQEILPRVKAINAILEVEIGVVGGEEDGVSHDINEHLYTTLDDAIATVEALGFGEQGRYMAALTFGNVHGVYKPGNVRLRPELLREIQDGLQKKYGTEALPLDLVFHGGSGSTDEEIAEAVRNGVVKMNIDTDTQYAFSRSVADTVLKNYDGFLKVDGEVGNKKVYDPRSWGKIAESAMAVRVAEATRQLGSAGHSGK
>NZ_CP047180.1|WP_127886142.1|2853396_2853957_+|hypothetical-protein
MTNAHDQPSGSPRPEPQYGEYAPPGWSWTPPEDAVVVPDPRGSETDPRPATAPSARTVAHPVDRLITIILLALGVFFAVPTLLDPSSFATTLSELYTSQGIGTYASPDLARTLGLVVALAQALIVAFAVWISIRRLRAGKRAVLVPILGIVATVVLSLTVAAIAILGDPTFADYVSRMSAGTGTDV
>NZ_CP047180.1|WP_123445422.1|2854033_2855080_-|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase
MPRMPRATGRLRDEPVDGAKRVLLAAPRGYCAGVDRAVVAVEKAIEHYGAPVYVRKQIVHNVHVVSTLESQGAIFVEEVDEVPEGSHIVFSAHGVSPAVVQGAADRGLQAIDATCPLVTKVHREAVRFARDDFEILLIGHEGHEEVEGTAGEAPDHVTLVGSPDDVPNIVVKDPDKVVWLSQTTLSVDETMETVRRLRERFPNLQNPPSDDICYATQNRQVAIKKVAEHAELVIVVGSANSSNSVRLVEVALEYGAKAAYRIDYASEIKQEWLDGIRTVGVTSGASVPEVLVREVLDDLAAAGYGDVEEVKTAEEDLMFSLPKELRKDVAGKRDARGAGGRVSASVSA

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Crispr_ID: NZ_CP047180_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_10

3039534-3039655

Orphan

Consensus_repeat	Method
CTCGATACGCCCCTTCGGGGCTACTCGACCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_10

>merge|NZ_CP047180|10|3039534-3039655|CRISPRCasFinder
CTCGATACGCCCCTTCGGGGCTACTCGACCAACATGACGGGGCGCAGCCGCGTCTTTTCACCCGCCACCAAGACGCGAAGCGGCTTCGCCGCTCGATACGCCCCTGCGGGGCTACTCGACCA

>NZ_CP047180|10|9|3039534-3039655|CRISPRCasFinder
CTCGATACGCCCCTTCGGGGCTACTCGACCA	ACATGACGGGGCGCAGCCGCGTCTTTTCACCCGCCACCAAGACGCGAAGCGGCTTCGCCG
CTCGATACGCCCCTGCGGGGCTACTCGACCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159423289.1\|3030990_3032220_+\|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|223239
NZ_CP047180.1\|WP_123445261.1\|3044199_3045198_+\|sugar-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225263
NZ_CP047180.1\|WP_123445264.1\|3039745_3041260_-\|glycerol-kinase-GlpK	unknown	unknown	gnl\|CDD\|234594
NZ_CP047180.1\|WP_159423298.1\|3046309_3047782_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|238045
NZ_CP047180.1\|WP_159423295.1\|3037934_3038669_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423301.1\|3051695_3052511_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|369777
NZ_CP047180.1\|WP_159423292.1\|3034755_3036348_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|100079
NZ_CP047180.1\|WP_159423293.1\|3036344_3037196_+\|phosphotransferase	unknown	unknown	gnl\|CDD\|223584
NZ_CP047180.1\|WP_159423288.1\|3029869_3030994_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423297.1\|3045287_3046166_-\|DUF559-domain-containing-protein	unknown	unknown	gnl\|CDD\|380141
NZ_CP047180.1\|WP_159424122.1\|3048022_3049873_+\|phosphoenolpyruvate-carboxykinase-(GTP)	unknown	unknown	gnl\|CDD\|235256
NZ_CP047180.1\|WP_159423300.1\|3051215_3051659_+\|type-II-3-dehydroquinate-dehydratase	unknown	unknown	gnl\|CDD\|235443
NZ_CP047180.1\|WP_123445263.1\|3041329_3042088_-\|aquaporin-family-protein	unknown	unknown	gnl\|CDD\|223653
NZ_CP047180.1\|WP_159423290.1\|3032216_3033497_+\|iron-containing-alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|341481
NZ_CP047180.1\|WP_159423299.1\|3050224_3051181_+\|acyl-CoA-thioesterase	unknown	unknown	gnl\|CDD\|224523
NZ_CP047180.1\|WP_159423296.1\|3038665_3039382_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423287.1\|3028914_3029103_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423294.1\|3037221_3037938_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213235
NZ_CP047180.1\|WP_159424121.1\|3042289_3044161_-\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|223651
NZ_CP047180.1\|WP_159423291.1\|3033931_3034759_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|379312

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_159423289.1\|3030990_3032220_+\|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|223239	COG0161, BioA, Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Coenzyme metabolism].	4.42603e-53
NZ_CP047180.1\|WP_159423293.1\|3036344_3037196_+\|phosphotransferase	gnl\|CDD\|223584	COG0510, ycfN, Thiamine kinase and related kinases [Coenzyme transport and metabolism].	0.000343382
NZ_CP047180.1\|WP_123445264.1\|3039745_3041260_-\|glycerol-kinase-GlpK	gnl\|CDD\|234594	PRK00047, glpK, glycerol kinase GlpK.	0
NZ_CP047180.1\|WP_159423298.1\|3046309_3047782_-\|helix-turn-helix-domain-containing-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.	1.07725e-14
NZ_CP047180.1\|WP_159423301.1\|3051695_3052511_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	2.04707e-19
NZ_CP047180.1\|WP_159423292.1\|3034755_3036348_+\|hypothetical-protein	gnl\|CDD\|100079	cd06158, S2P-M50_like_1, Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains.	2.99535e-05
NZ_CP047180.1\|WP_123445261.1\|3044199_3045198_+\|sugar-binding-transcriptional-regulator	gnl\|CDD\|225263	COG2390, DeoR, Transcriptional regulator, contains sigma factor-related N-terminal domain [Transcription].	3.64322e-80
NZ_CP047180.1\|WP_159423297.1\|3045287_3046166_-\|DUF559-domain-containing-protein	gnl\|CDD\|380141	pfam18741, MTES_1575, REase_MTES_1575. Vsr REase Fold. Fused to HEPN (SWT1/Abi2 family), along with Transglutaminase and wHTH.	3.20402e-05
NZ_CP047180.1\|WP_159423300.1\|3051215_3051659_+\|type-II-3-dehydroquinate-dehydratase	gnl\|CDD\|235443	PRK05395, PRK05395, type II 3-dehydroquinate dehydratase.	1.53917e-79
NZ_CP047180.1\|WP_123445263.1\|3041329_3042088_-\|aquaporin-family-protein	gnl\|CDD\|223653	COG0580, GlpF, Glycerol uptake facilitator and related permeases (Major Intrinsic Protein Family) [Carbohydrate transport and metabolism].	5.41421e-63
NZ_CP047180.1\|WP_159423290.1\|3032216_3033497_+\|iron-containing-alcohol-dehydrogenase	gnl\|CDD\|341481	cd08551, Fe-ADH, iron-containing alcohol dehydrogenases (Fe-ADH)-like. This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.	1.57546e-10
NZ_CP047180.1\|WP_159423299.1\|3050224_3051181_+\|acyl-CoA-thioesterase	gnl\|CDD\|224523	COG1607, COG1607, Acyl-CoA hydrolase [Lipid metabolism].	8.04996e-42
NZ_CP047180.1\|WP_159424122.1\|3048022_3049873_+\|phosphoenolpyruvate-carboxykinase-(GTP)	gnl\|CDD\|235256	PRK04210, PRK04210, phosphoenolpyruvate carboxykinase (GTP).	0
NZ_CP047180.1\|WP_159423294.1\|3037221_3037938_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213235	cd03268, ABC_BcrA_bacitracin_resist, ATP-binding cassette domain of the bacitracin-resistance transporter. The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.	6.70894e-82
NZ_CP047180.1\|WP_159424121.1\|3042289_3044161_-\|FAD-dependent-oxidoreductase	gnl\|CDD\|223651	COG0578, GlpA, Glycerol-3-phosphate dehydrogenase [Energy production and conversion].	1.95098e-135
NZ_CP047180.1\|WP_159423291.1\|3033931_3034759_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	8.34445e-11

>NZ_CP047180.1|WP_159423296.1|3038665_3039382_+|hypothetical-protein
MTDAAAEGPLTRAVAAESRRVVASRTPLWGLVFGLLPVLPLLLAVTQVDLGALPPGEAASLEHAISAALLQGGVVGAAAFGALRTASAFEKGILARDVLSSGLRPALAARFLVAAGAGAVLATAAVAVGVAGVAVVSAGRVTPDVGVETLVPMTGIGGAIWGALVGTIVRAPLFVLFAALAPLSVATFTSGTALEDVAPLAALSASAPPTVAAVLAGPAWLLALALVAVASGRRRPLL
>NZ_CP047180.1|WP_159423295.1|3037934_3038669_+|hypothetical-protein
MSGAGALARAEILRSRSGSSFPVLLAYAILIPVFALNMPGTTDRLTGLDDAPASRFVFGFAACAALGACFYGSYAYTRETYYHSLDRTLLLGSRDAILSAKALAGAVSGAVFGVVAVVGWWPISAVVLATAGRRLTPDITLLSASLGVVLACALSGVLGVGVGYAVRNYYACIPIALVLPAALAVPFLGVARDAGRLLPIGAVAGATGAPVDGMLPAPLALAVLAVWALLAIGGARILEQRRAR
>NZ_CP047180.1|WP_159423294.1|3037221_3037938_+|ATP-binding-cassette-domain-containing-protein
MSSALDFLHFTKSFRGRRVVDDLSFSVRQGTVVGLLGPNGAGKSTALRGLVGLLRPDSGEARIGGHRFAELRAPARVVGVHLDGLGFENGITGRRHLAIVCRAVGAPLSRVDELLETVGLAEAARRPVRGYSTGMRQRLGLATALAGDPEILVLDEPANGLDPEGIRWLRRLIRAEAERGRTVLVSSHQLAELEYTVDEVVVLRRRMLFHGPLEDLTRSGGRSLEDGYFDLVDGEAGR
>NZ_CP047180.1|WP_159423293.1|3036344_3037196_+|phosphotransferase
MTGGNALEHAFEQALRVLAVARDGDTVPGWRGRTLSGPVRRDRERLWLRLVSSPSALAHGTWWTGTADSAVLPALPKPVVLAVEEWDPPSVEGFRLRAELMTRLPGRALSPTAELAPETEVDPAVWVELGGTLDALAAVPTQRESTVPATVDRLLHSFFGDRFPRGTPCWTTAHGDLHPGNLLVAPLGLADWEAWGRGPQHLDVATLYVHTLAAPDARRSLVEVLGERLHSDDARPALAFAAAKVLARSVSGDYPTLVDPVHRLLDDLTARPLGAGGTTARRR
>NZ_CP047180.1|WP_159423292.1|3034755_3036348_+|hypothetical-protein
MSDPAPRLADTVTIDEPIAPGAPWILSVRGVPRARVGPAVATFAAGLRPSAHETDETDGTGTARLSDEETAALLREFAAAGLLAGSERREPRSHRLQFRPPASFQLTLLDATRPALVLARLLRRRPIRLLAVAAVVAVLLLGTASAIAHSAEIAAVLSEPLPLPSLLAVSVAFLLAGAVHEAGHAVSLAAFGGRPRRAGVMIFYLAPAFFCDVTDGWRLGDRRSRAAVALAGPAVHLVLAAGAATALLWSSTGRSALACFVVAAALSAVTNLIPLVHLDGYLALVAVLDRPFLRRAAIGAVGDAVLRLLGGTAPRASPWLVLFGVGCRGFALLLIGWAYVRSVPVLILTEPGAIIALVFAAALSCALVVSLVRFARAARKARVGGLRVAVASAVLAAALAGVGALPLEERIEAGYVVRDGEAFLVRTSADPRIVPGTPVRLTSNGIAVRSPRSTAVVSGPAEPLLAPIAALAPLTGLDDVPAVGYPLALPDSASTPPVGGASVSLGGGTIGGAVLDLVAGDALRRLGVGR
>NZ_CP047180.1|WP_159423291.1|3033931_3034759_+|methyltransferase-domain-containing-protein
MQHPSDPPPLTAASAALLGALSPATVAPEDLYGPDGSVVYEHFTAEDRSEISPLLAAVRRTEGPILELACGGGRLTVPLLGLGRPVVGLDLSPTMVDILRSRIAALPAARIADGSRALVGDMTCFHLPERFGAVVLGATSIALLNRAGRHAFLRAAREHLGADGVLLITASSPDHAYVAGSRSSRIRAVPGPSGGPGAAVVTSAVTPDGLHRDVEVVQLGLDPQGRAAARFFRSRVNVVDADQVAVEAERAGLRLVARTALVETEDSTLLQLVRA
>NZ_CP047180.1|WP_159423290.1|3032216_3033497_+|iron-containing-alcohol-dehydrogenase
MSVRSTDLRTGLASDAATTGSRQTLFVLDSALVRRGAVEPERLHGRVVVLDVASEQGRLLDTVDRALRAVRPDRLVGIGGGRLHDVVALARLFAADRTLRSRLDGLLSRHGGLLAPDLPASTEVPRLVLVPTTIGPGSETSAAACREIGGLRSVVVGEALRADAAVLDAELTATLTRSSVLEGAAEAALRLIGSRSGSPADRSADDRSRRLLEALAEAGGRVAGSAGLVRRADRATLAAASADSHGVLRSATADPFAATHWYLANEVSSRAGLRKVPATMPLLPVLWSRDSPERRARRRAVWQWFAAPLGLDPDPVVGSAEWSERWGITAPAVADRALRDAALAIVARWDSSALPGLAVDDALRLLRAAFPPARALRPNEGGEHMNTTNELEFHELEQAVAPDWESATSGFTTGLLVAGVFVGLLT
>NZ_CP047180.1|WP_159423289.1|3030990_3032220_+|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme
MTASPVLVPLVSPTAAARTVAAVSATGTRVRFADGVEAIDLTSGLWNAPFGCGRPEFTAAIAAALAEASYLSLFRRSHPWAERAAAALLAVVGDALPHASFRRVLLTTSGGSANDAVMKLLRQRAALLGRPERRLVVGLSGSYHGLTYGAHALSGDELGQDVYGVDRSGVRHVAHDDPDALKSLLHREGRRICGIVVEPVLGSGALPLSDALLAVLESASQDGVPVVADEVATGFGRTGPFLASSRWPFAPDAVVLSKALTNGTLAAAAVVVGERLLAEIDAADAPFVHAETQAGTPAVCAAVLQSLALLPELLGADGFPRVSTALDRAVTALSAHPRVLGSSGAGSFRALHIAGVASAEEVLGLVEDVRRRGAVVHPAPGGIQFLPAAVSSDHDLAGIPRIIGAALDA
>NZ_CP047180.1|WP_159423288.1|3029869_3030994_+|hypothetical-protein
MATNPGPIRSGGDATRSLDRGDRGSRTALSTPTGLADADTRATAVDRRGVARAVLQWVTGDRVDARRVVRLADRRWRGAVEPLLGPEDVLLLPAESTTDDDTRPEPPSAEGAAVLTYRNGLDEPGDVAWFGELRVQTEDYASIAFLPVTGATTARLRDANGWQAYLEDADAARASGRLVPQLLGAAVAVSGLPLTNDPAAGPVAAVDVGRDGVATLGPDGLVLGDARDPDGLAAALDRSYRPLDRLAALGGDVADDIARRPWLALYRAGLAFAAADDTGPAWSVVGLGTSLRPDGEVTTLTRSDLILLHRGDERVLVEPRTLRRFALAPATAIVVERLLSDGPDDEPRTPADEAFVSRLVERFEHEGVHLRRGA
>NZ_CP047180.1|WP_159423287.1|3028914_3029103_-|hypothetical-protein
MTVPKKKEDRVRRFALALLGVSMGVAVVTTIVGGIDDPYDVVTLVVCGSCASLVIVTLIRER
>NZ_CP047180.1|WP_123445264.1|3039745_3041260_-|glycerol-kinase-GlpK
MADYVIAIDQGTTSSRAIIFDKKGSIVSTGQKEHEQIFPRAGWVEHDPIEIWNNVREVIGQALSRADLTRHDIASVGITNQRETAVVWDKTTGKPVYNAIVWQDTRTQSIVDRLAGDEGADRFKSIVGLPLATYFSGTKIVWILENVEGAREKAEAGDLIFGTTDTWVLWNLTGGVDGGVHKTDVTNASRTLFLDLETLEWRDDILEAFGVPKSMLPEVCSSSEVYGQVESSSLLREVPIAGILGDQQAATFGQAAFDPGEAKNTYGTGNFLIFNTGTEIVHSKNGLLTTIGYKLGDGEVHYALEGSIAVSGSLIQWLRDNLGLIGSAPEVEALAATVEDNGGAYFVPAFSGLFAPYWRADARGALVGLTRYVNKGHIARAALEATAFQTREVLDAVNADSGVPLQELKVDGGMIANNLLMQFQADILGVPVVRPVVAETTALGAAYAAGLAVGFWENLDDLRQNWQEDSRWTPQMDQDEAARQYRLWKKAVTKTFDWVDEDVQ
>NZ_CP047180.1|WP_123445263.1|3041329_3042088_-|aquaporin-family-protein
MDNLGVVFLAEVVGTAMLVLLGCGVVANVALVKSKGLNGGTLMVNFGWGFAVFAGVIVSYNSGAHLNPAVTLGLAASGATEFGSGVPVNIVSILMYILAQMIGAILGAVFCWLAYKQHFDQEPDPANKLGVFSTGPAIRSYGWNFVTEVIGTFVLVFVVIGFGGGRQGDGGLAALGALPVAILVIAIGASLGGPTGYAINPARDLGPRIAHALLPIKGKGSSDWSYAWVPVAGPIVGGVLAGLASTALLPIL
>NZ_CP047180.1|WP_159424121.1|3042289_3044161_-|FAD-dependent-oxidoreductase
MCCRVKDGCIPSRYQPSIWGGHTRTRHSTQHLRHEGEYEVAQSVGTPGSSSLRESVSALRDTPRATVLVIGGGINGIGTFRELALNGVDVALVERGDYVSGASSASSHMIHGGIRYLENGEFRLVNEGVHERNGLLKIAPHYVKPLQTTIPIYSTFSGILAAPLRFLTHKSGKPQERGALLIKVGLTLYDFFSRDGGVVPRHQFHGRKRSLNELPKLDPKIKYTATYFDASVHEPERLALDVLRDALVGGTKARAANYVEAVGTSEGGVLLRDRESGEEFAFQADVVVNVSGPWTDFTNTALGTTTKFMGGTKGSHIVLDNPELVEACEGREMFFEHSDGRIVLIYPLKGRVMIGTTDIEADPNEPAVCTEEEIDYFFDLVNHVFPSIPVTREQIVFKFSGIRPLPRHDDETPGFVSRDYRIEPSTLPGGKTPVLSLVGGKWTTFRALSEHLSNEVFKRIGVTRRVSTVKTAIGGGKGFPRTDASRAQWISQHRSGLSSARTGQLLERYGTRAEEVIEALADGHDEALDFDKDFTTGEIRYLAQRESVVHLIDLVMRRTNHAFTGGLSRELLEELAQHTGEVLGWDEAERAQEVDATIEHLKKYNGVDVGGTSVQAPTAVAAS
>NZ_CP047180.1|WP_123445261.1|3044199_3045198_+|sugar-binding-transcriptional-regulator
MTPVRPVVELDETTHATHPDKTRDALRAAQLYYMQDLTMDAIAHELHTSRSSVSRLLSHARATGLVDIQIRSPLDRASALSAEVRAHFDITAHIVPVPDHTSEIDRLERVALSAARILGPFIDSNMIVGIAWGSTMSAMSRHLIAKETHNTQIVQLNGAGNTETTGINYSSEILRRFGDAYAAKVQQFPVPAFFDDPMTKKAVWRERSTKRVLELQQRMDVALFGLGSPFAAVPSKVYIGGYLEPSDFTSLSASGVVGDVATVFYRADGTWDDIPMNERASGPDLSTVRRASRRICVVSGASKLPGLRGALAAGLLTDLILDEGTARALISG
>NZ_CP047180.1|WP_159423297.1|3045287_3046166_-|DUF559-domain-containing-protein
MQDDTETRIVNASTSELARHRLVAEYPVGVFRGARAAIEPVTYGERITAFAAVMRPGEFFSHVTAAHLLQLPDRRATETTPLHVAVTPPMRAARRVGVKSHHLWDEAVTVVDAGHPVTDPASTFCHLADSRSLDELVVLGDALVRPDEELGRRGLRVDLEILAARAARYRGRGGRRAREAVGFVRVGSESPKETLLRLLLIRAGLPEPELNVELYDADGVFVARVDLLYPNQWVVVEYDGDQHRTDTRQYERDIARSEAIQALGYRHIRVRLSGLVDHPEATAARVRRALGL
>NZ_CP047180.1|WP_159423298.1|3046309_3047782_-|helix-turn-helix-domain-containing-protein
MTDTTAPTAGPSAGTDAALLGQRIRHFRTRRGLTLGQLAERVGVSGSQLSLIETGRREPRLSLMQALATALGVELAALLSDEPPSERAALEIELARVQKGSLYRSLGLPEFKVNKSLTTPVLEAFLGVYRELARRKSEASATPEEARRANTAQRLQLREHNAYLPEIEAVAGEMLRTVGHRGGALTHSSVSRMARHLGFEIIHVGDLPHSARSVIDLANGRIYLPPASIPGGHGLRALALQAMAHRLLGHERPVTYADFLRQRLEINYFAAACLMPLEPAVAFLEEAKRERDISVEDFRDGFGVTHEAAALRFTNLLTSHLDIRMHFLRVLGDGSIQKAYENDGLPLPTDVTGAVEGQIVCRYWSARSAFSRTNRTTEYYQYVDTPAGTFWSASQTGTTATEEFSITVGVPFAEARFFRGRDTDRREQSRCPDESCCRRAPAELAQRWDGNAWPSARLHAHVLAPLPSGTFPGIDDAEVYAFLDTHARES
>NZ_CP047180.1|WP_159424122.1|3048022_3049873_+|phosphoenolpyruvate-carboxykinase-(GTP)
MTAPTPVAAPVVPPAPLALRRWVRETAAILQPDAIEWCDGSPAEWYRLTARMVDEGKLIALNPEWRPGSFLARTDPDDVARVEDRTFLCTTDEADAGPTNNWREPSAMKAELAPYFAGSMRGRTMYVVPFSMGPVGGPLSQLGVQLTDSAYAVLNMRIMARVGAEPLAAFTEETAYVRGVHSVGFPLRDADGTTREDVAWPCNATKYITQFPETREIWSFGSGYGGNALLAKKCFALRIASAMGREEGWLAEHMLLIRIVSPEGRSYHVAAAFPSACGKTNLAMLQPTIPDWRVETLGDDITWMKKGEDGRLWAMNPETGFFGVAPGTGQSSNPNAVHTLWGNTIFTNVALREDGDVWWEGLTDEVPEFLTDWRGEPWTPASGTPAAHPNARFTAPAEQCPTLSREWDAFEGVPLDAIVFGGRRASNVPLVTQATSWQHGVFLGATIASEKTAAAEGTVGELRRDPFAMLPFCGYNMADYFAHWLAVGADLGEKAPAIFQVNWFRKGADGSFLWPGFGDNARVLQWLVRRIEGLAESRPSAIGDLPLSINTHGLNLSAAAKEELFSVPVEAWLDECALTEAFFARFGDRLPPELTAELRALRLRLLAEELPAAHAA
>NZ_CP047180.1|WP_159423299.1|3050224_3051181_+|acyl-CoA-thioesterase
MDDRITLRFLAAPQDATADGRSAQAGRVLEWIDKAGYACAVGWSGGYCVTAYVGNVHFTRPIAVGNLIEATAQVIHTGRTSMHVLVRVAQADPRTGRYEAATHCLLIFVAVDEEKRPRPVPEWTPRTIEDLALAEGAAARIDGRRALHEVMRAQEYTEAGTGPRIVFRFLAAPGDVNWGGNAHGGIVMRWIDEAANAVAQGWSGRDAVAVYSGGIHFYRPVRIGHLVEVEARLIHTGPRSMHLAIHVRSGDPRTGELELTTQCMSVFVVRGDDGAAEPVPALEPRSDEDRRLDEHARELIRLRAELPALPVGIAATLA
>NZ_CP047180.1|WP_159423300.1|3051215_3051659_+|type-II-3-dehydroquinate-dehydratase
MKILVVNGPNLNLLGTREPAVYGSDTLADAEALATRAAERLGLGIEFFQSNSEGAIIDRLHEARGTAAGLLLNVGAYTHTSIAIRDAVLATELPLVEVHVSNVNRREEFRRHSYLSDIAVAVIVGAGIAGYGYAVDVLARTLGATDA
>NZ_CP047180.1|WP_159423301.1|3051695_3052511_+|methyltransferase-domain-containing-protein
MTPSDATPSASPAELGRSFGSAVDAYDRGRPGYPYDAVDWLVGHAPARVAGAFVPERARAVGADASDRVRAVDLGAGTGKFTASLVARGLDVSAVEPDAVMLERLSAQLPSVRALAGTAEEIPLPDASVELVTAAQSWHWVDPERASAEVARVLVPGGVLALVWNIRDESVPWVRRLGEVAGSSAAERFETVQPPLGSALERVAYAEFDWEYELGRPALLDMFASRSYVIAMLEEERAAVLAAVGEVVDALPGDRVAMPYATRVTIARRAS

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Crispr_ID: NZ_CP047180_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_11

3175609-3175713

Orphan

Consensus_repeat	Method
GCGGGCGGCTACTCGACCAGCATG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_11

>merge|NZ_CP047180|11|3175609-3175713|CRISPRCasFinder
GCGGGCGGCTACTCGACCAGCATGCAGAGGGCGGCGGATGCAGCTGCTCGGAGGGCTGTGGGTGGGTCTCGATACGCCGCCTGCGGCGGCTACTCGACCAGCATG

>NZ_CP047180|11|10|3175609-3175713|CRISPRCasFinder
GCGGGCGGCTACTCGACCAGCATG	CAGAGGGCGGCGGATGCAGCTGCTCGGAGGGCTGTGGGTGGGTCTCGATACGCCGCC
TGCGGCGGCTACTCGACCAGCATG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159423365.1\|3181607_3182786_+\|galactokinase	unknown	unknown	gnl\|CDD\|223231
NZ_CP047180.1\|WP_123445137.1\|3174394_3175024_-\|DNA-directed-RNA-polymerase-subunit-beta	unknown	unknown	unknown
NZ_CP047180.1\|WP_127885969.1\|3167999_3169103_+\|phosphate-ABC-transporter-substrate-binding-protein-PstS	unknown	unknown	gnl\|CDD\|270283
NZ_CP047180.1\|WP_123445141.1\|3171265_3172045_+\|phosphate-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|184587
NZ_CP047180.1\|WP_123445374.1\|3170149_3171250_+\|phosphate-ABC-transporter-permease-PstA	unknown	unknown	gnl\|CDD\|273373
NZ_CP047180.1\|WP_159423364.1\|3180402_3181611_+\|galactose-1-phosphate-uridylyltransferase	unknown	unknown	gnl\|CDD\|238341
NZ_CP047180.1\|WP_159424131.1\|3179468_3180260_-\|DeoR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224268
NZ_CP047180.1\|WP_123445136.1\|3175826_3176312_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423362.1\|3177207_3178509_-\|DUF445-family-protein	unknown	unknown	gnl\|CDD\|377281
NZ_CP047180.1\|WP_159423357.1\|3166874_3167810_+\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|239645
NZ_CP047180.1\|WP_159423363.1\|3178505_3179459_-\|aldose-epimerase	unknown	unknown	gnl\|CDD\|185699
NZ_CP047180.1\|WP_159423359.1\|3172209_3173073_-\|anti-sigma-factor	unknown	unknown	gnl\|CDD\|378389
NZ_CP047180.1\|WP_123445129.1\|3183609_3184656_-\|NAD(P)-dependent-alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|176186
NZ_CP047180.1\|WP_123733778.1\|3173650_3174088_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423361.1\|3176828_3177107_-\|DUF3072-domain-containing-protein	unknown	unknown	gnl\|CDD\|371445
NZ_CP047180.1\|WP_159423360.1\|3175329_3175527_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_123445135.1\|3176525_3176720_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_123445139.1\|3173078_3173654_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|182015
NZ_CP047180.1\|WP_159423358.1\|3169196_3170141_+\|phosphate-ABC-transporter-permease-subunit-PstC	unknown	unknown	gnl\|CDD\|273992
NZ_CP047180.1\|WP_159423366.1\|3183079_3183571_-\|YbaK/EbsC-family-protein	unknown	unknown	gnl\|CDD\|239825

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_159423359.1\|3172209_3173073_-\|anti-sigma-factor	gnl\|CDD\|378389	pfam10099, RskA, Anti-sigma-K factor rskA. This domain, formerly known as DUF2337, is the anti-sigma-K factor, RskA. In Mycobacterium tuberculosis the protein positively regulates expression of the antigenic proteins MPB70 and MPB83.	4.1192e-16
NZ_CP047180.1\|WP_127885969.1\|3167999_3169103_+\|phosphate-ABC-transporter-substrate-binding-protein-PstS	gnl\|CDD\|270283	cd13565, PBP2_PstS, Substrate binding domain of ABC-type phosphate transporter, a member of the type 2 periplasmic-binding fold superfamily. This subfamily contians phosphate binding domain found in PstS proteins that serve as initial receptors in the ABC transport of phosphate in eubacteria and archaea. After binding the ligand, PstS interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The PstS proteins belong to the PBPII superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.	8.17078e-68
NZ_CP047180.1\|WP_123445374.1\|3170149_3171250_+\|phosphate-ABC-transporter-permease-PstA	gnl\|CDD\|273373	TIGR00974, 3a0107s02c, phosphate ABC transporter, permease protein PstA. This model describes PtsA, one of a pair of permease proteins in the ABC (high affinity) phosphate transporter. In a number of species, this permease is fused with the PtsC protein (TIGR02138). In the model bacterium Escherichia coli, this transport system is induced when the concentration of extrallular inorganic phosphate is low. A constitutive, lower affinity transporter operates otherwise. [Transport and binding proteins, Anions].	1.96423e-79
NZ_CP047180.1\|WP_123445141.1\|3171265_3172045_+\|phosphate-ABC-transporter-ATP-binding-protein	gnl\|CDD\|184587	PRK14241, PRK14241, phosphate transporter ATP-binding protein; Provisional.	0
NZ_CP047180.1\|WP_159423364.1\|3180402_3181611_+\|galactose-1-phosphate-uridylyltransferase	gnl\|CDD\|238341	cd00608, GalT, Galactose-1-phosphate uridyl transferase (GalT): This enzyme plays a key role in galactose metabolism by catalysing the transfer of a uridine 5'-phosphoryl group from UDP-galactose 1-phosphate. The structure of E.coli GalT reveals that the enzyme contains two identical subunits. It also demonstrates that the active site is formed by amino acid residues from both subunits of the dimer.	7.56043e-104
NZ_CP047180.1\|WP_159423361.1\|3176828_3177107_-\|DUF3072-domain-containing-protein	gnl\|CDD\|371445	pfam11272, DUF3072, Protein of unknown function (DUF3072). This bacterial family of proteins has no known function.	1.35367e-22
NZ_CP047180.1\|WP_159423362.1\|3177207_3178509_-\|DUF445-family-protein	gnl\|CDD\|377281	pfam04286, DUF445, Protein of unknown function (DUF445). Predicted to be a membrane protein.	4.30843e-122
NZ_CP047180.1\|WP_159423357.1\|3166874_3167810_+\|NUDIX-domain-containing-protein	gnl\|CDD\|239645	cd03673, Ap6A_hydrolase, Diadenosine hexaphosphate (Ap6A) hydrolase is a member of the Nudix hydrolase superfamily. Ap6A hydrolase specifically hydrolyzes diadenosine polyphosphates, but not ATP or diadenosine triphosphate, and it generates ATP as the product. Ap6A, the most preferred substrate, hydrolyzes to produce two ATP molecules, which is a novel hydrolysis mode for Ap6A. These results indicate that Ap6A hydrolase is a diadenosine polyphosphate hydrolase. It requires the presence of a divalent cation, such as Mn2+, Mg2+, Zn2+, and Co2+, for activity. Members of the Nudix superfamily are recognized by a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site.	1.51509e-44
NZ_CP047180.1\|WP_159423365.1\|3181607_3182786_+\|galactokinase	gnl\|CDD\|223231	COG0153, GalK, Galactokinase [Carbohydrate transport and metabolism].	9.64142e-123
NZ_CP047180.1\|WP_123445129.1\|3183609_3184656_-\|NAD(P)-dependent-alcohol-dehydrogenase	gnl\|CDD\|176186	cd05283, CAD1, Cinnamyl alcohol dehydrogenases (CAD). Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.	0
NZ_CP047180.1\|WP_159424131.1\|3179468_3180260_-\|DeoR-family-transcriptional-regulator	gnl\|CDD\|224268	COG1349, GlpR, Transcriptional regulators of sugar metabolism [Transcription / Carbohydrate transport and metabolism].	3.79593e-72
NZ_CP047180.1\|WP_159423363.1\|3178505_3179459_-\|aldose-epimerase	gnl\|CDD\|185699	cd09022, Aldose_epim_Ec_YihR, Aldose 1-epimerase, similar to Escherichia coli YihR. Proteins similar to Escherichia coli YihR are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.	2.66708e-121
NZ_CP047180.1\|WP_123445139.1\|3173078_3173654_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|182015	PRK09646, PRK09646, ECF RNA polymerase sigma factor SigK.	3.23109e-86
NZ_CP047180.1\|WP_159423358.1\|3169196_3170141_+\|phosphate-ABC-transporter-permease-subunit-PstC	gnl\|CDD\|273992	TIGR02138, phosphate_transport_system_permease_protein_PstC, phosphate ABC transporter, permease protein PstC. The typical operon for the high affinity inorganic phosphate ABC transporter encodes an ATP-binding protein, a phosphate-binding protein, and two permease proteins. This family consists of one of the two permease proteins, PstC, which is homologous to PstA (TIGR00974). In the model bacterium Escherichia coli, this transport system is induced when the concentration of extrallular inorganic phosphate is low. A constitutive, lower affinity transporter operates otherwise. [Transport and binding proteins, Anions].	2.38963e-79
NZ_CP047180.1\|WP_159423366.1\|3183079_3183571_-\|YbaK/EbsC-family-protein	gnl\|CDD\|239825	cd04333, ProX_deacylase, This CD, composed mainly of bacterial single-domain proteins, includes the Thermus thermophilus (Tt) YbaK-like protein, a homolog of the trans-acting Escherichia coli YbaK Cys-tRNA(Pro) deacylase and the Agrobacterium tumefaciens ProX Ala-tRNA(Pro) deacylase and also the cis-acting prolyl-tRNA synthetase-editing domain (ProRS-INS). While ProX and ProRS-INS hydrolyze misacylated Ala-tRNA(Pro), the E. coli YbaK hydrolyzes misacylated Cys-tRNA(Pro). A few CD members are N-terminal, YbaK-ProX-like domains of an uncharacterized protein with a C-terminal, predicted Fe-S protein domain.	2.4841e-53

>NZ_CP047180.1|WP_159423360.1|3175329_3175527_-|hypothetical-protein
MTHRLQPHQSTTVRLVRWFRTVDGWQSEIVRGRLLEHHDGVWRLLSIDDGEEREYPDAAWSLCHE
>NZ_CP047180.1|WP_123445137.1|3174394_3175024_-|DNA-directed-RNA-polymerase-subunit-beta
MTDGFHKPTKFPSRVFEAFQGGEDPAQISRVAHETAIALLSRVREDPDPVVIDRLVEYTDHNGIDALAELWARSSPSSLPGALWRIYLLRLVIRQDPESTSFLYQRGVELSATIDPVVAGAVTPTGPAEITELADRILRGVFDGDFAVALDRAAAFCRVSASGAASVADDVELIDGPRASQLTTRALRLSTTAAELVSCARLWRSDSLE
>NZ_CP047180.1|WP_123733778.1|3173650_3174088_-|hypothetical-protein
MKNRRALRIGARWWAGIALLVIAVLLFLSAPGVDDEIGALLGNGVVFSQGALMRTLAVLDTAAALWVLVRPRSSAGLTAALAAVIGLWLAPRMGAAALVDLGGFALDVRFVVLPLEVSVVIAGLAVTAFWMTRNLKSRARAGQGA
>NZ_CP047180.1|WP_123445139.1|3173078_3173654_-|sigma-70-family-RNA-polymerase-sigma-factor
MSDDTTAEGTAPDLGALLERIAAGEQAAFSQLYDLVASRVLGLITRVLVDRAQSEEVAQEVFLEIWQTAGRFAPNKGSATTWILTMAHRRAIDRVRAAQAGRDRDVRIGIRDLGRDYDQVAEQAEVSLEHEKVTAALERLTELQRQALQLAYYGGYSHSEIAGILNCPVGTIKTRLRDGMIRLREEMGVAL
>NZ_CP047180.1|WP_159423359.1|3172209_3173073_-|anti-sigma-factor
MQLPEDPRELAAGHALGILTPDETARYERFLDENPEARGEADAFSTVADALAADAPAVAPSPALKADLMALIATTPQLPRDDTADAPAEDLADRREAVPTLHAVEPSAAAVSGPSAVAPSATSGRHGAEARARGRWFTRPAVYLSAAAAAAVIVVGGVALPPLLTPDAGQSQQLSALEQIRSAPDVQETVGAVATGETATLVWSASLGRSALVVDDLAPLPDDKTYELWYIGSSGPVSAGTFDGGDGRTVAPLEGTLAEGAVVAVTVEDAGGSEVPTTDPILAIATA
>NZ_CP047180.1|WP_123445141.1|3171265_3172045_+|phosphate-ABC-transporter-ATP-binding-protein
MSKRIEVNDLNVYYSKFLAVEGVGLTIEPRTVTAFIGPSGCGKSTFLRTLNRMHEVIPGAYVDGEVLIDGNNLYGPGVDPVLVRRQVGMVFQRPNPFPTMSIRDNVLAGVKLNNRRISKSDADDLVEKSLQGANLWNEVKDRLEKPGSGLSGGQQQRLCIARAIAVSPDVLLMDEPCSALDPISTLAIEDLIEELKNDYTIVIVTHNMQQASRVSDRTAFFNIAGTGKPGKLIEYDDTATIFSRPSVQATEDYVSGRFG
>NZ_CP047180.1|WP_123445374.1|3170149_3171250_+|phosphate-ABC-transporter-permease-PstA
MTPPRQRRVEDAVPAPVNTLTSGQLPKWAPVALLVGSIAVMALVYALLAVTGTTQGFDVVGTVFFGAVLYTVAVFVLARLVEGPRRATDRVVTTLVTAAFVVALIPLISLMYTAVTAGAARFDLLFFTSSMRNVVGEGGGALHAIMGTLIITALAAVISIPIGLMTAIYLVEYGRGALARGITFFVDVMTGIPSIVAGLFAYALLVLLFGDGIRMGFGGAIALSVLMIPVVVRSTEEMLRLVPNELREASFALGVPKWLTVVKIVLPTSIAGIVTGVMLSIARVIGETAPLLIVAGFTQSMNYNPFDDRMMTLPVFVFRQYADQGADAAAYIDRAWTGALVLILIVMLLNLLARLVARIFAPKLGR
>NZ_CP047180.1|WP_159423358.1|3169196_3170141_+|phosphate-ABC-transporter-permease-subunit-PstC
MTTAERPVGAIKAKQRPADRIFSGTAVASGALILVILAAVALFLVVQSIPALTASPDTISGGAGFWSYVGPLVFGTVYAAGLAMVIAVPIAIGIALFISHYAPRKLAQGLGYVIDLLAAVPSVVFGLWGITVLAPFVQPFYAFLTDACGWFPLFNGPVSGTGRTILTVALVLAVMILPIVTAISREVFLQTPTLHEEAALALGATRWEMVRTAVLPFGRPGIISASMLGLGRALGETMAVAIVLSPSFVVNFALLQSTNSNTVAANIALSFPEAYGLKVNELVASGLMLFVITLLVNMLARYIINRRKAFSGAN
>NZ_CP047180.1|WP_127885969.1|3167999_3169103_+|phosphate-ABC-transporter-substrate-binding-protein-PstS
MRFSRLGQAAVIAAVAAITLTSCAANEGPAATGDSSSSGSASTLEGTLNGIGASSQGSAQEAWVSAFQQANTGVTVNYSPDGSGAGREAFIAGGADFAGSDRALKLEELDGSFGKCADGTSAIDVPAYISPIAIVFNVEGLDELNLDAATIAGIFKGTITTWNAPEIAALNPDATLPSSNITAVHRSDDSGTTENFAAYLNATAPTVWDAEPDGVWPYEGGEAAQGTSGVIDTVTNGQNTIGYADASRAGSLGTAKVKVGDDFVAYSPEAAAAIVDASPEATDRPENDIVYEIDYASEEAGVYPVVLVSYLIACQEYQDAATGELVKAYLGYVTSEEGQQEAATSAGAAPLSSELSTQVATAIESIK
>NZ_CP047180.1|WP_159423357.1|3166874_3167810_+|NUDIX-domain-containing-protein
MTGTVYAAGAVCWRIIEGRLHVLVIHRPHRKDVSLPKGKVDPGESLPETAVREIREETGFAVALGVPLGTVQYALPNGRPKTVHYWAARVTEKAVLASDFVPNREVEALEWVTIKRARSYLTYPHDVEIVDEFARIVSRGTHDTFAVVVLRHAKAVPASSWDGRDSTRRLNRRGDEEAAAASRAVAAWRPRRLVTSTAKRCRATIAPLSTLLKRPVRLSEDLSQDAHEHGTADVRSVVGKRVRARKSAVLCSHGPVIPEILRELALATATPIGPYLEEASDLPTGGFAVVHLSVEHPGSGIVAIETHAPLE
>NZ_CP047180.1|WP_123445136.1|3175826_3176312_-|hypothetical-protein
MPSFRSTLLALAASVALVGAAATPALADHNAGANLDGYASTDISSNGSCYYGALLPAAPGYSLQTKDYRFVRSGTSLTLVCVFTGIPAFVPADDTVTGDDYTAPTRLTRYVSLGSCLPPGVDSASELYPDYEREVPRVDAVTYSYRSTTTMVCHWRVDPTR
>NZ_CP047180.1|WP_123445135.1|3176525_3176720_-|hypothetical-protein
MAMSRTTQTALDLIDAVRIPEGIDPRLARQVSLSLRLLLESDSFGPSDRTLRRRSRRLRAGRLV
>NZ_CP047180.1|WP_159423361.1|3176828_3177107_-|DUF3072-domain-containing-protein
MSDDIPNTTDPDVKTEGDVLGARAADGSDTSASKDPSDWVTGDEPMTGPQRSYLDTLAREAGETLPADITKAEASEHIDRLQSATGRGDGSK
>NZ_CP047180.1|WP_159423362.1|3177207_3178509_-|DUF445-family-protein
MTTSSTSAVSTSAGGTSAGRDDEAKRAALVAMKRLATGLLVLMAIVFAVSFALQDRYPWLQWVRAASEGGMVGALADWFAVTALFRRPLGLPIPHTAIIPTKKDEIGASLAQFVEENFLRGAIVREKLDSFGIARRAGLWLAEPENAHRVGGESAAAVRSAIALLDDSDVQRVIEALARRHLLDPQWGPPLGSLVGSVVEAGHHRRLVDTLVEQAEAWLIANPESFTKMVSGRLPSWLPSAVSRAVDERLYREALVLVETIRDDQGHPFRIAVDGYLATLAKDLGSDPDLIARVEEIKNRAFDSPRVRELAGDAWESTKSSLLGAMDDPESPLRASIESIVVDLGRRLSTDQALASTVDTWIGTVAANLVDRYRGDIASIIGETIGRWDPQETSEKLELQVGKDLQFIRINGTVVGSLAGLVIFTVAHALLGS
>NZ_CP047180.1|WP_159423363.1|3178505_3179459_-|aldose-epimerase
MADFTPAPATGRQFALDLTAEGRTLHAVVTEVAAGLRHLSVDGVEITAGYPETVVPPFGSGIVLMPWPNRVKDGRWHHAGRTQQLDITEPKYHNAIHGLLRSASYRVVEQGPSFVELAAPVVPQAGYPFHLETTVRYELQADGLKVVHRVVNVGADEAPVAIGTHPFLAIGDVPTDELEITVDAAVHIEVDERLNPTGQSPVDGTEWDLRRGRRIGELELDDAWADVTIVDGESVHGLRADDGRRVLLWADASHNFIQVFITRIFPDGDDVRTAIAVEPMTAPAEALNSGQGLRWLEPGEEWSVAWGIRHEGFPASS
>NZ_CP047180.1|WP_159424131.1|3179468_3180260_-|DeoR-family-transcriptional-regulator
MRLLAEKQGFVSVADLSDRLGVSVVTVRSDLDRLAGEGTVQRVRGGAVPTGERSGERSFEEGLASASDEKAAIGREAAASVASGESVILDVGTTTLAIAHALVARDDLRDVTVVTNGLSVALALEPAIPRFTVVVTGGTLRPLQHSLVEPLASEVLERIRADVVFVGCTGVHPEAGVTNVNLPEATLKRRMLHAATRRVVVADSSKLGVVDLGRVAGTEEFDRLLTGAAAGDAVMGRLEAAGLAVTRCGTLRPGPQADGGAGP
>NZ_CP047180.1|WP_159423364.1|3180402_3181611_+|galactose-1-phosphate-uridylyltransferase
MNEAIPLSAGVVKRPHVLADGRDLIYFDDADTSLPPERSADARELDPRPATARMRQDVLTGEWVSIAASRQNRVFLPPAELDPLAPASPTNPSEVPSVYDVAVFENRSPSFGPLLEDEEAPASLEDLRTLGLGRTLTSVGRCEVVCFSPEHEGSFATLSASRARTVVEAWADRVAALSALPGVQQVFPFENRGEAIGVTLHHPHGQIYSYPYVTPRTTRLLASLDAYGPGMFADILAFEQAGERVLVRGEHWTAFVPFAARWPIEVHVLPHRHVADISETTPEERDELAVVYQRLLRGIDALYDSPTPYISAWHQAPVHERRDEVRLMLQITSPRRAATKLKYLAGSEAAMGAWIGDIAPETSAAALREAIERADAATLAAETAANPDASLPAADTTPEENR
>NZ_CP047180.1|WP_159423365.1|3181607_3182786_+|galactokinase
MTTSASLDAVAERAAQDFERAYGHPAVGVWAGPGRVNLIGEHTDYNDGFVFPFAIDRATAMAVAPREDRVVRISSAFSPEHVEISLDDLGPDALDGWSAYPLGVVWALTEYGVDLGARSGFDAFVDSDVPVGAGLSSSAALMCATAVALNELWELGLDRATLARVGRRAENVAVGAPTGIMDESASLFGERDAAVFLDCRSLDTEVVPLGFEEAGLVLLVIDTRVEHAHATGGYAERRASCELGASTLGVESLRELSVDDLPRAEALLDDVTYRRVKHVVTEDARVLTTVRTLREQGPRAIGELLDAGHVSLRDDFEISIPELDTAVEASRGAGAIGARMTGGGFGGSAIALTPVEKEEEVRAAVLAAFAEKGFRTPELFLVTAADGAGRVR
>NZ_CP047180.1|WP_159423366.1|3183079_3183571_-|YbaK/EbsC-family-protein
MSERSHPAVDRVLADLEVHGVRPPVRWLDEAASTAALAAAALGIEVGQIANSLIFLLDGSPLLVLTSGAHRVDTDWLGAELGGTITRASAAVVKAATGQTIGGVAPVGHPTPLPTVVDSALAEFDTVWAAAGHAHTVYPTSAAELVHVTGGALRPVVPPAPAE
>NZ_CP047180.1|WP_123445129.1|3183609_3184656_-|NAD(P)-dependent-alcohol-dehydrogenase
MLTVNAYAAPSATEPLVPTTIERRDVGAHDVLIEIAYAGICHSDIHTVRGEWGPVQYPLTVGHEIVGVVAEVGSEVSKHKVGDRVGVGCMVNSCRECENCLAGEEQYCLKGNTGTYASVDRDGTVTQGGYSTHVVVVEDFVLRVPESIPYEAAAPLLCAGITTYSPLSHWEAGPGKRVAVVGLGGLGHMAVKFAHAMGAEVTVLSQSLSKKEDGLRLGADHYYATKDEETFSTLKNTFDIIINTVSAPLDLDAYLGLLRRNGTMVNVGAPAEALPLHVFTLFAARRSFAGSGIGGIRETQEMLDFCAEKGIASEVEVVSASQINEAYERVLASDVRYRFVIDIATLTE

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Crispr_ID: NZ_CP047180_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_12

3545653-3545723

Orphan

Consensus_repeat	Method
AGGAGGGCAGCTACGTCGACACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_12

>merge|NZ_CP047180|12|3545653-3545723|CRISPRCasFinder
AGGAGGGCAGCTACGTCGACACCTCCTCGCACGAGGAGTCGAGCACCGAGAAGGGCAGCTACGTCGACACC

>NZ_CP047180|12|11|3545653-3545723|CRISPRCasFinder
AGGAGGGCAGCTACGTCGACACC	TCCTCGCACGAGGAGTCGAGCACCG
AGAAGGGCAGCTACGTCGACACC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_159423538.1\|3545801_3546680_-\|serine-hydrolase	unknown	unknown	gnl\|CDD\|224594
NZ_CP047180.1\|WP_159423529.1\|3529108_3531004_-\|prolyl-oligopeptidase-family-serine-peptidase	unknown	unknown	gnl\|CDD\|224423
NZ_CP047180.1\|WP_123444829.1\|3546723_3547563_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP047180.1\|WP_159423535.1\|3539731_3540928_+\|AI-2E-family-transporter	unknown	unknown	gnl\|CDD\|223701
NZ_CP047180.1\|WP_159423530.1\|3531025_3532810_-\|N-acetylglutaminylglutamine-amidotransferase	unknown	unknown	gnl\|CDD\|274430
NZ_CP047180.1\|WP_159423543.1\|3555850_3556498_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237864
NZ_CP047180.1\|WP_123734409.1\|3553160_3553829_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_CP047180.1\|WP_127888345.1\|3553825_3555142_+\|HAMP-domain-containing-protein	unknown	unknown	gnl\|CDD\|273593
NZ_CP047180.1\|WP_127888349.1\|3547851_3548721_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224045
NZ_CP047180.1\|WP_159423541.1\|3551835_3553089_-\|amino-acid-permease	unknown	unknown	gnl\|CDD\|129987
NZ_CP047180.1\|WP_159424151.1\|3540972_3541791_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|236841
NZ_CP047180.1\|WP_159423531.1\|3532811_3535319_-\|YbdK-family-carboxylate-amine-ligase	unknown	unknown	gnl\|CDD\|379601
NZ_CP047180.1\|WP_159423534.1\|3538191_3539613_-\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|274522
NZ_CP047180.1\|WP_159423536.1\|3542240_3543545_+\|DUF222-domain-containing-protein	unknown	unknown	gnl\|CDD\|367155
NZ_CP047180.1\|WP_159423533.1\|3537057_3538095_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|239264
NZ_CP047180.1\|WP_159423537.1\|3543758_3545237_-\|cryptochrome/photolyase-family-protein	unknown	unknown	gnl\|CDD\|225588
NZ_CP047180.1\|WP_159423542.1\|3555237_3555831_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379323
NZ_CP047180.1\|WP_159423539.1\|3548717_3549773_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|238566
NZ_CP047180.1\|WP_159423532.1\|3535390_3537061_-\|sodium:proton-antiporter	unknown	unknown	gnl\|CDD\|129911
NZ_CP047180.1\|WP_159423540.1\|3549769_3551872_+\|Fe(3+)-hydroxamate-ABC-transporter-permease-FhuB	unknown	unknown	gnl\|CDD\|236720

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_159423538.1\|3545801_3546680_-\|serine-hydrolase	gnl\|CDD\|224594	COG1680, AmpC, Beta-lactamase class C and other penicillin binding proteins [Defense mechanisms].	4.87962e-16
NZ_CP047180.1\|WP_159423529.1\|3529108_3531004_-\|prolyl-oligopeptidase-family-serine-peptidase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	3.60505e-73
NZ_CP047180.1\|WP_123444829.1\|3546723_3547563_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	9.50767e-22
NZ_CP047180.1\|WP_159423535.1\|3539731_3540928_+\|AI-2E-family-transporter	gnl\|CDD\|223701	COG0628, yhhT, Predicted permease, member of the PurR regulon [General function prediction only].	1.26149e-46
NZ_CP047180.1\|WP_159423530.1\|3531025_3532810_-\|N-acetylglutaminylglutamine-amidotransferase	gnl\|CDD\|274430	TIGR03104, trio_amidotrans, asparagine synthase family amidotransferase. Members of this protein family are closely related to several isoforms of asparagine synthetase (glutamine amidotransferase) and typically have been given this name in genome annotation to date. Each is part of a conserved three-gene cassette sparsely distributed across at least twenty different species known so far, including alpha, beta, and gamma Proteobacteria, Mycobacterium, and Prosthecochloris, which is a member of the Chlorobi. The other two members of the cassette are a probable protease and a member of the GNAT family of acetyltransferases.	0
NZ_CP047180.1\|WP_159423543.1\|3555850_3556498_-\|hypothetical-protein	gnl\|CDD\|237864	PRK14950, PRK14950, DNA polymerase III subunits gamma and tau; Provisional.	4.00632e-08
NZ_CP047180.1\|WP_123734409.1\|3553160_3553829_+\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	3.03144e-80
NZ_CP047180.1\|WP_127888345.1\|3553825_3555142_+\|HAMP-domain-containing-protein	gnl\|CDD\|273593	TIGR01386, Probable_sensor_protein_PcoS, heavy metal sensor kinase. Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.	5.79625e-50
NZ_CP047180.1\|WP_127888349.1\|3547851_3548721_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224045	COG1120, FepC, ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase components [Inorganic ion transport and metabolism / Coenzyme metabolism].	2.18705e-103
NZ_CP047180.1\|WP_159423541.1\|3551835_3553089_-\|amino-acid-permease	gnl\|CDD\|129987	TIGR00909, putative_amino_acid_transporter, amino acid transporter. [Transport and binding proteins, Amino acids, peptides and amines].	8.86644e-43
NZ_CP047180.1\|WP_159424151.1\|3540972_3541791_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|236841	PRK11088, rrmA, 23S rRNA methyltransferase A; Provisional.	5.20782e-45
NZ_CP047180.1\|WP_159423531.1\|3532811_3535319_-\|YbdK-family-carboxylate-amine-ligase	gnl\|CDD\|379601	pfam14403, CP_ATPgrasp_2, Circularly permuted ATP-grasp type 2. Circularly permuted ATP-grasp prototyped by Roseiflexus RoseRS_2616 that is associated in gene neighborhoods with a GCS2-like COOH-NH2 ligase, alpha/beta hydrolase fold peptidase, GAT-II -like amidohydrolase, and M20 peptidase. Members of this family are predicted to be involved in the biosynthesis of small peptides.	2.5659e-121
NZ_CP047180.1\|WP_159423534.1\|3538191_3539613_-\|FAD-dependent-oxidoreductase	gnl\|CDD\|274522	TIGR03329, Phn_aa_oxid, putative aminophosphonate oxidoreductase. This clade of sequences are members of the pfam01266 family of FAD-dependent oxidoreductases. Characterized proteins within this family include glycerol-3-phosphate dehydrogenase (1.1.99.5), sarcosine oxidase beta subunit (1.5.3.1) and a number of deaminating amino acid oxidases (1.4.-.-). These genes have been consistently observed in a genomic context including genes for the import and catabolism of 2-aminoethylphosphonate (AEP). If the substrate of this oxidoreductase is AEP itself, then it is probably acting in the manner of a deaminating oxidase, resulting in the same product (phosphonoacetaldehyde) as the transaminase PhnW (TIGR02326), but releasing ammonia instead of coupling to pyruvate:alanine. Alternatively, it is reasonable to suppose that the various ABC cassette transporters which are also associated with these loci allow the import of phosphonates closely related to AEP which may not be substrates for PhnW.	4.3608e-61
NZ_CP047180.1\|WP_159423536.1\|3542240_3543545_+\|DUF222-domain-containing-protein	gnl\|CDD\|367155	pfam02720, DUF222, Domain of unknown function (DUF222). This family is often found associated to the N-terminus of the HNH endonuclease domain pfam01844. The function of this domain is uncertain. This family has been called the 13E12 repeat family.	6.39972e-16
NZ_CP047180.1\|WP_159423533.1\|3537057_3538095_-\|hypothetical-protein	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	0.00033025
NZ_CP047180.1\|WP_159423537.1\|3543758_3545237_-\|cryptochrome/photolyase-family-protein	gnl\|CDD\|225588	COG3046, COG3046, Uncharacterized protein related to deoxyribodipyrimidine photolyase [General function prediction only].	4.41922e-143
NZ_CP047180.1\|WP_159423542.1\|3555237_3555831_+\|hypothetical-protein	gnl\|CDD\|379323	pfam13670, PepSY_2, Peptidase propeptide and YPEB domain. This region is likely to have a protease inhibitory function (personal obs:C Yeats). The name is derived from Peptidase & Bacillus subtilis YPEB.	0.000373396
NZ_CP047180.1\|WP_159423539.1\|3548717_3549773_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|238566	cd01146, FhuD, Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.	1.50223e-46
NZ_CP047180.1\|WP_159423532.1\|3535390_3537061_-\|sodium:proton-antiporter	gnl\|CDD\|129911	TIGR00831, Putative_Na+/H+_exchanger_Rv2287/MT2345/Mb2309., Na+/H+ antiporter, bacterial form. The Monovalent Cation:Proton Antiporter-1 (CPA1) Family (TC 2.A.36) The CPA1 family is a large family of proteins derived from Gram-positive and Gram-negative bacteria, blue green bacteria, yeast, plants and animals. Transporters from eukaryotes have been functionally characterized, and all of these catalyze Na+:H+ exchange. Their primary physiological functions may be in (1) cytoplasmic pH regulation, extruding the H+ generated during metabolism, and (2) salt tolerance (in plants), due to Na+ uptake into vacuoles. This model is specific for the bacterial members of this family. [Transport and binding proteins, Cations and iron carrying compounds].	1.9066e-44
NZ_CP047180.1\|WP_159423540.1\|3549769_3551872_+\|Fe(3+)-hydroxamate-ABC-transporter-permease-FhuB	gnl\|CDD\|236720	PRK10577, PRK10577, Fe(3+)-hydroxamate ABC transporter permease FhuB.	2.28839e-161

>NZ_CP047180.1|WP_159423537.1|3543758_3545237_-|cryptochrome/photolyase-family-protein
MTARTARTRWSVIGQLGPLFDDGGPMLLVEARSAFGRRPMHRAKAQLLLSALRHRGRELGDRAEYVRAETFAEGLAGRDDLEVIDPPTRGGRRLARRLGMSVLPSRGFVTEEEDFREWALAKSGKRLLLEDFYRWSRERTGVLMRGDQPEGGRWNYDHDNRNPPPKGASRLGLPDPWWPEEDDIDEEVRADLARWEREGAIRLVGEDGPRRFAATPAEAEAALADFVSSRLGDFGTYEDAMLSGDWTMAHSLLSAPLNLGLLDTRAVIDAAAAEHASGGAPLASVEGFVRQILGWRDYVWHLYWHLGPDYRERSNALGAKAPLPQQLLDLDPTGIEANCLHETLDDVRRHGWAHHIQRLMVLGNWGLQRGWDPAELNDWFVDVFVDGTEWVMPANVIGMSQHADGGVVATKPYSSGGAYINKMSDYCGGCRFNPKVRLGENACPVTAGYWAFLDRTEPVLRGNHRMAQPLAGLRALSDRAAVVDQERHRESY
>NZ_CP047180.1|WP_159423536.1|3542240_3543545_+|DUF222-domain-containing-protein
MSEDENAAALAEVRNCFDDSAAAERAASPTRLRAAERMHRGYRVALTVPEAFARGASRSETRDLVERSIRAELAVTLGVSEREVSRRLETAQMLLEHLPLTRALLRDSRILWEVGEAICKTASSLPETSRSALDERAADAALTTTTTQLRRMLGRWREELHEQPLAERHARAKEDRAVWVTPDVDGMATLCVHAPAPAVSGAYDRLRRIARTLREEGDPRTLQQLSADAAIDLLCDGDIAGTTPDDSHRPDPTFAPGLRAEVRLTLAASTAVGLDDAPADLDGYGPVPADVARELIRTAASFTRVLTDPDTGAVLSVGRTQRLPPSRMRLHLQLRDQTCRFPGCTRTAATSEADHTLEWRNGGETSLENLVSLCTSHHHVRHGEQWSYDRVDDDGTLEWTSPTGRRISNRPPPLPGRPPDRPPGPRFDTLPAPF
>NZ_CP047180.1|WP_159424151.1|3540972_3541791_+|methyltransferase-domain-containing-protein
MPALACPVCGAPLAPDALPRPTLLRCPVGHSADLARQGYVSLLRGRHATSGDTAAMVQAREELLGSGHYRPIQDAVAAAVPADARLVVDLGCGTGAYLAAVLEARPEASGLGLDLSAAAARRAARAHPRAAVATADLWQPLPLADGCADALLTVFAPRNAPEMRRVLRAGGVAIVVTPRERHLGEIRPVFGMLGIDAGKAERLDEQLQGFERVAREELDYAVAMTPGELRAEVLMGPSAHHVDAAAVDALLAGREETTAVTVAVTVSVYRAG
>NZ_CP047180.1|WP_159423535.1|3539731_3540928_+|AI-2E-family-transporter
MRGRRPRDGGRDSVATPAAAAPPGATPPVATPSDAVGDEPHDVSPGMRIAAAWGWRVLAVAALLWLVVKLVALVPVVVVPVLIAILVTALLTPLRDRLERWRLPRPLAVLVSILALLLALVGLIGLVVVQSRAGFGGVGQRALDAVDDVEAWLQGPPLGFSDVQLGDWAQKAIDWADTQASTIASGALAVGSQVAEVFAGALLTLFSLIFLLLDGRRIWTWFLRLMPRAARLPLETGAAAGWRTLSQFVRAQLGVAAINAIGIGIGALALQLPLVVPIAIVVFLGSFVPFLGAIVTGALAAVVALLFSGPVAALIMIGVVVVVHLLEGHVLQPLILGSAVKVHPLAVVLGVATGLEVAGLAGALFAVPVIATLNSAITAMRHDPEQLDSVPRDPGRSA
>NZ_CP047180.1|WP_159423534.1|3538191_3539613_-|FAD-dependent-oxidoreductase
MALTSTVFERSAPDPTVVDAALAGTRRGVFWLEDPDAPRPALAGAVRADLVVVGGGYTGLWSALRAKERDPSRRVVLLEARSLGWAASGRNGGFVESSLTHGRENGLARWPAEAARLEELGVRNLDDIEATVARYGMDCDFERTGSLAVAVEEYQVGPLADGDGVAGGRFLDTAEVRALVDSPTFLAGLAAPAEQCALVHPGKLVRELARVAEELGVEIHEDSRVLGLERAGAGVLVRTAGGSVAADLAILGTSAFPSLLARTRLMTVPVYDHVLMTEPLDADQLASIGWTGREGLSDVANQFHYYRRTADDRILWGGYDAVYHPGGRIRSAYEDRPETDRALAAHFLTTFPQLEGLRFSHRWAGVIDTSTRFAAFYGTALAGRVAYAAGYTGLGVGTTAFAADVLLDLLAGEPTERTELEMVRKRPLPFPPEPFATAGIQATRWSLDRADHDGGRRNPLLRTLDALGLGFDS
>NZ_CP047180.1|WP_159423533.1|3537057_3538095_-|hypothetical-protein
MLASALEVLLAVAGAAAGAVLVVSGVLKLGRTERFRASLAALGLPARLSAGPLFARAFPVVEIALGLAILLAPSPLHRGALLGAVAVDVVFLVVAIRAVRAPEPVECECFGGLGDARMTGRTVARNAVLLALALAGLVGAGAPAELLVPGVPALLVPGVPALLAVLLALALVPVRDRLAARAPAASTPASAPVSPSDLGDLAFLTAAGEPIALAEWADPPTHLVFFSPSCISCHELVERFRWWPNGLREGEELMPVFLGAPADFAAHEVFAPLVEHALYDPDRSIAAALGRGATPGHVLLDPEHPLGDGWSSGAFEIEKRVLRPDFFEDVRRGAVGPASDAAGHA
>NZ_CP047180.1|WP_159423532.1|3535390_3537061_-|sodium:proton-antiporter
MTPLLVVLVLALVVIAGAAVVGPRLGVASPLVLVGIGVAASFLPVVGPIEIEPEWILAGVLPPLLYSSAVSMPAMNFRREFGAISGLSVLLVVGTSLVLGLFFQLVLPDLGFAWGVALGAIVSPTDAVATSIVKGTSVSRRVVAMLDGESLLNDATALVLLRTAIAAAAASFSFWGALGSFGYSVLIAGIVGGLVGWLNLAVRRRVQDPTVNTILSFTVPFLASVPAELLGASGLVAAVVAGVVTGIRAPRELSPQNRLSDSQNWRTVELVLEGTVFLTMGLQVRAIVTSVEEDHAGVGPAVLIAVGALLLTILVRAAYVAPLLGVLRSRGRLRERMRPRVEGLQEQMGTEEGREESLKRISRGRRSPTARDLERFATRLTRMLADLEYFVRAPLGWREGTAVVWAGMRGAVTVAAAQTLPEDTPQRSVLVLIAFAVAALSLLLQGGTVGPLLRAIAPDVDEAAEERAREEERARVFALLRTSAEAVQEPPPAPDAPRTEAFLQAQRHRLAVIAAQRADLLDARDNGTFDADVLASVLAALDASQIDLEIRARTAR
>NZ_CP047180.1|WP_159423531.1|3532811_3535319_-|YbdK-family-carboxylate-amine-ligase
MRAELTLGAEEELHLIDLESRQLSPHAPQVLARLPKESFSAELQRTTVETNTAVVDSLDGLREQLISLRRAVIDAAAPDGIGIAAVGTAPRSEHGDFELTSTGRYGRMQEQYRMLVDEQLICGTQIHVGVSDRELAVQIAQRIARDLPVLLSASASSPYWNGQDTGYASIRTIIWQRWPSAGATGPLESAAEYDRLLDDLIATGVIADSKMAYFDVRPSSHAPTLELRVCDAMPIVDDAVLIAGLFRGLVRTAELDIEAGRPFRHTPPPIQRAATWQAARGGLSGPLLDHTEHPRPVPAAEALRSLIARLQPALDELGDLEQVRALAEALIARGNSADRQRAVLAERGTLDAVVDAVVAETHGPASGPILPAPSLRTYRVRAGDEAVATGGRAKSAYQPILEHFRGLGPERLETLHESRDRLVEQAGLTFRVGEEDRPFPVDLVPRVLQAHEWSELAAGLEQRARALECFLQDVYGEGRAVRAGVVRDLRGVPGWSEDAARLPAGTVRGAVMGFDLVRNEFGGWRVLEDNLRNPSGLAYAMGIRALLDDVLPDLPRPAGLLDASTALAGLRATLAHGTKRADPVLGLLSSGASSSAWFEHRRLAEGAGLLLLEAGDLTVEGGRVLAGGTVVDALYLRLDVELADLVAGDRAIGREILEVAAAGDVYLANAPGNGVADDKALYCAVPELIGYYLDERPLLESVPTYRPEDEAERRIVLERVGELVTKPVDGYGGRGVMIGPSAPAARVAERRAEIAADPGAWVAQEVVRLSSLPAFSGTDLQPRHIDLRAFVFVTGTGPGDVRLADLALTRVAAEGSMIVNSSRGGGAKDTWIVGG
>NZ_CP047180.1|WP_159423530.1|3531025_3532810_-|N-acetylglutaminylglutamine-amidotransferase
MCGIAGEIRFDGARADIGAVDRMTGCLVHRGPDGDGLWAAGRVALGHRRLVIIDLSAAGAQPMVDAALGLTIVFNGCIYNHRELRAELEGKGHRFFSHSDTEVIGKAYAQWGEDCVDHLLGMFAFAIVERESGRVVLARDRLGIKPLYLDETRERIRFASTVQSLLAAGGVDTSIDRTALMLYLSFHSVVPAPRTILAGVTKLPPATVRVIEPDGTSRERVYWEPVFTRDPDRAAWTERDWQEALLASFRTAVSRRMVADVPVGVLLSGGIDSSLIVALLAEAGQTGLQTFSIGFDAAGGESGDEFEYSSLVAERFGTDHHRLPIDSARLLPGIDAAVGAMSEPMVSHDAVAFHLLSEDVSQHVKVVQSGQGADEVLGGYDWYPPLARVPRERAVEAYADVFVDRPFAALQALLAPAWRGDPDAATAFLAERFARPGADTAVDAALRNDTAVMLVDDPVKRVDNMTMAWGLEARVPFLDHEFVELVGTIPPELKLADGGKGILKRAVRGIVPDEVIDRTKGSFPVPAIRQLEGPYLERVRAALTDPAARRRGVFDPATVDALLADPNATRTRLGSNELWQLALLEMWLQEHGVG
>NZ_CP047180.1|WP_159423529.1|3529108_3531004_-|prolyl-oligopeptidase-family-serine-peptidase
MTPPLIVSPQADRVAAAEELALGLVHAWGSWGPTMTPDAARVAFLSDRGGSPEVWVQDVVVGAEPSEARRIALTEDPVLEVSWSADSAWLACLVATDGGVRSQVWVVRPDGSDARRIAGSRDAHAELGPWTRSGHHVVVTIPSAEPEQPTRSFLVDPVTGERKPLVDGDLISVLDLSVEERLVVVRDGQRGQQYCVVVDRLTNENHALLPDSGTGSTDVALLRPSPLHDTESPMVAYLATDVDLPRRQLVAMPLGPDGWRGRIRRLAARDDAELEGLDADDAGRMLMLVWNVAGSSEIELLDTTTGERVPVAGLPGLVATTPVLSRDGGAVILGVEGPERPRELWRLDTATHEWSRITGVPALDAPPLIVPTLERFTGRDGLALSGWLYRAPGSTGPGAAMLSLHGGPESQERPTFSAQHQAVAAAGITVFAPNVRGSSGFGRDFVHADDVEKRRGAFDDVLAAAEHLVDAGIADPARIAVTGRSYGGYLTLASLAFSPGVFAAGVDICGMSHLQTFYRDTEPWIASAAVTKYGHPEHDAELLEELSPLNAAAAIDMPLLVVHGELDTNVPIGEARQIVAALEELGRPVRYLQLDGEGHEYRRADSKETLLRELLHFLTETLAAPPSMLVE
>NZ_CP047180.1|WP_159423538.1|3545801_3546680_-|serine-hydrolase
MTAAQIFRDRLVEHIDAVGFGAHGLHVLIGDDTAEHRWTPDVREDVHSVAKGVCVLAAGLAVDEGLISLDEPLGSLTADVTADLGEGVAELTLRRLLSMTSGIDLPWSPTLMTDWPDLAVEFLRRPSAGPVFQYSNASSYTAMRLLETRVGDVGEYVDRRLLRPLGIEGAEWERCPNGRIVAGSGLALRTEETARIGRLIRDRGVWRNERILAPEWSDLMHSEWVAAGTGPGYRRYALAGWDGPGASWRLHGAYGQLLVFAGDAVVTISADDHPGADAIAAFIAAERAAAQR
>NZ_CP047180.1|WP_123444829.1|3546723_3547563_+|helix-turn-helix-transcriptional-regulator
MDEDSARGTWRREPSTVVVADTGAPTRIAEPFAIAAGSVRLEAPHEFAPHRHALHELVWVRGGTMTVRLEHRILTVPDGFGVWIPAGTEHAGRTTARTALCDALFDPERSPVPITAPVLVEITPVLAALLTRLARTDLEAAARLRAEAVVFDVIAPSAAQYSVTVPQGERLAPLVAALLDDPTDRRTLADWAEHLGVGERTLSRVLRAQTGLSFLQWRQALRAHRALALLAEGRSVQDVSELMGHTHPSTFIAAFKRVMGTTPGAFAQDQRTAAASAAG
>NZ_CP047180.1|WP_127888349.1|3547851_3548721_+|ABC-transporter-ATP-binding-protein
MPPSPEPARASSRLAGTDLVLGFGRRTVVDGVSVRLEPGRVTALVGPNGSGKSTLLRALARLHAPSGGAVVLAGDRPATALSSRDFAREVTLFAQSRTAPQGLSVREVVAFGRHPHRRAFAGPSARDREAVEQAMATTGVLSMAERAAGELSGGELQRVWLAACLAQETGVVLLDEPTNHLDLRYQVETLDLIRDLAEVHGAAVGVVLHDLDHAARVADRLLLLSDGRVLAEGDPLAVLTAEHIEAAYGLRVEVAVDERTGHLRIDPVSRHSVRLHDQTPARSREDTEE
>NZ_CP047180.1|WP_159423539.1|3548717_3549773_+|ABC-transporter-substrate-binding-protein
MTRAPLLPAALAAAAVGVLLLTGCGTTAVESADAAGTVDSAECAADDTATATGAVSLTDSLGRTVELDAPAERIVVLEWQQTEDLLTLCVAPVGAASTEDYATYVSAETLPASTADVGERGEPDLDTLYGLDPDLIVMEAYSADDELLAQLEERDVPVLATIGADASGQIDNMKEVFSLLGEATGRTERADAVLAEFDQHLADAKTEVAEAALATPEFVFFDGWIESGNVVIRPYGKGALFTELGEELGLEGAWTDEINDSYGSGGVDPSYGLAQTDIEGLTAVGEANLVYSNDGTPDSYVTELAKSPVWSALPAVQQGRAFEFPPGVWGAGGPKSGEQAIDAFVDVIVGE
>NZ_CP047180.1|WP_159423540.1|3549769_3551872_+|Fe(3+)-hydroxamate-ABC-transporter-permease-FhuB
MTTTPTAAERRATAPSGRRAALGGVGVLAALAVAVVLIGLWHLTQGTSGIGADGLLRALLGEDVSVGGVSAGDVFAGSRLPRLSAGIAVGLALGAAGALLQSISRNALASPDTLAVTAGAYFALTAVAAFSLTVPLWASSGVAFLGGLAAAALVLALTGRAAGTSSTRLILAGSAIAMALDSGTAMLLILFRENTTGLFAWGSGSLGQLNIDASARAAPLIVVVLALALLLSRRLDVLGLGEDGAASLGVPVRSTRALAVLCAVLLTSTSVTLAGPIAFVGLGAPVLTRLLAARVPALRRHVFLVPASALIGAALIVLADALLRAILSPEGATAIPTGIPTAVLGGLVIVVLALRMRDAGAARSARTVRSTLRTARRFRVVLGVVAVLLAVTIVLALLAGSLQLRLGDVVLWLQSAAPDLVARALDERAPRIAAAVLAGGALALAGTAVQGTVRNPLAEPGLLGITAGAGLGAVIVVTTGLGGGGRPVLIAMAIAAGLATFGAIALLSWRGGLQPDRFVLVGIGAGYALSAVTAFLLLSSDPWRTPRILTWLSGTTYGRSLPDVLPVALGILVLLPVLLGLRRRLDLLAIDEDTPRILGVRPERTRLGVLALAAVLASLAVVAVGTVGFVGLVAPHLARTLVGARHGRIVPVAMLLGGLLVLVADTLGRTLIAPSQLPAGLMIALVGAPYFVWLLRRTRD
>NZ_CP047180.1|WP_159423541.1|3551835_3553089_-|amino-acid-permease
MTADASLARRLGFRDAVVIGLGSMIGAGLFSAFSPAAAAAGPWLLVGLALAAIVAWANASSTAQLAAQYPRSGGAYLYGRERLGEWPGFLAGWSFVVGKTASCAAMALTVAAYAAPAGWERPVAVAAVVALVAVNVLGVTRTALATRILLSIVLVVLVVAMAAAAASGPASVTGADRPFDAYGVLQSAGLLFFAFAGYARLATMGEEVRDPARTIPRAILGALVLAVLLYTVVGAGLLAALGPERLAASTQPLVDAAAAWPWTAVPIRVGAAAASLGALLALIAGIGRTSLAMARNGDLPRALAVIDPIRSVPRRAEIAVGLIVVVLVLVADLRSAIGFSSFGVLLYYLVANVAALTQEAPHRRYPRPLAVVGVAGCLLLVATLPPASIAGGLAVLAAGAAYRLLAQSRVRRSSQTK
>NZ_CP047180.1|WP_123734409.1|3553160_3553829_+|response-regulator-transcription-factor
MRILIVDDEINLLGALEAGLQGEGFAVDTATNGTDALWLAQEAEYAAIVLDLMLPDISGFRVCERLRAAEDWTPILMLTAKDGDLDQVEALDTGADDYLTKPFSFPVLVARLRALIRRGAAERPTVLTVGDLVLDPAARRVERGGVAIPLTAREFSVLEYLVSRAGDVVSKRDVLGAVWDFDFDGDPNIVEVYIRTLRNKIDRPFGRETIRTQRGAGYTVLP
>NZ_CP047180.1|WP_127888345.1|3553825_3555142_+|HAMP-domain-containing-protein
MRGLATRRRSLRSRITLAAAAVVALAAVLGAAGFLLVLSSVLAGSAATAAETEAERVATLVERGGADAVRASEGVVQLVVDGRVVAAGEDADDLPALATEERDEPFTTTPADEDPLVVATQELDDGALLVVGLPDEGRAEALATTAGLLAVAVPLLVAFVAIVCWIVVGRALRPVDRMRAEADAVTAAALDRRVAEPGSGDEIDRLAQTLNRMLGRLEDGQERQRRFVSDASHELRSPVAALRQSAEVALAHPDRLDAARLATTVAEESVRMGGLIEGLLLLARADEARLAVLAVPVDLDDLALREVRRLRDSGIAVDASGVSPVQAVADEALLGRALRNLVDNAVRHRAARLAIATRGEGDSAVLVVDDDGPGIPAADRERVLERFVRLDEGRARDAGGSGLGLAIVAEIAAAHGGSVAIEESPWGGARVTLRVPLR
>NZ_CP047180.1|WP_159423542.1|3555237_3555831_+|hypothetical-protein
MKKKTGIIVGVAGAIVLVGAGTGIAFAATDGFERSDALTGADLDRASEVAIAEIGGGTVTSAERDDDGTPGYELELRGDDGLEYDVRLDGSFGVLVVDPDDDAVRGTGGSATGSTDDGTTGTAEDSTAGAVDPDDLVGEELTRASEAAIAAIGGGTVTEAERSDDADHAFDVEVTRADGTDVDVDLDASYAVVRTEE
>NZ_CP047180.1|WP_159423543.1|3555850_3556498_-|hypothetical-protein
MLAAVLVLSGCSAADPSIDDGTAQALDDAVVAVAEKASADDWDGALTELDALQATLDAAIAGGNVREDRATSIREQADLVRADLAALIAAVPTPEESIEPEPEETTPVEEEPPAEETPEEETPAPVETPEEEPSPTPEETEPVEPTEPPEEESPAPAATTPAAGAPAVQAPATQAPVEEPVEGPGNSGGNGGGNGDGRSPESGQNPGNGNGPGKG

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Crispr_ID: NZ_CP047180_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_13

3711028-3711117

Orphan

Consensus_repeat	Method
GCTGGTCGAGCAGCCCGAAGGGCGTATCGAGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_13

>merge|NZ_CP047180|13|3711028-3711117|CRISPRCasFinder
GCTGGTCGAGCAGCCCGAAGGGCGTATCGAGAGCCACCCTCGCCCGAGGGCGGTCCATGCTGGTCGAGTAGCCCGAAGGGCGTATCGAGA

>NZ_CP047180|13|12|3711028-3711117|CRISPRCasFinder
GCTGGTCGAGCAGCCCGAAGGGCGTATCGAGA	GCCACCCTCGCCCGAGGGCGGTCCAT
GCTGGTCGAGTAGCCCGAAGGGCGTATCGAGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_123444647.1\|3710651_3710861_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_127888234.1\|3714588_3716061_+\|cytosine-permease	unknown	unknown	gnl\|CDD\|271377
NZ_CP047180.1\|WP_159423632.1\|3705603_3706137_+\|acyltransferase	unknown	unknown	gnl\|CDD\|100053
NZ_CP047180.1\|WP_159423631.1\|3704209_3705607_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274360
NZ_CP047180.1\|WP_159423633.1\|3706141_3707134_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133029
NZ_CP047180.1\|WP_123445325.1\|3711399_3711786_+\|DUF1772-domain-containing-protein	unknown	unknown	gnl\|CDD\|227787
NZ_CP047180.1\|WP_123444641.1\|3718326_3719583_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225208
NZ_CP047180.1\|WP_127888241.1\|3703190_3704171_+\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|366154
NZ_CP047180.1\|WP_159423639.1\|3719888_3721538_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|275079
NZ_CP047180.1\|WP_159423637.1\|3712843_3714412_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377939
NZ_CP047180.1\|WP_159423641.1\|3723067_3724138_+\|DUF418-domain-containing-protein	unknown	unknown	gnl\|CDD\|225193
NZ_CP047180.1\|WP_159423640.1\|3721655_3722525_-\|SIP-domain-containing-protein	unknown	unknown	gnl\|CDD\|99790
NZ_CP047180.1\|WP_159423636.1\|3712528_3712774_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_127888243.1\|3700488_3701358_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423638.1\|3716154_3717666_+\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|238623
NZ_CP047180.1\|WP_127888244.1\|3698803_3700474_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377422
NZ_CP047180.1\|WP_159423630.1\|3701808_3703194_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340831
NZ_CP047180.1\|WP_123444648.1\|3707130_3708285_+\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340831
NZ_CP047180.1\|WP_159423634.1\|3708628_3710494_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|173803
NZ_CP047180.1\|WP_159423635.1\|3711869_3712505_+\|isochorismatase-family-protein	unknown	unknown	gnl\|CDD\|238496

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_127888234.1\|3714588_3716061_+\|cytosine-permease	gnl\|CDD\|271377	cd11484, SLC-NCS1sbd_CobB-like, nucleobase-cation-symport-1 (NCS1) transporter CobB-like; solute-binding domain. This NCS1 subfamily includes Escherichia coli CodB (cytosine permease), and the Saccharomyces cerevisiae transporters: Fcy21p (Purine-cytosine permease), and vitamin B6 transporter Tpn1. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and solute carrier 6 family neurotransmitter transporters (SLC6s).	2.90846e-71
NZ_CP047180.1\|WP_159423632.1\|3705603_3706137_+\|acyltransferase	gnl\|CDD\|100053	cd04647, LbH_MAT_like, Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.	5.38264e-42
NZ_CP047180.1\|WP_159423631.1\|3704209_3705607_+\|hypothetical-protein	gnl\|CDD\|274360	TIGR02946, Putative_diacyglycerol_O-acyltransferase_Mb3115, acyltransferase, WS/DGAT/MGAT. This bacteria-specific protein family includes a characterized, homodimeric, broad specificity acyltransferase from Acinetobacter sp. strain ADP1, active as wax ester synthase, as acyl coenzyme A:diacylglycerol acyltransferase, and as acyl-CoA:monoacylglycerol acyltransferase. [Unknown function, Enzymes of unknown specificity].	3.85194e-21
NZ_CP047180.1\|WP_159423633.1\|3706141_3707134_+\|glycosyltransferase	gnl\|CDD\|133029	cd04186, GT_2_like_c, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	5.03637e-52
NZ_CP047180.1\|WP_123445325.1\|3711399_3711786_+\|DUF1772-domain-containing-protein	gnl\|CDD\|227787	COG5500, COG5500, Predicted integral membrane protein [Function unknown].	4.54044e-08
NZ_CP047180.1\|WP_123444641.1\|3718326_3719583_-\|hypothetical-protein	gnl\|CDD\|225208	COG2327, WcaK, Polysaccharide pyruvyl transferase family protein [Cell wall/membrane/envelope biogenesis].	1.15004e-19
NZ_CP047180.1\|WP_127888241.1\|3703190_3704171_+\|glycosyltransferase-family-2-protein	gnl\|CDD\|366154	pfam00535, Glycos_transf_2, Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.	4.50573e-24
NZ_CP047180.1\|WP_159423639.1\|3719888_3721538_+\|hypothetical-protein	gnl\|CDD\|275079	TIGR04247, nitrous_oxide_maturation_protein_NosD, nitrous oxide reductase family maturation protein NosD. Members of this family include NosD, a repetitive periplasmic protein required for the maturation of the copper-containing enzyme nitrous-oxide reductase. NosD appears to be part of a complex with NosF (an ABC transporter family ATP-binding protein) and NosY (a six-helix transmembrane protein in the ABC-2 permease family). However, NosDFY-like complexes appear to occur also in species whose copper requiring enzymes are something other than nitrous-oxide reductase.	7.97587e-13
NZ_CP047180.1\|WP_159423637.1\|3712843_3714412_-\|hypothetical-protein	gnl\|CDD\|377939	pfam07905, PucR, Purine catabolism regulatory protein-like family. The bacterial proteins found in this family are similar to the purine catabolism regulatory protein expressed by Bacillus subtilis (PucR). PucR is thought to be a transcriptional activator involved in the induction of the purine degradation pathway, and may contain a LysR-like DNA-binding domain. It is similar to LysR-type regulators in that it represses its own expression. The other members of this family are also annotated as being putative regulatory proteins.	1.87069e-23
NZ_CP047180.1\|WP_159423641.1\|3723067_3724138_+\|DUF418-domain-containing-protein	gnl\|CDD\|225193	COG2311, COG2311, Predicted membrane protein [Function unknown].	1.46416e-06
NZ_CP047180.1\|WP_159423640.1\|3721655_3722525_-\|SIP-domain-containing-protein	gnl\|CDD\|99790	cd06193, siderophore_interacting, Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).	3.77573e-79
NZ_CP047180.1\|WP_159423638.1\|3716154_3717666_+\|amidohydrolase-family-protein	gnl\|CDD\|238623	cd01298, ATZ_TRZ_like, TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.	1.17229e-115
NZ_CP047180.1\|WP_127888244.1\|3698803_3700474_-\|hypothetical-protein	gnl\|CDD\|377422	pfam04932, Wzy_C, O-Antigen ligase. This group of bacterial proteins is involved in the synthesis of O-antigen, a lipopolysaccharide found in the outer membrane in gram-negative bacteria. This family includes O-antigen ligases such as E. coli RfaL.	0.000750556
NZ_CP047180.1\|WP_159423630.1\|3701808_3703194_+\|glycosyltransferase	gnl\|CDD\|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	1.22584e-36
NZ_CP047180.1\|WP_123444648.1\|3707130_3708285_+\|glycosyltransferase-family-4-protein	gnl\|CDD\|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	1.62436e-16
NZ_CP047180.1\|WP_159423634.1\|3708628_3710494_+\|hypothetical-protein	gnl\|CDD\|173803	cd07477, Peptidases_S8_Subtilisin_subset, Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. 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. The S53 family contains a catalytic triad Glu/Asp/Ser. 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. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	1.85778e-37
NZ_CP047180.1\|WP_159423635.1\|3711869_3712505_+\|isochorismatase-family-protein	gnl\|CDD\|238496	cd01014, nicotinamidase_related, Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.	6.10223e-39

>NZ_CP047180.1|WP_123444647.1|3710651_3710861_+|hypothetical-protein
MSDTQNGPVMDGAEDASNDDKLSGLIEQVDHDHGDEGAGAMADALRDRADETDTEITSSDETETRTETE
>NZ_CP047180.1|WP_159423634.1|3708628_3710494_+|hypothetical-protein
MIPRSTPSRRPAGRLRRFLAATAAAAVVTAGLVGAAALPAQAAESAQTGAGRYVVTVDSKAVSTTLASALGLSLDASYGGGVSGFTATLTARQHAILAADSRVLGLSPADQVVEGQAQTMPSHVLTAEADKAPVTAGDGVTNWTGPAVAVIDSGVSAHPDYNLAKQVNCFGSGTAEDANGHGTGVSGYMTALDNGSGTVGIAPGAPVYSVRALDANNKGSISTLMCALDWVSQNAATYNIKVVNMSLATNGVDDNNCGRTNGDTIHQAVCDLVAKGVTVVSAAGNSAADLSAYIPAAYDEVLAVTNFANYDGKPGSLAAVPCSNVTTKDDNYTLNSNFASTADAGHTIAAPGTCPYTTKKGNTYAYIQTGTSMSTAAASGVVLDCLAAGGSCVGKSPAQVIAQVIAQAKSATVDRGRTFAGDPTRPVSGRYYGYGVSTIPVGTVVTPTPTATPTPTATPTATATPTATPTPTATPTATATPKPTATPTATPTATATPTPTATATPKPTATPTATATPTPTPTSGADTVKPQAKIVSPASQTTVTGTVTLVANASDNVAVTSLAFWSGSTKLGDGVKQADGSWSLTANSKNWPNATYAVVARATDAAGNVGSSASITLVIKN
>NZ_CP047180.1|WP_123444648.1|3707130_3708285_+|glycosyltransferase-family-4-protein
MIPGGTRTLRGRLRTRVRGLLSGEDARSRRLRVEAEPAFRTRYANPYNARLYTAMTAEGVLVRDLSWLRLLVAKVDVVHLHWPDLTFLSGVRRYRIVARLVFFFAFLRVARLRGTRLIWTAHNVTSHEERGTPFLRNWYRRLLTENLDAIVCLSEEGVTAMRRSYPELAAVPAFVTPHGHYRHDYDFSATRAEARAELGLDPDARLVVSVGQIRPYKNVPTLIERFREREDDGTLLAVAGNPARGPLRGVIEEAAAGDARIRLELSFLSDERMALWLRASDLVVLPYSAIQNSGSAILAVSADRPVLVPDLGAMHELAALVGPDWVRLYDGAFDTAALDGALAWLDERAVAADASADLSALEWDAIARATIDVYRRVLRAPRPR
>NZ_CP047180.1|WP_159423633.1|3706141_3707134_+|glycosyltransferase
MDTSLAIVVVSYNTREKTLACLASIPLGDAPTPPHVIVVDNGSEDGSAEAIRAAHPEATVIEAGDNLGFARGVNRGVAAATERFVLLLNPDTLVLEGSFRALLEFAVANPRYGVYGGRTLRPDGSVDPSSCWGAPSLWSLLTYATMLSTAFRGNPLLDPESLGGWQRDSVREVPIITGCLLLMPREEYERVGRLDERFFLYGEDAEFSIRARRAGLRPVIVPTAVIVHDVGASTRDAATAGNSGRKMCMVMAGKATMIRLAWKPLPARIGIALLQAGALVRTVLETATRRKRRAWTEVWQRRADWRVGYPEAERTLFGRVPGTGAAEVTR
>NZ_CP047180.1|WP_159423632.1|3705603_3706137_+|acyltransferase
MSQGGGPLRTLTKVRTYLQAVRLLHFHAYSHADQVPRLTRGADVSFAPNVSFRNAERITLGAGTHIGENSLLWAGNSTGRITLGAKCLLAPNVTITASNYGIVQGTPVMDQPKVEKDIVIGRDVWLGANVVVVAGVTIGDGAIVGAGAVVTKDLPANCIAGGVPAKVIGQRPEADRA
>NZ_CP047180.1|WP_159423631.1|3704209_3705607_+|hypothetical-protein
MTRPPRRTGRPHAEPLRTLDEKFVSNAVVYEVARPTGSMIIDGAPFRRADGSLDRDLVYSAWEAFIRTSPSVRQRLARAPLGLFTPSWVSVDTIDVRDHVRFHPGVVEWDPRHVELLTGAFNGPMDPKGPLWDILVIELSTGQLGFAVRIHHALGDGMFGLVLIQAFTSGEPIEFPAYSRAPMRFPDDPRPPRGPLSLTLAARRQIASTHASLADEWTEWKRKPLKKRITRVGGRNIRSARDWWIRRSGLLERSIKPRDAAILTVDLKTAKAAARAAGGSVADLTVALALHAFAALHPERAEIATLVPVSPRRDKNEVKRNHVSMVRVAVPVSLRLAETVASVREQVQLAVETGESGITRGRKDWQGYASYLPVFLRPRWFGGAELASMTLWPVTEPDDEAAVFASSFTKRLDIAISVRSDLDADRFIGSIAASLTEIGAPVIDPLAEQTPAGSPDDHEPNGAGR
>NZ_CP047180.1|WP_127888241.1|3703190_3704171_+|glycosyltransferase-family-2-protein
MNPSVLTPGDVSIILCTRERPDMLREALAAIAAGTDPAVEVIVVDSASTDSRTREVALAAGVRYVRTDTKGLSIARNLGLDSSDRPIVVYTDDDCSPTPGWIEALLRAFEEERVTVATGRMLDHTLVDTDVPPTDRIVYRSAVRGLDAGHGAVMAFRRDVLQTLGAFDDTLGAGRYLAGAEDLDIFCRALAAGGTAVFVPDSVVLHVNTRNPVAYRRLMRGYGLGLGALVGKWWRLSPKVGARLTATLAVRSGRRLVRSAQRRGRGAKDELAMVEGILRGYLRSRHLRLSGSTFVDEYPPTPIRLPATPAQPGTAQADPAPAGTPS
>NZ_CP047180.1|WP_159423630.1|3701808_3703194_+|glycosyltransferase
MDDEHQCSTTAAGPPDHRDDPEHDRTDRDARPLTSVASGAPAGAPLSILYSFPHGIGSPGIGWTALQQVRSLVAAGHRVTVVAASITESLGPVARAVTTLTVGGVRLPHRLFGRSRSIAHHDRVTARILAEGDYDVVHGWPWGSARTFDEAARQGVPAVREAPNTHTAHAFEVVAEEYERLGITPPVGSPHTYNAVRLRREEREWASATAILVPSASVEQTFLEKGFSPRKLLRHRYGALVDTTRSFDPDPRDEPDHVFTAVFVGRIEPRKGLLYALQAWQQSKASSTGRFLIYGDFTPGYQERLAGLLEQPSVELRGFTGDVAGVFASADVLILPTIEEGSALVTSEAQAAGCVPLVSSAAGANLEDGVQGLVHEPRDVETLTAQIDLVSSDRALLARMRRAALDNRGNLTWERASIDLVAAYRAAMVLVREDLASTGSAATGSAADSDDRSDQPRTDTP
>NZ_CP047180.1|WP_127888243.1|3700488_3701358_-|hypothetical-protein
MSVPLYLRVLWSYKWLLAVGLVVAVLAAMVAGYTVKDGEIVSRAESAYRSDTTILLGGGSRNPLQAVEPGQALQEGTSEAQQNDLTNTAVIYAYIVSGSEIRTQVEQAIGGFAPTEALSAVRRTTQPAGTEQNPGRFSLPILSIVGESTDPARAVLISQTATQIFQGYITAQQDAQGVAPELRVTLQTTDQGAAVEQEGSNPIIPIAITGLGVFLAFIALAFILYNIRISRERVTANRGNQRRGESFRRGPALTGTASENGQRPAALGTAPENTAGPGELASSGKRSAT
>NZ_CP047180.1|WP_127888244.1|3698803_3700474_-|hypothetical-protein
MSTPTLKGTPLGVPGNDDPYAGEILVRRTFTVRAVLSTVLLAAVAVAAVYYLNPLYAGAILFGISFLYLTRKLVFNWTGAFIVLLGVIMFIPVRYYALPIPLGFALEPYRLVIVLMVVAAIVALMIDPTFVWRPAAFGWPLGIWVASSLLSIAANVQFISEGALGSGVAGAIVNDLLMLSVYFVARLVMRNEKLVEAFLTFLVWSAVVVAFFAVIERATQQNVFTMLDKFLPLERLGAEQEAYRAGGYRSFGSSQHPIALAVMFTMMIPIAIYLSKYARWPFNEINRRIIYYGTILALLLGVVTAVSRTAIVTLGVMFLLTVILRPKVGGYLLLGMVPVLGLGFVLIPKILTDMIGSFLDPDALIASQYTSAGMAGAGRLADLEPAMAIVREHPFFGTGVGSRIVVGEDKNAFILDNQWLGTLLDGGAVGVIGLAVLFLVPIVMLLRYSFKSTTTPQYASLAFAVAVLLLGYTIAAYFYDAFGFFQSFMLFWILLAVGAWVLTEAPRKSTRRRLSPEEAGHVSAFTRGGPHIPVGQPALGSHVGAHVVRKPTQIES
>NZ_CP047180.1|WP_123445325.1|3711399_3711786_+|DUF1772-domain-containing-protein
MPGLSRTDDRAFVSAMTAINAAVQNPLFALSFVGSGLSSAAALVAALAGGAGAATTSAVAGALALAVLQYVVTFGRSIPLNLRLDRAAGGPLSDARRGFERAWVRANTARVLASGGSLLLLGIALATT
>NZ_CP047180.1|WP_159423635.1|3711869_3712505_+|isochorismatase-family-protein
MTAPRRALILVDVQLEYFAGPLEIRYPPHATSLPAITAALDAATAAGLPIAAVQHSSGEGAPVFAPGTPGFELHPEIEGRRSDEWKSITKRFGTVFAGTDLLAWLRERDVDTITLVGYMTNNCILASAAEAETHGLTAEVLSDATGAIAISNAAGSVDAETVHTTLLALLNSNFAAVADTEAWTEAVASGEPLPQSDLGSSAVAGVALPPR
>NZ_CP047180.1|WP_159423636.1|3712528_3712774_-|hypothetical-protein
MHTSSVDPRDVDAEVTTPVYRVYFAETETMVDELRITGARDVLEVVDWAERDARGVPFTVYCEHPSPFNPGKVTLQLLLSR
>NZ_CP047180.1|WP_159423637.1|3712843_3714412_-|hypothetical-protein
MVIPLSEALLDPLLAAAGPVVVAGGEAAARVPIRWAHASEQLDVAPLLLGGELLLMEGVNLSSDQDPEECRRYVESLVTAGIGALAVELSERLPSVPAPLVAAADDLGLAVLALPRRVPFVQVCESINTRLTEQKFRSLRVADRVSGLLGEAAAADAGIDELLKVVASATGASAALVSPAGEEIVRAHPGRGVDTARTAGASSGVLRAGDSLLGTLYLRAHDEADLHGVAVALDRAPDVLAIALLRRRPPTARERLTAQLFAVATAPSARPDPSAELQIDALLGRLGVGGRECFLGVWADVGDDERTLRAVRAALDRSMRGSADSASVICVAGGELLALLAFADSAARERARALLLGEWPPAAGAAALVCVGSGADAVARVPRELAEVRGVREWTRAESGVVDARLHRLERFASTLRDDPEADALVEEVLGPLRRGRPELLATLESFASHWGSKTATAAALGIGRQTLYDRLARIESLIGLLDASPARTRVLLTAVSLHRARAALPPAAPRSTRPFPPPADR
>NZ_CP047180.1|WP_127888234.1|3714588_3716061_+|cytosine-permease
MSSDTLHGTTDTEDALTPLPESRRNARLDGQFWIWAGANIAPINWVLGALGVNMGLGLWDTITVLVLGNVVGMAVFGFFVLLGQRTGATGMLVGRAVFGRRGNYAPAVIQAVVVIGWCAINTWIVLDLVIALLGSVGLVDPEAANIGWKVAVAAVIMAIQVAISFLGYRAIAAFERWTVPPTLLVLAVMSIVAWFFLDIDWSYAGPAEGALTGGDRIAAMSIVMTAIGIGWGLTWLAYAGDYSRFVSPRASRRKLYFASVLGQFVPVVWLGVLGATLATKNGSVDPGQLIVENFGALAIPVLLLVVHGPIATNVLNIYSFGMATQALDIRLGRRTLSLIVGVLAFAASVFFVFQDDLATTLDAWLVGLVGWVAPWGAIVLVHYTVFEPRVRSFGHLFAPVGSPLLPDVRWRALLSFAIGATLTWLFMNGSVPALQGPAATALGGVDVSWLAGGVSAGLAYLLLGRGDAASWVRKREALEPAARESEPVLG
>NZ_CP047180.1|WP_159423638.1|3716154_3717666_+|amidohydrolase-family-protein
MPLLITDAAVITMDPVSGAVPIMASIRIVDDVITAIGPGLEPEPGDEILDGRDRLVTPGFVNAHTHSWEYLYKGRYDNLPLELWMLLSYPILGDSRVAPDLIRLRSSLFALESLKAGVTTLVDDVLENPDQDAAQLAAVFDAYDEIGIRANISGHVISKPFFETMPFLEEYLPAELLDSVRGAARPTTEGYLDFSRTAFATQHGRGGGRLRYMVAPSAPQRVGADLLVGATELALEHDAECHIHVLETKTQLVTGEEFHGSTLVEYMAGIGALSANTTFAHGIWLTDSDMASIAAAGTSVSHNPISNLKLGSGIAPWRALHDAGVNLGLGTDGCSSSDSPRMLDVIKAAALLHKVTDPDLSSWPTVAEVLTAGTIGGARSAVLGDVTGSIEVGKQADLVLFDLETLAFTPRQRLENQLVYSENGSSIDTVIVAGRVVVAGGESTTVDEAALRADLAAQLGDIVAWQDALDRSNGVLTEPFHRMYERAMRRDAPIDRFSGRRLV
>NZ_CP047180.1|WP_123444641.1|3718326_3719583_-|hypothetical-protein
MLGGLRKRTAPLLKSPAVLSLGARGVFLDAPRLRSARRSGGARGASGAQGRAILIAPPGAGNIGDAALVGAFLENVAGPITVITRYKGDFRIPAEQADRVEIVSLGTLLYGGLPSFVRDLRRFRAMLPGAASVSIVGADIMDGAYNFRASTSRALVARSAASAGVDTRVLGFSWNGKAHPGALAQLRDADRAGTTLFLRDPLSVERARRDGLDAKASADIVFSARSVDQGRASTELAALDTTGGIAIVNVSGLIDTDQTGAYVEIIGGLRARGLAVVLLPHVIKHGPDDLAACRKVFAALPDTTGVAFVEDVLTPAEVRGFTERATVTVTGRMHLAIMSLMKGVPAITLATQGKVEGLMAMFELPYLCVEPGAGLAGRVGDALERVLSDRESVSAAILAKLPAVQELSAANFAGLPRA
>NZ_CP047180.1|WP_159423639.1|3719888_3721538_+|hypothetical-protein
MTRTLSATLAALLVVIAAFFAAAPSFAAANRYASPNGTGTACSAAAPCALTTAVQNAAAGDTVLLTAGTYPTTTLKGGKATVAAPVVVQPAPGASPVLGSTKVYTPNTVWNDIFSKSTFYTYGSGITVNRMHIDGAGIFVRSANVVVRDSLFENGSSMDGIQVGGTDNGLIENNLVRNFDQNIDNGLHADCIQVFESNDVTLRGNTLMNCYNAGIIFSPGGGDGMTDITVESNFVSGCIVITSDCRGGSSADFREASADGIHIRNNTFESGALRVGGAKNTVFDRNIVSYLSSCTSPMTNTIVENWNTKLCKTPSLLNQQGNVQGAPALASAATGDLHVLSATGTQIAGWGSTTSARTDIDGQVMGSRTAGADQFGGVTAPSPTATPTATPTATATPTATPTATPTATPTATPTATATPTATPTPTATPTPTATPTPTATPTATPTPTATPAPVDRTAPTVAIVSPGSGSSVTGVVSLMATAADDTAVTGVTYWVGTTKLGDAVKASDGNWYLTVNTAVFPKGTYSVTAKAVDEAGNATTSAPILLKRV
>NZ_CP047180.1|WP_159423640.1|3721655_3722525_-|SIP-domain-containing-protein
MTDATTPAAPSERRARPPRPQLVLTVLRTERLTEHFVRVHLGGEGFDAFVEAADPDRLAATDRYVKLLLAPPGVALEPPHDLDALRARLAPEELPVRRTYTIRSVDLEARSLAIDFVLHGDEGVAGPWAASARPGDRLEMSAPGGAWAPRADAANLLLGDESALPAIAAALEAMPAQARGIALIEVHGAEDELPLTVPAGVEVRWLHRGDEEAGQALTAAVAELTRPDGAVEVFAHGERTAMKRLRAILQDDWGVERAALSLSAYWALGRAEDRFQAEKREPVGAIFAD
>NZ_CP047180.1|WP_159423641.1|3723067_3724138_+|DUF418-domain-containing-protein
MDATTTVPRAAPLAPRLQPDRVLVPDVLRGVAIVAMLIAHAMPLLPSLRDGAAGFAAGNINDLASPLFALVMGMSAALVLARPGASGGRVVVQNLIRGAVLVALGVWLGGWGSWIAIVLPHLGLTLALGTPILLLRSRLVAIVAAVVLVAGAPLNALVAASVDPAVLYARTPVGYLLQWSFVDPHYRLTNLLPFLLLGALLLRHGFRRDRLLAVLALVAVLAYPVRPALERLIGLQSVSGSHPDTLHDLGLVLAAYVAVVLLATVRGRPASTVIAAVLTPFRAVGSLALSVYVLQVAVVAAFATQGLGYVADTPGAALLLVLGVWAVAVLWWRFVGIGPLEWLIGRLTRLVPAPRR

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Crispr_ID: NZ_CP047180_14

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP047180_14

3717826-3717980

Orphan

Consensus_repeat	Method
CCGCCCGCAGCCACCTCCGGCACGCGGAACCCGCCTCGGCACGCCGGATCCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP047180_14

>merge|NZ_CP047180|14|3717826-3717980|CRISPRCasFinder
CCGCCCGCAGCCACCTCCGGCACGCGGAACCCGCCTCGGCACGCCGGATCCGCTCGATTCGACGAGCCGGACGTGATGTCGCGTGCCGAACTCCCTCACCCAGCCGCCCGCAGCCACCTCCGGCACGCAGAACCCGCCTCGGCACGCCGGATCCG

>NZ_CP047180|14|13|3717826-3717980|CRISPRCasFinder
CCGCCCGCAGCCACCTCCGGCACGCGGAACCCGCCTCGGCACGCCGGATCCG	CTCGATTCGACGAGCCGGACGTGATGTCGCGTGCCGAACTCCCTCACCCAG
CCGCCCGCAGCCACCTCCGGCACGCAGAACCCGCCTCGGCACGCCGGATCCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP047180.1\|WP_123444647.1\|3710651_3710861_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_127888234.1\|3714588_3716061_+\|cytosine-permease	unknown	unknown	gnl\|CDD\|271377
NZ_CP047180.1\|WP_123444641.1\|3718326_3719583_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225208
NZ_CP047180.1\|WP_159423633.1\|3706141_3707134_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133029
NZ_CP047180.1\|WP_123445325.1\|3711399_3711786_+\|DUF1772-domain-containing-protein	unknown	unknown	gnl\|CDD\|227787
NZ_CP047180.1\|WP_159423643.1\|3726647_3727181_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423642.1\|3725931_3726519_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423644.1\|3727215_3727890_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423639.1\|3719888_3721538_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|275079
NZ_CP047180.1\|WP_159423637.1\|3712843_3714412_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377939
NZ_CP047180.1\|WP_159424161.1\|3725008_3725626_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|236605
NZ_CP047180.1\|WP_159423641.1\|3723067_3724138_+\|DUF418-domain-containing-protein	unknown	unknown	gnl\|CDD\|225193
NZ_CP047180.1\|WP_159423640.1\|3721655_3722525_-\|SIP-domain-containing-protein	unknown	unknown	gnl\|CDD\|99790
NZ_CP047180.1\|WP_159423636.1\|3712528_3712774_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423638.1\|3716154_3717666_+\|amidohydrolase-family-protein	unknown	unknown	gnl\|CDD\|238623
NZ_CP047180.1\|WP_159423645.1\|3728067_3728565_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP047180.1\|WP_159423646.1\|3728649_3729840_-\|arsenic-resistance-protein	unknown	unknown	gnl\|CDD\|223869
NZ_CP047180.1\|WP_123444648.1\|3707130_3708285_+\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340831
NZ_CP047180.1\|WP_159423634.1\|3708628_3710494_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|173803
NZ_CP047180.1\|WP_159423635.1\|3711869_3712505_+\|isochorismatase-family-protein	unknown	unknown	gnl\|CDD\|238496

Protein	Function_ID	Function_description	E-value
NZ_CP047180.1\|WP_127888234.1\|3714588_3716061_+\|cytosine-permease	gnl\|CDD\|271377	cd11484, SLC-NCS1sbd_CobB-like, nucleobase-cation-symport-1 (NCS1) transporter CobB-like; solute-binding domain. This NCS1 subfamily includes Escherichia coli CodB (cytosine permease), and the Saccharomyces cerevisiae transporters: Fcy21p (Purine-cytosine permease), and vitamin B6 transporter Tpn1. NCS1s are essential components of salvage pathways for nucleobases and related metabolites; their known substrates include allantoin, uracil, thiamine, and nicotinamide riboside. NCS1s belong to a superfamily which also contains the solute carrier 5 family sodium/glucose transporters (SLC5s), and solute carrier 6 family neurotransmitter transporters (SLC6s).	2.90846e-71
NZ_CP047180.1\|WP_123444641.1\|3718326_3719583_-\|hypothetical-protein	gnl\|CDD\|225208	COG2327, WcaK, Polysaccharide pyruvyl transferase family protein [Cell wall/membrane/envelope biogenesis].	1.15004e-19
NZ_CP047180.1\|WP_159423633.1\|3706141_3707134_+\|glycosyltransferase	gnl\|CDD\|133029	cd04186, GT_2_like_c, Subfamily of Glycosyltransferase Family GT2 of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	5.03637e-52
NZ_CP047180.1\|WP_123445325.1\|3711399_3711786_+\|DUF1772-domain-containing-protein	gnl\|CDD\|227787	COG5500, COG5500, Predicted integral membrane protein [Function unknown].	4.54044e-08
NZ_CP047180.1\|WP_123444648.1\|3707130_3708285_+\|glycosyltransferase-family-4-protein	gnl\|CDD\|340831	cd03801, GT4_PimA-like, phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.	1.62436e-16
NZ_CP047180.1\|WP_159423637.1\|3712843_3714412_-\|hypothetical-protein	gnl\|CDD\|377939	pfam07905, PucR, Purine catabolism regulatory protein-like family. The bacterial proteins found in this family are similar to the purine catabolism regulatory protein expressed by Bacillus subtilis (PucR). PucR is thought to be a transcriptional activator involved in the induction of the purine degradation pathway, and may contain a LysR-like DNA-binding domain. It is similar to LysR-type regulators in that it represses its own expression. The other members of this family are also annotated as being putative regulatory proteins.	1.87069e-23
NZ_CP047180.1\|WP_159424161.1\|3725008_3725626_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|236605	PRK09645, PRK09645, ECF RNA polymerase sigma factor SigL.	9.54998e-38
NZ_CP047180.1\|WP_159423641.1\|3723067_3724138_+\|DUF418-domain-containing-protein	gnl\|CDD\|225193	COG2311, COG2311, Predicted membrane protein [Function unknown].	1.46416e-06
NZ_CP047180.1\|WP_159423640.1\|3721655_3722525_-\|SIP-domain-containing-protein	gnl\|CDD\|99790	cd06193, siderophore_interacting, Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).	3.77573e-79
NZ_CP047180.1\|WP_159423638.1\|3716154_3717666_+\|amidohydrolase-family-protein	gnl\|CDD\|238623	cd01298, ATZ_TRZ_like, TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.	1.17229e-115
NZ_CP047180.1\|WP_159423646.1\|3728649_3729840_-\|arsenic-resistance-protein	gnl\|CDD\|223869	COG0798, ACR3, Arsenite efflux pump ACR3 and related permeases [Inorganic ion transport and metabolism].	7.93029e-44
NZ_CP047180.1\|WP_159423639.1\|3719888_3721538_+\|hypothetical-protein	gnl\|CDD\|275079	TIGR04247, nitrous_oxide_maturation_protein_NosD, nitrous oxide reductase family maturation protein NosD. Members of this family include NosD, a repetitive periplasmic protein required for the maturation of the copper-containing enzyme nitrous-oxide reductase. NosD appears to be part of a complex with NosF (an ABC transporter family ATP-binding protein) and NosY (a six-helix transmembrane protein in the ABC-2 permease family). However, NosDFY-like complexes appear to occur also in species whose copper requiring enzymes are something other than nitrous-oxide reductase.	7.97587e-13
NZ_CP047180.1\|WP_159423634.1\|3708628_3710494_+\|hypothetical-protein	gnl\|CDD\|173803	cd07477, Peptidases_S8_Subtilisin_subset, Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. 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. The S53 family contains a catalytic triad Glu/Asp/Ser. 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. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	1.85778e-37
NZ_CP047180.1\|WP_159423635.1\|3711869_3712505_+\|isochorismatase-family-protein	gnl\|CDD\|238496	cd01014, nicotinamidase_related, Nicotinamidase_ related amidohydrolases. Cysteine hydrolases of unknown function that share the catalytic triad with other amidohydrolases, like nicotinamidase, which converts nicotinamide to nicotinic acid and ammonia.	6.10223e-39

>NZ_CP047180.1|WP_159423638.1|3716154_3717666_+|amidohydrolase-family-protein
MPLLITDAAVITMDPVSGAVPIMASIRIVDDVITAIGPGLEPEPGDEILDGRDRLVTPGFVNAHTHSWEYLYKGRYDNLPLELWMLLSYPILGDSRVAPDLIRLRSSLFALESLKAGVTTLVDDVLENPDQDAAQLAAVFDAYDEIGIRANISGHVISKPFFETMPFLEEYLPAELLDSVRGAARPTTEGYLDFSRTAFATQHGRGGGRLRYMVAPSAPQRVGADLLVGATELALEHDAECHIHVLETKTQLVTGEEFHGSTLVEYMAGIGALSANTTFAHGIWLTDSDMASIAAAGTSVSHNPISNLKLGSGIAPWRALHDAGVNLGLGTDGCSSSDSPRMLDVIKAAALLHKVTDPDLSSWPTVAEVLTAGTIGGARSAVLGDVTGSIEVGKQADLVLFDLETLAFTPRQRLENQLVYSENGSSIDTVIVAGRVVVAGGESTTVDEAALRADLAAQLGDIVAWQDALDRSNGVLTEPFHRMYERAMRRDAPIDRFSGRRLV
>NZ_CP047180.1|WP_127888234.1|3714588_3716061_+|cytosine-permease
MSSDTLHGTTDTEDALTPLPESRRNARLDGQFWIWAGANIAPINWVLGALGVNMGLGLWDTITVLVLGNVVGMAVFGFFVLLGQRTGATGMLVGRAVFGRRGNYAPAVIQAVVVIGWCAINTWIVLDLVIALLGSVGLVDPEAANIGWKVAVAAVIMAIQVAISFLGYRAIAAFERWTVPPTLLVLAVMSIVAWFFLDIDWSYAGPAEGALTGGDRIAAMSIVMTAIGIGWGLTWLAYAGDYSRFVSPRASRRKLYFASVLGQFVPVVWLGVLGATLATKNGSVDPGQLIVENFGALAIPVLLLVVHGPIATNVLNIYSFGMATQALDIRLGRRTLSLIVGVLAFAASVFFVFQDDLATTLDAWLVGLVGWVAPWGAIVLVHYTVFEPRVRSFGHLFAPVGSPLLPDVRWRALLSFAIGATLTWLFMNGSVPALQGPAATALGGVDVSWLAGGVSAGLAYLLLGRGDAASWVRKREALEPAARESEPVLG
>NZ_CP047180.1|WP_159423637.1|3712843_3714412_-|hypothetical-protein
MVIPLSEALLDPLLAAAGPVVVAGGEAAARVPIRWAHASEQLDVAPLLLGGELLLMEGVNLSSDQDPEECRRYVESLVTAGIGALAVELSERLPSVPAPLVAAADDLGLAVLALPRRVPFVQVCESINTRLTEQKFRSLRVADRVSGLLGEAAAADAGIDELLKVVASATGASAALVSPAGEEIVRAHPGRGVDTARTAGASSGVLRAGDSLLGTLYLRAHDEADLHGVAVALDRAPDVLAIALLRRRPPTARERLTAQLFAVATAPSARPDPSAELQIDALLGRLGVGGRECFLGVWADVGDDERTLRAVRAALDRSMRGSADSASVICVAGGELLALLAFADSAARERARALLLGEWPPAAGAAALVCVGSGADAVARVPRELAEVRGVREWTRAESGVVDARLHRLERFASTLRDDPEADALVEEVLGPLRRGRPELLATLESFASHWGSKTATAAALGIGRQTLYDRLARIESLIGLLDASPARTRVLLTAVSLHRARAALPPAAPRSTRPFPPPADR
>NZ_CP047180.1|WP_159423636.1|3712528_3712774_-|hypothetical-protein
MHTSSVDPRDVDAEVTTPVYRVYFAETETMVDELRITGARDVLEVVDWAERDARGVPFTVYCEHPSPFNPGKVTLQLLLSR
>NZ_CP047180.1|WP_159423635.1|3711869_3712505_+|isochorismatase-family-protein
MTAPRRALILVDVQLEYFAGPLEIRYPPHATSLPAITAALDAATAAGLPIAAVQHSSGEGAPVFAPGTPGFELHPEIEGRRSDEWKSITKRFGTVFAGTDLLAWLRERDVDTITLVGYMTNNCILASAAEAETHGLTAEVLSDATGAIAISNAAGSVDAETVHTTLLALLNSNFAAVADTEAWTEAVASGEPLPQSDLGSSAVAGVALPPR
>NZ_CP047180.1|WP_123445325.1|3711399_3711786_+|DUF1772-domain-containing-protein
MPGLSRTDDRAFVSAMTAINAAVQNPLFALSFVGSGLSSAAALVAALAGGAGAATTSAVAGALALAVLQYVVTFGRSIPLNLRLDRAAGGPLSDARRGFERAWVRANTARVLASGGSLLLLGIALATT
>NZ_CP047180.1|WP_123444647.1|3710651_3710861_+|hypothetical-protein
MSDTQNGPVMDGAEDASNDDKLSGLIEQVDHDHGDEGAGAMADALRDRADETDTEITSSDETETRTETE
>NZ_CP047180.1|WP_159423634.1|3708628_3710494_+|hypothetical-protein
MIPRSTPSRRPAGRLRRFLAATAAAAVVTAGLVGAAALPAQAAESAQTGAGRYVVTVDSKAVSTTLASALGLSLDASYGGGVSGFTATLTARQHAILAADSRVLGLSPADQVVEGQAQTMPSHVLTAEADKAPVTAGDGVTNWTGPAVAVIDSGVSAHPDYNLAKQVNCFGSGTAEDANGHGTGVSGYMTALDNGSGTVGIAPGAPVYSVRALDANNKGSISTLMCALDWVSQNAATYNIKVVNMSLATNGVDDNNCGRTNGDTIHQAVCDLVAKGVTVVSAAGNSAADLSAYIPAAYDEVLAVTNFANYDGKPGSLAAVPCSNVTTKDDNYTLNSNFASTADAGHTIAAPGTCPYTTKKGNTYAYIQTGTSMSTAAASGVVLDCLAAGGSCVGKSPAQVIAQVIAQAKSATVDRGRTFAGDPTRPVSGRYYGYGVSTIPVGTVVTPTPTATPTPTATPTATATPTATPTPTATPTATATPKPTATPTATPTATATPTPTATATPKPTATPTATATPTPTPTSGADTVKPQAKIVSPASQTTVTGTVTLVANASDNVAVTSLAFWSGSTKLGDGVKQADGSWSLTANSKNWPNATYAVVARATDAAGNVGSSASITLVIKN
>NZ_CP047180.1|WP_123444648.1|3707130_3708285_+|glycosyltransferase-family-4-protein
MIPGGTRTLRGRLRTRVRGLLSGEDARSRRLRVEAEPAFRTRYANPYNARLYTAMTAEGVLVRDLSWLRLLVAKVDVVHLHWPDLTFLSGVRRYRIVARLVFFFAFLRVARLRGTRLIWTAHNVTSHEERGTPFLRNWYRRLLTENLDAIVCLSEEGVTAMRRSYPELAAVPAFVTPHGHYRHDYDFSATRAEARAELGLDPDARLVVSVGQIRPYKNVPTLIERFREREDDGTLLAVAGNPARGPLRGVIEEAAAGDARIRLELSFLSDERMALWLRASDLVVLPYSAIQNSGSAILAVSADRPVLVPDLGAMHELAALVGPDWVRLYDGAFDTAALDGALAWLDERAVAADASADLSALEWDAIARATIDVYRRVLRAPRPR
>NZ_CP047180.1|WP_159423633.1|3706141_3707134_+|glycosyltransferase
MDTSLAIVVVSYNTREKTLACLASIPLGDAPTPPHVIVVDNGSEDGSAEAIRAAHPEATVIEAGDNLGFARGVNRGVAAATERFVLLLNPDTLVLEGSFRALLEFAVANPRYGVYGGRTLRPDGSVDPSSCWGAPSLWSLLTYATMLSTAFRGNPLLDPESLGGWQRDSVREVPIITGCLLLMPREEYERVGRLDERFFLYGEDAEFSIRARRAGLRPVIVPTAVIVHDVGASTRDAATAGNSGRKMCMVMAGKATMIRLAWKPLPARIGIALLQAGALVRTVLETATRRKRRAWTEVWQRRADWRVGYPEAERTLFGRVPGTGAAEVTR
>NZ_CP047180.1|WP_123444641.1|3718326_3719583_-|hypothetical-protein
MLGGLRKRTAPLLKSPAVLSLGARGVFLDAPRLRSARRSGGARGASGAQGRAILIAPPGAGNIGDAALVGAFLENVAGPITVITRYKGDFRIPAEQADRVEIVSLGTLLYGGLPSFVRDLRRFRAMLPGAASVSIVGADIMDGAYNFRASTSRALVARSAASAGVDTRVLGFSWNGKAHPGALAQLRDADRAGTTLFLRDPLSVERARRDGLDAKASADIVFSARSVDQGRASTELAALDTTGGIAIVNVSGLIDTDQTGAYVEIIGGLRARGLAVVLLPHVIKHGPDDLAACRKVFAALPDTTGVAFVEDVLTPAEVRGFTERATVTVTGRMHLAIMSLMKGVPAITLATQGKVEGLMAMFELPYLCVEPGAGLAGRVGDALERVLSDRESVSAAILAKLPAVQELSAANFAGLPRA
>NZ_CP047180.1|WP_159423639.1|3719888_3721538_+|hypothetical-protein
MTRTLSATLAALLVVIAAFFAAAPSFAAANRYASPNGTGTACSAAAPCALTTAVQNAAAGDTVLLTAGTYPTTTLKGGKATVAAPVVVQPAPGASPVLGSTKVYTPNTVWNDIFSKSTFYTYGSGITVNRMHIDGAGIFVRSANVVVRDSLFENGSSMDGIQVGGTDNGLIENNLVRNFDQNIDNGLHADCIQVFESNDVTLRGNTLMNCYNAGIIFSPGGGDGMTDITVESNFVSGCIVITSDCRGGSSADFREASADGIHIRNNTFESGALRVGGAKNTVFDRNIVSYLSSCTSPMTNTIVENWNTKLCKTPSLLNQQGNVQGAPALASAATGDLHVLSATGTQIAGWGSTTSARTDIDGQVMGSRTAGADQFGGVTAPSPTATPTATPTATATPTATPTATPTATPTATPTATATPTATPTPTATPTPTATPTPTATPTATPTPTATPAPVDRTAPTVAIVSPGSGSSVTGVVSLMATAADDTAVTGVTYWVGTTKLGDAVKASDGNWYLTVNTAVFPKGTYSVTAKAVDEAGNATTSAPILLKRV
>NZ_CP047180.1|WP_159423640.1|3721655_3722525_-|SIP-domain-containing-protein
MTDATTPAAPSERRARPPRPQLVLTVLRTERLTEHFVRVHLGGEGFDAFVEAADPDRLAATDRYVKLLLAPPGVALEPPHDLDALRARLAPEELPVRRTYTIRSVDLEARSLAIDFVLHGDEGVAGPWAASARPGDRLEMSAPGGAWAPRADAANLLLGDESALPAIAAALEAMPAQARGIALIEVHGAEDELPLTVPAGVEVRWLHRGDEEAGQALTAAVAELTRPDGAVEVFAHGERTAMKRLRAILQDDWGVERAALSLSAYWALGRAEDRFQAEKREPVGAIFAD
>NZ_CP047180.1|WP_159423641.1|3723067_3724138_+|DUF418-domain-containing-protein
MDATTTVPRAAPLAPRLQPDRVLVPDVLRGVAIVAMLIAHAMPLLPSLRDGAAGFAAGNINDLASPLFALVMGMSAALVLARPGASGGRVVVQNLIRGAVLVALGVWLGGWGSWIAIVLPHLGLTLALGTPILLLRSRLVAIVAAVVLVAGAPLNALVAASVDPAVLYARTPVGYLLQWSFVDPHYRLTNLLPFLLLGALLLRHGFRRDRLLAVLALVAVLAYPVRPALERLIGLQSVSGSHPDTLHDLGLVLAAYVAVVLLATVRGRPASTVIAAVLTPFRAVGSLALSVYVLQVAVVAAFATQGLGYVADTPGAALLLVLGVWAVAVLWWRFVGIGPLEWLIGRLTRLVPAPRR
>NZ_CP047180.1|WP_159424161.1|3725008_3725626_-|sigma-70-family-RNA-polymerase-sigma-factor
MTQPDPRPAPVPAAGPAVPPLDPPPLDPPPLDPAPGDPAPLDLTAAFDEHGSALLGFAVNALRDRGLAEDCVQETFLRAWRSRERYSAERASPRTWLFAIARNVIVDAHRSLQRLPRIVPAEMLDDVPGDDVDPLEPLMMVEALARLSPEHRQVVVAIHLRGESYAEVSAATGVAVATLRTRTFYALKALRTHLAAPDPTPEDRS
>NZ_CP047180.1|WP_159423642.1|3725931_3726519_-|hypothetical-protein
MASEQDGPPRFADPRRLGAVVGLAGAFVFAFSYSPAEPVAIVARVLVGATVAAALWFLFVRPRPLGPFAPPRPARLAVYGACVVAEFALIAVGSRVLESAGRGELRPALIALVVGLHFLPFAWAFSERMFALLGGALVVLGGLGLLVGSGDAAVLAAVASGAAMALLLLAYALGAFAPGSRAPRSRAPRSRPRRS
>NZ_CP047180.1|WP_159423643.1|3726647_3727181_+|hypothetical-protein
MTEIHHSAAASSASSGSSASRGLSRRALTAAAWTVPVVAVAVATPAAAASTADIGAFVLAGSCGNAGITGPGFTLRAGSGDVPVGTTIVIVGSRVSSIGTFTATSDIVTISSPSSTARLVTFIGPLPAGAFLGLRTTLSLTTAFVLTATLTLPEGSVGSGAKSTASVSSDRVFCSVS
>NZ_CP047180.1|WP_159423644.1|3727215_3727890_-|hypothetical-protein
MQDLDPETMGALLAAQHTANQREWPFFVIAAGLPDLPRVLTETRSYAERLFNYRRIGTLAPTDAAQALREPAERLGAEYATDALTTLLEAAGGYPYFLQEYGHAAWNLAADRLIDRSDAIAAVQYGTEQLDAGFFRSRWQRATRSERRMLLAMAADGEGPCSTALVAQRMGLQTSSVGPYRAALISKGLVYSPEHGQIAFTVPGMAGYVERNREELDDARRSVT
>NZ_CP047180.1|WP_159423645.1|3728067_3728565_-|hypothetical-protein
MPDPTAPAAPLARRTLVGAAWAAPVVALAVSAPTAAASGTLPPLGARADGPAEYRPSSSTEYRVFVTNTGSTPLEGGSVIAVLQDPGDGYVFDGYNGQQWSYAYGFPEGRIALRYDPALAPGEESVVLFLLIANTDRTQSPVPVADLVITAPGFDVTVLSLSVPY
>NZ_CP047180.1|WP_159423646.1|3728649_3729840_-|arsenic-resistance-protein
MEGPLLDRRERGVSSARPAPRAEPLALACAPPTAVPPPVSALVARLERRQVAVYLGAIAAGAVLGLLLPAARHLEGAIEPVLGLLLFATFLGVPFAALGRALRDVRFLAAVGVLNFVVVPVVAYGLSRFVAESPALLFGVLLVLLTPCIDYVIVFAGLAGGASDRLLAAAPLLMLAQLLLLPLYLLLFLGPESVAVVEVAPFARALLLLIVLPLTAAALVQALGRWHRAGRFVESTMLGLMVPLMAATLLVVVASQIGAVGAAAGRLLVLVPLYAAFLAVMVAAGLGVARLFRLDVPSSRALVFSGATRNSLVVLPLALALPAPLALAPVVVVTQTLVELIGMVVLVRLLPRLVRHAPTPDAPTPDAPTPDAPTPDAPTPDAPTPDAPTPDTPTPE

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP047180_2	2.1\|302753\|47\|NZ_CP047180\|PILER-CR	302753-302799	47	NZ_CP047180.1	302936-302982	2	0.957

1. spacer 2.1|302753|47|NZ_CP047180|PILER-CR matches to position: 302936-302982, mismatch: 2, identity: 0.957

cgtgtcgcgtaccgaaccggcatctcgcggactgccgccggggctcg	CRISPR spacer
cgtgtcgcgtaccgaactggcatctcgcggactgccgccggagctcg	Protospacer
*****************.***********************.*****

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP047180_13	13.1\|3711060\|26\|NZ_CP047180\|CRISPRCasFinder	3711060-3711085	26	KY676784	Streptomyces phage ToastyFinz, complete genome	37590-37615	5	0.808
NZ_CP047180_13	13.1\|3711060\|26\|NZ_CP047180\|CRISPRCasFinder	3711060-3711085	26	KY092484	Streptomyces phage Raleigh, complete genome	38929-38954	5	0.808
NZ_CP047180_7	7.1\|1792318\|32\|NZ_CP047180\|CRISPRCasFinder	1792318-1792349	32	NZ_CP024583	Roseomonas sp. FDAARGOS_362 plasmid unnamed2, complete sequence	88174-88205	7	0.781
NZ_CP047180_7	7.1\|1792318\|32\|NZ_CP047180\|CRISPRCasFinder	1792318-1792349	32	FR687252	Pantoea phage LIMElight complete genome	27706-27737	8	0.75
NZ_CP047180_7	7.1\|1792318\|32\|NZ_CP047180\|CRISPRCasFinder	1792318-1792349	32	NC_019454	Pantoea phage LIMElight, complete genome	27706-27737	8	0.75

1. spacer 13.1|3711060|26|NZ_CP047180|CRISPRCasFinder matches to KY676784 (Streptomyces phage ToastyFinz, complete genome) position: , mismatch: 5, identity: 0.808

gccaccctcgcccgagggcggtccat	CRISPR spacer
cccgccctcgcccgagggcgggcccc	Protospacer
 **.***************** ** .

2. spacer 13.1|3711060|26|NZ_CP047180|CRISPRCasFinder matches to KY092484 (Streptomyces phage Raleigh, complete genome) position: , mismatch: 5, identity: 0.808

gccaccctcgcccgagggcggtccat	CRISPR spacer
cccgccctcgcccgagggcgggcccg	Protospacer
 **.***************** **

3. spacer 7.1|1792318|32|NZ_CP047180|CRISPRCasFinder matches to NZ_CP024583 (Roseomonas sp. FDAARGOS_362 plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.781

gagcgcgcgtatcgagatacaccagcatgtga	CRISPR spacer
gcccgcgcgcatcgagatacaccaccacgagg	Protospacer
*  ******.************** **.* *.

4. spacer 7.1|1792318|32|NZ_CP047180|CRISPRCasFinder matches to FR687252 (Pantoea phage LIMElight complete genome) position: , mismatch: 8, identity: 0.75

gagcgcgcgtatcgagatacaccagcatgtga	CRISPR spacer
ggctgcgggtatcgaggtacaccagcaggaca	Protospacer
*. .*** ********.********** *  *

5. spacer 7.1|1792318|32|NZ_CP047180|CRISPRCasFinder matches to NC_019454 (Pantoea phage LIMElight, complete genome) position: , mismatch: 8, identity: 0.75

gagcgcgcgtatcgagatacaccagcatgtga	CRISPR spacer
ggctgcgggtatcgaggtacaccagcaggaca	Protospacer
*. .*** ********.********** *  *

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site	Prophage annotation

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP047181

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CRISPR-Cas detection and classification

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NZ_CP047180

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection