CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP023777	Chitinophaga caeni strain 13 chromosome, complete genome	11 crisprs	csa3,WYL,cas9,cas1,cas2,DEDDh,cas3,RT,PD-DExK	0	17	3	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP023777_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_1

320422-320524

Orphan

VI-B2

Consensus_repeat	Method
GTTGTTTTTACCCTTCAAAATTAGAGCAGTCACAACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023777_1

>merge|NZ_CP023777|1|320422-320524|CRISPRCasFinder
GTTGTTTTTACCCTTCAAAATTAGAGCAGTCACAACGGAAAGCTAATTGACTGGATGGATTTCATCGTTGTTTTTACCTTTCAAAATTAGAGCAGTCACAACG

>NZ_CP023777|1|1|320422-320524|CRISPRCasFinder
GTTGTTTTTACCCTTCAAAATTAGAGCAGTCACAACG	GAAAGCTAATTGACTGGATGGATTTCATC
GTTGTTTTTACCTTTCAAAATTAGAGCAGTCACAACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098192283.1\|303972_305076_+\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP023777.1\|WP_098192300.1\|330159_330813_-\|biopolymer-transporter-ExbD	unknown	unknown	gnl\|CDD\|376792
NZ_CP023777.1\|WP_098196054.1\|309459_312558_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP023777.1\|WP_098192288.1\|313918_315337_+\|serine-hydrolase	unknown	unknown	gnl\|CDD\|365903
NZ_CP023777.1\|WP_157760581.1\|312659_313226_-\|ATP/GTP-binding-protein	unknown	unknown	gnl\|CDD\|366285
NZ_CP023777.1\|WP_098192291.1\|320878_321974_-\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|372671
NZ_CP023777.1\|WP_098196053.1\|306077_306530_-\|YqgE/AlgH-family-protein	unknown	unknown	gnl\|CDD\|376864
NZ_CP023777.1\|WP_157760582.1\|323102_323861_+\|DUF2971-domain-containing-protein	unknown	unknown	gnl\|CDD\|378585
NZ_CP023777.1\|WP_098192284.1\|305108_305957_-\|3-methyl-2-oxobutanoate-hydroxymethyltransferase	unknown	unknown	gnl\|CDD\|376814
NZ_CP023777.1\|WP_098192294.1\|324071_325490_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_157760583.1\|325582_325819_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098192285.1\|306622_307570_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098192292.1\|322297_323062_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098192289.1\|315423_318597_-\|PDZ-domain-containing-protein	unknown	unknown	gnl\|CDD\|143478
NZ_CP023777.1\|WP_098192286.1\|307601_309404_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_CP023777.1\|WP_098192299.1\|329515_330103_-\|biopolymer-transporter-ExbD	unknown	unknown	gnl\|CDD\|376792
NZ_CP023777.1\|WP_098192298.1\|328636_329473_-\|energy-transducer-TonB	unknown	unknown	gnl\|CDD\|367555
NZ_CP023777.1\|WP_098192290.1\|318899_320225_-\|Fic-family-protein	unknown	unknown	gnl\|CDD\|225718
NZ_CP023777.1\|WP_098192297.1\|327136_328525_-\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE	unknown	unknown	gnl\|CDD\|235392
NZ_CP023777.1\|WP_098192296.1\|325884_326904_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376162

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098192283.1\|303972_305076_+\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	1.48429e-37
NZ_CP023777.1\|WP_098192300.1\|330159_330813_-\|biopolymer-transporter-ExbD	gnl\|CDD\|376792	pfam02472, ExbD, Biopolymer transport protein ExbD/TolR. This group of proteins are membrane bound transport proteins essential for ferric ion uptake in bacteria. The Pfam family consists of ExbD, and TolR which are involved in TonB-dependent transport of various receptor bound substrates including colicins.	6.74215e-13
NZ_CP023777.1\|WP_098196054.1\|309459_312558_-\|TonB-dependent-receptor	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_CP023777.1\|WP_098192288.1\|313918_315337_+\|serine-hydrolase	gnl\|CDD\|365903	pfam00144, Beta-lactamase, Beta-lactamase. This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	1.32944e-53
NZ_CP023777.1\|WP_157760581.1\|312659_313226_-\|ATP/GTP-binding-protein	gnl\|CDD\|366285	pfam00754, F5_F8_type_C, F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.	1.17731e-05
NZ_CP023777.1\|WP_098192291.1\|320878_321974_-\|IS3-family-transposase	gnl\|CDD\|372671	pfam13683, rve_3, Integrase core domain.	7.49427e-28
NZ_CP023777.1\|WP_098196053.1\|306077_306530_-\|YqgE/AlgH-family-protein	gnl\|CDD\|376864	pfam02622, DUF179, Uncharacterized ACR, COG1678.	2.57671e-30
NZ_CP023777.1\|WP_157760582.1\|323102_323861_+\|DUF2971-domain-containing-protein	gnl\|CDD\|378585	pfam11185, DUF2971, Protein of unknown function (DUF2971). This bacterial family of proteins has no known function.	1.72205e-08
NZ_CP023777.1\|WP_098192284.1\|305108_305957_-\|3-methyl-2-oxobutanoate-hydroxymethyltransferase	gnl\|CDD\|376814	pfam02548, Pantoate_transf, Ketopantoate hydroxymethyltransferase. Ketopantoate hydroxymethyltransferase (EC:2.1.2.11) is the first enzyme in the pantothenate biosynthesis pathway.	9.67427e-109
NZ_CP023777.1\|WP_098192299.1\|329515_330103_-\|biopolymer-transporter-ExbD	gnl\|CDD\|376792	pfam02472, ExbD, Biopolymer transport protein ExbD/TolR. This group of proteins are membrane bound transport proteins essential for ferric ion uptake in bacteria. The Pfam family consists of ExbD, and TolR which are involved in TonB-dependent transport of various receptor bound substrates including colicins.	2.11534e-20
NZ_CP023777.1\|WP_098192289.1\|315423_318597_-\|PDZ-domain-containing-protein	gnl\|CDD\|143478	cd07562, Peptidase_S41_TRI, Tricorn protease; serine protease family S41. The tricorn protease (TRI), a member of the S41 peptidase family and named for its tricorn-like shape, exists only in some archaea and eubacteria. It has been shown to act as a carboxypeptidase, involved in the degradation of proteasomal products to preferentially yield di- and tripeptides, with subsequent and final degradations to free amino acid residues by tricorn interacting factors, F1, F2 and F3. Tricorn is a hexameric D3-symmetric protease of 720kD, and can self-associate further into a giant icosahedral capsid structure containing twenty copies of the complex. Each tricorn peptidase monomer consists of five structural domains: a six-bladed beta-propeller and a seven-bladed beta-propeller that limit access to the active site, the two domains (C1 and C2) that carry the active site residues, and a PDZ-like domain (proposed to be important for substrate recognition) between the C1 and C2 domains. The active site tetrad residues are distributed between the C1 and C2 domains, with serine and histidine on C1 and serine and glutamate on C2.	3.81357e-66
NZ_CP023777.1\|WP_098192286.1\|307601_309404_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	4.16403e-44
NZ_CP023777.1\|WP_098192298.1\|328636_329473_-\|energy-transducer-TonB	gnl\|CDD\|367555	pfam03544, TonB_C, Gram-negative bacterial TonB protein C-terminal. The TonB_C domain is the well-characterized C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance.	1.4867e-17
NZ_CP023777.1\|WP_098192290.1\|318899_320225_-\|Fic-family-protein	gnl\|CDD\|225718	COG3177, COG3177, Fic family protein [Function unknown].	6.18329e-49
NZ_CP023777.1\|WP_098192297.1\|327136_328525_-\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE	gnl\|CDD\|235392	PRK05291, trmE, tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE.	0
NZ_CP023777.1\|WP_098192296.1\|325884_326904_-\|hypothetical-protein	gnl\|CDD\|376162	pfam18739, HEPN_Apea, Apea-like HEPN. Apea-like HEPN nuclease. In epsilonproteobacteria embedded in R-M operons.	6.08365e-08

>NZ_CP023777.1|WP_098192290.1|318899_320225_-|Fic-family-protein
MRLPERPPLIPKGFDFTKLLTTLAQIGRIDEFNFIASDKYYYYDKWKYRAKEWGIDPKLLWGAVKIYRRFSNKKMAIGGLRELEFFISFPSLVQEYLHEFDMNLGGSLQGEMIIPREDRDRYLISSLMEEAIASSQLEGAATTRKVAKQMLESNRKPKNQAEQMIVNNYNAMQWIVRNKEIPITLSNIKHLHAILTKSTMADVNEEGAFRTDDDVKVVDVQTGTAIYTPPKAEDLDRLMAAFCDFANDRETYGFFLHPIVKAIIIHFLVGYIHPFADGNGRTARTIFYWYLLKHGYWLIEFMSVSRIILSSKAQYSRAYLHTEQDDNDLTYFLNYNLKCIRLALVDLKLYIKKKSEEKQHAMSMLRSTTLNERQIVLVQEVLRTPTAYFTVKQVEIKFGISNQTARNDLNGLVNEGLFEERRLGKKSQYLPVKEFEKKIVS
>NZ_CP023777.1|WP_098192289.1|315423_318597_-|PDZ-domain-containing-protein
MKKFLFLAALLSAFRLSAQTSPVYFLSNPCLTPDGQTVIFSFEGDLWKAPVKSGEATRLTAMQGYETNPRVSPDGKWIAFTGRQFGNGDIFIIPFEGGEIQQLTYHSGNDEVASWSWDSQWIYFNSSRMGQSAGFKVALKGGTPQRVFGDYFFQYDHNLVENPVSGEIFFNDTWESSNQVQRKRYKGPFNPDIQSYNPKTKQYKKYTTWEGKDFGATIDKQGNVYFISDEGNGQYNLYTLDKSGAKKALTRFNASIKTPQVNADGGSIVFEKDYQLWLYDVKAGKERKLNIPIIRNNILPKEKDFDVKSNITAFDVSSDNKKIAFVSRGELFVSDIEGKFVQQINRGSAERVREVKWMSDDKTLLFNQTYKGYTNLYTIAADGKGAMKQLTSDARNNRQIVLNKKRDKAVYLGGRDEVRLLDLETGKSKLLAKEEIWGFQNSDPSFSPGDEYVMFSVYRNFEREIFVHNLKNNKTTNLTKTDITESDPAWSPDGKYIYFTSQLLKPSYPFGMPDAKVYRIALENIDEPFRSDKFEELFKDDKKDESKKDDKKASDTKKDMAKKDEEKDAAGSIVIDTVRIMERLEHIGPNTGTQFFAGVYKKGDKTTVLYISNHGGGRNALWKTVKEPFEDDKTEKIAGTEGGLRSIVDAGDKLYVLLNGSIQKLNLDANKVEPISISNTFRRNLASEFAQMFEEAWAQMEENYYDGNFHGIDWKKTKQYYQQFIPYLNNRADLRVLLNDMLGELNSSHQGFGTFGSDESIDLSNSTMETGIIFENTDPYTVKYVVKRSAADKKGVDIQPGDVLVKVNDEVVDKSMDRYYYFTRPSRDNEINLEFTRAGKPVKVKLHPQGSLYANLYDEWIDHNQQRVDEKSKGRIAYGYMKNMGQGELAEFIMDMTRELNNKDALIFDLRYNTGGNVHDEVLKFLSQRAYLRWKYRDGSFALQPNFSPADKPIVLLINEQSLSDAEMTSQGFKALKLGKIIGNGTYRWIIFTSGVGLVDNSSVRMPAWGCYSLEGNDLESTGVEPDIKVINTFEDKLNGRDPQLDRAIDEILKQLR
>NZ_CP023777.1|WP_098192288.1|313918_315337_+|serine-hydrolase
MNNYLFSISIVMLCNIFLPAKSQHIKPDNQHNIQFNNKYYRLDSLYSELYKYDEFNGNVLIAEHGKIIFNKQYGIANKSDLSPLTGQSSFYLASVTKQFTAYAMLLLEKMHLLSFNDELSKFLPELGFYKGVTINQLIHHTSGIPDYVGLFDKDWPNGKTVSNTDVIKRLAKMKPQALFAPNEKWQYSNTGYLLLAAIVEKVSGQSFSQFLAEHIFTPLKMDQTGVLSPYTDNSAHPAIAWPFLEDASDRDYVKKFDSIYGPGRIYSTVNDLFLWDRALNNPGWISPAEKKLLYTNWQLNGGKSTNYGYGWFLEKDSTYGQIVYHGGSWPGYLTLLERHLRDDKTIIILQNDAKGTGKRRLPKQETQKILYDLPLESTVRLPDSTLQKYTGTYISEKGKTSEIVLLHRSIWIQFSPTTRFELMPATETKFIVNGFYPEVSYNFILADDGSVEKCRILQPEEGVDRITVKKKP
>NZ_CP023777.1|WP_157760581.1|312659_313226_-|ATP/GTP-binding-protein
MLKSTKIRTVFLLGLLLLGLASCDKKTERTYDLLPPSPEEEKDMTDVGDLFVNIENSGGDAANEGSKKVVDGAADTKFLTNPFIDTMWMELNLIASQRIDAYTLTSANDAESRDPMQWTLKASTDRENWVELDHRENELFSARFEKRRFEFENPEKYKYYRLYIEKVNGSSLFQLAEWRIISRPEDAE
>NZ_CP023777.1|WP_098196054.1|309459_312558_-|TonB-dependent-receptor
MKKFIVMNTLLLVGLLITTNILAQQGAGTIKITGTVKDELNAPMPGVTIINLATKAGTFTKDDGTFEIEAKRGDSLSARMIGYQSFNVVINNVIHFDIKLEAANNSLNEVVVVGFGEQKKISLVGAQSSVKVEDIQTPVANLSAALAGRIAGLVGVQRSGLPGSNSADLWIRGISTFNGSGNSASPLIVVDGVQGRDINSFDPEDIASFTILKDAAATAVYGVAGANGVILITTKQGKPGKVNLMFNYNQGITSFTKTPDLVDGVTYMLLRNEAQKNSGMTPEYSNNYINNTIKQEDPYLYPDVDWMDALFGSTAMNRRANFSARGGSDIANFYTSLAYYEEESLLRTDALQSYDASTKFRRYNFTSNVSMNWTKTTKFDLGIQGYVTQTNYPGVNPEDAFANVMQTNPVLYPTMYPGGYVPGVSTEGAQPNPYAQITQSGYQNLFGNQIYSNARLTQDLNSIVPGLTATAMYSFDVNNTHNISRTRTRSQYLLNRVIPYFDDGTMNLKLIKEGIDNLNYSRSNSGRRSNYFEAGLNYQHDFGPDHKITGMVLYNQRELVEAFASNVTSSLPYRRVGIAARGTYAYKDKYFFEADLGYNGSENFIPSRRFGTFPALGIGWVISNEKFFEPLKNTVSFLKLRYSDGVVGDGSGGNRRFGYLTLVDTDADGFSFGSRGGAVQKSYGGTVISSYGTDVTWAKSHKRDLGLEFNLFKDRFTVVTDIFTERREGVFLQRSLPGYLGLNSMPWGNLGIIENKGIDGTVTLNPVQIAKDLFIDFRGTFSYNRDKVIENDEPIPPYDYMDRRGVNYLSTFGYVAEKLFENQDEIDKSPDQSALGNTRPGDIKYKDLNGDGVIDPYDRTRIGNGDVPTTIYGFGFNLTYKGFYVGAFLQGISGADRVISGDGVIPFNNSTGPERSNLFWQAEDRWTEENPNPQAFYPRLGYGSSANKMNSYTSSWWVKDIDFIRLKTIDFGYNVPKKFANRLKMKNARVYLQGVNLFYWSKFKLWDPELNTGNGTKYPNVRTVSLGVQANF
>NZ_CP023777.1|WP_098192286.1|307601_309404_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKIFIIFTVALVTGITSCSKYLDQVPDDVITIEDIFKSKVNIDKFLANIYASLPNENTERYTNVQHSGVFTGAADEAVYNWSFPYSTQLNSSTWAKTDGNIASWWNDYYKAIRNASYFLQEIEAVPINQAGKLTQEEKNSYKAEARALRAMFYYFLVRTYGPVPIVGETPLDLNTPLSDLQLKRDHIDTCINYIVSELDAAAEVLSTAPLNGEIGRITKGACKAFKVEALLLAASPLWNGNTDYADFKNVDGTDLVNTTYSEAKWQRAATAAKEFINEFDGPVYNLFTIDDADPFKAAYLSCRELHLRDWNAEWIFARARSGQYQRYDRTPRHIGASADFQGGGALGATQTQVDAYFMANGLPITDPASGYQNSGFTSFKAPYDPSSRSTYNQWINREPRFYADITYNNSFWWYSSNVITNMEYDGNSGRKQSTSDVSPTGYIPRKAVQGSGFDWGALYIRLGTIYLDYVEALNEADPTNPDILTYLNAIRHRAGIPGYGEGIVPVPAGKEAMRAAIRAERRVELAFERVRFFDTRRWKIAENTNNAPIMGMNMNANGEDFYTPTIIQQRVFRKDRDYLFPIPNDETLLNLNLAQNPGW
>NZ_CP023777.1|WP_098192285.1|306622_307570_-|hypothetical-protein
MRIILLGLGLFAAVSTSCSKTNSKHVDLGGGSNPGVDSSAPAATWQEHWFEHKQLVKNVAYTEEVALYYDDDMDRTVTWPLRKAEEIWKYTKKTYAPFKGEDKRLNVILHYGKYGGGHPYGYFDASHDNRTGVDIGSNNSWKDSSGWNLDVITHEIGHIVEGAFKGVKESPAFDIWGDSKWMEIYIYDVYKGLGWDAEAERCYNSTINGSDNFPRPGTQWFKNWFYPIYDQYGGATVLNNFFTLLSEHFPQKKHNYGMEYTRRMNMGEFVHFWSGAANADLKDLAIAAFGTKDRNGGDWTIQLENAKKDFPGITY
>NZ_CP023777.1|WP_098196053.1|306077_306530_-|YqgE/AlgH-family-protein
MDTGKYIESTALLKGTFFENTRIIITEYNQEGAMGFVFNKLFPRKFNELAEFADCPPFPLYDGGPVDREHLYFIHRRPDLIEGGIKISAGIYYGGDFATAVACMKNGDLREDDIKLFIGYCGWNWKEIDGELAEGSWKPLEGVNLLQVIL
>NZ_CP023777.1|WP_098192284.1|305108_305957_-|3-methyl-2-oxobutanoate-hydroxymethyltransferase
MKKTISYLHAKKHNRQKISVLTSYDYPTTKILEEVGVDMIILGDSVGTNMLGYQDETEVTLEDMIHHTKAVCRAIENIFLVTDLPYNTYQTPGMAVENARKITAAGADAVKFEGGRIDILQALKSEGILVMCHLGLNPQHDQDRMRSGKISKGKQFSEAIELIQAAKNLESAGADLLILEKIPGKLAKIITGNVNIPTIGIGAGKDCDGQVLIIHDLLGLNDKKYKHAPRYFDMKSMVKDVIGRYQDEVAEGIFPALEHTNIIKESELSLVQAWCMEHEMDI
>NZ_CP023777.1|WP_098192283.1|303972_305076_+|Gfo/Idh/MocA-family-oxidoreductase
MRLIIFFLFCNFSLQPIFAQQQKMRVAVAGTSHGHAAFIFGRPSKGDLEIVGIYEPDTAVAKLRMRQFKLPAELFYTDLDKMLDATKPTAVLAFGSTFEHRKVVEAAAPRHMHIMVEKPLATTLEDARYMHMLAKKNKVYLLTDYETSWYPSVAKTFELIEDSSFTGQPRKIFVNDGHKGPKEIGCGPEFLDWLTDPVLNGGGALMDFGCYGANLMTRLAHNRLPISVTAVTRQFKPDVYPKVDDDATILLDYGDMQCTINASWNWTFNRKDMEIYGDKAYIKALDKNTLVRKSGERSAAEIQRITDQDIAVYEDPFSYMIDVIKGKQTIQPEDLYATDNNVIVVAILQAARESAKTGKTVYMSAIK
>NZ_CP023777.1|WP_098192291.1|320878_321974_-|IS3-family-transposase
MKKTRFTETQIVSILKQQENGFATKDICREHGISEATFYNWKSKYGGMEASDVKRLKDLEEENSRLKRMYADLSLDNQILKDLFTKKALGPSTKRQVAEELVADQGVSVSRACRIVSFPRSKFYYRSRRNDQVLIDALQDLAFKHTSYGFRKLFAYLRRAGHHWNHKRVYRVYRLLKLNKRKKLKRRVPARIKQPLQQQTNVNIIWSMDFMSDSLTGNKRFRTFNVIDDGSREVLGIEIDTSLSSYRIVRVLEKIIESRGKPAAIRTDNGPEFTSGYFEQWCHQHDIRLQYIQPGRPMQNGYIERFNRLYREAVLDAYIFEDLYQVRELTDAWIEEYNQRRPHESLKNMTPCEWKTELQKSRNSI
>NZ_CP023777.1|WP_098192292.1|322297_323062_+|hypothetical-protein
MSLTFQIEEFLLRKEFKELFVQVIKTDDNDIQEGEHLLDYLLRKGRQDDYNHIIKMNLIVGLLSDICYFTQEALVCSLKQRLTVTFSLLRKPFVYTLIIILRLLFEENFIEKFNNEEGFDPASVSPEDRTALINASIEAIQNNPITADDLNTMIFDKLVANSIINLSEKALHLTTTRSKLFNTEKQNFNFIFSNQESIDSQWEYIYSRLPALLLYVLQVADILVFTSIQVDEGTYEKRLKNRIKIFKKYSGSLG
>NZ_CP023777.1|WP_157760582.1|323102_323861_+|DUF2971-domain-containing-protein
MNEYIIDEEYVYRLNDEKNNIWDIYKNGNKNPKSCKQLYKYYSLNLYSIDALLRNYFYLANPSSFNDPFDCNINLIKDVQNISKYTSVKRNNVRNIGICCLSETLDNHLMWAHYTNNYNGFCLGFRGDNIDANANREIFPRHSFTKVIYPASPVSIEQQLPFAQNYLFTTKFKHWEYEQEWRLIAEITNEREMIFYPESVEAIYIGHSIVDTNPSAYKLLLEIQEIKFPQIPVYVVYPAPFELKLKFEKVWN
>NZ_CP023777.1|WP_098192294.1|324071_325490_-|hypothetical-protein
MNMRKIKYVREEIALIERLVNGTPRYYKIVQNEVDNSAAILKKAFTKGFDAWILTRKLEIKDEVKSKSFTLTRGNNLVIIKDFFVANRSERIRRGLAPLSAIKVNVNEMRGSKEHSSTAFFKTFIPISKDFKWHSIFDDDVIDLDTGKSVHGLLTVKVDNISLDLYSFKHNSKNYLVLEATTEIDLETFDNYCWSTLIAVAFINGQLWQGDQFYFSYQDMDMKVFDTWSYVRRRNSITSIYPAITSNPHSWMKDSDDADQYNDGSLVNIGSTPLSKLCQWVHDKDMHKSIALLIIESKSASLLLMPAGFAIAIEGLATLFELKEGEKVKPISNKARGVEFVNKLLQVLNDYDDDEHFVGKKILRTNIMQNVNRATNRERLLIPFNLLGIEISQDDRMALDYRNDLLHGNVILEPIVRKKYEMNTTELSMRLMTLANAIIMKNIGYNGRILNHVKLQEQSMERVIQEDHFRKI
>NZ_CP023777.1|WP_157760583.1|325582_325819_-|hypothetical-protein
MRQNVFMVTHIEQCIPGFVDKLKHIETEAYLDVKAAKIPDFRSKQQKVDWRRFEWKPYPTLRNAALLLNIAPLHSAGG
>NZ_CP023777.1|WP_098192296.1|325884_326904_-|hypothetical-protein
MKYYKIIAFCSNRVTGHFKFKDIFQIYPLDTVDAPTSDFVKYYPFVLEFRLSDNGQIELDGELKEVSNIIGELTAEVNFQNRILKLLTAFSNYRFFIPPIEPQWFVHAEGLSKDEMDNQTSAAGLNIYFYPKLKEVVPFTEFTKVDYPQIDTGEHPQCFQHIDLSGKEEVTFSHYLSTALHNYFLLSDEQQAPVDSAIELINQGVALRATTKSLSFIAFVSSIETMVAHETKDVPLEKCAACGQDKYKVMAKFRDYLFEYVADGPDAKKTINEIYGLRSKIAHTGLLLFGDGKIDWTANAEGDKHYDLHLKSSMISRLSLMNLILMRGDKEKKAGGGTV
>NZ_CP023777.1|WP_098192297.1|327136_328525_-|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE
MLGKLANYDDTIVALATAPGIGAIAVIRLSGAEAIEVVDKLFPSKDLTTQKGYTIHFGALTNPVNQQVIDEVLVSLFKGPKSYTGEDTIEISCHGSPYIQQQIIDACVQAGARMAKPGEFTQRAFINGKLDLTQAESVADLIASNTAASHQTAMQQMRGGFSKELRDLREELIKFSALVELELDFSQEDVAFADRTQLYELVSRSGSLVRKLIDSFQMGNVIKNGVSTAIVGKPNAGKSTLLNTLLNENRAIVSEIAGTTRDTIEEILNIQGILYRLIDTAGIRESIDAIESIGVQKSLEKMRSAGLVIYLFDALETTPEALAQQKAELAQANINYLLVANKIDILGEDAAKAKFADTPGIIYISAKNHDHIQQLKDALVTSVMGGKINTEDTIITNARHYAALQSVRKSLEDVRTGMDNDLPGDLLALDIRHCLHYLGEITGEVTNEDRLDFIFSKFCIGK
>NZ_CP023777.1|WP_098192298.1|328636_329473_-|energy-transducer-TonB
MDSAKILKSDFLDILFENRNKEYGAYELRRQYNRRVRNSIIATASFALIIIGGYLISKSLKGNEDVQKKKPVIEDIKLEDVKLPDDPKTPPPPPPPPAPPPAVKPTVKFTPPVIKKDEEVPAEEEPPKVEEIKDQAIGTKTVEGDPNGIDPGLLSDSKGTGVVEAPPPPPKEQIFTFVENPPTFPGGEEALQKYLRKNVRYPHMASENGISGTVFVTFVVDSEGKIKDVKTVGAKKGGGLEEEAVRVVKGMPDWKPGKQNGRNVSVQFNLPIRFTLQE
>NZ_CP023777.1|WP_098192299.1|329515_330103_-|biopolymer-transporter-ExbD
MAEMDTSSSGGGKKHGGTKSKKLSTRVDMTPMVDLGFLLITFFMLTTTMSKPKTMDLALPKDTKDEAEQNKVKESTALTILLGKDHKVYYYEGLAQDPEASADPNFFNVSSFANKGGIRDVIIKKRDEVSQKRNAKGEPEDVVVIIKPDDESTYKDFVDILDEMAINRIQRYATVDISDQDKEWIKSTEAANSAQ
>NZ_CP023777.1|WP_098192300.1|330159_330813_-|biopolymer-transporter-ExbD
MPKVKMPRKSTNIDMTAMCDVAFLLLTFFMLATKFKPDEPVTVVTPSSINTQLLPDSDVILITVDEKGRVFFSMDGQPKRRELLTNLNDNFNLGLGKQEIDNFAIGSSIGTDFKSLKTVLDMTPAERKDSQVETGIPTDSTDNQLAIWIEYARSAQGNNRNLKYCIKADNKTPYPKIEAVLSTFKEKGIQKLNLVTDLEGIPPGTAAAALQEEQLKK

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Crispr_ID: NZ_CP023777_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_2

651441-651538

Orphan

Consensus_repeat	Method
CCACGGTTGTAGCCGCGGTCACGGTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023777_2

>merge|NZ_CP023777|2|651441-651538|CRISPRCasFinder
CCACGGTTGTAGCCGCGGTCACGGTCACCATAACCACCGCCACCATCGCGATCACGGCCATAACCTCCACCTCCACGGTTGTAACCGCGGTCACGGTC

>NZ_CP023777|2|2|651441-651538|CRISPRCasFinder
CCACGGTTGTAGCCGCGGTCACGGTC	ACCATAACCACCGCCACCATCGCGATCACGGCCATAACCTCCACCT
CCACGGTTGTAACCGCGGTCACGGTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098192537.1\|649406_649721_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_CP023777.1\|WP_098192534.1\|646973_647702_+\|DUF2807-domain-containing-protein	unknown	unknown	gnl\|CDD\|371327
NZ_CP023777.1\|WP_098192543.1\|659369_660743_-\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_CP023777.1\|WP_098192531.1\|643836_645690_-\|2-oxoacid:acceptor-oxidoreductase-subunit-alpha	unknown	unknown	gnl\|CDD\|274738
NZ_CP023777.1\|WP_098192540.1\|653342_654131_-\|TIGR00266-family-protein	unknown	unknown	gnl\|CDD\|376704
NZ_CP023777.1\|WP_098192532.1\|646235_646553_+\|carboxypeptidase-regulatory-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|379297
NZ_CP023777.1\|WP_098192536.1\|648375_649380_+\|FecR-family-protein	unknown	unknown	gnl\|CDD\|226235
NZ_CP023777.1\|WP_098192528.1\|640680_641028_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098192544.1\|660758_661367_-\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP023777.1\|WP_098192542.1\|658229_659339_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_CP023777.1\|WP_098192539.1\|651824_653105_-\|kynureninase	unknown	unknown	gnl\|CDD\|130873
NZ_CP023777.1\|WP_098192548.1\|664724_665945_+\|DUF1015-domain-containing-protein	unknown	unknown	gnl\|CDD\|377633
NZ_CP023777.1\|WP_098192538.1\|650002_650566_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098192529.1\|641228_643451_+\|DNA-cytosine-methyltransferase	unknown	unknown	gnl\|CDD\|223348
NZ_CP023777.1\|WP_098192545.1\|661671_662307_+\|DUF502-domain-containing-protein	unknown	unknown	gnl\|CDD\|225480
NZ_CP023777.1\|WP_098192546.1\|662386_663364_+\|S1/P1-Nuclease	unknown	unknown	gnl\|CDD\|211380
NZ_CP023777.1\|WP_098192541.1\|654641_658184_-\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911
NZ_CP023777.1\|WP_098192547.1\|663514_664585_+\|3-phosphoserine/phosphohydroxythreonine-transaminase	unknown	unknown	gnl\|CDD\|235428
NZ_CP023777.1\|WP_098192535.1\|647710_648322_+\|RNA-polymerase-sigma-70-factor	unknown	unknown	gnl\|CDD\|274376
NZ_CP023777.1\|WP_098196073.1\|650653_651199_-\|RNA-2',3'-cyclic-phosphodiesterase	unknown	unknown	gnl\|CDD\|379265

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098192537.1\|649406_649721_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	3.16592e-13
NZ_CP023777.1\|WP_098192534.1\|646973_647702_+\|DUF2807-domain-containing-protein	gnl\|CDD\|371327	pfam10988, DUF2807, Putative auto-transporter adhesin, head GIN domain. This bacterial family of proteins shows structural similarity to other pectin lyase families. Although structures from this family align with acetyl-transferases, there is no conservation of catalytic residues found. It is likely that the function is one of cell-adhesion. In Structure 3jx8, it is interesting to note that the sequence of contains several well defined sequence repeats, centred around GSG motifs defining the tight beta turn between the two sheets of the super-helix; there are 8 such repeats in the C-terminal half of the protein, which could be grouped into 4 repeats of two. It seems likely that this family belongs to the superfamily of trimeric auto-transporter adhesins (TAAs), which are important virulence factors in Gram-negative pathogens. In the case of Parabacteroides distasonis, which is a component of the normal distal human gut microbiota, TAA-like complexes probably modulate adherence to the host (information derived from TOPSAN).	1.12302e-35
NZ_CP023777.1\|WP_098192543.1\|659369_660743_-\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	6.17422e-31
NZ_CP023777.1\|WP_098192546.1\|662386_663364_+\|S1/P1-Nuclease	gnl\|CDD\|211380	cd10981, ZnPC_S1P1, Zinc dependent phospholipase C/S1-P1 nuclease. This model describes both the bacterial and archeal zinc-dependent phospholipase C, a domain found in the alpha toxin of Clostridium perfringens, as well as S1/P1 nucleases, which predominantly act on single-stranded DNA and RNA.	4.79881e-66
NZ_CP023777.1\|WP_098192541.1\|654641_658184_-\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
NZ_CP023777.1\|WP_098192540.1\|653342_654131_-\|TIGR00266-family-protein	gnl\|CDD\|376704	pfam01987, AIM24, Mitochondrial biogenesis AIM24. In eukaryotes, this domain is involved in mitochondrial biogenesis. Its function in prokaryotes in unknown.	1.55407e-84
NZ_CP023777.1\|WP_098192532.1\|646235_646553_+\|carboxypeptidase-regulatory-like-domain-containing-protein	gnl\|CDD\|379297	pfam13620, CarboxypepD_reg, Carboxypeptidase regulatory-like domain.	0.000616489
NZ_CP023777.1\|WP_098192544.1\|660758_661367_-\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	1.877e-14
NZ_CP023777.1\|WP_098192542.1\|658229_659339_-\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	5.11412e-51
NZ_CP023777.1\|WP_098192539.1\|651824_653105_-\|kynureninase	gnl\|CDD\|130873	TIGR01814, kynureninase, kynureninase. This model describes kynureninase, a pyridoxal-phosphate enzyme. Kynurinine is a Trp breakdown product and a precursor for NAD. In Chlamydia psittaci, an obligate intracellular pathogen, kynureninase makes anthranilate, a Trp precursor, from kynurenine. This counters the tryptophan hydrolysis that occurs in the host cell in response to the pathogen. [Energy metabolism, Amino acids and amines].	2.12341e-171
NZ_CP023777.1\|WP_098192548.1\|664724_665945_+\|DUF1015-domain-containing-protein	gnl\|CDD\|377633	pfam06245, DUF1015, Protein of unknown function (DUF1015). Family of proteins with unknown function found in archaea and bacteria.	0
NZ_CP023777.1\|WP_098192531.1\|643836_645690_-\|2-oxoacid:acceptor-oxidoreductase-subunit-alpha	gnl\|CDD\|274738	TIGR03710, OAFO_sf, 2-oxoacid:acceptor oxidoreductase, alpha subunit. This family of proteins contains a C-terminal thiamine diphosphate (TPP) binding domain typical of flavodoxin/ferredoxin oxidoreductases (pfam01855) as well as an N-terminal domain similar to the gamma subunit of the same group of oxidoreductases (pfam01558). The genes represented by this model are always found in association with a neighboring gene for a beta subunit (TIGR02177) which also occurs in a 4-subunit (alpha/beta/gamma/ferredoxin) version of the system. This alpha/gamma plus beta structure was used to define the set of sequences to include in this model. This pair of genes is not consistantly observed in proximity to any electron acceptor genes, but is found next to putative ferredoxins or ferredoxin-domain proteins in Azoarcus sp. EbN1, Bradyrhizobium japonicum USDA 110, Frankia sp. CcI3, Rhodoferax ferrireducens DSM 15236, Rhodopseudomonas palustris BisB5, Os, Sphingomonas wittichii RW1 and Streptomyces clavuligerus. Other potential acceptors are also sporadically observed in close proximity including ferritin-like proteins, reberythrin, peroxiredoxin and a variety of other flavin and iron-sulfur cluster-containing proteins. The phylogenetic distribution of this family encompasses archaea, a number of deeply-branching bacterial clades and only a small number of firmicutes and proteobacteria. The enzyme from Sulfolobus has been characterized with respect to its substrate specificity, which is described as wide, encompassing various 2-oxoacids such as 2-oxoglutarate, 2-oxobutyrate and pyruvate. The enzyme from Hydrogenobacter thermophilus has been shown to have a high specificity towards 2-oxoglutarate and is one of the key enzymes in the reverse TCA cycle in this organism. Furthermore, considering its binding of coenzyme A, it can be reasonably inferred that the product of the reaction is succinyl-CoA. The genes for this enzyme in Prevotella intermedia 17, Persephonella marina EX-H1 and Picrophilus torridus DSM 9790 are in close proximity to a variety of TCA cycle genes. Persephonella marina and P. torridus are believed to encode complete TCA cycles, and none of these contains the lipoate-based 2-oxoglutarate dehydrogenase (E1/E2/E3) system. That system is presumed to be replaced by this one. In fact, the lipoate system is absent in most organisms possessing a member of this family, providing additional circumstantial evidence that many of these enzymes are capable of acting as 2-oxoglutarate dehydrogenases and.	0
NZ_CP023777.1\|WP_098192529.1\|641228_643451_+\|DNA-cytosine-methyltransferase	gnl\|CDD\|223348	COG0270, Dcm, Site-specific DNA methylase [DNA replication, recombination, and repair].	6.05565e-33
NZ_CP023777.1\|WP_098192547.1\|663514_664585_+\|3-phosphoserine/phosphohydroxythreonine-transaminase	gnl\|CDD\|235428	PRK05355, PRK05355, 3-phosphoserine/phosphohydroxythreonine transaminase.	0
NZ_CP023777.1\|WP_098192545.1\|661671_662307_+\|DUF502-domain-containing-protein	gnl\|CDD\|225480	COG2928, COG2928, Uncharacterized conserved protein [Function unknown].	2.56011e-30
NZ_CP023777.1\|WP_098192536.1\|648375_649380_+\|FecR-family-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	2.98196e-30
NZ_CP023777.1\|WP_098192535.1\|647710_648322_+\|RNA-polymerase-sigma-70-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	1.40611e-44
NZ_CP023777.1\|WP_098196073.1\|650653_651199_-\|RNA-2',3'-cyclic-phosphodiesterase	gnl\|CDD\|379265	pfam13563, 2_5_RNA_ligase2, 2'-5' RNA ligase superfamily. This family contains proteins related to pfam02834. These proteins are likely to be enzymes, but they may not share the RNA ligase activity.	4.63847e-31

>NZ_CP023777.1|WP_098196073.1|650653_651199_-|RNA-2',3'-cyclic-phosphodiesterase
MYFIALLPTAEVGKEIIKIKQEFAENYGPVYALKVLPHITLQVPFTADPSLERAFCEELTEFAKDQAPFEVTLNGFGTFPNKQNRVLFINVEKSEEMSALHRQLINYLRKEFGFSTMLARTGFTPHVTVAFKDLTDEQFEKAWPEYENKEYTASFKVNNLYFLRHNGKSWEVLQKCKLGGA
>NZ_CP023777.1|WP_098192538.1|650002_650566_+|hypothetical-protein
MKKYLLALVTLSMMFSCQKNSNVKYSADKTTSVAVALTFDRKENAQRIEEAYKKLNLPESEMEKYIEKMLSIVDYSDAKKAENFVSLNAKLDTIIADNSCNFLRYSELPHMNYIAPAPTMIWDLSQCKYEFIDDAILPTYKCVAGVYIPVGVGTSKLAFIKGHLTPNYSTGISVFNPDTDTKFCMEP
>NZ_CP023777.1|WP_098192537.1|649406_649721_-|helix-turn-helix-transcriptional-regulator
MNYGRTLQRLRKLKGVSQLEVAEHINVSRTTYVNLEKGMGELTLSKIITLAEYYKVNINYFINIILNTDNYTDCLPTKNQEFCDIKNMLEEILLKIHDLNEVNK
>NZ_CP023777.1|WP_098192536.1|648375_649380_+|FecR-family-protein
MMLDNLEHIETLIARQLDGSLTEKEQGELRAWRQADPQNDLAYKELLRTWELAAGETNVPGVDIESQWQRFQGMVDLGSGGGSTPIINIPWYKQSWFKVAAVLIPVVGLALFIWKQPQHDLANNNITVATIDNEIKNVQLPDGSQIELNENSRLTYSTDFGTTAREIQLLGEAFFDVAPQSTQPFTVFAGNSKTVVLGTSFNIKAYQQDSIEIVVTTGKVAFSLKDAPDQPVILTRGNRASMQEITIRKSTNESVAFTQWRDKTFKYQDQSLGDVINDIEKNFGIRVIVEDSTLVEMNFNGTISTSYAVSEILDILTGATNSEYHIIDNIYYIR
>NZ_CP023777.1|WP_098192535.1|647710_648322_+|RNA-polymerase-sigma-70-factor
MKVSESLNPRNVKSSSQPGNLYICNMPGNDQLQVLLKEDERRFMAALFKSYFTPACKTIYRFVQDMSVAEDLAQDVFIKIWNKRAGLGEVYFKAYIQRSAINAALDYLDKKKRRGVHTELEEENMQIPVLPMQGNLRETAAKIDAAVNELPEKCREVFILSRYEELSYKEIASTLNISVKTVENQVMTALKKLRVSLKELISN
>NZ_CP023777.1|WP_098192534.1|646973_647702_+|DUF2807-domain-containing-protein
MMQKAYKKISVYLICFLYILNYSCTRENIFGSGNIKTERRSVSNFESITVEGDLDVWITQDNNRSVKVEAEDNVLKFIETYTSGNTLKIRVRPDIHVKSWITPKVYISNDIYSQLNLAGSGNLYSEDTLQVNALHCELWGSGHIKLAASAEELTSNVQGSGHIDLVGNASDYRSEINGSGSIKALDLSCRNAKIRLNGSGEQVVKVRDYIDIKILGSGIVRYKGNPQKVDTEVLGSGTIVKL
>NZ_CP023777.1|WP_098192532.1|646235_646553_+|carboxypeptidase-regulatory-like-domain-containing-protein
MKRIKTSMLALAAIAIGTFAFKAIEGGSIGGTVTPGDAATEAWAVSATDTLKTAVTNGAFSFQNAAAGTYTVVIDAKEPYKDATINDVKVEDGKATDLGEIKLSE
>NZ_CP023777.1|WP_098192531.1|643836_645690_-|2-oxoacid:acceptor-oxidoreductase-subunit-alpha
MPNTTIEQLEDVVIKFAGDSGDGMQLTGSQFTNNTALVGNDLSTFPDFPAEIRAPQGTLAGVSGFQLHFSSNRIFTPGDACDVLVAMNAAALKANLKGLKKGGIIIANSDGFDSKNLRLANYPDGINPLEDGSLVDYQLHTIDVTKMTREALKETTLGMKEKDRAKNMFVLGFIYWLYNRDMSSTEDFLKEKFGKKPEILESNLKVLHAGYHFGETVEAFATRYKVEKARMEPGTYRSITGNVALAYGLIAAAQKAQLPIFLGTYPITPASDILHELSRHKNFGVRTFQAEDEIAGITSAIGAAYGGHLGVTTTSGPGMALKGEAMGLAVMLEIPLVIVNIQRGGPSTGLPTKTEQSDLLQAYYGRNGECPMPIIAASTPSDCFSAIYEASRIAVQHMTPVIFLSDGYIANGAEPWRFPQSSDLAPIEVKFKKGLDEGEEVFFPYQRDENLVRPWAIPGTAGLEHRIGGLEKQNITGNVSYDPENHEVMVKIRQEKVDKIADFLPLQKIELGPEKGKVLVLGWGSTFGAIKSAVLELLSEGHEVAHAHLRHLRPFPKNLAEILSNYEHILVPEINNGQLIKIIRDQFLVDAKGYNKIMGVPITKSELAVKIREILAQ
>NZ_CP023777.1|WP_098192529.1|641228_643451_+|DNA-cytosine-methyltransferase
MSVKFYLDKADKRDCAPIHLVLRHKSVQIKVATGEKVHKSEWDPQSQLVDEKHPHHKEINRYLFFLKEQVIHFMDTAAPAQLTEKKLKVKILSFVKGRKANNDKTILPATSDFEKGKQKFTFLDLFAGAGGFSEGFLQAQFKDKIFDFLLASDINENCELTHLARYNYQLGLDVAFLRQDISEPGFLDNLVKSLDGKTVDVVCGGPPCQSFSLAGKRSKFDKKDELFAHYLKVIRQLRPKYFVMENVKGILTKERGKIKEMILQEIRSIIDLNDFHILLDFIKRLGKQTKKSTFLLNCYLDRLQFETAIDKELDELKSKYILLVEKKFKQLTPKIVSYKESKTSIHINTIRHGFKLLERSRELTALKKRVIHEKSSSDLDNDLFVGDFNAFLTAIDPGYIIERIQKAFQFLSPSKEYKADVDELLASLKIYTTTFDDCMQGLKPYVKEAKASREFEQILNQIRLYNIEEPFVAHAADYGVPQNRERVLFIGCRKDQSPVKEVPPTVSAKERVTVFEALHDLDFINMGEEKFQYEEVDLKAKYNGSSKVMAALLKKRDLDGSMNAKSGLSYSDWSKKGRLSGRFPHAKHPFFVKHATELSNIQSHFVAPLLNHKTSKQNSSVVKRLEVILQEGDYDLAKKRLRTEGLASDKRSYNVLKPNQQSPTVVTIPDDYIHYASPRALTVREMARLQSFDDSFVFQGKRATGGIKRKMEVPQFTLVGNAVPPLLARAVAQEILKHIH
>NZ_CP023777.1|WP_098192528.1|640680_641028_-|hypothetical-protein
MPDTNNGGAFIDSLRRNNAKIREDRAIAIAEDAQLIYKRETEDLSLMIKKLKREQENMLDMSPTDANSLVLASDFDAKSFVSKDLELAVKIRNLEIKLELAVRRYQHLFGGNLNL
>NZ_CP023777.1|WP_098192539.1|651824_653105_-|kynureninase
MNLFEASLSFARELDGQDELRNFRDEFYFPERDGKDAIYFCGNSLGLQPKGVEAAIAQELADWRQHAVEGYWNAKNPWLFYQTALREPLAKIMGSRETEISVMNTLTVNLHFMMLSFYKPTKSRFKVLMEEGAFPSDQYAVETQVKMHGFDPEEAIVEIKPRPGEHLLRSEDILQIINEHNDTIAVILLGGINYYTGQLYNLAEITKAAHQVGAIAGFDLAHVAGNVPMQLHEWQVDFAVWCSYKYLNSGPGAVGGAFVHEKHAANRGYPRLGGWWGNEESTRFKMEKGFIPKATAEGWQMSTAQVMNMVSLKASLELFDTAGIHNLRAKSIQLTNYLEFLLAQVKGLNFEIITPKDCNERGAQLSLRFNEKGKEIHQQLTNAGIIVDWREPGVIRVAPTPMYNSYEDVFHFYEIIENIASKRLIK
>NZ_CP023777.1|WP_098192540.1|653342_654131_-|TIGR00266-family-protein
MPQNHEIDYRIFGEEMQIVEIELDPQETVIAESGSFMMMNQEIQMQTMFGDGSQQNQGFFGKLMSAGKRLLTGESLFITAFTNSGYGKKNVSFAAPYPGKIIPLNLQLLGGKVICQKDAFLCAAKGVSIGIEFQRRLGTGIFGGEGFIMQKLEGDGLAFVHAGGMVIEKELMPGEVLKIDTGCIVAYTQNIDFDIEFIRGIKNMVFGGEGLFFAVLRGPGKVWIQSLPISRLASRIVSMSGPGGRKEEGSILGGLGNLLDGD
>NZ_CP023777.1|WP_098192541.1|654641_658184_-|efflux-RND-transporter-permease-subunit
MKDTNKEFKPTSWSIDNKVSIYIATIIISLAGILSYMKLPKEQFPEVVFPQFIISTYYEGTAPEDIETLITKPIEKKLNAISGVKTIKSNSVQDYSMITIEFNANEDIEAARQQVREKVDEAKPDLPNDMKVAPEVIKIDVSQMPIMNVNLSGDFDLQTLKRYADEMQDRIEALNEITRVDIVGALDREIQVNLDKYKMDAARISFDDVAMAISAENKTISGGLVSVDGQKRTLSIKGEYKDPKKIEDIVIRGSSGATVYLKDIAEVKDGFKEQESYARLGGKNVITLNVIKQSGKNLIDASDKIREIIKEMKENYLPTNLEVTITADQSTSTRVTLHDLINTIIIGFILVTVILMFFMGAVNALFVAASVPISMFIAFIMMPMYGFTLNMMVLFSFLLALGIVVDDAIVVIENVHRIFYERKDLGVVKAAKLAAGEVFLPVLSGTLTVLAPFVPLLFWPGIIGKFMFYLPVTLITTLVASLFVAYIINPVFAVDFMDRHEGENHPKPTWNKRMWIVTIVFAVLALIGYGNGFGTGNLVVFIYLLLILERFWLGNVARKFQTNFWPKVQERYKAILLWCLKGWRPVMILLGTFGLLVFSLVLTMVRSPKVVFFPQADPNFVYTYLELPIGTDQKYTDSITQIVEKRITKVVGAHNPIVESIISNVAVGAGDPNEMDMSVNSNKGKVTVAFVEFGKRNGQSTVQYLDKIREAVKGIPGVDITVEQEQGGPPTGKPINIEIAGDEFEELANTSTKLKNYLDSLQIGGVEELKSDFKSNKPEIVVSIDRERANREGISTRAIGDALRTALLGLEVSKFRDPEDDYPIMVRLKEDQRNNINTLMNLNITYRDMNMGGVIRQVPLAAVADIRYSNTYAGIRRIDQKRVVTLYSNILTGYNANEVVSQIKTAVDNFPKPPSVSVKMTGEQEDQEETMNFLGMAALGAFGLILMIMVIQFNSIGKPLIIMMEILFSIIGVFLGFAIFGMDISVVMTGVGIMALAGIVVRNGIVLVEFTDLLIMQNTPVYPAVVEAGKTRMTPVLLTAIAAILGLIPLAVGLNIDFATLFSEFNPHIYFGGDNVAFWGPLAWTMVFGLIFATFLTLILVPVMYAMNKRSIDILDLYHLPRWLKYIPFLVLILKIFTRRETVRKLHDWDYVSEKPYDFFPVKDDEVVDSDHELKHISAN
>NZ_CP023777.1|WP_098192542.1|658229_659339_-|efflux-RND-transporter-periplasmic-adaptor-subunit
MNKSYYLLPVLALSIAACGGGGNNQRAKDSLKLVELKKEVADLEAKLKEGDTSKTVKMKNVQVASVSDTTFYHYIDVQGSVDARENVQVSTRSQGGVITAIYVKEGQYVKKGQVLAQIDDQVQRAGIEELKTQLQLAEDLYRKQANLWSQKIGSEVQYLNAKNQKEALEKKLTTMKEQLALNQIVSPINGTVDAVIAKLGDIASPAVPAFRVVNTNDLKVVANIAETFAAKVKTGDQVVVSFPDINKEIHTKIGFASKTIDPISRTIKVEIPLANTAELRPNMIAHIKIIDYKAADAIVIPVNVIQYSLGKPYVMIIYKEGDKLVAGRKTVELGRTYDDKAEIISGLKVGEQIVTTGYQGLNEGDQVQL
>NZ_CP023777.1|WP_098192543.1|659369_660743_-|TolC-family-protein
MQLNWKLLCSWVARMLILMNANAQTQSPNSTSNSAPTPLSIQEAIDYALQNQAAVKTAKIDELIQLAKNREVSGMALPNVSATGQFQDNPVIQKQLIDASNFSDTIPKGTLVPFAFGLKYNLVGQVVLNQVLFDPSVMVALQARKTLEEMARKNVARTKIDVKESVYKSYYGVLVNKKAHEIILENIQRVERTLFETKEIYKNGFAEKLDVDRLTVQLTNLKTEEIRLKNALEVNTALLKFQIGMPIQTPVILTDTLSIEQVKAQMQDVQDFDYKQRPDYDYLDVSKQALEYDLKRYKLNALPSLSLSAAGGASRASNEFDYFKSRVWYGYAYYSLNLNVPIFTGLQRRRQVDQAALNVEKANVNLENMRLSIDLEQVQATANFRDNIQSLTAQEDNMQLATDVYETTIVKYREGVGSSTEMITAETGLLTAQNNYFTALYNAILAKISYLKAYGKL
>NZ_CP023777.1|WP_098192544.1|660758_661367_-|TetR/AcrR-family-transcriptional-regulator
MEVQERILDTAFMLFRQFGTRSITMDDIAVKMGISKKTLYAHFEDKDDLVFHAISRYLNVMQAQCEEGKEQSKDALEEMFLVMKMLEDKLRNMNPVALLDLQKFHAKSYQRFEEYKDVYIVETIKENLKRGIAEGLYREDIDIEIMSQFRAASCLICFRPDLFNMSGLDVGRVQRVLLEHFLFGISSTKGYKLIEKYKQKLP
>NZ_CP023777.1|WP_098192545.1|661671_662307_+|DUF502-domain-containing-protein
MSPKLRFKIFLSRILRYFFQGLLILAPIGITVFTIYWVFVSIDNLVPRDLVPVDAPYNILKYKGVGFAFVLILIIGVGYLSSSFIVSRIFDMFDHLLEKTPFIKYIYSSVKDVFDAFVGEKKKFDHPVLANIYGEDVWELGFITQQDVTSLGLDNDYIAVYVPHAYAITGKVFMVRRAKVKELSNVSAGEAMKFAVSGGVTQIHGDAGSEK
>NZ_CP023777.1|WP_098192546.1|662386_663364_+|S1/P1-Nuclease
MKSIVCLSILLIAIAIIPFKSGAWGFFAHKRINRLAVYSLPPGMLVLFKPGLEYVTEHACDPDKRRYMIPAEGPRHYIDIDLYGTYPYPELPRNYRDALAKFGRDSLQSRGILPWHFEWMLARLTKAFDTTDTRYILKIATELGHYVADAHVPLHACSNHNGQFSQQEGIHGLWESKIPELVADADFNYWVGKARYIDDPGSFIWKVILESAAAADTVLRLEKQLSDSLPLQQKYSFTLRSNQLVYQYSEMYTRAYQELLGDMVQRRMRNAIFAVASCWYTAWINAGQPVLDKHFSPTATSAEETEIQKLNQHWRKGKIFGRNHE
>NZ_CP023777.1|WP_098192547.1|663514_664585_+|3-phosphoserine/phosphohydroxythreonine-transaminase
MKVHNFNAGPSVLPNEVLYKASKALIDYDGTGMSILEIGHRTEYFMAVMDEARSLARELMQLDDDFEVLFLHGGASTQFMQVPMNLLDSGETAAYIDTGVWSNKAIKEAKLFGYVDVIASSKEGGYNYIPKQFNIPGQAKYLHITSNNTIYGTQWHEMPKTDLPIVVDMSSDILSRQMDYNQFSLIFAGVQKNMGAAGATMVAIRKSLLGKVGRKIPTMLDYQQHIENGSMLNTPPVFAVYISMLTLRWLKSQGGLAGIEKINAKKAALLYDEIDHNPLFRGTAVKEDRSLMNVCFVMDKPELEEEFLKFCKKEDIVGIRGHRTVGGFRASIYNALPYESVEVMVEAMKYFSLKKV
>NZ_CP023777.1|WP_098192548.1|664724_665945_+|DUF1015-domain-containing-protein
MAKIQPFAALRPKVDVASKVAARPYDVLSSDEAKAEASGNPHSFYHVSKSEIDLPAGTDIHSPEVYAKAAENLKALRENGTLIQENQPCYYIYKLIMHGRSQVGLVCVSSVDDYNNDIIKKHEFTRPEKEQDRINHITATRAQTGNVFLAYNDVPSINSIIDSWQEHHSPVYDFVAEDGITHTIWVMNEPGTVQEITKLFASEVPCTYIADGHHRAASAALVHNSLQSEASAWFLTTIFPASQLAILDYNRVVKDLNGHSKEEFLSALEYDFTIEAVGHSPKKPAMLHEFGMYLDKTWYHLVAREGTYTTDPIGVLDVTILQNNVLDKLLGIKDPRTDKRIDFVGGIRGLEALIKRVDSGEMQVAFALYPVTIQQLFDISDSGNVMPPKSTWFEPKLRDGLLTHVV

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Crispr_ID: NZ_CP023777_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_3

972627-972729

Orphan

Consensus_repeat	Method
CCTTAAGATGTTTTATCGCGGATGTTGTTTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023777_3

>merge|NZ_CP023777|3|972627-972729|CRISPRCasFinder
CCTTAAGATGTTTTATCGCGGATGTTGTTTTTGATATTTCACGGTTGATCAATGTTTCATACCTATCTATTACCTTAAAATGTTTTATCGCGGATGTTGTTTT

>NZ_CP023777|3|3|972627-972729|CRISPRCasFinder
CCTTAAGATGTTTTATCGCGGATGTTGTTTT	TGATATTTCACGGTTGATCAATGTTTCATACCTATCTATTA
CCTTAAAATGTTTTATCGCGGATGTTGTTTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098192792.1\|971026_971476_-\|DUF1569-domain-containing-protein	unknown	unknown	gnl\|CDD\|369441
NZ_CP023777.1\|WP_098192798.1\|979059_979956_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098192784.1\|949240_950653_-\|MATE-family-efflux-transporter	unknown	unknown	gnl\|CDD\|240544
NZ_CP023777.1\|WP_098192793.1\|971748_972501_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|180440
NZ_CP023777.1\|WP_098192797.1\|977828_979070_-\|DUF4350-domain-containing-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098192801.1\|981853_982309_-\|RDD-family-protein	unknown	unknown	gnl\|CDD\|377640
NZ_CP023777.1\|WP_098192791.1\|970496_970967_+\|DNA-starvation/stationary-phase-protection-protein	unknown	unknown	gnl\|CDD\|153102
NZ_CP023777.1\|WP_098196091.1\|983105_983516_+\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|225168
NZ_CP023777.1\|WP_098192799.1\|979975_980959_-\|stage-II-sporulation-protein-M	unknown	unknown	gnl\|CDD\|376676
NZ_CP023777.1\|WP_098192800.1\|981031_981835_+\|RDD-family-protein	unknown	unknown	gnl\|CDD\|377640
NZ_CP023777.1\|WP_098192788.1\|955048_965692_-\|gliding-motility-associated-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|372639
NZ_CP023777.1\|WP_098192794.1\|972871_975031_+\|alpha-galactosidase	unknown	unknown	gnl\|CDD\|307952
NZ_CP023777.1\|WP_098192789.1\|966421_969010_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098192787.1\|953947_954958_-\|type-IX-secretion-system-membrane-protein-PorP/SprF	unknown	unknown	gnl\|CDD\|274625
NZ_CP023777.1\|WP_098192786.1\|951877_953941_-\|OmpA-family-protein	unknown	unknown	gnl\|CDD\|143586
NZ_CP023777.1\|WP_098192790.1\|969550_970459_+\|transglutaminase	unknown	unknown	gnl\|CDD\|376628
NZ_CP023777.1\|WP_098192796.1\|976844_977825_-\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
NZ_CP023777.1\|WP_157760609.1\|951141_951606_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098192803.1\|983651_984266_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|350620
NZ_CP023777.1\|WP_098192795.1\|975492_976836_-\|DUF58-domain-containing-protein	unknown	unknown	gnl\|CDD\|224635

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098192792.1\|971026_971476_-\|DUF1569-domain-containing-protein	gnl\|CDD\|369441	pfam07606, DUF1569, Protein of unknown function (DUF1569). A family of hypothetical proteins identified in Rhodopirellula baltica.	1.00155e-06
NZ_CP023777.1\|WP_098192803.1\|983651_984266_+\|hypothetical-protein	gnl\|CDD\|350620	cd14845, L-Ala-D-Glu_peptidase_like, L-Ala-D-Glu peptidase, also known as L-alanyl-D-glutamate endopeptidase. This L-Ala-D-Glu peptidase family includes L-alanyl-D-glutamate peptidase (bacteriophage T5) (also known as L-alanoyl-D-glutamate endopeptidase), and Ply118 and Ply500 L-Ala-D-Glu peptidase. Bacteriophage endolysin degrades the peptidoglycan of the bacterial host from within, leading to cell lysis and release of progeny virions. The bacteriophage endolysin Ply118 cleaves between L-Ala and D-Glu residues of Listeria cell wall peptidoglycan. This family belongs to the MEROPS peptidase M15 subfamily C.	5.48916e-18
NZ_CP023777.1\|WP_098192784.1\|949240_950653_-\|MATE-family-efflux-transporter	gnl\|CDD\|240544	cd13139, MATE_like_14, Uncharacterized subfamily of the multidrug and toxic compound extrusion (MATE) proteins. The integral membrane proteins from the MATE family are involved in exporting metabolites across the cell membrane and are responsible for multidrug resistance (MDR) in many bacteria and animals. A number of family members are involved in the synthesis of peptidoglycan components in bacteria.	0
NZ_CP023777.1\|WP_098192793.1\|971748_972501_+\|SDR-family-oxidoreductase	gnl\|CDD\|180440	PRK06172, PRK06172, SDR family oxidoreductase.	8.10658e-100
NZ_CP023777.1\|WP_098192801.1\|981853_982309_-\|RDD-family-protein	gnl\|CDD\|377640	pfam06271, RDD, RDD family. This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. This region contains two predicted transmembrane regions. The arginine occurs at the N-terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this region is unknown. However this region may be involved in transport of an as yet unknown set of ligands (Bateman A pers. obs.).	6.73788e-11
NZ_CP023777.1\|WP_098192791.1\|970496_970967_+\|DNA-starvation/stationary-phase-protection-protein	gnl\|CDD\|153102	cd01043, DPS, DPS protein, ferritin-like diiron-binding domain. DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.	6.06912e-54
NZ_CP023777.1\|WP_098196091.1\|983105_983516_+\|DoxX-family-protein	gnl\|CDD\|225168	COG2259, COG2259, Predicted membrane protein [Function unknown].	4.67353e-20
NZ_CP023777.1\|WP_098192799.1\|979975_980959_-\|stage-II-sporulation-protein-M	gnl\|CDD\|376676	pfam01944, SpoIIM, Stage II sporulation protein M. SpoIIM is on e of four stage II sporulation proteins that is necessary for the forespore inside the mother-cell to be properly internalized through the breakdown of peptidoglycans trapped between the membranes of the septum separating the forespore and the mother-cell. The four proteins working in sequence are SpoIIB, pfam05036, SpoIIM, SpoIIP, pfam07454, and finally SpoIID, pfam08486. D, M and P are in a complex with each other and the complex assembles in a hierarchical manner such that M, which serves as a membrane anchor, recruits P to the septum and P, in turn, recruits D to the septum.	6.15324e-29
NZ_CP023777.1\|WP_098192800.1\|981031_981835_+\|RDD-family-protein	gnl\|CDD\|377640	pfam06271, RDD, RDD family. This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. This region contains two predicted transmembrane regions. The arginine occurs at the N-terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this region is unknown. However this region may be involved in transport of an as yet unknown set of ligands (Bateman A pers. obs.).	4.96115e-12
NZ_CP023777.1\|WP_098192788.1\|955048_965692_-\|gliding-motility-associated-C-terminal-domain-containing-protein	gnl\|CDD\|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	2.80212e-24
NZ_CP023777.1\|WP_098192794.1\|972871_975031_+\|alpha-galactosidase	gnl\|CDD\|307952	pfam02065, Melibiase, Melibiase. Glycoside hydrolase families GH27, GH31 and GH36 form the glycoside hydrolase clan GH-D. Glycoside hydrolase family 36 can be split into 11 families, GH36A to GH36K. This family includes enzymes from GH36A-B and GH36D-K and from GH27.	1.04877e-117
NZ_CP023777.1\|WP_098192787.1\|953947_954958_-\|type-IX-secretion-system-membrane-protein-PorP/SprF	gnl\|CDD\|274625	TIGR03519, bacteroidetes-specific_membrane_protein, type IX secretion system membrane protein, PorP/SprF family. This model describes a protein family unique to, and greatly expanded in, the Bacteriodetes. Species in this lineage include several, such as Cytophaga hutchinsonii and Flavobacterium johnsoniae, that have type IX secretion systems (T9SS) and exhibit a poorly understood rapid gliding phenotype. Several members of this protein family are found in operons with other genes whose loss leads to a loss a this motility.	1.35064e-58
NZ_CP023777.1\|WP_098192786.1\|951877_953941_-\|OmpA-family-protein	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	5.16426e-41
NZ_CP023777.1\|WP_098192790.1\|969550_970459_+\|transglutaminase	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.	0.000221589
NZ_CP023777.1\|WP_098192796.1\|976844_977825_-\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	5.98757e-106
NZ_CP023777.1\|WP_098192795.1\|975492_976836_-\|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].	8.5333e-48

>NZ_CP023777.1|WP_098192793.1|971748_972501_+|SDR-family-oxidoreductase
MEQLFQGKVAVVTGAGSGIGKATAELYSQHGAKVVVSDISLEHGKQTVDDIKAKGGDATFIACDVADPKACKNLIDETVKVYGRLDAACNNAGIGGEANPVADYSIENFDKIIAINLSSVFYCMKYEIPAMLKNGGGAIINMASILGQVGFANSAGYVAAKHGVVGLTQNAGIEYSSQGIRVNAVGPGFIDTPLLNNLDPEMKKALVKLHPIGRLGKAEEIAELVVWLSSNKASFITGSYYPIDGAYLAL
>NZ_CP023777.1|WP_098192792.1|971026_971476_-|DUF1569-domain-containing-protein
MKNFFDQADAATIISRVQHINPASTPHWGKMTAAQMLAHCNAAMEMALGKKQVKRAWFSYLVGWLAKPMFLNEKPFPKGLPTDPSLLAGDGNGVEEEKNKLIGQIQELASGGPGVVTTAAHSFFGKLTAEQWARGMYKHLDHHLQQFGV
>NZ_CP023777.1|WP_098192791.1|970496_970967_+|DNA-starvation/stationary-phase-protection-protein
MKVNIGVPEKNLQAVADKLQVLLADESILYTKTRNYHWNVEGQNFSEMHLFYEGQYGDLAEMIDEVAERIRQLGHYSVGRLADFLKLTHLLEPEYTNDQKTQLKNLLDDHETIIRFIRECIREFDETHNDAGSSDFVTGLMEKHEKMAWMLRSYLK
>NZ_CP023777.1|WP_098192790.1|969550_970459_+|transglutaminase
MANEDSRYTTVQTFLLNLLSLLTILPLAPFLNRFIPPVIIGDIHIDLFISLLIAFLITRIILWIFKPLMIPAFVLVCSVLVYNFFIGSYTFTNVINDYKGMVQGNWGAKDQKQQDILSLYPRRVETYYDKTVRGIREKVNDQDSVVRNYAVKYSLTDFDEYFSKYGKIVRFLSLYKHIRNNFKYVNDSQRDEYFATPQETIRNGLGGDCDDHSILMVSCMQSIGAKCRIVLVKGHAYPELYCGNKDDFEILKQAIVLLFNNPPVKQLYYHEMKGEYWINLDYTARHPGGPYMNNQVYALIDL
>NZ_CP023777.1|WP_098192789.1|966421_969010_+|hypothetical-protein
MIDLSYDYIVMLQNEVLRQFGVDNITPGLCKPLSTAILGRTTKIVSETTLKRFFGFAAAQHSFSRYTLNTLSHYCGYKDWDEFQSKNVAATIKTSIAPSPTIEGCTSKWMELKAKANAVSQYTIQTLKNRSGIPFNYTVVRQETIQHIERFLNSDYPATVFIAPPGWGKSISLVHAVEHCWFNQNAAHTEDICWFINAHAAGSLMMKGFSLANWLDNQLNLGPGENLREYFSNNPQARSGKLVLIIDGFDELNLGSDKTKMLYSKLEDFVYSNDEHPWVKVILSVRSSTWSELFQRSQHYANFRKFWFMGRKMDEETNINIPLLSKEEMKSVLNHYHFDAQKVEQLSDLFLQKLIHPYYLQLFCQLNEEHGDGFFDERLSLFEIASKFIQNRVFQSNKNTFKIAIIDKLLQLLDYGRNGLYADKALLLNKNTDLFPAYKELVTDNILVEENLSQEIMFNVKVRFTHNFMLEYFVAMHFYQNYGEHVREDMLNHILSYFPPSSFRISVLNWLVRCCINKQQYECIHAILKLPLTTNERSQILEYIVLHHNQEDRKPVALEEVFPIGFFKKHPISGFVNDDFVQYRKKKILDTFLGLAESTEDKLKIRSNLFVMALMQLDAESCEFELTNIRKLTADDEALTAMSIQPYEIFLFIYEYLKFGEVNEDIKEKIYDCKWLWLIGGQKIGVAEEIVCKAMCFAFLLMGDYQQLLNFTQRLFERYPQMLYSKGDVFRLTLLCWEAQAHLRVGNTKEGKRIHEHIDRVLKLNLADQFSTKHVQTLQKIIGAEICYQNGDYNRAIKLAESAMEMAQKLDFKLFALINYTILNKVYQDLNMEHQTELAMQQVALIQKNTTFKKAVSNFIYQ
>NZ_CP023777.1|WP_098192788.1|955048_965692_-|gliding-motility-associated-C-terminal-domain-containing-protein
MTFNVTPKKHYGAFILVLSIFMMAIIPGMLSAQRVYATSQTNGVSGLCLLCGVTNAANPVNNANLDDYSQFSVTVGLLGVSVQQTLIFPTINPNESCDSLVIGIGNSGALLSANLLGGVSFETLNGTTPNNDAVSGQAALLRLLSGDNQGEIVLRPTSKFDRVRVTLSSNLLGALADFRLYYAYYNEVDIIPPTITTPASLNVCEGNSIDLTATTATPEAVISWYTVPTGGTPITNPVADGTTLTVTPASGTTTYYAQTALDVCTNTTRSAVSVTTTALPAVPALANTTHTICAGDQTTFNVQNPVSGVTYNWYDAPTGGNLLASGLTYTTPNLNAATDYYVEAALSTGCVSATRAQASVAVNPSPAAPSVNNSNVTINSGQSVTFSIPSPEPGVTYTWYDSPAKVNTLATGASYTTPILFGTTNYYVEAMNGTGCTSPLTTLTATINAQNNVPCSFANQDNGVTTSGICLLCNVSNPANVVDLDTSTASTMSVPVGVAGSINHLIGFSNTYAAGDSIVIVLQSPGQLLNLDLLSAISVRPYLNATALGSGPISLNNSLVGLKLLGIIGGTGRYRVSIPVDEDFNGVMISLGSLVSALATVNVFYVAATVQYPVPLASDVNICTGNTADLSVTAAANTSVNWYDVPTGGTALATNTTSFTTPALTNTKTYYVGISRFGCENGTRVPITVNVNQVPTAPALAVDTVSLCAGNTATFAIAAPDGDLTYRWYSTATGGTPLDSGATFTTAVLNNNATYYVESSANGCTSAARSTAAAVVTQAPANVTVTPSTTSVVQGGSATFTASSTSGNVTYNWFVTPTGGTSIYTGASFTTPPLVANTTYYVEAVDNTTGCVTLNRTAATVTVNSGAIDLSCGAAISQSNTSNGLCIGCSVQNPGLSVDSSTETGSRIGVVLGLLNAYAAQRLTFDGVANVGDSIQIGLTLPSSLADVGLLSTVQVVTYNGGTANNDLQDINAAPITLKLLAGNQKALVTFAATATFDAVELRLNSGALTALNAINLDYARVITAVPTVQEDTVSVCPGQTATLNAISRPNTTFRWFADATGGSPLFTGASYTTPAITANTTYYVEALSASGCTSPTRTAVYVQTGLPSVTVTSNSVSIPVGETADLSVNTPEPTFTYQWYNVPTGGTALSTGPNFTTPNLFVTTVYYVEASNGAGCASATRVPVTVNVTQTPGAADVPCGSATSQTNAADGLCVGCYVENPGFAVDSSTTTGSTIHLILGLLSGSVSQTLEFPTASNIGDTLVVGLTFPSSLADLGLLANVQIGTANGGTSNNDLQAINGGGLISLTLLNNNQQAIIKYAPTAAFDKVQIQMNAGLAQAISAVNVDYATRIIAPAVPVSNSVNVCVGDTATLEATARLNTTFRWYATATGGSSLYNGQSFKYGPVMNDTTFYVEAVSSTGCISPVRVPVSIMVGLSNVSVTANEVTVDRGQSATLSVDNPDANFTYDWFDEETGGTSVHTGATFVTPAINVTTVYYVEATNANGCKSNMRIPVTVYVRQDPGSPDADCGAANSQTNAANGICVGCYVENPGLAIDSSKSTGSTIHVILGLVGGSVSQTLIYPSPSNVGDSVVIGLTFPSSIADVGLLANIQVGTYNGATFNNDYADLNSSLINLQLLNNSESAILKFAPGATFDRVEIKMNSGVAQALSAINVDYASRVYAKPLLQSDTVAVCTGQTATLSITPQANTTYRWYNKPVGGSVLATGNSFTTGNISVDSIFYVEAVTSSGCVSSERTPAVVTVGLPGVEVTSDDVTVNLGETAHLSVNNPDTTYTYEWYDVATGGTALATGADFTTPAMTVSTVYYVEATNNIGCKTASRIPVRVTVLQAPGPNDVPCGAATTQTNTANGLCVGCYIENPGLAIDSSSVTGSTVHVILGLVNAYASQTLIFPSVSNVGDSIHLSLTFPSSLADVSVLGGVQVLTYNGTTSNNDLQSINSSVISLQLLANNTGALISYAPTKAFDRIEVRLNSGLAQALNAVNVNYAARIVGPAMPSADSVTICQGTTAILSADVQPNTSYRWYANATGGTPLASADNFTTPNLNTNTTYYLEAISSAGCISPVRVPVQVIVTSAPNAPTVADTTILTCGGTTARLEATGPAGASFRWYNQASGGTTLADSAVFITPVLDSSAIYYVESYLAAGCASASRTAVKVEVTTRPEPPVVTPDAPTICAGNTATMVANSTSASATIYWYASETADTALATGSTFTTPALNANTTYYVGTSNGQCESATRTAVTVMVNPLPVAPTIVSNPANGIVPYGSSAELTASSATSNVTYHWYRTATGGTEDFVGATFQTPQLTDDVVYYVEAVSASGCTSGRTAIALTVDKNFNPGCDIANAQTAVVDGVCVLCAITDPNNSVDNDTTNFAQINIPVGVVGASYGQRLNFGSVSNLGDSVSIILEVPNTVINASILGAITINSINAGASNNENIQLNNAAIKIDLLGGGTNKFKVTFKPAAAFDEVEVKIGGGLVTGFNNLRVYYAYRVVPAPEIALNDVTICAGSTATFNATAPAGVQVNWYTTAVGGTPIATNTTSFTTPALDTFAIYYAESVRESTSCPNPIRKAVFVNVLPVPDPPVIVTSDTTICPGNTVVLKAVASNSTTQIRWFDAATNGNLLATDSIYITPALSSTTTYYVETYNGTCTNSGARAAVTVNVGSIAPTPVLQAPTLALCAGGTATFNVVAETGVTYRWYNTSTGGTAIFTGATFTTPVLNASAVYYVEASTGDCASATGRVAATATVNAIPGVPVLVNDQLISCGNNSVTFNIQNPQANLTYNWYDAAVNGNLLHTGINFTTVPASDSVTYFVEALNGSSCASSTRALATVKGGEIPPAPTVDSTSYTVCSGTNLSLNVKSPQSGHIYQWFDAPTGGNLLFTGSKFITPILTMDRSFYVADSTASGCSSSSRTQVDITVKAVPTAPVVVDGTEICAGNTTTLLVQNRQNGIEYRWYDAMIGGSLLATDTAYTTPSLTNTTTYFVEAYNGTCTNTSGRVAVVVSVKAVPTDVVVDADSVAICSGSTAMLHVSNPLSGITYRWYDAATGGNVVATGADFTTPVLSVSTDYYVEAININNCMSANRTKVTVSVNDGIDVPELENADVVICRNTMAILTIKSPRAELQYDWYDAPSGGNLVFTGSIYQTPALSTDATYYVAASLKGGTCTSASRATVKVTVADAPTTPVLVNGAITTCSNSTATFEIQNPQPNVTYRWYDADMNGNLVFTGASFTTGNLTANITYYVEAVIGNTCASTGKAEATATVGPRPGTPMVTGNADPICPNSPDTLTATSTDAGVIFNWYTSSTATTPVFTGNTFITPALAATTTYYVEAAYANSGCTSTSREQATVTVLETLAQPTVTVQSKTASSVTFQWDAIPGAIGYRVSFDNGVTSVFRSKDSLTYTVSGLQPAQSVSLQVMAIGLSECANSGWFMSDTDTDNPAGNLVFVPNAFTPNNDGLNDILYVYGTTISNMQIWIYNQWGQLVFQSKDQTVGWDGTMSGKKQPVGVYNYVLKAQLQDGTIVNKRGTITIIR
>NZ_CP023777.1|WP_098192787.1|953947_954958_-|type-IX-secretion-system-membrane-protein-PorP/SprF
MRNKIIIVVLAFCVFVPALAKAQVDPHFSQYYAYPLWLNPGLTGVVDGDYRLNGNYRTQWNNFGKPFSTAGVSFDAPTAKNLGLGVNVLNMSAGDAGYNYLNAMASIAYNGVKLGRNQTSQFSFGVQAGIINRRIDQSKLQFGSQYNPVIGFDPNMISGENLGRTSSTVFDVNAGVMFFDGNPNHTVNPFVGVAAAHLTQPEDPFLEADNGDRKLPVRYVAHGGMRIKVSDMLNITPTGLYMRQGNAEEIVGGAYAQILVNPMCDVLLGANYRWKDCVIPFAGARYQHFTLGLSYDANTSNLRRLVNGSNSFEVSLSYVFRKKRIFDPEYFICPRL
>NZ_CP023777.1|WP_098192786.1|951877_953941_-|OmpA-family-protein
MKRIHIIYRRFLLPSIQINGIPMKKFTFLFVISLVIVNAALAQYVADYRRTADVYYMNKDFYSAAQYYNKALNTFDTKEAKFIPYVVDKSSRKEKKKVKDYEEVKYRLAESYRHYYDYASAEKWYASIINDNATEAVAMFPLIRYQYAVCLRALGRYDEALQQFKQFKEEYKGYDDYSTQALVEIATCEFAVEEMKKTPRFTVMKVTGDVNRAGANYAAVLEKAGNIIFTSSRPDSGALDKKGNPYVNKLYTASGSGHEFENSSLVDIPLEKNMDMGVATLSPGGNTMYLTKWTTKNGQKMSAIYESKRSGSSWSEPVKLGANVNADGYSSKEPMLTSDGKYLLFSSDRPGGNGKFDLWYATLQNGTPNAPVNMGNIINSKEDDCAPFYDTRNKMLLFSTNGRVGFGGMDFFSSKGSFGDWVNPVNMGYPLNSPKDDIYFCPNTTDNGMQQGFFSSDRESVCCLEVFTLQKVAKVMMGMVNDCDGGAPLTGAKITLLLQPENKIIDQVVLNETGKYEFEVELDKDYKILAEKENYFSKTISANTATLHTADTLFNPGICLKRYEVGKPIILKDIYYDFDKATLRPQSLVVLDTLYTILVDNPDIEIELSAHTDSKGTDAYNLKLSDARAQSCVDYLISKGISRSRIIAHGYGESMPIAPNTLPNGKDNPDGRQLNRRTEFKVLRNKH
>NZ_CP023777.1|WP_157760609.1|951141_951606_+|hypothetical-protein
MLTKKALKRSLMAIALPAMLCFTVTACSDDDDDAPRMRTKEYAFTSTDSTANGKVTIKEKADSTIEIAITLNKSIKDTTYNFGVFKGEDVAVTTDTLLALPSVKSTGAGLESKATVNSISYDSAMKVKAFARISFVDGETEEAVATKKILDAAN
>NZ_CP023777.1|WP_098192784.1|949240_950653_-|MATE-family-efflux-transporter
MRLSQRVSRVQRIFGLIGNAITGKEYNYTSGSIKQAIVLLAIPMILEMVMESLFAVVDIYFVSELGKNSIATVGLTESMLMIIYSLAMGIGMAATALVARRTGEKDKDGASRAAAQTLLVGIIVSLLISIPGAFFAPQLLKLMGAGNEVLQVGTSYTRIMLGSNIVITLLFLVNGIFRGAGNAVMAMQSLWLANIINIICCPIFIFGWGPIPAFGLKGAAIATVVGRSTGVIFQLWFLFRGNKNINFNFALFKPNMALMKQVVKIASSAAGQFLINSASWIVLIRIISSFGEAAIAGYTIGIRVVIFSLLPAWGLANAAATLVGQNLGAQQPDRAEQSVYRAAFYNMAVLGTISVFFIVFTKGIIGMFTHEPEVIRYGVDCLRIVSIGFLVYAFGMVIIQSINGAGDTRTPLLINIVGFWLIQIPLAYILAIIFRFGPPGVFIAICIAETVVAAIGFAIFRRGKWKLVHI
>NZ_CP023777.1|WP_098192794.1|972871_975031_+|alpha-galactosidase
MKKILFLFLLALGIPFATIAQKGGYIVIKTAHTGLVFHEEKDGSLHQIYYGQALKNPADYYLLPGTRDEAYPTFGTKYLFTPAIRTVHNDGNPSLALVYKSHQQLLVAPGVEETTIHLHDPKYPVEVDLHFKAYLSSDVIAQWVTVSHHEKKPIVLYQYASAALSVSASNYTLEHFHGDWAAEMQMESTNLTAGKKTLSSQLETRAHMYQSPSFLISLNGTSTEEYGDVIGGTLAWSGNFKLDFEVDEINQLRILAGMNELGAEYHLLPGKTFTTPAFLFSYSNEGKGLISRNFHKWARDYGVLNGHGSRYTLLNNWEATYFDFNEEKLTNLFDDAKQLGVDLFLLDDGWFGNKYPRNNDRAGLGDWQENKAKLPHGIGYLVKEAAARDLKFGIWLEPEMVNPKSELYEKHPEWIIKLPNREEHYYRSQLVLDLTNPTVQDFVYHIVDDMMSKNPGIAYIKWDCNRMVTNAYSQFEGNQQSNLYVDYVNGLYKVLDRVRQKYPELPIMLCSGGGGRVDYGALPYFTEFWPSDNTGATERVFIQWGYSYFFPSIATSAHVTEWGDAPLKFRLAVSMAGRLGFDLVPKKLNAEELALCQQALHEYKAIQQTVWQGDLYRLQSPYDHNVASWMYAANDKAEAVIFMFRIKKLFDSKIAENIKFKGLDPGKKYLVKELLVQQGQKAINKANGKTYSGDYLMKVGLPSNLNKVQQAVILQLKSL
>NZ_CP023777.1|WP_098192795.1|975492_976836_-|DUF58-domain-containing-protein
MNRLKHFFASLYLKQRTYLSLLLVIGFFLLSFFFPGLFEIAIGLFFLCCALVLVDILVLYLPGNAIQVERDIADRLSNGEENPVSLLVRSNYPLKMQLDVIDELPFQLQERNFNWKTSIDVNGTTKYNYMLRPVERGEYKFGYVNVYVNSFLGLVKRRFLTAGQRTIKVYPAFQQLKQLGFKGANNLLQDSGAHRHKVMGFSMEYDHIKEYVQGDDIRALNYKASARRGHLMVNSYTEEKSQQVYCVIDKSRNMRMPFNGLTLLDYAINASLIFSNTAINKGDKAGLITFSDQQPEWLKASNRKVQMNAILEKLYAQGTTWLESDYEKLVSGLRKNISQRSLLILFTNFESVSNLQRQIAYLRTLAKYHLLMVVFFENTELKSVSERPAENIEGIYTQVIAQKMMHDKKLIQKELAKYGILSLLTAPASLTVNLINRYLDLKQRRVI
>NZ_CP023777.1|WP_098192796.1|976844_977825_-|MoxR-family-ATPase
MEENTTLQPNAFETMSNTIQNIKDEISKVVIGQDALIDMLLVGIIAKGHLLVEGVPGVAKTLTAKLLAQCIHADFSRIQFTPDLMPADVLGTSVFNAQQQVFEYKKGPIFGNIVLIDEINRAPAKTQAALFEVMEERQVTNDGHTHKMGNPFMVVATQNPIEQEGTYRLPEAQLDRFLFKLEVTYPGLQDEISMLQAANSNKLGDHALQSVKPVVTAAEIIALQDKAEQVFVEEHIIRYIVHLVKATRENGSLFMGASPRASIAVLASAKAYALVAGRDFVTPDDVVTVVPAILRHRIVLTPEREMEGITTNDVIAEILKSVEVPR
>NZ_CP023777.1|WP_098192797.1|977828_979070_-|DUF4350-domain-containing-protein
MKFRFIWIGLLVLLVVIIIFGSVFQGGMRNKRKVEDFNAASASFEYRDKKPYGSFVAYKLLKQYLNGANHGTLHQIVKKPVAELFKTTFNQNALYCIIANNLFLSADDVDRLGNFIENGNEVFIAATDPDSLLAERLHFNYKAGIVDNGVFNKKLHTVQNFVNKNFGKDTSFAYKGIYNSGYFTAVDTAVTTVLGTNEEGKPNFIRIVHGNGAVYISLNPFACTNYFLLHGENHRSFRNMMGYIPDSKNIVYWDEYYKHQYSREGKDFDNWSVLMRYPSIRWALILILCLMILFALFESKRQQRYVPAVEPVLNNSLDFVKTLGKLYFNHHDNKNLVHKMTTQFLDHVRNKYFIDTKYLDENFVNQLARKSNQPREEIQLLINMMHNLQLEFEVSDKQLEMYYQALYKFYQIA
>NZ_CP023777.1|WP_098192798.1|979059_979956_-|hypothetical-protein
MKHPYLLIYMLTLLSLFCAGDIKAQRLNTLDSVSYDQDEEVFIDSVAVDKQGIQHYQDEAVEPDTTTLEGQVRLLWPGGLAYDQNNFGEFQDGQGRYFYNNVRIHTGSPAGLKELKEDSDMDYEKDLRALDPEHKKDAKHFPLTIPILMSFFIVASIVLIVVIVYNSRGTLRRIFKSSKNNTFSAAGVPDAESKVDYRSLADAAMKEAHWAEAVRYLYLYTLQVLASSQKLILHKDKTNRDYVNELSGTELQMPFLALTRQYEITWFGKKNVDEARFSDIRFSFQSFLKSINNTGHEI
>NZ_CP023777.1|WP_098192799.1|979975_980959_-|stage-II-sporulation-protein-M
MRESLFIKKNLARWKSYEQEVSQDPDEMAERFTTIVDDLAYSKTFYSYSKTTQYLNGLAAGMYQSIYSTPIKEPGRFKKLLMYQVPLIVAKYKKVFLFAALLFMSICMLSAFSASVDDTFVRGVLGDNYVNMTEENIAKGDPFNVYKDSNELMMWVQIANNNLNVALSSFVMGVLLGLGSLYILVNNAFMVGAFQYFFFAKGLGMASVLVIWIHGTLEISAIIISSAAGLILGYNLLFPGTLKRVEALKRAAFEGLKIMFTIIPIITLAAFLEGFVTRHTEMPVFLSTSILAISFVIIIGYYVIWPIQLVRKGFSLDEKGRVLFPKN
>NZ_CP023777.1|WP_098192800.1|981031_981835_+|RDD-family-protein
MSTIKIPTPFNIDLEFAAADSGIRLLAYILDFIIRIIAVFGLVFLVARLNLPEQVDTIVNVLFIFIPFTLYYLLSEIFMDGQTLGKKIVKIKVRNLSGNAPSLDQYIIRNLFRLIESPAMIFAVLAYLTQVDRVSSFGFMLFVLCPAVIPLVFLIKTKYNQRLGDVVANTIVISSKKSQPLTNTIFREITDANYQVQFPQIMRINDKDLNKIKDLLDRATQNIDVTLADRVAERIQQVLGIQTQMNSLEFLETILNDYNYLATREPK
>NZ_CP023777.1|WP_098192801.1|981853_982309_-|RDD-family-protein
MSEQMNPSSAQEGSFLDDFDTPQYIDASRGIRFANFILDYIFILVVIGVLAAISGMEEYDYYGSLNYSYYFLNMTVYIVYYTIFEGLWGRTPAKFITGTIVIMEEGTQLEFAKAFLRSLCRFIPFEPFSGFGIPWHDSLTHTRVVKYSSIQ
>NZ_CP023777.1|WP_098196091.1|983105_983516_+|DoxX-family-protein
MKDWPLLILRLVLAFGFFWPAQLKWSNIQGVIDNFSNLGVPLPTISAYFVAGIEAIGVIFLALGLATRIVTIPLMIIMLVAINVVHWQNGFPVANGGFEIPLYYLVMLFVLLIYGPGKFSIDHLVNRNKRRSPNLR
>NZ_CP023777.1|WP_098192803.1|983651_984266_+|hypothetical-protein
MTYDRDPKYLHPHIRLHLDSILSAIQNKLPAGHTAKVVSAYRTPEDQFIIYKKGRTFQGGKWVKTGAVYTNIDGYTRLSRHNYLPCLAIDIGLFEGNTYLGNSNLYKYVKQGTQFQMDWGGNWNSFKDLPHLEVPGNILKPSIEKNIALIWQKYLLIDGYYTAALDGIFGPKSIAALEAATGINARNKAAWDKLFAKYGPPENL

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Crispr_ID: NZ_CP023777_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_4

1224863-1224996

Orphan

Consensus_repeat	Method
TTTTTCACCAAATCATTTAATGCTTCAAAATCCTCCAAAAACTTAGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023777_4

>merge|NZ_CP023777|4|1224863-1224996|CRISPRCasFinder
TTTTTCACCAAATCATTTAATGCTTCAAAATCCTCCAAAAACTTAGAAATCTCCCCAAAATCGGGGTGAAAAAAATTATGATACCATTTTTTCACCAAATCATTTAATACTTCAAAATCCTCCAAAAACTTAGA

>NZ_CP023777|4|4|1224863-1224996|CRISPRCasFinder
TTTTTCACCAAATCATTTAATGCTTCAAAATCCTCCAAAAACTTAGA	AATCTCCCCAAAATCGGGGTGAAAAAAATTATGATACCAT
TTTTTCACCAAATCATTTAATACTTCAAAATCCTCCAAAAACTTAGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098193003.1\|1215772_1216108_-\|PadR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224609
NZ_CP023777.1\|WP_098193007.1\|1219407_1220499_-\|mannose-1-phosphate-guanylyltransferase	unknown	unknown	gnl\|CDD\|223906
NZ_CP023777.1\|WP_098193009.1\|1223870_1224644_+\|DUF3050-domain-containing-protein	unknown	unknown	gnl\|CDD\|378614
NZ_CP023777.1\|WP_098193001.1\|1211575_1213705_-\|ferrous-iron-transport-protein-B	unknown	unknown	gnl\|CDD\|223447
NZ_CP023777.1\|WP_098193015.1\|1230147_1231041_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098193018.1\|1233562_1235431_-\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-enzyme-MnmG	unknown	unknown	gnl\|CDD\|235362
NZ_CP023777.1\|WP_098193019.1\|1235589_1236012_-\|rRNA-maturation-RNase-YbeY	unknown	unknown	gnl\|CDD\|272871
NZ_CP023777.1\|WP_157760633.1\|1227738_1229292_-\|PAS-domain-S-box-protein	unknown	unknown	gnl\|CDD\|182070
NZ_CP023777.1\|WP_098193006.1\|1218681_1219350_+\|carbonic-anhydrase	unknown	unknown	gnl\|CDD\|237927
NZ_CP023777.1\|WP_098193014.1\|1229686_1230049_-\|glyoxalase	unknown	unknown	gnl\|CDD\|319909
NZ_CP023777.1\|WP_098193012.1\|1226431_1227730_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340925
NZ_CP023777.1\|WP_098193016.1\|1231307_1231844_+\|CopD-family-protein	unknown	unknown	gnl\|CDD\|367596
NZ_CP023777.1\|WP_098193008.1\|1221655_1223857_+\|DNA-helicase-RecQ	unknown	unknown	gnl\|CDD\|273594
NZ_CP023777.1\|WP_098193010.1\|1225125_1225644_+\|damage-inducible-protein-DinB	unknown	unknown	gnl\|CDD\|225200
NZ_CP023777.1\|WP_098193017.1\|1231836_1233198_-\|oxygen-independent-coproporphyrinogen-III-oxidase	unknown	unknown	gnl\|CDD\|236430
NZ_CP023777.1\|WP_098193004.1\|1216445_1216748_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098193002.1\|1213888_1215730_-\|PspC-domain-containing-protein	unknown	unknown	gnl\|CDD\|377200
NZ_CP023777.1\|WP_098193011.1\|1225647_1226319_-\|ribose-5-phosphate-isomerase-RpiA	unknown	unknown	gnl\|CDD\|234816
NZ_CP023777.1\|WP_098193005.1\|1217025_1218660_+\|SulP-family-inorganic-anion-transporter	unknown	unknown	gnl\|CDD\|223732
NZ_CP023777.1\|WP_098196101.1\|1220504_1221467_-\|KpsF/GutQ-family-sugar-phosphate-isomerase	unknown	unknown	gnl\|CDD\|182814

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098193003.1\|1215772_1216108_-\|PadR-family-transcriptional-regulator	gnl\|CDD\|224609	COG1695, COG1695, Predicted transcriptional regulators [Transcription].	7.04231e-19
NZ_CP023777.1\|WP_098193007.1\|1219407_1220499_-\|mannose-1-phosphate-guanylyltransferase	gnl\|CDD\|223906	COG0836, {ManC}, Mannose-1-phosphate guanylyltransferase [Cell envelope biogenesis, outer membrane].	2.82969e-126
NZ_CP023777.1\|WP_098193009.1\|1223870_1224644_+\|DUF3050-domain-containing-protein	gnl\|CDD\|378614	pfam11251, DUF3050, Protein of unknown function (DUF3050). This bacterial family of proteins has no known function.	1.81577e-142
NZ_CP023777.1\|WP_098193001.1\|1211575_1213705_-\|ferrous-iron-transport-protein-B	gnl\|CDD\|223447	COG0370, FeoB, Fe2+ transport system protein B [Inorganic ion transport and metabolism].	0
NZ_CP023777.1\|WP_098193018.1\|1233562_1235431_-\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-enzyme-MnmG	gnl\|CDD\|235362	PRK05192, PRK05192, tRNA uridine-5-carboxymethylaminomethyl(34) synthesis enzyme MnmG.	0
NZ_CP023777.1\|WP_098193019.1\|1235589_1236012_-\|rRNA-maturation-RNase-YbeY	gnl\|CDD\|272871	TIGR00043, Endoribonuclease_YbeY, rRNA maturation RNase YbeY. This metalloprotein family is represented by a single member sequence only in nearly every bacterium. Crystallography demonstrated metal-binding activity, possibly to nickel. It is a predicted to be a metallohydrolase, and more recently it was shown that mutants have a ribosomal RNA processing defect. [Protein synthesis, Other].	1.70782e-31
NZ_CP023777.1\|WP_157760633.1\|1227738_1229292_-\|PAS-domain-S-box-protein	gnl\|CDD\|182070	PRK09776, PRK09776, putative diguanylate cyclase; Provisional.	5.9347e-39
NZ_CP023777.1\|WP_098193014.1\|1229686_1230049_-\|glyoxalase	gnl\|CDD\|319909	cd07245, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	6.59663e-22
NZ_CP023777.1\|WP_098193012.1\|1226431_1227730_+\|MFS-transporter	gnl\|CDD\|340925	cd17367, MFS_KgtP, Alpha-ketoglutarate permease of the Major Facilitator Superfamily of transporters. This subfamily includes Escherichia coli alpha-ketoglutarate permease (KgtP) and similar proteins. KgtP is a constitutively expressed proton symporter that functions in the uptake of alpha-ketoglutarate across the boundary membrane. Also included is a putative transporter from Pseudomonas aeruginosa named dicarboxylic acid transporter PcaT. The KgtP subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	0
NZ_CP023777.1\|WP_098193016.1\|1231307_1231844_+\|CopD-family-protein	gnl\|CDD\|367596	pfam03653, UPF0093, Uncharacterized protein family (UPF0093).	3.83907e-43
NZ_CP023777.1\|WP_098193008.1\|1221655_1223857_+\|DNA-helicase-RecQ	gnl\|CDD\|273594	TIGR01389, recQ, ATP-dependent DNA helicase RecQ. The ATP-dependent DNA helicase RecQ of E. coli is about 600 residues long. This model represents bacterial proteins with a high degree of similarity in domain architecture and in primary sequence to E. coli RecQ. The model excludes eukaryotic and archaeal proteins with RecQ-like regions, as well as more distantly related bacterial helicases related to RecQ. [DNA metabolism, DNA replication, recombination, and repair].	0
NZ_CP023777.1\|WP_098193010.1\|1225125_1225644_+\|damage-inducible-protein-DinB	gnl\|CDD\|225200	COG2318, DinB, Uncharacterized protein conserved in bacteria [Function unknown].	2.18252e-21
NZ_CP023777.1\|WP_098193017.1\|1231836_1233198_-\|oxygen-independent-coproporphyrinogen-III-oxidase	gnl\|CDD\|236430	PRK09249, PRK09249, coproporphyrinogen dehydrogenase.	0
NZ_CP023777.1\|WP_098193005.1\|1217025_1218660_+\|SulP-family-inorganic-anion-transporter	gnl\|CDD\|223732	COG0659, SUL1, Sulfate permease and related transporters (MFS superfamily) [Inorganic ion transport and metabolism].	4.65196e-81
NZ_CP023777.1\|WP_098193002.1\|1213888_1215730_-\|PspC-domain-containing-protein	gnl\|CDD\|377200	pfam04024, PspC, PspC domain. This family includes Phage shock protein C (PspC) that is thought to be a transcriptional regulator. The presumed domain is 60 amino acid residues in length.	4.7391e-25
NZ_CP023777.1\|WP_098193011.1\|1225647_1226319_-\|ribose-5-phosphate-isomerase-RpiA	gnl\|CDD\|234816	PRK00702, PRK00702, ribose-5-phosphate isomerase RpiA.	3.82593e-106
NZ_CP023777.1\|WP_098193006.1\|1218681_1219350_+\|carbonic-anhydrase	gnl\|CDD\|237927	PRK15219, PRK15219, carbonic anhydrase; Provisional.	2.68542e-73
NZ_CP023777.1\|WP_098196101.1\|1220504_1221467_-\|KpsF/GutQ-family-sugar-phosphate-isomerase	gnl\|CDD\|182814	PRK10892, PRK10892, arabinose-5-phosphate isomerase KdsD.	2.86488e-104

>NZ_CP023777.1|WP_098193009.1|1223870_1224644_+|DUF3050-domain-containing-protein
MEIGKIQEAIAPVREKIIHHPLYASLESFEDIQLFMEHHIFAVWDFMSLLKGLQQSLTCVKVPWVPVGSPNTRYFINEIVTGEESDVDAAGNRCSHYELYLQAMQQAGANTEAILSLVAAAQAGIPIQTAISEANLPADIKGFLKFTFDTIESNQPHLMAAVFTFGREDLIPGMFHELVKDMHQKFPGKLDIFQYYLERHIEVDGDHHSILSMQMVAELCGDDARLWKEAEAAAITALEWRYRLWTAVLEEKSKILS
>NZ_CP023777.1|WP_098193008.1|1221655_1223857_+|DNA-helicase-RecQ
MADAKVSLLDALQEHFGFESFKGNQEPIINSILANKDTFVIMPTGGGKSLCYQLPALMSPGCALIVSPLIALMKNQVDLVRSYSSKDNVAHFLNSTLTKAQIKKVRTDLLSGKTKMLYVAPETLTKQENIDFFKDLEISFIAVDEAHCISEWGHDFRPEYRRLKEMIEQINDDLPIIALTATATPKVQSDIVKNLGLREPEIFISSFNRPNLYYEIRQKRKKDQTIKDIVKFIHLHKGKSGIIYTLNRKTTEELASMLSANGIKAVAYHAGLDAGTRAQRQDMFLHEEVEVIVATIAFGMGIDKPDVRFVIHYNIPKSLENYYQETGRAGRDGLEGICVCFYSHKDVQKLEHLMRDKPLSEREMGAQLINETVAYAESAVCRRKVILHYFGEPLEEENCGNCDNCRNPKEKIEVKNRVVIVLKALKELGERFGSEYVVNVIMGNINPQITTYKHDKLAVFGSGKEFDAHFWNSLIRQMMLEGLIEKDIEEYGLLKIKDKGRSFLKKPYSIMVALNHQFDEEAAEDDEEIAAGAQASADSVLFEMLKDLRKTVAKEKNLPPFVIFLETSLEDMATHYPTTTQELEKIQGVSKGKAIRYGKQFLEVITKYVEENDIVKPDDFVMKSVVNKSGLKVFIIQNIDKKIPLETIAKNKELSMSKLLDEMETIVASGTKLNLDYCLDEELDDYAQDEILEYFKNCETSSLALAREELIDSNYTLEQLKLMRIKFLVVYGN
>NZ_CP023777.1|WP_098196101.1|1220504_1221467_-|KpsF/GutQ-family-sugar-phosphate-isomerase
MNENISSIALKTIALEAAAIDNLQGYINEEFEQCVKLLANCTGRIVITGIGKSAIVAQKIVATLNSTGSPALFMHAADAIHGDLGMIGPQDVVIIISKSGESPEIKVLVPLVKGFGNIIIAIAGKKDSYLAQSADYLLDTTVSQEACPNNLAPTTSTTAQMVMGDTLAVCLMELKGFTAADFAKYHPGGTLGKRLYLKVGDLSRLNAKPKVSLQSSLREVIVEISSKMLGVTAVLDEKQHLAGIITDGDLRRMLEKNEATQHLTAKDIMSTQPKTIQQSELAVNALELMRQNNITQLLVMDGPGYAGIIHLHDLIREGII
>NZ_CP023777.1|WP_098193007.1|1219407_1220499_-|mannose-1-phosphate-guanylyltransferase
MTSMNNHFYVAIMAGGIGSRFWPYSRTDYPKQFLDILNTGKSLLQWTYERFVQFIPPENIYVVTHHQYADMVAKQLPELAKDNIVKEPSRKNTAPCIAYISHKIHQKDPKACMICAPADHLIMDSTSFISVCLNALLFVQKHSALLTLGIKPTRPDTGYGYIQYETLQAADNVYPVKTFTEKPDLELAKTFIASGDFLWNAGIFVWNSKTIIAAFKKYLAEIEEMFEANLEAFNTPAEKEVMERIYSQCTNISIDYGIMEKADNVYVIPANFGWSDLGTWASAYENLEKDYLENAVQGKNVMVIDATNNMVRAPHDKLVVLQGLDDFIVVDTSDVLLICKRQNEQQIKEYVAEVKRHKGDKYL
>NZ_CP023777.1|WP_098193006.1|1218681_1219350_+|carbonic-anhydrase
MNAYNKITQESLSPADVLKILRDGNARFVNNLRINRNLLQQMNDTRDGQWPIAAIVSCMDSRTSAELIFDLGLGDIFSIRLAGNVISEFVLGSLEYACAVAGSKFIVVLGHTKCGAIKGACDGVKMGNLTPLLSEIQPSIDAETTITDNRTASNPDFVSAVTNIHVEHSVKIIMERSPILRELIEEGKVGIIGAVYDVENGAVTFCDHTMIINHPKAAPVAG
>NZ_CP023777.1|WP_098193005.1|1217025_1218660_+|SulP-family-inorganic-anion-transporter
MSVKTSPLSNIKGDLSAGLVVFLIAVPLCLGIALASGAPLFSGMIAGIVGGIVVGSLSGSNLSVSGPAAGLTAIVLSAITSLGAFDIFLASVVIAGMIQLALGFARAGVIANYFPSNVITGMLTAIGIIIILKQIPHAFGYDADAEGDMNFIQVDGENTITALLSTLNHIHLGATLICAISILIIVYWNKIPKLKAVPAPLVAVMAGVGINELFVATGSSLAISASHLVSLPVADSFSDFIGQFTTPNFSAFARGDVWVTAATIAVVASIETLLNLEATDKLDPLKRYSSPNRELRAQGVGNIISGFIGGLPVTSVIVRSSANINSGGRTKVSAVWHGILLLSCTALIPVVLNKIPLATLAAVLLVTGYKLCKISIFKKMFAKGKYQWVPFVVTVLAVVFTDLLLGVALGLAVSVIGILRGNLKSPYFFSKEKYRTGDLIRIELAQEVSFLNKANILLTLDHMPKDSTVVIDASTTVYIDNDVLEILREFTQIKAPQKNIKVVLTGFKDVYNIRNTEHIFIEQPGEGQKTNGNHTQLIKELTLN
>NZ_CP023777.1|WP_098193004.1|1216445_1216748_+|hypothetical-protein
MRKFLAILLFGLMCVQLLPIKEVGKLLFNNQIVEEHIDGGCSSKSPVKLVKDFHLNYTEQGSLYDPRFTLISGGHQYFEHLPPNPIQEIQTPPPNFLAIA
>NZ_CP023777.1|WP_098193003.1|1215772_1216108_-|PadR-family-transcriptional-regulator
MNIDNTQSQMRKGVLEFCILSIIKQGEAYPSDIIEKMKEAKLDILEGTLYPLLTRLKNAELLTYRWVESSSGPPRKYFSMTEKGENFYKVLENTWNELANAVHQLTDHSTL
>NZ_CP023777.1|WP_098193002.1|1213888_1215730_-|PspC-domain-containing-protein
MKKIININLSSRLIPIEDSAYDTLRLYLDSLKKYFAQEDGADEIMSDIEGRIAEVFQDKLKKGAHCITDQDIEDIKASMGTPSQLEDETNAGSQGMGAEQAEKKTAFDFEQYIRPTKRFYRDPDHKLIGGVCGGLGAYFNIDPVVFRVLFVVFAVLYGTGFIIYLVLWFATPEAQSTAEKLEMRGEKVDLNNIKTTVQEEMKEFKSRMSNVGTDFKNFSAGRGKQMGSEIGGAVDRLARGFGKFVVFIAKSFFYIFAVILLFVLIGVLITTSFTAAWFPILNTIFTTNQSILFWLSSTLLLGIPILSLIMFLVRKMTGSKYNNKYVGYAFGTFWVIGLVSSILLGISLAKSFRAGAKTMQTVALEDVKGDKLYIKKSDDALVMDNIDFFDSRFRVLEDTAIVDAISLRIIQSNSDRFEMQIDRFSRGRTYSQARSYAESIRIPLVQKDSVIYLPSGFSIPTKLKYRGQRVAIYIKVPKGKTVEVDRSAYWNYRFLGNHDNYWDNDYYDGRVEIKSGKNGLEKVYDSWDRNDDKNLDNSPGQDAAPSAKNKRDSVRQHYRYQQDTSLAPPSGPAVQPKKEKKQENDTANAMKKSIAQVEKFNFLFAPYDKIRQS
>NZ_CP023777.1|WP_098193001.1|1211575_1213705_-|ferrous-iron-transport-protein-B
MQAPLNIALVGNPNSGKSSLFNVLTGLNQKVSNFPGVTVDKKTGSAKISPNLTANIIDLPGTYSLYPKSADEFVTYDVLINPQNRDKPDMILVIADASNLKRNLLFCSQIIDLKIPIIIALTMMDLAKSKGVEIDLPGLERELGVPVVAINPRKNKGMAELRKNIELLASEKFGAPARDFIDNQSLASNVIHDVKEVFPTSSDYAALHVAVNYEELTFLSGSQKKVIGDSIKNNQFNKTKVQAEEIMQRFARIKHVMKAAVVETAPFQKQLQTERIDNILLHRTWGYVILLVVMFLLFQSIFWFASYPMDVIEAGFGSLGGWLTDILPSNNFSDLLINGVIAGLGGIAVFIPQIMILFGLITILEDTGYMARISFLTDRLMRQVGLNGKSVMPLISGVACAVPAIMATRNIENRKERLITILVTPLMSCSARLPIYTIMIALVIPSKTILGFLSLQGLVMMGLYLLGFIMAIMIAAVLKWLIRIKEKSYFIMELPDYRAPRWKNVGTTMVEKAKIFITDAGKVIMVISIILWFLASYGPSKKMDAVHAKFEPLIEQASTDSIRAEIEKSFQSEKLANSYAGILGHAIEPAIRPLGFDWKIGIALITSFAAREVFVGTMATLYSVGEDADENDATLREKMEAATWKDGRPVYTLGAGLSLMLFYAFAMQCMSTLAIVKRETKSWKFPVIQFVYMTVLAYVSSLIIFQLFK
>NZ_CP023777.1|WP_098193010.1|1225125_1225644_+|damage-inducible-protein-DinB
MILTTSKPISNTLSVVMKNFALYNAWANKTMIYWLQSHPEKLMDKETISSFPTIRLTLLHILSCQDFWLSVLEESPQHTPNYELLSTRACFDMLLEQSEQMTAYILSLSDAELSQEVVFTSPWVQGKESRFEYIHHVFNHSTYHRGQIVTMGRNLGITDAPMTDYGYYLTVR
>NZ_CP023777.1|WP_098193011.1|1225647_1226319_-|ribose-5-phosphate-isomerase-RpiA
MEINLAKKAAGEKAAEYVESGMNIGLGTGSTVYYTILKLGEQVKSGMKLKAIATSLATEKLAKECGIPIVDFSATQELDLTIDGADEVDGKWNLIKGGGGALMREKIVAAASREFIVVVDASKKVDYLGKFPLPVEVIPFGWEVTLKHIKALCRTAYLRTKGAEIFVTDNNNYIVDMPIKSIISPKQLELQLREIPGVAVTGLFIGMASKVIVGETDGKVVEL
>NZ_CP023777.1|WP_098193012.1|1226431_1227730_+|MFS-transporter
MSPGKNQHGSAMWRYKAILSGTIGNLVEWYDWYVYTTFALYFAPVFFPGDNKTVQLLNTAAIFAVGFLMRPLGGWIFGKMADQKGRKTSMTLSVLLMSFGSMLIAFTPGYHSIGIMAPVLLLVARLLQGLSVGGEYGSSATYLSEIAPASRRGFFSSFQYVTLIGGQLLALSIQVLLQKVILTHEQLASWGWRIPFVIGALLAIVALYMRKNMEESLHLSPKVQEKGSLKLLLKQHPKAVFTVVGLTLGGTLAFYTYTTYMQKFLVNTVHLSIERSSMLTFYLMLIYAAIQPLFGLLSDKIGRKPLLMGFGILGTIFTVPILATLSHVTEEWQAFLLILAALIIVSGYTSINAVVKAELFPAQIRALGVGLPYALTVAIFGGTAETVALYCKKIGHEQYFYFYVATCIFISLIVYTLVKDTKTTSYIDHEKH
>NZ_CP023777.1|WP_157760633.1|1227738_1229292_-|PAS-domain-S-box-protein
MQRKFMFIHQIDHQIDNGITEAILNTIDEGILLVSNEGIIKGCNRQALEIIKLSSDQVLGKSYKDEMWIATTEELMPISSEQFPIATSIKSGSPVKNFVMGLKVDKVSIWINVNTHILEIKNERFILASFYDISEPIRARRSLQMLTNQLIEKDKQLLIDQKFTNAFHYASIGIALVTDTGLFVDVNNSLCQMLGYSKEELLSLNFQSLTHPGDLEIDLDFVRKMLNNELDTYQMEKRYYHKNGSIIWVLLSVSMVRDPYSPMFISQIVNISEHKKLIDDLNSNNIILGRTSGELQRRVNQLSEFNQIVAHNLRGAAGNIISLLGLMKDSRDEQERMMYFPYLEQSSKALMDILNNLIKLLHVRLNNEPVNQEMLNINKSIDQCIYQLYQEIHSSKAMIRMDLQVLHVKYNKAYLDSIIYNLLSNAIKYAKRDTAPIILISTYKKDGACYLDVADNGMGIDLDRFGDQLYKANKNFHKTKNSHGFGLYILKNQLDAMNSEITVESALGKGTKFTVRL
>NZ_CP023777.1|WP_098193014.1|1229686_1230049_-|glyoxalase
MIQFERIHHVQLCIPIDAEDQAREFYGTILGLQEIERPLSLQDRPGMWFKMGNIELHIGLEESSLSKRHPAFEVKDIEFTRAYCISKGIKVKDEIPIPGQTRFSIWDPFENRIELLERWK
>NZ_CP023777.1|WP_098193015.1|1230147_1231041_-|hypothetical-protein
MNTQLNQLCILYGKALQQELNNLLDTFQFLSKEEIEHYKSMNIGIIAANLYPDAQFERLQTISRLLLWMLLCKDVYSFYSSKQLKPIHQCYLLAFEGKPNAACDDELCMLIQTLGAEVRKFASTSCWYRFIFHFNDYLKGIRWMTDIKQSTVCPVFSKYIVQCEQYSFTHMLIDFMEIAIGAPLSTNILHSSLYQRHINISNRALMISMELQPRDQFPGSLRWNFEDCLSKKQQLSYQVAFHDLENLRTKLLEENLRQQEELQGVFRREKLLDEYLLTFQQMIYSLSPDWNNNIDIS
>NZ_CP023777.1|WP_098193016.1|1231307_1231844_+|CopD-family-protein
MHYLSIKALHIIFIVTWFAGMFYIVRLFVYNTEAQTEVEPKKSILQEQFTIMIKRLWYGITWPSAIITLILGPYLLYQYGTIQPWMWVKLGFVLALYLYHLSLHKLVKEQQNGIFRYSSTQLRIWNEVATVLLVAIVFLVVLKSLAGLAWGISGLMAFTLLLLLAIRIYKKIRDRKSK
>NZ_CP023777.1|WP_098193017.1|1231836_1233198_-|oxygen-independent-coproporphyrinogen-III-oxidase
MDQQDLLLKYNIPAPRYTSYPTVPYWNESMNTLSWKEMFYEQFKIHNLKEGLALYIHLPFCESLCTYCGCNKKISLQHHVELPYVEAVLKEWKMYLNLMNQAPIIREIHLGGGTPTFFSPENLVRLLTTIFNDAIIHPQYEFSFEGHPNNTTREHLEALYQLGFRRVSFGVQDNDPVVQKAINRIQPLENVKSVTGWARDTGYTSVNYDLIYGLPFQNTSGLEKTLHEVLSLRPDRIAFYNYAHIPWKSKSQRLYSEQDLPLAQDKIKLYTLGKEIFMDYGYVDIGMDHFALAHDSLVKAKYLKNLHRNFMGYTQTNTSLLLGLGVSSISDASKAYAQNEKELKTYYESIAAGELPIAKGLLLDKKDEYFRQHILNIACNGTTTLDQEFPVEVNKIVLPRLKELEADGLVEIRGKTVFLTAIGQQLTRIVCHAFDLYASGQQEKIQNQFSKAI
>NZ_CP023777.1|WP_098193018.1|1233562_1235431_-|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-enzyme-MnmG
MFPSYDVIVVGAGHAGCEAAAAAANMGSKVLLVTMNMQTIAQMSCNPAMGGIAKGQIVREIDALGGYSGIVTDQSMIQFRMLNRSKGPAMWSPRTQNDRMLFAAKWREALENTSNIDFYQDMVKGLLVKNNTCYGVVTGLGHEIKAKAVVLTNGTFLNGVIHIGDKTFGGGRVAERAATGITEQLIELGLESDRLKTGTPPRIDGRSLDYSKMEEQKGDEEIIGFSYLDVKKIQPSEQRSCHITYTNSKVHELLKTGFDRSPMFQGRIQGVGPRYCPSIEDKINRFAERDRHQLFVEPEGFDTVEIYVNGFSTSLPEDVQYKALQSVPGFENCKMFRPGYAIEYDYFPPTQLKFSLETKLIGNLFFAGQINGTTGYEEAACQGLMAGMNAHLKTKGQDPFILKRSEAYIGVLIDDLINKGTDEPYRMFTSRAEFRTLLRQDNADLRLTERSHLMGLAKEERMEKVNVKREGVEKIKKILKELSLDPSDINGYLEANNSSPLTQKQRALQVLLRPNIDIFSMKEQVLKLKQALEGFDIDTLQQAEIQIKYEVYIEKENELVKKMSQLEDLVIPDSFDYSKLVSLSAEAKQKFMKIKPRTLGQASRISGVNPSDVQILMVYMGR
>NZ_CP023777.1|WP_098193019.1|1235589_1236012_-|rRNA-maturation-RNase-YbeY
MAVRFSNLDVKLVLEDKTRLKKFIAELFKRESQGLQDLQYVFCTDAYLLEINQQFLDHDTYTDIITFELSPNPDITEGEIYISVERVQENATAFEESFNRELHRVIFHGALHLCGYRDKSDTEEKLMRQKEDEYLSLYFA

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Crispr_ID: NZ_CP023777_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_5

1725909-1726646

TypeII

Consensus_repeat	Method
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	PILER-CR
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	CRISPRCasFinder

9 spacers

cas2,cas1,cas9

The CRISPR arrays of NZ_CP023777_5

>merge|NZ_CP023777|5|1725909-1726646|PILER-CR,CRISPRCasFinder
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTCAAGGTTAAGGGGATTAATTGCTTTTGCGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACGTCCTTTGTGATGGCACCTATACGCAACTTGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTTTTCAGCCACGGTATAAACTAATTCTAGAGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACGCAAGCCCCTTAAAATCAATTTCTAGCAGGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTATGTCTGTATATGCAATTAATGTAAGCGCGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTGATAAAGTAAAGGAAGAAAGCGATAGGTGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTGGTATGGTTAGCGGCGCATTACGGCAGCTGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACAAATTTGGAGCGTTTTCGGGAACGAATTTAGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACGAGGGAGGGCGGCGATGACCAGCCCGATGAGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGTGGAACTGCTAC

>NZ_CP023777|5|1|1725909-1726568|PILER-CR
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TCAAGGTTAAGGGGATTAATTGCTTTTGC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GTCCTTTGTGATGGCACCTATACGCAACTT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TTTTCAGCCACGGTATAAACTAATTCTAGA
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GCAAGCCCCTTAAAATCAATTTCTAGCAG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TATGTCTGTATATGCAATTAATGTAAGCGC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TGATAAAGTAAAGGAAGAAAGCGATAGGT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TGGTATGGTTAGCGGCGCATTACGGCAGCT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AAATTTGGAGCGTTTTCGGGAACGAATTTA
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC

>NZ_CP023777|5|5|1725909-1726646|CRISPRCasFinder
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TCAAGGTTAAGGGGATTAATTGCTTTTGC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GTCCTTTGTGATGGCACCTATACGCAACTT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TTTTCAGCCACGGTATAAACTAATTCTAGA
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GCAAGCCCCTTAAAATCAATTTCTAGCAG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TATGTCTGTATATGCAATTAATGTAAGCGC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TGATAAAGTAAAGGAAGAAAGCGATAGGT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TGGTATGGTTAGCGGCGCATTACGGCAGCT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AAATTTGGAGCGTTTTCGGGAACGAATTTA
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GAGGGAGGGCGGCGATGACCAGCCCGATGA
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGTGGAACTGCTAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098193378.1\|1726692_1727010_+\|transposase	unknown	unknown	gnl\|CDD\|225511
NZ_CP023777.1\|WP_098193381.1\|1730542_1731037_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098193377.1\|1725482_1725818_+\|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|226043
NZ_CP023777.1\|WP_098193384.1\|1732782_1733019_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_157760679.1\|1733539_1734118_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274376
NZ_CP023777.1\|WP_098193369.1\|1714395_1714809_+\|OsmC-family-peroxiredoxin	unknown	unknown	gnl\|CDD\|274650
NZ_CP023777.1\|WP_098193370.1\|1714950_1715811_-\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP023777.1\|WP_098193383.1\|1732058_1732802_+\|ImmA/IrrE-family-metallo-endopeptidase	unknown	unknown	gnl\|CDD\|368753
NZ_CP023777.1\|WP_098193380.1\|1729893_1730172_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379565
NZ_CP023777.1\|WP_157760677.1\|1718124_1719861_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|143479
NZ_CP023777.1\|WP_098193387.1\|1734194_1735349_+\|FecR-family-protein	unknown	unknown	gnl\|CDD\|226235
NZ_CP023777.1\|WP_098193382.1\|1731727_1732066_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|376540
NZ_CP023777.1\|WP_098193371.1\|1715898_1716831_+\|NADP-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|176191
NZ_CP023777.1\|WP_157761068.1\|1726937_1727867_+\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|222853
NZ_CP023777.1\|WP_098193376.1\|1724572_1725469_+\|type-II-CRISPR-associated-endonuclease-Cas1	cas1	cd09720_cas1_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|274694
NZ_CP023777.1\|WP_098193375.1\|1720327_1724560_+\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|375967
NZ_CP023777.1\|WP_098196129.1\|1713746_1714331_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP023777.1\|WP_098193385.1\|1733067_1733391_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|181371
NZ_CP023777.1\|WP_098193372.1\|1716877_1717273_+\|DoxX-family-membrane-protein	unknown	unknown	gnl\|CDD\|311556
NZ_CP023777.1\|WP_098193373.1\|1717450_1718122_+\|DNA-alkylation-repair-protein	unknown	unknown	gnl\|CDD\|132880

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098193378.1\|1726692_1727010_+\|transposase	gnl\|CDD\|225511	COG2963, COG2963, Transposase and inactivated derivatives [DNA replication, recombination, and repair].	3.01606e-07
NZ_CP023777.1\|WP_157760679.1\|1733539_1734118_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	1.25159e-28
NZ_CP023777.1\|WP_098193377.1\|1725482_1725818_+\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	2.07784e-26
NZ_CP023777.1\|WP_098193369.1\|1714395_1714809_+\|OsmC-family-peroxiredoxin	gnl\|CDD\|274650	TIGR03562, osmo_induc_OsmC, peroxiredoxin, OsmC subfamily. pfam02566, OsmC-like protein, contains several deeply split clades of homologous proteins. The clade modeled here includes the protein OsmC, or osmotically induced protein C. The member from Thermus thermophilus was shown to have hydroperoxide peroxidase activity. In many species, this protein is induced by stress and helps resist oxidative stress. [Cellular processes, Detoxification].	1.35922e-56
NZ_CP023777.1\|WP_098193370.1\|1714950_1715811_-\|AraC-family-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	4.64473e-24
NZ_CP023777.1\|WP_098193383.1\|1732058_1732802_+\|ImmA/IrrE-family-metallo-endopeptidase	gnl\|CDD\|368753	pfam06114, Peptidase_M78, IrrE N-terminal-like domain. This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.	3.7853e-13
NZ_CP023777.1\|WP_098193380.1\|1729893_1730172_+\|hypothetical-protein	gnl\|CDD\|379565	pfam14338, Mrr_N, Mrr N-terminal domain. This domain is found at the N-terminus of the Mrr restriction endonuclease catalytic domain, pfam04471. Fold recognition analysis predicts that it is a diverged member of the winged helix variant of helix turn helix proteins. It may play a role in DNA sequence recognition.	0.00778263
NZ_CP023777.1\|WP_157760677.1\|1718124_1719861_-\|hypothetical-protein	gnl\|CDD\|143479	cd07563, Peptidase_S41_IRBP, Interphotoreceptor retinoid-binding protein; serine protease family S41. Interphotoreceptor retinoid-binding protein (IRBP) is a homolog of the S41 protease, C-terminal processing peptidase (CTPase) family. It is thought to facilitate the compartmentalization of the visual cycle that requires poorly soluble and potentially toxic retinoids to cross the aqueous subretinal space between the photoreceptors and the retinal pigment epithelium (RPE). IRBP is secreted by photoreceptors into the interphotoreceptor matrix (IPM) where it is rapidly turned over by a combination of RPE and photoreceptor endocytosis. It is the most abundant soluble protein component of the IPM, consisting of homologous modules, each repeat structure arising through the duplication (as in teleost IRBP) or quadruplication (in tetrapods) of an ancient gene, arisen in the early evolution of the vertebrate eye. IRBP has been shown to promote the release of all-trans retinol from photoreceptors and facilitates its delivery to the RPE. Conversely, IRBP can promote the release of 11-cis-retinal from the RPE, prevent its isomerization in the subretinal space, and transfer it to photoreceptors. In vivo evidence implicates IRBP as a retinoid transporter in the visual cycle, suggesting a critical role for IRBP in cone function essential for human vision. IRBP is a dominant autoimmune antigen in the eye; IRBP proteolysis analysis has proven a useful biomarker for autoimmune uveitis (AU) disorders, a major cause of blindness. This family also includes a chlamydia-secreted protein, designated chlamydia protease-like activity factor (CPAF), known to degrade host proteins, enabling Chlamydia to evade host defenses and replicate.	2.74771e-12
NZ_CP023777.1\|WP_098193387.1\|1734194_1735349_+\|FecR-family-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	5.32977e-21
NZ_CP023777.1\|WP_098193382.1\|1731727_1732066_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|376540	pfam01381, HTH_3, Helix-turn-helix. This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within Neisseria gonorrhoeae NGO_0477, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteristic of the whole family.	5.02737e-13
NZ_CP023777.1\|WP_098193371.1\|1715898_1716831_+\|NADP-dependent-oxidoreductase	gnl\|CDD\|176191	cd05289, MDR_like_2, alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases. Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	7.35376e-113
NZ_CP023777.1\|WP_157761068.1\|1726937_1727867_+\|IS3-family-transposase	gnl\|CDD\|222853	PHA02517, PHA02517, putative transposase OrfB; Reviewed.	1.44526e-70
NZ_CP023777.1\|WP_098193376.1\|1724572_1725469_+\|type-II-CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|274694	TIGR03639, cas1_NMENI, CRISPR-associated endonuclease Cas1, subtype II/NMENI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is a prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 variant of the NMENI subtype of CRISPR/Cas system.	1.26222e-103
NZ_CP023777.1\|WP_098193375.1\|1720327_1724560_+\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	gnl\|CDD\|375967	pfam18541, RuvC_III, RuvC endonuclease subdomain 3. Cas9 proteins are abundant across the bacterial kingdom, but vary widely in both sequence and size. All known Cas9 enzymes contain an HNH domain that cleaves the DNA strand complementary to the guide RNA sequence (target strand), and a RuvC nuclease domain required for cleaving the noncomplementary strand (non-target strand), yielding double-strand DNA breaks (DSBs). The crystal structures of type II-A and II-C Cas9 proteins highlight the features in Cas9 enzymes that support their function as RNA-guided endonucleases. Cas9 enzymes adopt a bilobed architecture composed of a nuclease lobe containing juxtaposed RuvC and HNH nuclease domains and a variable alpha-helical lobe likely to be involved in nucleic acid binding. The RuvC domain forms the structural core of the nuclease lobe, a six-stranded beta sheet surrounded by four alpha helices, with all three conserved subdomains (I, II, III) contributing catalytic residues to the active site.	1.35646e-56
NZ_CP023777.1\|WP_098196129.1\|1713746_1714331_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	3.90774e-11
NZ_CP023777.1\|WP_098193385.1\|1733067_1733391_+\|hypothetical-protein	gnl\|CDD\|181371	PRK08306, PRK08306, dipicolinate synthase subunit DpsA.	0.000727749
NZ_CP023777.1\|WP_098193372.1\|1716877_1717273_+\|DoxX-family-membrane-protein	gnl\|CDD\|311556	pfam07681, DoxX, DoxX. These proteins appear to have some sequence similarity with pfam04173 but their function is unknown.	0.000400606
NZ_CP023777.1\|WP_098193373.1\|1717450_1718122_+\|DNA-alkylation-repair-protein	gnl\|CDD\|132880	cd06561, AlkD_like, A new structural DNA glycosylase. This domain represents a new and uncharacterized structural superfamily of DNA glycosylases that form an alpha-alpha superhelix fold that are not belong to the identified five structural DNA glycosylase superfamilies (UDG, AAG/MNPG, MutM/Fpg and helix-hairpin-helix). DNA glycosylases removing alkylated base residues have been identified in all organisms investigated and may be universally present in nature. DNA glycosylases catalyze the first step in Base Excision Repair (BER) pathway by cleaving damaged DNA bases within double strand DNA to produce an abasic site. The resulting abasic site is further processed by AP endonuclease, phosphodiesterase, DNA polymerases, and DNA ligase functions to restore the DNA to an undamaged state. All glycosylase examined to date utilize a similar strategy for binding DNA and base flipping despite their structural diversity.	1.2062e-26

>NZ_CP023777.1|WP_098193377.1|1725482_1725818_+|CRISPR-associated-endonuclease-Cas2
MNSRYSAYRVMWILVFFDLPTETKRDRKNYAKFRKQILSDGFAMFQFSIYIRHCNSKENADVHMKRVKGILPPKGHVGIMCVTDKQFSMLEIFRGKVGIDPPPTLQQLELF
>NZ_CP023777.1|WP_098193376.1|1724572_1725469_+|type-II-CRISPR-associated-endonuclease-Cas1
MIKRTLYFGSPAYLKTNLEQLQIELPKTGETKIAPIEDIGLLILDHQQITITQALLAKLLAQNVAVITCDHTHHPVGLLLNLDGNTLQSQKFRAQVEASVPLKKQLWQQTVITKISNQAKLMAMERLEHQRLLKLAGAVKSGDSDNCEAQAATYYWKNLFPDFLQFRRERYGPPPNNLLNYGYAILRALVARSLVGSGLLPTLGIFHRNQYNAYCLADDIMEPYRPFVDKIVCHIVSMNGRFLEMTPRMKEQLLSIPTMDVLVQGRKSPLMHAVQRSTASLAKCFEGSARKIIYPELI
>NZ_CP023777.1|WP_098193375.1|1720327_1724560_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9
MVKNVLGIDLGVTSIGWAFVHEDTNFGELSKIVQAGVRLVALSTDEQLEFEKGKPLSINANRTLKRSMRRNLQRYKMRRKQLIKLFKQYNIIPEDAILAEDGKHTTFETYELRAKAVHEKISLLQFARVLLMLNKKRGYKSSRKVQSEEEGQAIDGMDVAKKLFHDKITPGQYCLELLKNEKKSLPSFYRSDLQDEFMKVWNFQMAFHPSILTTDLLKKLDGVGQKATAAIFYKELNITTAEIKGKRDEKKLASYQLRSDAIQKELSIEEVAFVLAQVNNDINSSSGYLGAIGDKSKELFFNKQTVGEYLYKQLKENPHARLKNQVFYRQDYLDEFERTWSCQAQFHPELTNDLKKEIGDITIFYQRKLKSQKGLISLCQFEQQKRLVTKNGRQIIKTTGYRVCPKSSPLFQEFKVWQNLQNVEIKADGVKGRLSEEQKQLLFEHLNMKGELSKTEALKLLKLNPKTADMNFTKLEANRTNNTLYNVYCRILEDAGYDLADILKVKSDKDQITVSDSTLPAKEITRIIAEIFGSLGIKTSILDFDAQLDGKAFEKQDSYLLWHILYSYESDDSASGNEKLYQTLEKKFGFSKEQAKVLASISFEDDYANLSTKALRKIMPFIITNKYDEACALASYNHSNSLTKEEKESRKLEDRLELIPKNSLRNPVVEKILNQLVHVINAIIEDPNMGKPDEIRIELARELKKNAAEREEMSRQIAQADRDHKAIRDTIQKEFGIANPSRNDIIKFKLYEELSFNGYHDLYTNAYINRKELFSNKYDVDHIIPQQSLFDDSFSNKTLTPRDVNLNKGNRTAYDYIEQVHGAEKLEAFKSRVQDYLDKNIKANPGAKAKAKKLLMPASEIGDGFIERDLRNSQYIAKKARTILETICRDVVATSGSITARLREDWDLMNIMQELNLPKYRAINYTELRERKDGSQKEVIKDWTKRNDHRHHAMDAITVAFTKHNHVQYLNYLNARKNESHKMHGNIIAIEKKETEYIQDKDGNGKKRFKSPMPNFRVAAKKALEEILVSFKAKNKVVTNNRNRYKVKKLKEGVQYPPIQLTPRGSLHKETVYGILHRYNTKEETIGAKFNAELIETVANPKYKAALLQRLAANGHDPKKAFTGKNSPAKNPIYINGEGSEVLPAKVKVVKLEPEYTIRKDITPENFSDEKSIMKVIDVGIRNILLERLKASKDAKEAFSNLDINPIWLNKAKDGDPSKNIPIKRVTITGVSNAEALHHKRDHLGNHILDKEGNKQPVDFVSTGNNHHVAIYRDANGKLQDKLVSFYEAVERANQGLPIIDKSYNQGEGWQFLFTMKKNEYFLFPGDGFDPKEVDLLDPKNKTLISKYLFRVQKLADRYFVFRHHLEAKEDDNLTLKGMTFHRLQSLEPLDGIIKVRINHLGNIVKVGEY
>NZ_CP023777.1|WP_157760677.1|1718124_1719861_-|hypothetical-protein
MKKCIYFLLISMTHLCASAQKNSYTVFFKTWNYLKYYHPDFATGKLNADSLFLQDVKKITATTDHNAVIALLTNNLQQHFSTAAAKATATDVIKSNQDFSWFRESAGIDKGHKQLLENIYQHRFTGPQHYYIPNNGYEADIPHEKVYDFPKEENLPLEYRLLALAKIQGCIDYLYPHKQLMNKNFDAYFESLLSRTITCQSRKDFEIILAKLVAPLEDTHAFSFYKQLHFAKDIFHTKLYAPFDYSVFDHYLLVTKLMIPDACQKAGIHAGDRIVAVNGKSIQDIIQSKKELLSASNPSVLLYRISQYQDNLIWPDDMALKKLAIQRNNSGDTVETAIEFIKPTDKKHIDSIVQYLNDEAKRKRQHRLEHPGIAYFRIDQTYKFISGVADDHIDQTMDSLLLAASQQKAIIFDMRGYPDWGGFVYTYIYKYFADKDNYFGKYYQQYHQNIGTFIYADQPAIYFPVLTNKSRHTYNGKVFIIVNPQTLSASEWNTMNLQYIFPGSVTIGQQSAGADGDIKRMALPGNYSLEFTGNGIFYPGGAPAQKVGVHIDEKITYRDIDLLKGQDLEFDWIIKEIL
>NZ_CP023777.1|WP_098193373.1|1717450_1718122_+|DNA-alkylation-repair-protein
MTLKETLAKLESLGSEKMRLQHKKAGASDHQYGVKMGDIRKVAQSIKSDHELALELWDTGIIDAQFLAILIMKPKKVSKDDIKELIRSVQFVNVVDWLYSYIIKAHPDKEALRLEWMKSKDPVAARLGWSLTSGRVAREPEGIDIEALLDRIEKEMPKAAPQVQWTMNSTLAQIGICMPGYRERALSIGEKLGIYRDYPVSKGCTSPFAPIWINEMVRRNNQG
>NZ_CP023777.1|WP_098193372.1|1716877_1717273_+|DoxX-family-membrane-protein
MNKTSYLLLRLGVALSMFGHGLVRLPKLNAFSGWMMKSFEQSWMPAPAVQAFSYALPIAEFIVGLLLVLGLFTRQALVAGAIVMLLLIFGTTVVENWEALPAQLVHLAFFAVLLHFLSSNSFAMDIKRNVS
>NZ_CP023777.1|WP_098193371.1|1715898_1716831_+|NADP-dependent-oxidoreductase
MKAILLQKPGGTENFEYQDIHKPAIHPGEVLIEVKAISINPVDIKTRMGKGVYGRIKDESPLILGWDVSGLVVESLSDEYKAGDEVFGMIRFPGHGKAYAEYVAAPAAHLAKKPGNVSHEEAVAATLAALTAYQVIVEQAQVKDGQKVLIHAASGGVGHYAVQVAKSLGAYVIGTSSEKNRDFVLGLGADEHIDYHTADLDALKDIDFALDALGDANVLRTIPLMKKGGTIISIPSGLGQEVVEAAKVNQVNAGFSMVQSSGENMKAIADLLANGTLRSHVSTAFSFDDITGAHQQIESGRTVGKIVLTF
>NZ_CP023777.1|WP_098193370.1|1714950_1715811_-|AraC-family-transcriptional-regulator
MKQELLHAPYSISYITLDEGPEPAHRHHFFELVYIISGTGTQCINQSKFDYHDGHMFLVTPEDCHSFDIKSTTTFFFLKFNNIYLKDSGIPGENIQRLEYILQNASHKQGCILKNLTDKQLVRPVVEAIIRETINQDIYNRELIQQLVNTLIVVVARNIAKFQQLDVSEQTEAKALDILHYIQNNIYDPEKLKADHLGKQFNISSAYLSRYFKQHTGETMQQYLGNYKTQLIVHRLLHSDKRITEIANEFNFTDESHFNKYFKKQKGLSPKEFRKQAREKVVEKMA
>NZ_CP023777.1|WP_098193369.1|1714395_1714809_+|OsmC-family-peroxiredoxin
MKRKAIAVWNGDIKSGAGHLTTQSTTLNKTQYSFNSRFADGVGTNPEELLAAAHAGCFTMKLDLDLTQAGYTVESLETESVITLDNGKITLSELTLKAKVPGITEEKFQELAAGAEKTCPVSNAFSFEIKLNATLIA
>NZ_CP023777.1|WP_098196129.1|1713746_1714331_+|TetR/AcrR-family-transcriptional-regulator
MAGRPKIYDEDAILEKALNVFWEKGFENASADDLLKAMGIGKGSFYLAFKGGKQELFEKTMDRVVHRHFDEFRKGVQSCANPVRLVKDFFLSLVTEQSPVGDKGCYFGNALVQVSDQNLQLKLQAVKNLDILEAIFKEAMDRGKKMGLLETKLSSKELALYLVNLWNGINITKRMQHEPKALKQLMLLNLDIIA
>NZ_CP023777.1|WP_098193378.1|1726692_1727010_+|transposase
MSKKERRSYDKSFKLMAVELRRSGKPAVTVAKELGIAAEMLRRWTREFSVHDTRSFPGNGKQDLTPEQKEIQALKKALQEAELENRILKKAVSIFSREDNKYSGS
>NZ_CP023777.1|WP_157761068.1|1726937_1727867_+|IS3-family-transposase
MGKSDTKKGSEHFLQGRQQIFRFIKDHQAEFDVEKMCKVFKVSRSGYYAWSIRKPSKLSLYRQVLCKGVEDIYHKSKGRYGSPKIVAELRSMGLHASRPRVARIMKDKGFRSIITGKFKVCTTDSNHKLEVSANILNREFTARAPSEKWVSDLTYIRTKNGWLYLTAIMDLFDRRIVGWSMSTGMTTRETTVAAWNMAIRNRSVAPNMVFHSDRGVQYASEEFRDLLKGNSVQQSMSRKGNCWDNAVMENFFKILKSETGHHTVYDSVEVAKKELFEFIEIWYNRQRRHSILGYLPPEEFSKSILKKAA
>NZ_CP023777.1|WP_098193380.1|1729893_1730172_+|hypothetical-protein
MNTMHQRSVNINVLKLLNDELHSLQDIFQEQVCEMLNLSPEALAQKLENEAICFNLAEQQALAAIFNDLADNLSKYNADYMLEDYIQDAVVA
>NZ_CP023777.1|WP_098193381.1|1730542_1731037_+|hypothetical-protein
MKNMNIFNAEIPQEKIQSAINKIDEAFNELKPYLITLQPEERQMLPKMGNKMFSFVNKVHELAKRNPDLAPSFFSIEDLEIDVAGAQSLEPLLNAVKQLYDGIDDTRMKCGSEAYTNSLAFYSSVKVASKHSVQKAKAVYDDLSGHFIKGANTESAPAAENKPA
>NZ_CP023777.1|WP_098193382.1|1731727_1732066_+|helix-turn-helix-transcriptional-regulator
MTNADTIIRTLREKFGYSQEVVANFLGVKREMISYYETGAREAPLEVLEKLADLFGVDLDIFFSDTMEAASTELAFAFRANEFNEKDLESIAAFRRVIKNYQRITNLEGKNA
>NZ_CP023777.1|WP_098193383.1|1732058_1732802_+|ImmA/IrrE-family-metallo-endopeptidase
MLKERYLEFRANKFREEHGLTPTEPADVYKLLARLNVITVFKEITGNFSGMAVKNGTGNFMMVNSNDILARQHFTIGHELYHLIIQENFKNRICEVGTFDKKDSEEYNADWFASYLLMPEGGIFELLPREELSLNKISLNTIVKMEQYFGVSRAALLNRLMFIDLVSKAKKDELQTTGSIKRSALLMGYSSELYENGNAGKVIGDYGEKAKKLYDKELISETDFYGLMLDIGIDLDTKFEEDDKTER
>NZ_CP023777.1|WP_098193384.1|1732782_1733019_+|hypothetical-protein
MTKQKGDPKILLDADVVIHFLKAGYQMMLPAIFPHRLVMLDKVKQELIKRKSEALGIENFLYWCKIPVEPMPKDFEIL
>NZ_CP023777.1|WP_098193385.1|1733067_1733391_+|hypothetical-protein
MAVARFRNEFIASSNVKDIKDYCELYGIVYFTTMDILEVAITNSIMTESQCDSFIYEVKQKGSKLPCDTMAAYRKRNEKWVSLQLLNRYMSRNFINTFSTPGFSPCY
>NZ_CP023777.1|WP_157760679.1|1733539_1734118_+|sigma-70-family-RNA-polymerase-sigma-factor
MSSFSTYTDLQLLESLKFSEEGAFTEIYNRYWEKLYKSAYNKLNNGEDAKEIVHDVLLDIWKRRADLSIEHLPAYLEKAVRFRVINHINRKKSTALIDSFESVLQSPFKADSEVNMNEFIKLLEAWIAVLPGKQREIFVKYYFDNLSTQEIAVEMNLSRKTVQNNLSITTQYLKARFKHLSILLLLLTNPPH
>NZ_CP023777.1|WP_098193387.1|1734194_1735349_+|FecR-family-protein
MLSEKDKIYLRQVLERYETGRATPEEIHFVEVYMDYLDELHKDVDPLHNLGAEGKPGIEQEIKERLFESIHNTPVPVINIHRRPRFTWQAAAAIIFVILGAATTWILYNQYNKHPSIVAMEDVGPGAERAVLKLGNGRVIMLDTSRGNIVQSGGLTVANDSGILNYQGKAAVAEYHTLSVPRGGQYKLQLPDGTDVWLNAASSITYPTFFDGSERLVKVTGEVYFEVAQMAGKPFRVKSPNGSDIQVLGTRFNINSYADEPTLKATLLEGAIRFNTATEHQVMKPGQQAILNKSGSLEILSNVNTEAVTAWRKGYFYFDATDLQTVMRQIARWYDVTVTYEGEVPDMKFSGEISKSNNISLVLEMLKANNIRFEIKGRKIIVKP

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Crispr_ID: NZ_CP023777_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_6

1727943-1729523

TypeII

Consensus_repeat	Method
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	CRISPRCasFinder
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	PILER-CR

19 spacers

cas2,cas1,cas9

The CRISPR arrays of NZ_CP023777_6

>merge|NZ_CP023777|6|1727943-1729523|CRISPRCasFinder,PILER-CR
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACGGTAAAATCAAGGGGTTCGTCATTTAAAGGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACAAGCGCAAGCCTCGTCCCACATCTGAGTCGGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACAAAGATGTTTTTGATATTTTAGACCTAAATGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTATCTCATTTATTTGCCTTGATGATAAATTGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACGCTCCATTCAACCAATTTGCCGCTTTGCTCGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTACTGAGTTCAATGAATATTTCTTGCCAACGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACGACAATTAAATGATAAAAACTATGTTAGAGGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTAACCCTGTAGGTGATAGACGGTTAGTTCCGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACCTAGCTACGTGGATTTATGTTACAAATTGTGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACGGCGCCTGTATTTCCTAAAATAAAAATTAAGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTATCATAATGACAATGCTTTTTACCAGATGGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACAGCCGTCACGAAGCAGTAATCGCTAAAATTGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACACGGAAGCATCAGGCACGTCTAGTACAATTGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACAAAGTTTCGAATTAGAATCAAATGACCACGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACACCATCATGTAATCATCTTCAGGTACCGGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACAATACGCAGTAGAGGTATATCCATTGCTCCGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTCACTTGGAATGTTGTACGCCTTTCCAAGGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACCAACGCCTTTAATGCCCAGGATGTTAATTGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACCGATCGCTGTGTTGGGGTGTTTTCCTATTTGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACTAACGCGGTTACTACGCGAGGATGTTCGACGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATAAGGAT

>NZ_CP023777|6|6|1727943-1729523|CRISPRCasFinder
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GGTAAAATCAAGGGGTTCGTCATTTAAAG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AAGCGCAAGCCTCGTCCCACATCTGAGTCG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AAAGATGTTTTTGATATTTTAGACCTAAAT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TATCTCATTTATTTGCCTTGATGATAAATT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GCTCCATTCAACCAATTTGCCGCTTTGCTC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TACTGAGTTCAATGAATATTTCTTGCCAAC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GACAATTAAATGATAAAAACTATGTTAGAG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TAACCCTGTAGGTGATAGACGGTTAGTTCC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	CTAGCTACGTGGATTTATGTTACAAATTGT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GGCGCCTGTATTTCCTAAAATAAAAATTAA
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TATCATAATGACAATGCTTTTTACCAGATG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AGCCGTCACGAAGCAGTAATCGCTAAAATT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	ACGGAAGCATCAGGCACGTCTAGTACAATT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AAAGTTTCGAATTAGAATCAAATGACCAC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	ACCATCATGTAATCATCTTCAGGTACCGGTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAACAATACGCAGTAGAGGTATATCCATTGCTCC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TCACTTGGAATGTTGTACGCCTTTCCAAG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	CAACGCCTTTAATGCCCAGGATGTTAATT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	CGATCGCTGTGTTGGGGTGTTTTCCTATTT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TAACGCGGTTACTACGCGAGGATGTTCGAC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATAAGGAT

>NZ_CP023777|6|2|1728019-1729446|PILER-CR
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AAGCGCAAGCCTCGTCCCACATCTGAGTCG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AAAGATGTTTTTGATATTTTAGACCTAAAT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TATCTCATTTATTTGCCTTGATGATAAATT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GCTCCATTCAACCAATTTGCCGCTTTGCTC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TACTGAGTTCAATGAATATTTCTTGCCAAC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GACAATTAAATGATAAAAACTATGTTAGAG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TAACCCTGTAGGTGATAGACGGTTAGTTCC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	CTAGCTACGTGGATTTATGTTACAAATTGT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	GGCGCCTGTATTTCCTAAAATAAAAATTAA
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TATCATAATGACAATGCTTTTTACCAGATG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AGCCGTCACGAAGCAGTAATCGCTAAAATT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	ACGGAAGCATCAGGCACGTCTAGTACAATT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AAAGTTTCGAATTAGAATCAAATGACCAC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	ACCATCATGTAATCATCTTCAGGTACCG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	AATACGCAGTAGAGGTATATCCATTGCTCC
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	TCACTTGGAATGTTGTACGCCTTTCCAAG
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	CAACGCCTTTAATGCCCAGGATGTTAATT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC	CGATCGCTGTGTTGGGGTGTTTTCCTATTT
GTTGTGTTAGCACTAAGCTACAGAAAAATTTGAAAGCAAATCACAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098193378.1\|1726692_1727010_+\|transposase	unknown	unknown	gnl\|CDD\|225511
NZ_CP023777.1\|WP_098193381.1\|1730542_1731037_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098193388.1\|1735507_1738810_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP023777.1\|WP_098193377.1\|1725482_1725818_+\|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|226043
NZ_CP023777.1\|WP_098193384.1\|1732782_1733019_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_157760679.1\|1733539_1734118_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274376
NZ_CP023777.1\|WP_157760677.1\|1718124_1719861_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|143479
NZ_CP023777.1\|WP_098193383.1\|1732058_1732802_+\|ImmA/IrrE-family-metallo-endopeptidase	unknown	unknown	gnl\|CDD\|368753
NZ_CP023777.1\|WP_098193389.1\|1738825_1740274_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|185760
NZ_CP023777.1\|WP_098193380.1\|1729893_1730172_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379565
NZ_CP023777.1\|WP_098193387.1\|1734194_1735349_+\|FecR-family-protein	unknown	unknown	gnl\|CDD\|226235
NZ_CP023777.1\|WP_098193382.1\|1731727_1732066_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|376540
NZ_CP023777.1\|WP_098193371.1\|1715898_1716831_+\|NADP-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|176191
NZ_CP023777.1\|WP_157761068.1\|1726937_1727867_+\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|222853
NZ_CP023777.1\|WP_098193376.1\|1724572_1725469_+\|type-II-CRISPR-associated-endonuclease-Cas1	cas1	cd09720_cas1_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|274694
NZ_CP023777.1\|WP_098193375.1\|1720327_1724560_+\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|375967
NZ_CP023777.1\|WP_098193372.1\|1716877_1717273_+\|DoxX-family-membrane-protein	unknown	unknown	gnl\|CDD\|311556
NZ_CP023777.1\|WP_098193385.1\|1733067_1733391_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|181371
NZ_CP023777.1\|WP_098193370.1\|1714950_1715811_-\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225117
NZ_CP023777.1\|WP_098193373.1\|1717450_1718122_+\|DNA-alkylation-repair-protein	unknown	unknown	gnl\|CDD\|132880

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098193378.1\|1726692_1727010_+\|transposase	gnl\|CDD\|225511	COG2963, COG2963, Transposase and inactivated derivatives [DNA replication, recombination, and repair].	3.01606e-07
NZ_CP023777.1\|WP_157760679.1\|1733539_1734118_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	1.25159e-28
NZ_CP023777.1\|WP_098193388.1\|1735507_1738810_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_CP023777.1\|WP_098193377.1\|1725482_1725818_+\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	2.07784e-26
NZ_CP023777.1\|WP_157760677.1\|1718124_1719861_-\|hypothetical-protein	gnl\|CDD\|143479	cd07563, Peptidase_S41_IRBP, Interphotoreceptor retinoid-binding protein; serine protease family S41. Interphotoreceptor retinoid-binding protein (IRBP) is a homolog of the S41 protease, C-terminal processing peptidase (CTPase) family. It is thought to facilitate the compartmentalization of the visual cycle that requires poorly soluble and potentially toxic retinoids to cross the aqueous subretinal space between the photoreceptors and the retinal pigment epithelium (RPE). IRBP is secreted by photoreceptors into the interphotoreceptor matrix (IPM) where it is rapidly turned over by a combination of RPE and photoreceptor endocytosis. It is the most abundant soluble protein component of the IPM, consisting of homologous modules, each repeat structure arising through the duplication (as in teleost IRBP) or quadruplication (in tetrapods) of an ancient gene, arisen in the early evolution of the vertebrate eye. IRBP has been shown to promote the release of all-trans retinol from photoreceptors and facilitates its delivery to the RPE. Conversely, IRBP can promote the release of 11-cis-retinal from the RPE, prevent its isomerization in the subretinal space, and transfer it to photoreceptors. In vivo evidence implicates IRBP as a retinoid transporter in the visual cycle, suggesting a critical role for IRBP in cone function essential for human vision. IRBP is a dominant autoimmune antigen in the eye; IRBP proteolysis analysis has proven a useful biomarker for autoimmune uveitis (AU) disorders, a major cause of blindness. This family also includes a chlamydia-secreted protein, designated chlamydia protease-like activity factor (CPAF), known to degrade host proteins, enabling Chlamydia to evade host defenses and replicate.	2.74771e-12
NZ_CP023777.1\|WP_098193383.1\|1732058_1732802_+\|ImmA/IrrE-family-metallo-endopeptidase	gnl\|CDD\|368753	pfam06114, Peptidase_M78, IrrE N-terminal-like domain. This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.	3.7853e-13
NZ_CP023777.1\|WP_098193389.1\|1738825_1740274_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|185760	cd08977, SusD, starch binding outer membrane protein SusD. SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.	2.42093e-41
NZ_CP023777.1\|WP_098193380.1\|1729893_1730172_+\|hypothetical-protein	gnl\|CDD\|379565	pfam14338, Mrr_N, Mrr N-terminal domain. This domain is found at the N-terminus of the Mrr restriction endonuclease catalytic domain, pfam04471. Fold recognition analysis predicts that it is a diverged member of the winged helix variant of helix turn helix proteins. It may play a role in DNA sequence recognition.	0.00778263
NZ_CP023777.1\|WP_098193387.1\|1734194_1735349_+\|FecR-family-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	5.32977e-21
NZ_CP023777.1\|WP_098193382.1\|1731727_1732066_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|376540	pfam01381, HTH_3, Helix-turn-helix. This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within Neisseria gonorrhoeae NGO_0477, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteristic of the whole family.	5.02737e-13
NZ_CP023777.1\|WP_098193371.1\|1715898_1716831_+\|NADP-dependent-oxidoreductase	gnl\|CDD\|176191	cd05289, MDR_like_2, alcohol dehydrogenase and quinone reductase-like medium chain degydrogenases/reductases. Members identified as zinc-dependent alcohol dehydrogenases and quinone oxidoreductase. QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR actin the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	7.35376e-113
NZ_CP023777.1\|WP_157761068.1\|1726937_1727867_+\|IS3-family-transposase	gnl\|CDD\|222853	PHA02517, PHA02517, putative transposase OrfB; Reviewed.	1.44526e-70
NZ_CP023777.1\|WP_098193376.1\|1724572_1725469_+\|type-II-CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|274694	TIGR03639, cas1_NMENI, CRISPR-associated endonuclease Cas1, subtype II/NMENI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is a prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 variant of the NMENI subtype of CRISPR/Cas system.	1.26222e-103
NZ_CP023777.1\|WP_098193375.1\|1720327_1724560_+\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	gnl\|CDD\|375967	pfam18541, RuvC_III, RuvC endonuclease subdomain 3. Cas9 proteins are abundant across the bacterial kingdom, but vary widely in both sequence and size. All known Cas9 enzymes contain an HNH domain that cleaves the DNA strand complementary to the guide RNA sequence (target strand), and a RuvC nuclease domain required for cleaving the noncomplementary strand (non-target strand), yielding double-strand DNA breaks (DSBs). The crystal structures of type II-A and II-C Cas9 proteins highlight the features in Cas9 enzymes that support their function as RNA-guided endonucleases. Cas9 enzymes adopt a bilobed architecture composed of a nuclease lobe containing juxtaposed RuvC and HNH nuclease domains and a variable alpha-helical lobe likely to be involved in nucleic acid binding. The RuvC domain forms the structural core of the nuclease lobe, a six-stranded beta sheet surrounded by four alpha helices, with all three conserved subdomains (I, II, III) contributing catalytic residues to the active site.	1.35646e-56
NZ_CP023777.1\|WP_098193372.1\|1716877_1717273_+\|DoxX-family-membrane-protein	gnl\|CDD\|311556	pfam07681, DoxX, DoxX. These proteins appear to have some sequence similarity with pfam04173 but their function is unknown.	0.000400606
NZ_CP023777.1\|WP_098193385.1\|1733067_1733391_+\|hypothetical-protein	gnl\|CDD\|181371	PRK08306, PRK08306, dipicolinate synthase subunit DpsA.	0.000727749
NZ_CP023777.1\|WP_098193370.1\|1714950_1715811_-\|AraC-family-transcriptional-regulator	gnl\|CDD\|225117	COG2207, AraC, AraC-type DNA-binding domain-containing proteins [Transcription].	4.64473e-24
NZ_CP023777.1\|WP_098193373.1\|1717450_1718122_+\|DNA-alkylation-repair-protein	gnl\|CDD\|132880	cd06561, AlkD_like, A new structural DNA glycosylase. This domain represents a new and uncharacterized structural superfamily of DNA glycosylases that form an alpha-alpha superhelix fold that are not belong to the identified five structural DNA glycosylase superfamilies (UDG, AAG/MNPG, MutM/Fpg and helix-hairpin-helix). DNA glycosylases removing alkylated base residues have been identified in all organisms investigated and may be universally present in nature. DNA glycosylases catalyze the first step in Base Excision Repair (BER) pathway by cleaving damaged DNA bases within double strand DNA to produce an abasic site. The resulting abasic site is further processed by AP endonuclease, phosphodiesterase, DNA polymerases, and DNA ligase functions to restore the DNA to an undamaged state. All glycosylase examined to date utilize a similar strategy for binding DNA and base flipping despite their structural diversity.	1.2062e-26

>NZ_CP023777.1|WP_157761068.1|1726937_1727867_+|IS3-family-transposase
MGKSDTKKGSEHFLQGRQQIFRFIKDHQAEFDVEKMCKVFKVSRSGYYAWSIRKPSKLSLYRQVLCKGVEDIYHKSKGRYGSPKIVAELRSMGLHASRPRVARIMKDKGFRSIITGKFKVCTTDSNHKLEVSANILNREFTARAPSEKWVSDLTYIRTKNGWLYLTAIMDLFDRRIVGWSMSTGMTTRETTVAAWNMAIRNRSVAPNMVFHSDRGVQYASEEFRDLLKGNSVQQSMSRKGNCWDNAVMENFFKILKSETGHHTVYDSVEVAKKELFEFIEIWYNRQRRHSILGYLPPEEFSKSILKKAA
>NZ_CP023777.1|WP_098193378.1|1726692_1727010_+|transposase
MSKKERRSYDKSFKLMAVELRRSGKPAVTVAKELGIAAEMLRRWTREFSVHDTRSFPGNGKQDLTPEQKEIQALKKALQEAELENRILKKAVSIFSREDNKYSGS
>NZ_CP023777.1|WP_098193377.1|1725482_1725818_+|CRISPR-associated-endonuclease-Cas2
MNSRYSAYRVMWILVFFDLPTETKRDRKNYAKFRKQILSDGFAMFQFSIYIRHCNSKENADVHMKRVKGILPPKGHVGIMCVTDKQFSMLEIFRGKVGIDPPPTLQQLELF
>NZ_CP023777.1|WP_098193376.1|1724572_1725469_+|type-II-CRISPR-associated-endonuclease-Cas1
MIKRTLYFGSPAYLKTNLEQLQIELPKTGETKIAPIEDIGLLILDHQQITITQALLAKLLAQNVAVITCDHTHHPVGLLLNLDGNTLQSQKFRAQVEASVPLKKQLWQQTVITKISNQAKLMAMERLEHQRLLKLAGAVKSGDSDNCEAQAATYYWKNLFPDFLQFRRERYGPPPNNLLNYGYAILRALVARSLVGSGLLPTLGIFHRNQYNAYCLADDIMEPYRPFVDKIVCHIVSMNGRFLEMTPRMKEQLLSIPTMDVLVQGRKSPLMHAVQRSTASLAKCFEGSARKIIYPELI
>NZ_CP023777.1|WP_098193375.1|1720327_1724560_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9
MVKNVLGIDLGVTSIGWAFVHEDTNFGELSKIVQAGVRLVALSTDEQLEFEKGKPLSINANRTLKRSMRRNLQRYKMRRKQLIKLFKQYNIIPEDAILAEDGKHTTFETYELRAKAVHEKISLLQFARVLLMLNKKRGYKSSRKVQSEEEGQAIDGMDVAKKLFHDKITPGQYCLELLKNEKKSLPSFYRSDLQDEFMKVWNFQMAFHPSILTTDLLKKLDGVGQKATAAIFYKELNITTAEIKGKRDEKKLASYQLRSDAIQKELSIEEVAFVLAQVNNDINSSSGYLGAIGDKSKELFFNKQTVGEYLYKQLKENPHARLKNQVFYRQDYLDEFERTWSCQAQFHPELTNDLKKEIGDITIFYQRKLKSQKGLISLCQFEQQKRLVTKNGRQIIKTTGYRVCPKSSPLFQEFKVWQNLQNVEIKADGVKGRLSEEQKQLLFEHLNMKGELSKTEALKLLKLNPKTADMNFTKLEANRTNNTLYNVYCRILEDAGYDLADILKVKSDKDQITVSDSTLPAKEITRIIAEIFGSLGIKTSILDFDAQLDGKAFEKQDSYLLWHILYSYESDDSASGNEKLYQTLEKKFGFSKEQAKVLASISFEDDYANLSTKALRKIMPFIITNKYDEACALASYNHSNSLTKEEKESRKLEDRLELIPKNSLRNPVVEKILNQLVHVINAIIEDPNMGKPDEIRIELARELKKNAAEREEMSRQIAQADRDHKAIRDTIQKEFGIANPSRNDIIKFKLYEELSFNGYHDLYTNAYINRKELFSNKYDVDHIIPQQSLFDDSFSNKTLTPRDVNLNKGNRTAYDYIEQVHGAEKLEAFKSRVQDYLDKNIKANPGAKAKAKKLLMPASEIGDGFIERDLRNSQYIAKKARTILETICRDVVATSGSITARLREDWDLMNIMQELNLPKYRAINYTELRERKDGSQKEVIKDWTKRNDHRHHAMDAITVAFTKHNHVQYLNYLNARKNESHKMHGNIIAIEKKETEYIQDKDGNGKKRFKSPMPNFRVAAKKALEEILVSFKAKNKVVTNNRNRYKVKKLKEGVQYPPIQLTPRGSLHKETVYGILHRYNTKEETIGAKFNAELIETVANPKYKAALLQRLAANGHDPKKAFTGKNSPAKNPIYINGEGSEVLPAKVKVVKLEPEYTIRKDITPENFSDEKSIMKVIDVGIRNILLERLKASKDAKEAFSNLDINPIWLNKAKDGDPSKNIPIKRVTITGVSNAEALHHKRDHLGNHILDKEGNKQPVDFVSTGNNHHVAIYRDANGKLQDKLVSFYEAVERANQGLPIIDKSYNQGEGWQFLFTMKKNEYFLFPGDGFDPKEVDLLDPKNKTLISKYLFRVQKLADRYFVFRHHLEAKEDDNLTLKGMTFHRLQSLEPLDGIIKVRINHLGNIVKVGEY
>NZ_CP023777.1|WP_157760677.1|1718124_1719861_-|hypothetical-protein
MKKCIYFLLISMTHLCASAQKNSYTVFFKTWNYLKYYHPDFATGKLNADSLFLQDVKKITATTDHNAVIALLTNNLQQHFSTAAAKATATDVIKSNQDFSWFRESAGIDKGHKQLLENIYQHRFTGPQHYYIPNNGYEADIPHEKVYDFPKEENLPLEYRLLALAKIQGCIDYLYPHKQLMNKNFDAYFESLLSRTITCQSRKDFEIILAKLVAPLEDTHAFSFYKQLHFAKDIFHTKLYAPFDYSVFDHYLLVTKLMIPDACQKAGIHAGDRIVAVNGKSIQDIIQSKKELLSASNPSVLLYRISQYQDNLIWPDDMALKKLAIQRNNSGDTVETAIEFIKPTDKKHIDSIVQYLNDEAKRKRQHRLEHPGIAYFRIDQTYKFISGVADDHIDQTMDSLLLAASQQKAIIFDMRGYPDWGGFVYTYIYKYFADKDNYFGKYYQQYHQNIGTFIYADQPAIYFPVLTNKSRHTYNGKVFIIVNPQTLSASEWNTMNLQYIFPGSVTIGQQSAGADGDIKRMALPGNYSLEFTGNGIFYPGGAPAQKVGVHIDEKITYRDIDLLKGQDLEFDWIIKEIL
>NZ_CP023777.1|WP_098193373.1|1717450_1718122_+|DNA-alkylation-repair-protein
MTLKETLAKLESLGSEKMRLQHKKAGASDHQYGVKMGDIRKVAQSIKSDHELALELWDTGIIDAQFLAILIMKPKKVSKDDIKELIRSVQFVNVVDWLYSYIIKAHPDKEALRLEWMKSKDPVAARLGWSLTSGRVAREPEGIDIEALLDRIEKEMPKAAPQVQWTMNSTLAQIGICMPGYRERALSIGEKLGIYRDYPVSKGCTSPFAPIWINEMVRRNNQG
>NZ_CP023777.1|WP_098193372.1|1716877_1717273_+|DoxX-family-membrane-protein
MNKTSYLLLRLGVALSMFGHGLVRLPKLNAFSGWMMKSFEQSWMPAPAVQAFSYALPIAEFIVGLLLVLGLFTRQALVAGAIVMLLLIFGTTVVENWEALPAQLVHLAFFAVLLHFLSSNSFAMDIKRNVS
>NZ_CP023777.1|WP_098193371.1|1715898_1716831_+|NADP-dependent-oxidoreductase
MKAILLQKPGGTENFEYQDIHKPAIHPGEVLIEVKAISINPVDIKTRMGKGVYGRIKDESPLILGWDVSGLVVESLSDEYKAGDEVFGMIRFPGHGKAYAEYVAAPAAHLAKKPGNVSHEEAVAATLAALTAYQVIVEQAQVKDGQKVLIHAASGGVGHYAVQVAKSLGAYVIGTSSEKNRDFVLGLGADEHIDYHTADLDALKDIDFALDALGDANVLRTIPLMKKGGTIISIPSGLGQEVVEAAKVNQVNAGFSMVQSSGENMKAIADLLANGTLRSHVSTAFSFDDITGAHQQIESGRTVGKIVLTF
>NZ_CP023777.1|WP_098193370.1|1714950_1715811_-|AraC-family-transcriptional-regulator
MKQELLHAPYSISYITLDEGPEPAHRHHFFELVYIISGTGTQCINQSKFDYHDGHMFLVTPEDCHSFDIKSTTTFFFLKFNNIYLKDSGIPGENIQRLEYILQNASHKQGCILKNLTDKQLVRPVVEAIIRETINQDIYNRELIQQLVNTLIVVVARNIAKFQQLDVSEQTEAKALDILHYIQNNIYDPEKLKADHLGKQFNISSAYLSRYFKQHTGETMQQYLGNYKTQLIVHRLLHSDKRITEIANEFNFTDESHFNKYFKKQKGLSPKEFRKQAREKVVEKMA
>NZ_CP023777.1|WP_098193380.1|1729893_1730172_+|hypothetical-protein
MNTMHQRSVNINVLKLLNDELHSLQDIFQEQVCEMLNLSPEALAQKLENEAICFNLAEQQALAAIFNDLADNLSKYNADYMLEDYIQDAVVA
>NZ_CP023777.1|WP_098193381.1|1730542_1731037_+|hypothetical-protein
MKNMNIFNAEIPQEKIQSAINKIDEAFNELKPYLITLQPEERQMLPKMGNKMFSFVNKVHELAKRNPDLAPSFFSIEDLEIDVAGAQSLEPLLNAVKQLYDGIDDTRMKCGSEAYTNSLAFYSSVKVASKHSVQKAKAVYDDLSGHFIKGANTESAPAAENKPA
>NZ_CP023777.1|WP_098193382.1|1731727_1732066_+|helix-turn-helix-transcriptional-regulator
MTNADTIIRTLREKFGYSQEVVANFLGVKREMISYYETGAREAPLEVLEKLADLFGVDLDIFFSDTMEAASTELAFAFRANEFNEKDLESIAAFRRVIKNYQRITNLEGKNA
>NZ_CP023777.1|WP_098193383.1|1732058_1732802_+|ImmA/IrrE-family-metallo-endopeptidase
MLKERYLEFRANKFREEHGLTPTEPADVYKLLARLNVITVFKEITGNFSGMAVKNGTGNFMMVNSNDILARQHFTIGHELYHLIIQENFKNRICEVGTFDKKDSEEYNADWFASYLLMPEGGIFELLPREELSLNKISLNTIVKMEQYFGVSRAALLNRLMFIDLVSKAKKDELQTTGSIKRSALLMGYSSELYENGNAGKVIGDYGEKAKKLYDKELISETDFYGLMLDIGIDLDTKFEEDDKTER
>NZ_CP023777.1|WP_098193384.1|1732782_1733019_+|hypothetical-protein
MTKQKGDPKILLDADVVIHFLKAGYQMMLPAIFPHRLVMLDKVKQELIKRKSEALGIENFLYWCKIPVEPMPKDFEIL
>NZ_CP023777.1|WP_098193385.1|1733067_1733391_+|hypothetical-protein
MAVARFRNEFIASSNVKDIKDYCELYGIVYFTTMDILEVAITNSIMTESQCDSFIYEVKQKGSKLPCDTMAAYRKRNEKWVSLQLLNRYMSRNFINTFSTPGFSPCY
>NZ_CP023777.1|WP_157760679.1|1733539_1734118_+|sigma-70-family-RNA-polymerase-sigma-factor
MSSFSTYTDLQLLESLKFSEEGAFTEIYNRYWEKLYKSAYNKLNNGEDAKEIVHDVLLDIWKRRADLSIEHLPAYLEKAVRFRVINHINRKKSTALIDSFESVLQSPFKADSEVNMNEFIKLLEAWIAVLPGKQREIFVKYYFDNLSTQEIAVEMNLSRKTVQNNLSITTQYLKARFKHLSILLLLLTNPPH
>NZ_CP023777.1|WP_098193387.1|1734194_1735349_+|FecR-family-protein
MLSEKDKIYLRQVLERYETGRATPEEIHFVEVYMDYLDELHKDVDPLHNLGAEGKPGIEQEIKERLFESIHNTPVPVINIHRRPRFTWQAAAAIIFVILGAATTWILYNQYNKHPSIVAMEDVGPGAERAVLKLGNGRVIMLDTSRGNIVQSGGLTVANDSGILNYQGKAAVAEYHTLSVPRGGQYKLQLPDGTDVWLNAASSITYPTFFDGSERLVKVTGEVYFEVAQMAGKPFRVKSPNGSDIQVLGTRFNINSYADEPTLKATLLEGAIRFNTATEHQVMKPGQQAILNKSGSLEILSNVNTEAVTAWRKGYFYFDATDLQTVMRQIARWYDVTVTYEGEVPDMKFSGEISKSNNISLVLEMLKANNIRFEIKGRKIIVKP
>NZ_CP023777.1|WP_098193388.1|1735507_1738810_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MRLKLLLLFAACLLHCCELFAQEPTKKITLTVKKQRLENVFKEVKKQTGYTVFYNEGLADKIKSIKVSFAVKNADVTDVMKLCFKDHGLTYKLIGNAIIILEGNIPAAPGDTKEQTEETNPKFSVSGLILNGQGEMMDNVNVIVKRTGKGAITDKKGEFKIEDILPNDVIRCSMVGYATAEVPVNGQNMIYVTMAVATNTLDQVVLQGYGKTSQRFATGNITRITAKEIEDQPVSNPLLALQGRVPGLVITQTNGYASAPVNVAIRGVSSLNLNTEPLYIIDGVPVSVTGQQGILYGNSFTGGLSPLFNINPKDIESIDVLKDADATAIYGSRGTNGVVLITTKKGVPNATTFNLNVTQGIQKITRYWDMLNTQQYLQMRREAFKNDGITPTAANAPDLLAWDQDRYTNWQKELWGGTGLNTAISAGLSGGNRQTTFRINGGYSRVTDITVVSGASQRGTMALGLSHTTKDYRFSTDLSVNFANSLVDVVNGSGNPRLAPNSPAIFDKDGNLNWNEWNAGGGPDVFPFGTLKQSNPQRTNALTSSLRLSYKPFKGFSFNTLFGYTYTQNANDFFNPITSQNPNKNPVGYASFNTNRVSGWNIEPQADYHFLLGEASVDVLLGATLTSSSGVATSVVGRGYTDDNLLYSIVNAPVIERPTDAYFYSKYLGAFARISYNLKNRYVINLNGRRDGSSNFGPGRQFGNFGSIGVAWIASEEEWMDKILPSFISNVKFRGSYGTTGNTGGSTYQYLSLWGSSASPSQPYPLYDGMVPYIPQNPPNQNYYWEQNKKVEGAIEIGLLENTITLSVSHYRNRTGNQITGYPLPQFTGFNSIITNLPATIQNSGWEGLVNAQLLRKKDMTWSVSFNISTNKNLLVSFPDLETSPYASRYKVGYPLTTRYVFHYLGVNPLTGSFAIEDHDKNGDIGAAAGAFNPDSYISLDAAPQYYGGISSMYRYKQFSLGLQFNFTKQMGENALYTSGSFGSFNNNIAVEVYKKNWKKPGDITPYPAFSTSFNQRDNLFSMSDGAYTDASYIRLSNLSLTYNLPGTWLSKLKMKNCSIGLNAQNIFTITGYKGLDPETRNFGGMPPAKIYVLHLQLSI
>NZ_CP023777.1|WP_098193389.1|1738825_1740274_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKRIFLLLMLLPFISCKKLLEVPPPKEKVTAEQVFSTDIQANSAMIGVYVSMIGINEGTSNFANGLVSWVSALSSDELVSPYLGFIITHAAINMNKLTGESIAELDNIWTSLYATINGTNAVIDGIAQSSSSRLTAGMRKQLTAEAKCIRAFCYFYLVNLYGDVPLVLVSDPLKVAGMSRTPVEEVYKQIIQDLKDARSDLPTDYSVSNEKRIRVNAFAASALLARVYLYLEDYENAAAEATKVIDNTNLFGLEDDLNDVFLTDSKEAIWQLNQNVNDGLAGNATLEGYNLLPYGYSGASAYLSEQLLAAFEPDDNRKVKWTDSIFFYPIGSPVGQYYYYPYKYKVGPENRVIGGAATEYYMLLRLAEQYLIRAEAKAHGAPGGPQGAIADLNVIRKRAMLPVLPDTLSGNALLDAVAKEWQMEMFTEWGHRWLNLKRTGKAREVLSAIPIKQPWEGDYQLLYPIPQESILNGSGIKQNVGY

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Crispr_ID: NZ_CP023777_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_7

2189446-2189593

Orphan

Consensus_repeat	Method
AGAAACAATAAGTGTTGGAAATCTGGGTTCATAAATGTGAATACTTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023777_7

>merge|NZ_CP023777|7|2189446-2189593|CRISPRCasFinder
AGAAACAATAAGTGTTGGAAATCTGGGTTCATAAATGTGAATACTTCCCATCAAAGCCCGAAAGTCTTTCTGGTTAGAGCTTCCAAGCTCAGACCCACGCAAGAAACAATAAGTGCTGGAAATCTGGGTTCATAAATGTGAATACTTC

>NZ_CP023777|7|7|2189446-2189593|CRISPRCasFinder
AGAAACAATAAGTGTTGGAAATCTGGGTTCATAAATGTGAATACTTC	CCATCAAAGCCCGAAAGTCTTTCTGGTTAGAGCTTCCAAGCTCAGACCCACGCA
AGAAACAATAAGTGCTGGAAATCTGGGTTCATAAATGTGAATACTTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098196160.1\|2191849_2192980_+\|tRNA-guanosine(34)-transglycosylase-Tgt	unknown	unknown	gnl\|CDD\|234642
NZ_CP023777.1\|WP_098193703.1\|2179516_2180236_+\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	unknown	unknown	gnl\|CDD\|381175
NZ_CP023777.1\|WP_098193715.1\|2195715_2197827_+\|ATP-dependent-DNA-helicase-RecG	unknown	unknown	gnl\|CDD\|236794
NZ_CP023777.1\|WP_098193718.1\|2202825_2204238_+\|FAD-binding-protein	unknown	unknown	gnl\|CDD\|273050
NZ_CP023777.1\|WP_098193709.1\|2186829_2187039_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098193710.1\|2187084_2187495_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378633
NZ_CP023777.1\|WP_098196161.1\|2194282_2195608_+\|citrate-(Si)-synthase,-eukaryotic	unknown	unknown	gnl\|CDD\|99858
NZ_CP023777.1\|WP_098193717.1\|2201749_2202769_+\|type-IX-secretion-system-membrane-protein-PorP/SprF	unknown	unknown	gnl\|CDD\|274625
NZ_CP023777.1\|WP_098193708.1\|2186119_2186680_-\|DinB-family-protein	unknown	unknown	gnl\|CDD\|378981
NZ_CP023777.1\|WP_098193706.1\|2183186_2184041_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098196159.1\|2187506_2188067_-\|RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|224511
NZ_CP023777.1\|WP_098193712.1\|2189890_2190523_-\|16S-rRNA-(guanine(527)-N(7))-methyltransferase-RsmG	unknown	unknown	gnl\|CDD\|234637
NZ_CP023777.1\|WP_098193711.1\|2188441_2189341_+\|cation-transporter	unknown	unknown	gnl\|CDD\|224151
NZ_CP023777.1\|WP_098193719.1\|2204437_2205022_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098193707.1\|2184312_2185743_-\|matrixin-family-metalloprotease	unknown	unknown	gnl\|CDD\|239805
NZ_CP023777.1\|WP_098193704.1\|2180395_2180920_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098193705.1\|2181022_2182900_+\|M1-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341067
NZ_CP023777.1\|WP_157760715.1\|2198043_2201742_+\|PKD-domain-containing-protein	unknown	unknown	gnl\|CDD\|372639
NZ_CP023777.1\|WP_098193713.1\|2190557_2191694_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133035
NZ_CP023777.1\|WP_157760713.1\|2193050_2194136_+\|LptF/LptG-family-permease	unknown	unknown	gnl\|CDD\|367632

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098196160.1\|2191849_2192980_+\|tRNA-guanosine(34)-transglycosylase-Tgt	gnl\|CDD\|234642	PRK00112, tgt, queuine tRNA-ribosyltransferase; Provisional.	0
NZ_CP023777.1\|WP_098193703.1\|2179516_2180236_+\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	gnl\|CDD\|381175	cd11648, RsmI, Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase. RsmI is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.	3.7809e-122
NZ_CP023777.1\|WP_098193715.1\|2195715_2197827_+\|ATP-dependent-DNA-helicase-RecG	gnl\|CDD\|236794	PRK10917, PRK10917, ATP-dependent DNA helicase RecG; Provisional.	0
NZ_CP023777.1\|WP_098193718.1\|2202825_2204238_+\|FAD-binding-protein	gnl\|CDD\|273050	TIGR00387, Glycolate_oxidase_subunit_glcD., glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity. [Energy metabolism, Other].	9.71934e-128
NZ_CP023777.1\|WP_157760715.1\|2198043_2201742_+\|PKD-domain-containing-protein	gnl\|CDD\|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	9.50944e-19
NZ_CP023777.1\|WP_098193710.1\|2187084_2187495_-\|hypothetical-protein	gnl\|CDD\|378633	pfam11304, DUF3106, Protein of unknown function (DUF3106). Some members in this family of proteins are annotated as transmembrane proteins however this cannot be confirmed. Currently no function is known.	0.000915606
NZ_CP023777.1\|WP_098196161.1\|2194282_2195608_+\|citrate-(Si)-synthase,-eukaryotic	gnl\|CDD\|99858	cd06105, ScCit1-2_like, Saccharomyces cerevisiae (Sc) citrate synthases Cit1-2_like. Citrate synthases (CS) catalyzes the condensation of acetyl coenzyme A (AcCoA) with oxaloacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). Some CS proteins function as 2-methylcitrate synthase (2MCS). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and CoA during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). ScCit1 is a nuclear-encoded mitochondrial CS with highly specificity for AcCoA. In addition to its CS function, ScCit1 plays a part in the construction of the TCA cycle metabolon. Yeast cells deleted for Cit1 are hyper-susceptible to apoptosis induced by heat and aging stress. ScCit2 is a peroxisomal CS involved in the glyoxylate cycle; in addition to having activity with AcCoA, it may have activity with PrCoA. Chicken and pig heart CS, two Arabidopsis thaliana (Ath) CSs, CSY4 and -5, and Aspergillus niger (An) CS also belong to this group. Ath CSY4 has a mitochondrial targeting sequence; AthCSY5 has no identifiable targeting sequence. AnCS encoded by the citA gene has both an N-terminal mitochondrial import signal and a C-terminal peroxisiomal target sequence; it is not known if both these signals are functional in vivo. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS.	0
NZ_CP023777.1\|WP_098193708.1\|2186119_2186680_-\|DinB-family-protein	gnl\|CDD\|378981	pfam12867, DinB_2, DinB superfamily. The DinB family are an uncharacterized family of potential enzymes. The structure of these proteins is composed of a four helix bundle.	1.8879e-12
NZ_CP023777.1\|WP_098193717.1\|2201749_2202769_+\|type-IX-secretion-system-membrane-protein-PorP/SprF	gnl\|CDD\|274625	TIGR03519, bacteroidetes-specific_membrane_protein, type IX secretion system membrane protein, PorP/SprF family. This model describes a protein family unique to, and greatly expanded in, the Bacteriodetes. Species in this lineage include several, such as Cytophaga hutchinsonii and Flavobacterium johnsoniae, that have type IX secretion systems (T9SS) and exhibit a poorly understood rapid gliding phenotype. Several members of this protein family are found in operons with other genes whose loss leads to a loss a this motility.	1.13411e-47
NZ_CP023777.1\|WP_098196159.1\|2187506_2188067_-\|RNA-polymerase-sigma-factor	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	3.21761e-25
NZ_CP023777.1\|WP_098193711.1\|2188441_2189341_+\|cation-transporter	gnl\|CDD\|224151	COG1230, CzcD, Co/Zn/Cd efflux system component [Inorganic ion transport and metabolism].	4.06908e-90
NZ_CP023777.1\|WP_098193707.1\|2184312_2185743_-\|matrixin-family-metalloprotease	gnl\|CDD\|239805	cd04278, ZnMc_MMP, Zinc-dependent metalloprotease, matrix metalloproteinase (MMP) sub-family. MMPs are responsible for a great deal of pericellular proteolysis of extracellular matrix and cell surface molecules, playing crucial roles in morphogenesis, cell fate specification, cell migration, tissue repair, tumorigenesis, gain or loss of tissue-specific functions, and apoptosis. In many instances, they are anchored to cell membranes via trans-membrane domains, and their activity is controlled via TIMPs (tissue inhibitors of metalloproteinases).	4.44917e-63
NZ_CP023777.1\|WP_098193712.1\|2189890_2190523_-\|16S-rRNA-(guanine(527)-N(7))-methyltransferase-RsmG	gnl\|CDD\|234637	PRK00107, gidB, 16S rRNA (guanine(527)-N(7))-methyltransferase RsmG.	5.89898e-66
NZ_CP023777.1\|WP_098193705.1\|2181022_2182900_+\|M1-family-metallopeptidase	gnl\|CDD\|341067	cd09604, M1_APN_like, Peptidase M1 family similar to aminopeptidase N catalytic domain. This family contains bacterial 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.	3.63286e-150
NZ_CP023777.1\|WP_098193713.1\|2190557_2191694_-\|glycosyltransferase	gnl\|CDD\|133035	cd04192, GT_2_like_e, 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.	4.17419e-65
NZ_CP023777.1\|WP_157760713.1\|2193050_2194136_+\|LptF/LptG-family-permease	gnl\|CDD\|367632	pfam03739, YjgP_YjgQ, Predicted permease YjgP/YjgQ family. Members of this family are predicted integral membrane proteins of unknown function. They are about 350 amino acids long and contain about 6 transmembrane regions. They are predicted to be permeases although there is no verification of this.	1.33914e-55

>NZ_CP023777.1|WP_098193711.1|2188441_2189341_+|cation-transporter
MHDHSHTHHRSIAALNKAFTWGICLNIGYVIFEAIMGLAIGSLALLSDAGHNLSDVASLALSLLAFRLARLKPNETFTYGYRKSTVLISLLNAVILLLAVGIIGYEAIRRFSNPEPVAGKTVAIVAGVGIVINAFTAYLFLKDKEKDLNVKSAYLHMAADTLVSLGAVVAGLIILWKGWTWVDPVISLVFILVILWSTYGLLRDSLILSLDGVPRNIDLETVRGKMEKVSGVRDVHHLHIWAVSTTDNALTAHVKIEPGLNPERMDQIKNELKHVLEHLGIRHATLELELKHTDDDLGY
>NZ_CP023777.1|WP_098196159.1|2187506_2188067_-|RNA-polymerase-sigma-factor
MATEQDQRIQQTVQKERKRLLQFIQKRVDNMADAEDILQDVFFQFTQYLRLGSQVESITGWLFAVTRNKITDWFRKKKERSFSDEQVVKEDGEDALSLADILPDMQAETDAPLIRKIISEAIMEAVEQLPEEQRYVFIQHEIEGRSFKELAEETGVSVNTLLSRKRYAVLYLRERLLSVYQELSTK
>NZ_CP023777.1|WP_098193710.1|2187084_2187495_-|hypothetical-protein
MKRFTWVKLIKGIVCAVAIVAVIGTVTKYLWNWLMPELFNLPVITFWQALGLFLLSKLLLSGFHKGGGGHRKHWRDKMAEKMKHMSPEEREKMREKFQKCWSKAKYEDFFNETAHETKPPVENKDAANKDPEPPLT
>NZ_CP023777.1|WP_098193709.1|2186829_2187039_-|hypothetical-protein
MIGIFKTNIATPEAKSTVLDAIQNSFEITACNVDIEDCDRVLRIVDLKVPESTVIHFVRDIGYDCDVLE
>NZ_CP023777.1|WP_098193708.1|2186119_2186680_-|DinB-family-protein
MKKAIIHEQLILQFDAFADYIQNLSVHRFTVSPEGKWSAGQQLDHLIKSTKPVNSALALPRMLLRFWGAPKRPTMTYDEIVTEYQQVLSAGGHATKMYMPAIVEGYQREALLKQFIQQKDRLLQLLRQWHEDDLDKYLLPHPLMGKITIREVMYFTIYHTQHHLQSLKQRDQLNQSWSDQLERIFQ
>NZ_CP023777.1|WP_098193707.1|2184312_2185743_-|matrixin-family-metalloprotease
MKKIYVIFLSFIFISGNLIGQVKYDDGPINTSSSFAVNGDWNKTNISFNFMNGTSDIAGDNEKDAIREAFKIWQDYTNLNFTEVSSGGDIQISWAVLDHGDGYPFDGSNPILAHAFYPPPLGGSLAGDIHFDDDETWTNSERLGTSSQPIDLVTVAAHEIGHAIGLAHSNDTDALMYHTYYGSHRYLGSDDISGIRSIYESKSAVISNNYTCSGGEFNIRNLPTGATIEWTSSLTGAATISCSNCQSSILTWNGSSSGQTTISAQITLPTGDIVTESKDVYIGTINGAYSIKYFSTPEPTCYDLWSIHVFRPNYISGESTSDFQWGYRLIGQTGETLAPSPSYDYTFLPASAGTYEIFMRPQNACGTSMNEAIKTITVEETCFSGWAKISTFPNPATSQILIQIDSESKESSRAKVSNIEVSLIEMNTGNISNKWNLNSGQKSYTLDLKNIKSGIYILSLKKGKLITSKTIVIRKY
>NZ_CP023777.1|WP_098193706.1|2183186_2184041_+|hypothetical-protein
MKISLNLQKVLPGSIVCLLLLTVISSCSKSDDNGPGSGESEFKIDNIHLLTHCVNEEGITIDSFIYDDNNRILYHEVYNTLNGDMLSSIEYLYDNNGRLEKANFLNANHEVAHWAEYTYPDEHTLIYSPEPFFNFITKVEWSGDGNTWMISQKHKDSVNYLAATTYHFESGNLVAVEHQNHYDSTITFTYDEKTTNPYYLIRKKCPWFMILEPNVQESLMLKRISVNNIISADFPNENIVYNYKYEVTNHFEEHETVPSSIDYKNVNNSSTPVIGPRMYYMEIE
>NZ_CP023777.1|WP_098193705.1|2181022_2182900_+|M1-family-metallopeptidase
MTKSLLTGLLIVALCPATWAQSDRWQQRVKYDMDIKMDVSTHRFTGKQKLEYTNNSPDTLKRVYYHLYWNAFQPNSMMDTRSRELGKIVVGKDREGNNRYDWDGRVMDRISKLSPSETGYQKVLSLKLNGKSQKFTTDETVLIVDLSQPVLPHSTVTFDMDFEAQVPVQIRRSGRDNKEGVDYSMAQWYPKMAEYDYEGWHPDPYIAREFYGVWGDYDVKISIDQKYVLAATGYLQNPQEIGYGYEKAGSSVKRPRGKEMTWHFVAPNVHDFVWAADPEYKHITREIDGFTAHFFYIENDKTKDTWPHLPGKMAEAYAYAKAHFGPYPYKQYSFIQGGDGGMEYPMATLILGNGTMAGLYGVAVHEWMHSWYQGMLATNESLYPWMDEGFTTFAEDNIIYNTTPSLKGKWPLQNSYRSYFYLTGNGLEEPMSTHSDHYNTNMGYSITAYSKGAVFMEQLGYIIGAANRDQGLLNYYWEWRFKHPNVNDFIRVMEKQSGIQLDWYKLYFVYSTKHIDYGIQSVEERNGKTVVTLARVGKMPMPIDLVLTTKDGKKIMHYIPLGLMFNNKPNEDPSMTRVEHANWKWTSPTYECVIDMPKNEIQSLEIDPSQRMADVDRENNVYNVD
>NZ_CP023777.1|WP_098193704.1|2180395_2180920_+|hypothetical-protein
MTTLCNRLLSIVENFELDSWAELSQSLSLSEFLYCFDEDNQEPVDKLLGTNLVHYEMKSFELPVSHNPMSIFYRDEHWMKIELKCYQELYVEDIVPNHWPSPESILEFNMEEGQVGESVDIYPGKGIGLSIEACTGKILAIDFFQPTTTNNYLVFMKEEATNGADSDLEMQEIE
>NZ_CP023777.1|WP_098193703.1|2179516_2180236_+|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase
MSQLYLVPSPIGNLSDITYRAVKILEEADLILAEDTRTSGVLLRHYNINKPVTPYHQHNEHKVLQHLVSQIESGKTMALLTDAGTPGVSDPGFLLVRACIQAGIKVECLPGATAFVPALVNSGLPMNRFAFEGFLPLKKGRHTLLTQLAEDERSLVFYESPMRLVKTLSDFINYFGAGRNCCVSRELTKMFEENKRGTLQEVHDYFAAKTVKGEIVIVLEGFDPKSKKKSRYQDDDGGE
>NZ_CP023777.1|WP_098193712.1|2189890_2190523_-|16S-rRNA-(guanine(527)-N(7))-methyltransferase-RsmG
MEIINQYFSDFSPRQTEQFAALEGLYKEWNEKINVISRKDIDSLYEKHVLHSLAIVATGDFPPGSQILDLGTGGGFPGIPLAIYYPDIEFHLVDSIGKKLKVVEAVAEELGLKNITTAHMRVEDIKNRKFDFVVSRAVAPLKDLWRWSKPVLKKSSPEFWKSMKHGLICLKGGDLAQEISESGCRPMLTEIYELFPEEYFKEKYVVCVPC
>NZ_CP023777.1|WP_098193713.1|2190557_2191694_-|glycosyltransferase
MLDNLGLIIFYCFAAVAGIQVLYYLFVFSRLAFYKRQFDESAKPEVPLSVIICAKNEEAVLPKTLPQVLGQRYLNGAGPEYEVIVVNDNSEDDTKYYLRSIEPAYAHFRHIEIKQSAKFIPGKKYPLSVGIKGAKHDTLVLTDADCKPSSTYWLSYMSQGFEGDKEIVLGYGPYYKKKGFLNKVIRYETFFSAMQYLSYAMSGMPYMGVGRNLAYKKDLFFKNKGFTTHQHIASGDDDLFINKVSNAKNTAVVIDKNAFAFSEPKDSWKTWFRQKTRHMSTGKHYKFGHKLMLGIFSLTHFLFYPLFIAAIFYPPMQQITLGILGGKLLIQGIIMFCGMKKLGEQDLFWYSWFLDIFMLLYYIIFTPALLFKAKSTWK
>NZ_CP023777.1|WP_098196160.1|2191849_2192980_+|tRNA-guanosine(34)-transglycosylase-Tgt
MKFELLHKDPASKARAGKLTTAHGEIETPIFMPVGTVGSVKAVTQEQLREEINAQIILGNTYHLYLRPGLEILRQAGGLHGFNGWERPLLTDSGGYQVFSLANNRKIKEEGCVFQSHIDGSRHLFTPENVMDTQRVIGADIIMAFDECPPYPSEYKYAKQSMELTHRWLDRCIRRFKGTDPIYGYEQALFPIVQGSTYKDLRKISAEVIASKDCLGNAIGGLSVGEPEEDMYEMCELVCDILPTEKPRYLMGVGTPWNILENISLGVDMFDCVMPTRNGRNGMLFTWQGVINIKNKKWATDFTPIDANSPCIATSKYTKAYLRHLFAAGEILGMQLASIHNLAFYLELVKEARKRILEGTFAAWKEGMVKQLRQRL
>NZ_CP023777.1|WP_157760713.1|2193050_2194136_+|LptF/LptG-family-permease
MKKIDWYILWKFIGTFLFCLMVLLVISVVIDITEKVDNFIEHNLTFKQIVFEYYIGFIPHIVALLFPLFIFISVILFTSKMAYRTEIIAILSAGVSFRRFLRPYWVGAILFAVVLWFANQYVVPAANKIRTTFERKYVDKPDENKGKIVDRTFRIDTITYVTLGYFDRQANYGSSFLLQRIRDEKVFFKMRADRANYDTAHLAWKLTGVSMRRIDGLREHVSTVPDTLLKIPFEPSELVVDEKNIEEAMTTPELKKFIAREEIRGSEGLSTFKVELYRRTSAAFAIIVLTIIGAVLASRKVRGGSGFHMALGIVISALYILFLQFSTVFATKASLNPLLAVWIPNFIFGGLAIYLYRKAPK
>NZ_CP023777.1|WP_098196161.1|2194282_2195608_+|citrate-(Si)-synthase,-eukaryotic
MSYVKLKFKEKADELSVEVKELIKNHGSTKVDEVSLAQVYQGMRGVTGLVTETSLLDANEGIRFRGYSIPELREKLPKAPGGKEPLPEGLFYLMLIGELPTEADVQFLSSVFGRRSHVPTHVFSAIDSLPLHTHPMTMFTVGIMALQTESAFAKAYSEGISKKDYWSYIYEDAMNLIARLPRIAAYIYRRKYKNGQHIQPNAELDWASNFAHMLGFKDEDFHELMRLYMTIHADHEGGNVSAHTTHLVGSALSDPYLSFAAGMNGLAGPLHGLANQEVIKWILDMREELGGGMPTKDQIEAYVRKTLAEGKVVPGYGHAVLRKTDPRFTAQMEFAKKHLPNDELVRIVWMVYDTVPGILKELGKAKNPWPNVDAHSGALLVHYGLVEYEFYTVLFGVSRALGVLASLCWDRALGLSIERPKSVTTEWMKLFAEGKLEPIED
>NZ_CP023777.1|WP_098193715.1|2195715_2197827_+|ATP-dependent-DNA-helicase-RecG
MNYVASILSNPIEYLKGVGPQKGELLRKELAIHTFADLLSYFPFRYVDRTKIDKIRDIHGGMDFVQVRGRIVHKEVIGENRAKRLVATLRDETGELELVWFQGHQWVQKSIRENVNYLVYGRISSFNGALQISHPEMDLLTEEIAGGKQFLEPVYSTTEKLKARGLTAKGIGKLTKNLLEQLAPTEIQENIPADVTAQFKLMPRHLAYFKIHFPANDDDVRAAQRRLKFEELFIAQIRILRLKLRRQQQSQGFIFKNVGDHFNNFYNTFLPFPLTGAQKRVLKEIRQDTQAGKQMNRLLQGDVGSGKTIVALLTMLLAIDNGFQACLMAPTEILSQQHYKGISELLEGMPLKVALLTGSIKGKARKKILAELAAGEIHILIGTHALLEPEVVFQHIGMAIIDEQHRFGVAQRARLWQKNNTPPHILVMTATPIPRTLAMTVYGDLDVSVIDEMPPGRKPITTVHRNEVQRAQVMDFIKDEIRKGRQAYVVYPLIEDSEKMDYENLMRGYEEVKAFFPEPKYYISMVHGKQPADVRETNMHRFITGDTQIMVATTVIEVGVNVPNASVMVIESTERFGLSQLHQLRGRVGRGAEQSYCILMTGNKLGNDSKERIKVMVQTNDGFIISEKDMELRGPGDIEGTRQSGILDLRIADIVEDKVILAAARETAERILEKDPALELPQHRNLHEFLTRQRSKSNWSKIS
>NZ_CP023777.1|WP_157760715.1|2198043_2201742_+|PKD-domain-containing-protein
MKSTLPIGMICCIISMLWAGPAVSQSQNSMSYTPVVYKENKGQWDPAVLFKAELGGSTVYLRKTSILYQLFNKNDMDAIIEAIHGHGHSAGGDPPIIFDPSGNGKASVNVADIAKSYPKNDKIGSFDNLKLRSHSYEVNFIGANPDVFVKGDKAEKGVSNYLIGNNPSKWGTDVQSFQAVTYEGLYPNIDLLMYSGSGQVKYDLIVKPGGDVNQIRLEYKGAEKVELIKGQLNITTSVGKSYELEPYAYQYINNQRVKVKAKYELKGNQVTYKVSGKYDPNYPLILDPSVIFSTLTGSTASNWGYTATYDNQGNLYGAGIIFGGGRYPVSPGAISSGLNGGEFDIAVTKFYGNGSNIFYSTYLGGSGVEQPHSLFVDAQGNLVISGRTTSGDYPTTNGSTLAGGYDMVVTKLNQNGTGFIGSMYVGGSNNDGVNKSAEKAGMEDIKRNYGDDARSEVIIDNAGNIYVVGSTQSRDFPVTAGAFQPTFGGGAQDGVVVKIDPTCNNILWASFLGGSGNDAAFVIVSSDETNSIYVAGPTTSSNISSINTGINPNFSGGGCDSYIMRISSDGSTVRNFTYLQSSGSAPDMAYGVQLDRAGNVYAMGTTEGSWPIVRPTGTPTFYNDNSKQFIVKLLPDLSDYVYSTTFGQHSGKQPTLSPVAFLVDRCENVYVSGWGGGINVSAGYRSAADASALTINMPITRDAKSKISDGSDFYFFVMKRDALDILYGTYFGATGQAEHVDGGTSRFDYNGVIYQAICSSCNPNAPIGFPTTAGSYYTGTPHTCNLAVLKIAFNLDGVKASIKTTGNKSHFCSGDPITAEDTSVTKAVEWHWNWGDGTPDIVQTTKEPITHVYAQNGDYELRLIKYDPASCNVRDTAIIPIRIRSDRATLGFTMQRIGPCTNLEYQFVNTSQAPPGKPFTDQSFIWDLGDGTPPFYSNSTPDIIHGYPEGVYNISLQLVDTNYCNAPDEIIQQLRVAENVTAIIADPGEGCAPYTVRFNNVSKGGTRFEWDFFADGTIDSNDPYPTFTFPDVGTFPVKLTAYDPNTCNGMHDTTIYVVVRENPVAGYVFSPQQPVPNTPTQFTSTASGAQDYYWTFGDGDTSVLANPSHQFLRTGTYDVCQTVINQYGCLDTTCQTVSAIVVPQFDVPSAFSPNNDGLNDVFLVKVFGAVRFNMKIFNRWGQLVFESSDPNVGWDGKYKGALQSMDVYGYQVFVEFTDGTKGSRSGNVTLLR
>NZ_CP023777.1|WP_098193717.1|2201749_2202769_+|type-IX-secretion-system-membrane-protein-PorP/SprF
MKKIIPYLLTVTLCTLGFAATAQDLHFSQFFNSPLSTNPANTGFIPDGDYRVGVNYRNQWASIPVPYKTMSAFGDAQLFKDRLEYGWVGVGGMILHDVAGTGNLTSTKVYGSIAYHQLLGFSSLLSAGFNVGWANKRVDITKLTFGDQWNGQFFDSQIPTAEPFAQNNINYLDIQVGMNYAYFPNENVYINGGFSVHHVNKPQETFYNNNNQIDRRYIGFLNASIKLSDMVIINPGGYYSQQAKASEVVIGGNAAYNLSGDGAQQLFGGLYYRFNDAAIFLVGYQVKNVKMMFNYDVTTSQFSSSNRRQGAYEIGIIYTGLYPNLQFRNAARKTLCPSF
>NZ_CP023777.1|WP_098193718.1|2202825_2204238_+|FAD-binding-protein
MNQLQQVTGQDIAYFQNLLGAAYTLCDEESMQPYSHDETEDLIFFPQVVLKPANTAEMAAVMRYCNEHMLPVTPRGGGTGLSGGALAQLGGVLVSTERLNKILAVDERNLQVTVEPGVITEVLQDAVKEKGLFYPPDPSSRGSCFIGGNISENSGGPKAVKYGVVKDYVLNLELVLPDGSIIWTGASVLKNASGYNLTQLVIGSEGTLGIVTKIVLRLIPLPKHDLLMLVPFSSAENACAAVSAIFRAGYTPSAMEFMERDALDWVLRFVDSSLVKIDDNVQAHLLIEVDGNYPEVLMQEMEAIAEVVMGFDAGEILFAESHQQKEELWKLRRRVAEAVKANSVYKEEDTVVPRAELPALLNGVKAIGQKFGFQSVCYGHAGDGNLHVNIIRGQLTDEQWNGTLKDGIREIFTLVKSLGGTISGEHGIGLVQKEFMGIVFEPIQMQLMRKIKEVFDPNYILNRGKIFDGE
>NZ_CP023777.1|WP_098193719.1|2204437_2205022_+|hypothetical-protein
MKRLLTLAIILLLATQVSKAQYYKTDTVQRKGFDKSRLIVGGMLGLGFGDYTNINISPMVGYRFSQWISAGINVNFQYASSKTRDWGTNNVLDKYKYTVYGGGVWGRVHPFEFLYIHVQPEYNAISEKQTVYTNPRQVFTANYGAPSLLVGGGYMQAIGGNSYFTIGLLYDVLQDANSPYGSQPIYQGGINIGL

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Crispr_ID: NZ_CP023777_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_8

2740253-2740369

Orphan

Consensus_repeat	Method
GAACAGCGGGGCTTCCAATTTCTGATATCGAAAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023777_8

>merge|NZ_CP023777|8|2740253-2740369|CRISPRCasFinder
GAACAGCGGGGCTTCCAATTTCTGATATCGAAACTTGGGTTCGTATTAAGAAATTTTGCCGCTATGCCCCAAAAAGCAAGCTGAACAGCGGGGGCTTCCAATTTCTGATATCGAAAC

>NZ_CP023777|8|8|2740253-2740369|CRISPRCasFinder
GAACAGCGGGGCTTCCAATTTCTGATATCGAAAC	TTGGGTTCGTATTAAGAAATTTTGCCGCTATGCCCCAAAAAGCAAGCTG
AACAGCGGGGGCTTCCAATTTCTGATATCGAAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098194141.1\|2739325_2739871_+\|transposase	unknown	unknown	gnl\|CDD\|376616
NZ_CP023777.1\|WP_098194132.1\|2726513_2727110_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274376
NZ_CP023777.1\|WP_098194143.1\|2742082_2743468_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|225121
NZ_CP023777.1\|WP_098194142.1\|2740908_2742099_-\|N-acyl-D-glucosamine-2-epimerase	unknown	unknown	gnl\|CDD\|238153
NZ_CP023777.1\|WP_098194147.1\|2749653_2750577_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098194148.1\|2750586_2751615_+\|glycoside-hydrolase	unknown	unknown	gnl\|CDD\|366944
NZ_CP023777.1\|WP_157760773.1\|2728729_2732032_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP023777.1\|WP_098194139.1\|2736864_2738271_+\|acyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|214838
NZ_CP023777.1\|WP_098194137.1\|2734332_2735952_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|374525
NZ_CP023777.1\|WP_098194138.1\|2736035_2736485_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP023777.1\|WP_098194146.1\|2748119_2749643_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_CP023777.1\|WP_098194150.1\|2752590_2753259_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098194151.1\|2753377_2755057_-\|DUF5060-domain-containing-protein	unknown	unknown	gnl\|CDD\|379863
NZ_CP023777.1\|WP_098194133.1\|2727166_2728354_+\|FecR-family-protein	unknown	unknown	gnl\|CDD\|226235
NZ_CP023777.1\|WP_098194144.1\|2743496_2744663_-\|glycosidase	unknown	unknown	gnl\|CDD\|350107
NZ_CP023777.1\|WP_098194135.1\|2732048_2733452_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|185760
NZ_CP023777.1\|WP_098194149.1\|2751605_2752538_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|375080
NZ_CP023777.1\|WP_098194136.1\|2733481_2734303_+\|DUF4843-domain-containing-protein	unknown	unknown	gnl\|CDD\|374383
NZ_CP023777.1\|WP_098194145.1\|2745027_2748099_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP023777.1\|WP_098194140.1\|2738388_2739105_-\|aquaporin-Z	unknown	unknown	gnl\|CDD\|235453

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098194141.1\|2739325_2739871_+\|transposase	gnl\|CDD\|376616	pfam01797, Y1_Tnp, Transposase IS200 like. Transposases are needed for efficient transposition of the insertion sequence or transposon DNA. This family includes transposases for IS200 from E. coli.	2.82327e-07
NZ_CP023777.1\|WP_098194132.1\|2726513_2727110_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274376	TIGR02985, Sig70_bacteroi1, RNA polymerase sigma-70 factor, Bacteroides expansion family 1. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found primarily in the genus Bacteroides. This family appears to have resulted from a lineage-specific expansion as B. thetaiotaomicron VPI-5482, Bacteroides forsythus ATCC 43037, Bacteroides fragilis YCH46 and Bacteroides fragilis NCTC 9343 contain 25, 12, 24 and 23 members, respectively. There are currentlyonly two known members of this family outside of the Bacteroides, in Rhodopseudomonas and Bradyrhizobium.	2.6903e-33
NZ_CP023777.1\|WP_098194143.1\|2742082_2743468_-\|MFS-transporter	gnl\|CDD\|225121	COG2211, MelB, Na+/melibiose symporter and related transporters [Carbohydrate transport and metabolism].	1.78813e-122
NZ_CP023777.1\|WP_098194142.1\|2740908_2742099_-\|N-acyl-D-glucosamine-2-epimerase	gnl\|CDD\|238153	cd00249, AGE, AGE domain; N-acyl-D-glucosamine 2-epimerase domain; Responsible for intermediate epimerization during biosynthesis of N-acetylneuraminic acid. Catalytic mechanism is believed to be via nucleotide elimination and readdition and is ATP modulated. AGE is structurally and mechanistically distinct from the other four types of epimerases. The AGE domain monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which is also found in glucoamylase and cellulase. The active form is a homodimer. The alignment also contains subtype III mannose 6-phosphate isomerases.	1.44178e-49
NZ_CP023777.1\|WP_098194148.1\|2750586_2751615_+\|glycoside-hydrolase	gnl\|CDD\|366944	pfam02156, Glyco_hydro_26, Glycosyl hydrolase family 26.	3.25507e-40
NZ_CP023777.1\|WP_157760773.1\|2728729_2732032_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	1.65203e-153
NZ_CP023777.1\|WP_098194139.1\|2736864_2738271_+\|acyltransferase-domain-containing-protein	gnl\|CDD\|214838	smart00827, PKS_AT, Acyl transferase domain in polyketide synthase (PKS) enzymes.	1.97673e-102
NZ_CP023777.1\|WP_098194137.1\|2734332_2735952_+\|hypothetical-protein	gnl\|CDD\|374525	pfam16407, PKD_2, PKD-like family. This is a PKD-like family of proteins found in various Bacteroides species.	1.4757e-19
NZ_CP023777.1\|WP_098194138.1\|2736035_2736485_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	1.74136e-11
NZ_CP023777.1\|WP_098194146.1\|2748119_2749643_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	3.19896e-32
NZ_CP023777.1\|WP_098194151.1\|2753377_2755057_-\|DUF5060-domain-containing-protein	gnl\|CDD\|379863	pfam16586, DUF5060, Domain of unknown function (DUF5060). This is the N-terminal domain of a putative glycoside hydrolase, DUF4038. It is found in a number of different bacterial orders.	4.27813e-09
NZ_CP023777.1\|WP_098194133.1\|2727166_2728354_+\|FecR-family-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	3.64531e-20
NZ_CP023777.1\|WP_098194144.1\|2743496_2744663_-\|glycosidase	gnl\|CDD\|350107	cd08993, GH130, Glycosyl hydrolase family 130. This subfamily contains glycosyl hydrolase family 130 (GH130) proteins, as classified by the carbohydrate-active enzymes database (CAZY), are phosphorylases and hydrolases for beta-mannosides, and include beta-1,4-mannosylglucose phosphorylase (EC 2.4.1.281), beta-1,4-mannooligosaccharide phosphorylase (EC 2.4.1.319), among others that have yet to be characterized. They possess 5-bladed beta-propeller domains similar to families 32, 43, 62, 68, 117 (GH32, GH43, GH62, GH68, GH117). GH130 enzymes are involved in the bacterial utilization of mannans or N-linked glycans. Beta-1,4-mannosylglucose phosphorylase is involved in degradation of beta-1,4-D-mannosyl-N-acetyl-D-glucosamine linkages in the core of N-glycans; it produces alpha-mannose 1-phosphate and glucose from 4-O-beta-D-mannosyl-D-glucose and inorganic phosphate, using a critical catalytic Asp as a proton donor. This family includes Ruminococcus albus 4-O-beta-D-mannosyl-D-glucose phosphorylase (RaMP1) and beta-(1,4)-mannooligosaccharide phosphorylase (RaMP2), enzymes that phosphorolyze beta-mannosidic linkages at the non-reducing ends of their substrates, and have substantially diverse substrate specificity that are determined by three loop regions.	4.67627e-106
NZ_CP023777.1\|WP_098194135.1\|2732048_2733452_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|185760	cd08977, SusD, starch binding outer membrane protein SusD. SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.	3.43009e-25
NZ_CP023777.1\|WP_098194149.1\|2751605_2752538_+\|hypothetical-protein	gnl\|CDD\|375080	pfam17251, Pom, Protochlamydia outer membrane protein. This family represents an outer membrane protein found in environmental chlamydia. The protein shows porin function.	1.62984e-11
NZ_CP023777.1\|WP_098194136.1\|2733481_2734303_+\|DUF4843-domain-containing-protein	gnl\|CDD\|374383	pfam16132, DUF4843, Domain of unknown function (DUF4843). This family consists of uncharacterized proteins around 220 residues in length and is mainly found in various Bacteroides species. Distant homology analysis suggest distant relation between this family and other families of proteins with immunoglobulin-like folds, which are often involved in substrate binding. However, specific function of this family is unknown. There is distant homology to the Calx-beta family pfam03160.	2.09979e-20
NZ_CP023777.1\|WP_098194145.1\|2745027_2748099_+\|TonB-dependent-receptor	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_CP023777.1\|WP_098194140.1\|2738388_2739105_-\|aquaporin-Z	gnl\|CDD\|235453	PRK05420, PRK05420, aquaporin Z; Provisional.	2.43384e-95

>NZ_CP023777.1|WP_098194141.1|2739325_2739871_+|transposase
MSRKYKFRDAHGLYFVSFPVIGWIDIFTREVYCQLFVESLAYCRMNLGMEIYAWCIMPSHVHIIFRAKETDPGNLLKSLKGFTSRKILMAIAENPQESRKEWILSMAEHAGSLNSNIRFRQFWQQHNQPIELWSSHVIQQKVDYIHNNPVEAGFVLEPFFWKYSSAIDFAGGKGILEIDEL
>NZ_CP023777.1|WP_098194140.1|2738388_2739105_-|aquaporin-Z
MKATSSQKFLAEMFGTFVLVFMGCGSAVIAGSFVGNLGIAFAFGLSVLAMCYAIGHITGCHINPAISISMWAMGKLPAKDMVVYIIGQVVGGILAAGLLYYIAQGNPNYNIDMNGLGANGVGEASPANYSMVSGMIAEVVLTALFLFVVHGATSSYNGNTSFAGLAIGLCLTLIHIVGIPITGVSVNPARSIGPAIFVGGAALSQLWIFIVCPIVGGLIGGLLWKLVDNPPAEKASNY
>NZ_CP023777.1|WP_098194139.1|2736864_2738271_+|acyltransferase-domain-containing-protein
MTRKINTNDSDPADSYPGNTNDDPLGNQYQHGFDDELYSHGLHVLSAASPEDLQLQAKKLLSRIQSEPGWSLRDITYTLAGLQTNQQYNWLVYAETKDALVQGLEKKLAKKQHPAPAEQMDNRLAWIFTGMGPQWYGMGRQLYRENAVFRQVMDECNHLLLEYTGYSLLGELFFQPVNKVVTGNYLAQTANFFIQVSLSRMLHSMGLPMDVVVGHSVGEIAASVIAGGISLEDGIKIVHHWGSILEQVAGHGTLLSVGLGEHEAVPYLEDLPGLEIATINAPRSMTVAGNRDQLSRLEEMLKNDGIAARFVQVDVAYHSSQLSYLEHAVKDALGFVKPLKPVHKMYSTVTAELVEHPLHDADYWWRNIRQQVYFKDVVASLLKQGYTNFIEIGPHPVLRSALQETAMAEGKEIHTFFSLKKGTSELPMLINNLERSMGVGVPVNFSTSLTGERLKISLFEGEDVCQCC
>NZ_CP023777.1|WP_098194138.1|2736035_2736485_-|GNAT-family-N-acetyltransferase
MFTISRTNGQNPEFITLAKQLNAKLAEVNGEDHDFFMQYNQLDELKYVILVHKEAKAVGCGAIKAFDAKSMEIKRMFVLPGERRKGIAQLVLQGLETWAKELGMERCVLETSIDLIPAVKLYRGSGYATIPNYGQYVGIETSICMEKLL
>NZ_CP023777.1|WP_098194137.1|2734332_2735952_+|hypothetical-protein
MKSFQYKSIIPVCFLALLTMFSCKKDLGNYDYHETFDMEIQGIEDSYNLVLGDTVSIIPNFSKVEGQQMDTAAFSYTWTVSDPRLVDLYRLRTISTSRNLEGVLPLSVGDYTIYYTVLDTLTRVSWIREFSVKVEGNIKPKGWFVLSEVNQQSRLDYFIEDLDALGTYPQKYFDFTKLLLDPNSGKQLMLTGKPKFINYFMNNVAAAESGYKAYLYIGTDEMTEKINISNGLIWKDILYQFKLETATGTYPETVDWVKSVTSATGYAFKGEELFVCDYAQRAKFGLSLNRLAVTSEPIKLHPSLAILDFLIPNAVGFDITKKRFVSHSGSTNSSMALVPQDTSRSTFDPSDTKMDLVWMDATMAYGYMAVAILQDPGTSKRYMVRFNFEGASYNKIHIVDFKPVDDAPGMDKMTRFVVDNYYGYLVYESEGKLYRMNLDTGITILIKDYGANMRISMLKKSPNISYTNWSSISSRPNNFNLPQLEPVALGIMAGVYDPANPDASGIVDVIKIPNTTQLADSYYTLTGFGKVVDAVYINN
>NZ_CP023777.1|WP_098194136.1|2733481_2734303_+|DUF4843-domain-containing-protein
MKRSWILYIITLCMAGNFASCSEDNLDVYDQASSGGSIYFLDKYEQANDLYQSIPKDTLWTSFGYVSENKHDSIVKQVVRISGEKMDHDRTYKLTVLGSSTAKEGVHYELLNESYTIKANSITDTIKIKFNRTEDMKDSTFTVSLRLEPNENFNTDIPVMKSKAENGKYTYELTHMEFKVDDITGVPFLWTDPPYSSFTPYYLGTFSRTKLLLMIEVMNIDINLVTVPPPPGQYFSLDYYFAWKAYMTTWLEAEAAKGNYYYDEFGELIKFHL
>NZ_CP023777.1|WP_098194135.1|2732048_2733452_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MLRIRPIYIYVICLVCLSTAGCKKWLEVKPDDTFTEEMIYKTEAGTKDALNGILLKISSGSLYGMNLTGVYLDLLAQRYRVTNDASPYYSFYTLDLSQSTAKNVLQSFWEQMYQGVANTNRFLQMTEQYKANYSEQFYQQAKGEVHAIRALLYFDLLRMWGPVYDGDDSTAASIPVYSTITHVYPDYAPANEVMDFIVADLDSAIAYMANDPIIESNYDDDNNMRLNYYAAKALKARVLLYRGDKAGAYSMAKEVMQVQDKFPWVLRLNIASNRTNPDRIFGTEVLFGVYNRNLYDAYKGVFLSTLNEGSLLAAGPDFLNTVYESLLGDFRYGDTWLQASDGVSYRTFFKYAPVSDAAHYKFNYTVPVIRMSEMYLIAAETAPDPAEGLSYINEIRLHRGLDTEISDPAQLTNEIRKSYIKEFYGEGQLWFFYKRTKATSMISPAGNRAISLGKYVFDYPDSETQQR
>NZ_CP023777.1|WP_157760773.1|2728729_2732032_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MKLVMCLLLGCSLHISAKSYGQQVSISAKGARLEAVFQEIKSQTGYTFVYNTEWLREAKLVDLQVQNIPMEQALQLTFKDQPFTYMILRKTVILKKREQLIKILPSEDNRQQLIFRGKVLDEKGTPIPGASIFVLGEKKGVVSGEDGRFNLKIDKLGVVVRISFIGYESLDYRVKNLDKPVTFHMRLKDADLNQVVVTGMVNLDKQTFSGAAAVYSQEQIKTITNTNIVDALKTLDPSFMVLENNIMGSNPNVLPNIELRGQTSITTDELRDDFSENPNQPLFILDGFPASLRQILDMDINRIASVTILKDAASTAMYGNRASNGVIVIQTVRPLPGKIRVSYTSDWGFEFPDLSSYNRMDASEKLEFERLSGRYLPNERFDMSTYKYELYDPLYSMRKQEVLRGVNSYWLSDPLQNGISQRHSLLVNGGADNLLFVAGISYKDEKGVMIGSGRKEWSGNLKLDYNTGKFRFNNYVSVNGNSEDESPYGSFSTWVNVNPYYRKQPASEMYLEKYRDGSNGAEKVVYNPLYNAKLNSYDRSKLYSLWDNLSAIYQVTDNLRFETNLQVRKDVKEAETFKSPLHTDFISTVPEEKGKYTNTRFTTSSFTYNALLSYNKSFGDHTLGVNLRSEISESKSIRQDYSAIGFPLTSNGNPSFAYNYPENGAPYARTSISRYNNVSFISTYSYRNIYNLNATFTYNGSSVYGINNPYSPFYSIAGSWNLHNAQWFKRDWIDNARLRVSYGMTGNQNFSSTSSVSTYTYLSDFNSFGQGVLLSRLGNPNLESQTTYQFNTGLDLNIFKNRLGLVVDYYDKLTDPLVVPVALPSSTALVSYPFNVGSLKVKGFEFMLNGTPIRTKDFSWRISVMGSKYKKTYAGLGNRLLGLNEKLKTSNSFVQYKDGYSENDIWAVRSLGIDPATGREIYLKKDGTQSFDYDINDQVVVGNTLPDIQGVVGSQFTYKNFLLNFSFRYVFGQDAFNTVLFNTIENLSKSYIINNNLDKRALYERWKEPGDLAMYKDIADATRTYRSSRFVQTENSFGLESANITYNLTRGSFLDKLSLSRLQISGRTSDIFRFTTVRRERGTSYPYSRAFQLSLTANFK
>NZ_CP023777.1|WP_098194133.1|2727166_2728354_+|FecR-family-protein
MEQKGYYIDLFNRLLEGNCSPTDTEVLLQWLGSEEQDPLAASLILEEFNKSASSTDIDPAVREMLAAKLPGILKQEEVRIVQMQPRHDWRKWLGIAATVLLLAGSAFFWRWYSGQDAKTAGALSKQVDILPGSDKAILTLDDGKQVVLDSNGHINIQQGNTAVQQLSGVLQYEAAKSPGSKEIAYNRLSTPRGGQFQLVLPDGTKAFLNAVSSIRFPTAFTGNERLVEIEGQVNFDIAQDASKPFIVKTRNTRIEALGTSFDVMAYADEPTINTTLESGAVKVSIESTGESVVLQPGKQAIVNAKTEKMQVKSVNVNKIVAWKNGYFILDNDPVQTIMRQIQRWYDVDVKYEDGFSVEHISGEIPRDYTLVEVLKVMDICGVKCELEGRTIIVKK
>NZ_CP023777.1|WP_098194132.1|2726513_2727110_+|sigma-70-family-RNA-polymerase-sigma-factor
MTVLPLNNEASILQELQAGSADAFTSIYHHYSPIIYVAVLKMVKDPTTAQEIVQDVFSTIWRKHNSLEINNLSAYLFKAGQHKVFNFYKKLQQDKAKLQDFKVYAEAHYSHVEEALHYEESRDILQQVLDKLPQQQRKVYEMIRIEGRSYKDAAAQLGLSTYTVKEYLVYANKKIRNYFDNNLDVLVLLVMLFEIRKF
>NZ_CP023777.1|WP_098194142.1|2740908_2742099_-|N-acyl-D-glucosamine-2-epimerase
MPSSNNQLVTEMKDELKNILHFWKDHTIDQDKGGFYGRLLQDNKVDPYALKGSVLNARILWTFAAAAQVTGDPTDILIADKAYQYISDHFVDKEFGGVYWTVDYAGNPVDSKKQVYAIAFTIYALSEYYKIKQEQDILQMAQQLYQDLQRHAFDPVQKGYFEAFSREWHELKDQRLSLKDANEKKSMNTHLHVLEAYTNLYRVWPDQGVKNQIIDLLRVFDEYILDESKTHLQLFFSEDWSVKGNTVSFGHDIEAAWLMQEAAEVIEDPYYTGLFKAIALKIADSTNSGFDADGGLWYEFDIDKNHLVKEKHWWPQAEAVVGYVNAWQTSGQPGYLEQALKTWNFIQRYIIDHNYGEWFWGLDANYKIMPEDKVGIWKCPYHNGRACIEIIKRLDK
>NZ_CP023777.1|WP_098194143.1|2742082_2743468_-|MFS-transporter
MHNKITLREKVGYGFGDMASSMFWKLFGMYLLYYYTDIMGIQAAAVGTMFLITRIWDTAFDPVVGIMTDRTQSKWGKFRPYILYVAIPFGIIGILTFTTPDFSITGKLVYAYITYSAMMMVYSLINVPYASLLGVISPLASVRNTLASYRMAFAFAGSLIALAILEPMVSKFSLRFSLQTSWQLSVSVIAAICVILFLLCFAWVKERVVPKQAPSALKDDFRDLWQNRPWWILLGAGVAALIFNSIRDGATLYYFKYYIAQSEAFNVLGFEVTYSTLYLVIGQAANIIGVIIASPVANKFGKKSTYLGAMLIASVLSIIFYWLEKDQVVTIFIFQFVISICAGIIFPLLWSMYADIADYSEWKTGRRATGLIFSSSSMSQKLGWTIGGALTGWLLALFGFKANAIQGSTTENGIVMLMSLLPAIGAILSVVFIALYPLSESKIENITAALAAKREQNAIKQ
>NZ_CP023777.1|WP_098194144.1|2743496_2744663_-|glycosidase
MNFEARLAALKEAHEQLINTPNQIEKLGNGIFSRYENPVLTAEHTPLFWRYDFNPATNPYLVTRFGINATFNAGAIKWNGKYLVVVRVEGWDRKSFFAIAESDNGLDHFKFRDRPITIPETSEPDTNIYDMRVVQHEDGYIYGLFCTERRDPNAPDGDQSAAVAQCGIVRTKDLLQWERLPDLVTRSAQQRNVVLHPEFVNGKYMLYTRPQDSFIEAGKGGGIGVGFCDTMDGAVVNEERVIDNKLYHTIAESKNGQGPAPIKTAKGWLHLAHGVRNTAAGLRYTLYMFMTDLHDVTKVIYKPAGYFMAPEGTERTGDVSNVVFCNGWIADENGKIFIYYASSDTRLHVATTSIDQLLDYCMNTAADGLRSFTSVQTLQGIIDKNLSL
>NZ_CP023777.1|WP_098194145.1|2745027_2748099_+|TonB-dependent-receptor
MKRFIACCNTFLLVFLCSFVAVAQQKKISGKVLDNQSNPLPGATILVKNTQVATISDENGNFSLNLPAGGKTLVITYIGMETQEVEVGAKTSFNIQLQAKAGSLNDVVVVGYGSVKKSDLTGAVATLKGSELNKTPAASVDQLLQGKIAGVQVTTGGGAPGAGATIRIRGASSLNGSKDPLLVVDGYPWGGAGNLKQINPDDIESIEVLKDASAAAIYGSRGANGVIVITTRKGKLDQHRILFSTLQTKSFLANKPDVWRDPIEEATYANEAAITGGAIATDVPYIGIFRPVGNGMVYFPSIAELRGLDPNKPQWPYDTDWVDLVYRSPYSQNYTLTADGGSEKTRYAISGNYYKEQGMVIKNDYEKYTSRLNLDQKLTENITAGANVILAYTKAKGQQLGVGRSRIFPAYDSTGNFFRTSNTDFGNPIALANQLLNQTKTTDVLGNVYVNAKITDWLEFRTSLNSKFGNSVQDQYDPKNSTQRALDNKGSYGSIANGNYFDLLTENYFTANKNFGEDHQLTLVAGYSFQKTINRFSTLTGQNFVNDVLTNENLSTAGTMLISNDLQRFNLSSWYGRANYVFKDRYLLTVTGRADGSTKFGANNKWAFFPSAAFAWKAGEEQFIKDMGLFSELKFRASYGLTGNQGISPYQTLDRYGSYKYFTGSVFETGFGPGLAGANDEQGRTIVSGLGNNSLKWETTRSLDLGVDVGFFDQRLTVTADYYVKRTNDLLRLKTIAPSAGYDRQWINDGEIENRGVELGLNASIIEGADFNWSVGGMFTLNRNKVLAMGESDQVLIGSIYESVRQQISTYTVGQPMYVFYGYKSDGIIQTLDEGIAAGLTGVDAQPGEIKYVDISGPDGKPDGQIDSYDRTIIGNPNPDFIYSFNTSLRYKQFDLSMQLYGVQGNDVWDFQKMTPSRQLQRWTPDNPSNEYPRANATRGYRASDFYITDGSFLRLQNLTVGYNLLPGKINKVQSLRVFVSGNNLYTFTKFNKGFDPEVGENGINGGAYPRPRAVSLGVNVIF
>NZ_CP023777.1|WP_098194146.1|2748119_2749643_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MRKKFIPYIATAIMTVGLATSCSKMEEDPYGLINSQTFYKNADDARAAIIYAYSILPEVGYYSRGYYIITELPTENLTQKGDAGVGNLELDELRTTSTNTDLDNIWTYMYRGIARANAVIQNVPNIPGMVDAERNQITGEGYFLRALHFFNLVRMFGEVPLRTITIDDASQIPLAKSSIQEIYDQIISDLQNADQLLTQERISEGRANKAAVEGLLAKVYLHLASSKDYGSPGYDFVANADEMYQQAKLYAGKAVNDHQGKFNFSDQLPDVFSIDVYKKAAVSEHIFDAAVDRSGDREGSFSKLPNMFLPADRPMTILYDQIDSSSSSMDIGQGWGHFRTESAIYDSYATNDKRKTQLIVSSYSNNGSVYQLDINSSSRPFSRKFIDPDRIGDASSANSPIIRYSDILLVYAEACGPTTEGYAAVNKIRNRAGIGDLNPSLDITSFRNAVIQERAWELAFEGNRLFDLRRTNSMERVLVQQYGKTITSGAYFFPVPQRELDTNPLMK
>NZ_CP023777.1|WP_098194147.1|2749653_2750577_+|hypothetical-protein
MRHLYIIASFLAIISLVSCTKDPFKGVESNERSIEAITLGEGLVQVGPATIDREAGTASVKVLMQGNTDLSKVVAQIQTSYKSTISPANGQALDFAGNDNHYKFTITSESGNTREWTVELIPFTETLLGTYTIQNLVLYGGTGPEYGGGAVMNLTDKPWVWPATGGPGAELDNTITFEFSGITGDGKTTGTVTNDAGADGMYADFIFQNPVTDVNNFYRAIPEGTSTWERDYTDNSVTFIDGNGKRTKATFASASTIDLGNGLSKTITDNAFDFTLNGVDDWGNIYSDLDKFVKRPRRFWVDVKKQP
>NZ_CP023777.1|WP_098194148.1|2750586_2751615_+|glycoside-hydrolase
MRIMNVNILIVAAVLSFGACSKSDDKTTTNPPVEDTVKTGFKTLDYLYSISGKKTLAGIHNREPNSTPARWTNEIQKTTGKYPALWSGDFLFQQDNIDNRQLMINEAIAQWEKGAVVNIMWHACNPANSEPCGWDDGSGVLSELTNEQWNDLITDGTELNKRWKARVDEICVYLQQLKDAGVEVLWRPMHEMNQGKFWWAGRTGANGTRKLWQIMHDYMTKTKGLDNLIWVWDIQDFGSLASDAVDYYPGDDYFDIAALDVYDGSGYTQAKYEVMVKAAKGKPIAIGECDRLPTANELKTQSRWTFFMSWSELTYDKNSNTELQALYSANNIITLDQMPGWK
>NZ_CP023777.1|WP_098194149.1|2751605_2752538_+|hypothetical-protein
MEIKYIYIKYLCVALLFCHFSLKVQAQQGGATLYEPGWQVSVAPYYSIKQMHWSVAGNTSGMNPNILSELKWKSVQSIGGGIEIKKRIYNNLWGQVAFYKAGTVAGNATDADYRSDYRQDRTYFDRFDASRGFEWLFTPGVAYLLKINRYNSLNIYAGYYLNKEKYYLLPQGGNTRSDLKTTYQPTWKAWSVGFTYQLNINPNWNISPSFTYRQLDYDAAANWNLIEDFQHPVSFEHYAKGFEIQPQLDLSYFIKNGTALTFRVQYAHAATGHGSEALYLVNGETRATRLNGVTRDRFGLSLLTGIYGKK
>NZ_CP023777.1|WP_098194150.1|2752590_2753259_-|hypothetical-protein
MKKMTSLSLIILLLGSACKKDVKPLPQDEDNSTIARAAIPQSAFNLWTTCSSLPYLISGSDGICVPVGTCGTDINAAQQSSGQTANGMQFYGCFKGGSSAYSGASEQAVFVCDNVSSWTGNEMGFVKTLNDNTLKGYLQGGGAYIYQTISVNDNGYHTFKCQARSSNTHMVDFYVDGNYKFTLTNNSGSYYNLWYYFVGTNHWYGGGSHSGQQIEMYNMQTF
>NZ_CP023777.1|WP_098194151.1|2753377_2755057_-|DUF5060-domain-containing-protein
MRSRFGCMLLLALIGLYFQSDAQIKFNKIHQETQHIKQYQLAEWVVDFTADFTNPYDQQQVQLNMLLTDPRGLPLYLPCFFDPLDQGGTWKARFTPQSSGTYHYQFQVVNGKEALSSADATFSVTAGNGKGFIHSHDLWTFQYDDGSLFRGVGENIAWESRSFEDDKWTYDYLLPKLAENGGNFFRTWMCYWNLPLEWKKVRSTKRYQNSESYFNEGGIRRMDQLVRMCDSLHLHFMLAMDWHGHLMDKGGWKNSNYNIANGGPAKTPSDFFTMQKAQEQYKNRLRYIVARWGYSPSIAVWEFFNEVDNAVFTQQDSLLIKPVDVTQWHQEMSRYLKDIDPYKHLVSTSISHRDILGMNSIAYIDFNQKHIYKHTEKIPAIYPAYIQTFGKPYVVGEFGYRWEDQDPKYATEAVFDYKRGLWYGLFSPTPILPMSWWWELFDNQNMMPYLKGVRMISERMLQAGKGQFEPLTVDAWNVQAFGMRCGDEYYVYLLNNTAQHQDLRIKVDLPKKTQLVLFSTKDHSFTKSSFEQSAGGVISLPQHTIRGKEEALLIFSPAR

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Crispr_ID: NZ_CP023777_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_9

2904617-2904758

Orphan

Consensus_repeat	Method
CCTGCGAGTTTTATTTTGAAATTACTTGAAACCGCGGCTAGTTCGAGCTTCCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023777_9

>merge|NZ_CP023777|9|2904617-2904758|CRISPRCasFinder
CCTGCGAGTTTTATTTTGAAATTACTTGAAACCGCGGCTAGTTCGAGCTTCCAGCTACCCGTACTGGAAACCAGTTTTCCCTGTTTTGACCTGCAAGTTTTATTTTGAAATTACTTGAAACCGCGGCTAGTTCGAGCTTCCA

>NZ_CP023777|9|9|2904617-2904758|CRISPRCasFinder
CCTGCGAGTTTTATTTTGAAATTACTTGAAACCGCGGCTAGTTCGAGCTTCCA	GCTACCCGTACTGGAAACCAGTTTTCCCTGTTTTGA
CCTGCAAGTTTTATTTTGAAATTACTTGAAACCGCGGCTAGTTCGAGCTTCCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098194265.1\|2905699_2906164_+\|nuclear-transport-factor-2-family-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098194270.1\|2909799_2910222_+\|hemerythrin-domain-containing-protein	unknown	unknown	gnl\|CDD\|376622
NZ_CP023777.1\|WP_098194269.1\|2908491_2909790_+\|diacylglyceryl-transferase	unknown	unknown	gnl\|CDD\|183527
NZ_CP023777.1\|WP_098194271.1\|2910305_2911790_+\|arylsulfatase	unknown	unknown	gnl\|CDD\|293764
NZ_CP023777.1\|WP_098194258.1\|2898758_2899397_+\|orotate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234771
NZ_CP023777.1\|WP_098194264.1\|2903060_2904455_+\|arginine-decarboxylase	unknown	unknown	gnl\|CDD\|143503
NZ_CP023777.1\|WP_157760797.1\|2899904_2900360_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377000
NZ_CP023777.1\|WP_098194266.1\|2906182_2907040_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098194263.1\|2902105_2902744_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378083
NZ_CP023777.1\|WP_098194261.1\|2900483_2901416_-\|TolB-family-protein	unknown	unknown	gnl\|CDD\|223893
NZ_CP023777.1\|WP_098194254.1\|2896442_2896997_+\|methyltransferase	unknown	unknown	gnl\|CDD\|223813
NZ_CP023777.1\|WP_157760799.1\|2905255_2905426_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098194255.1\|2897015_2897498_+\|pantetheine-phosphate-adenylyltransferase	unknown	unknown	gnl\|CDD\|234674
NZ_CP023777.1\|WP_098194272.1\|2912216_2914670_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379720
NZ_CP023777.1\|WP_098194256.1\|2897550_2897982_+\|hotdog-fold-thioesterase	unknown	unknown	gnl\|CDD\|182360
NZ_CP023777.1\|WP_098194273.1\|2914910_2917448_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379720
NZ_CP023777.1\|WP_098194257.1\|2898040_2898667_-\|NUDIX-domain-containing-protein	unknown	unknown	gnl\|CDD\|239645
NZ_CP023777.1\|WP_098194268.1\|2907887_2908301_+\|BrxA/BrxB-family-bacilliredoxin	unknown	unknown	gnl\|CDD\|377667
NZ_CP023777.1\|WP_098194267.1\|2907229_2907676_-\|Hsp20/alpha-crystallin-family-protein	unknown	unknown	gnl\|CDD\|223149
NZ_CP023777.1\|WP_098194259.1\|2899447_2899825_+\|heavy-metal-associated-domain-containing-protein	unknown	unknown	gnl\|CDD\|225328

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098194270.1\|2909799_2910222_+\|hemerythrin-domain-containing-protein	gnl\|CDD\|376622	pfam01814, Hemerythrin, Hemerythrin HHE cation binding domain. Iteration of the HHE family found it to be related to Hemerythrin. It also demonstrated that what has been described as a single domain in fact consists of two cation binding domains. Members of this family occur all across nature and are involved in a variety of processes. For instance, in Nereis diversicolor hemerythrin binds Cadmium so as to protect the organism from toxicity. However Hemerythrin is classically described as Oxygen-binding through two attached Fe2+ ions. And the bacterial NorA is a regulator of response to NO, which suggests yet another set-up for its metal ligands. In Staphylococcus aureus the iron-sulfur cluster repair protein ScdA has been noted to be important when the organism switches to living in environments with low oxygen concentrations; perhaps this protein acts as an oxygen store or scavenger.	0.00126735
NZ_CP023777.1\|WP_098194269.1\|2908491_2909790_+\|diacylglyceryl-transferase	gnl\|CDD\|183527	PRK12437, PRK12437, prolipoprotein diacylglyceryl transferase; Reviewed.	2.71376e-20
NZ_CP023777.1\|WP_098194271.1\|2910305_2911790_+\|arylsulfatase	gnl\|CDD\|293764	cd16145, ARS_like, uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	0
NZ_CP023777.1\|WP_098194258.1\|2898758_2899397_+\|orotate-phosphoribosyltransferase	gnl\|CDD\|234771	PRK00455, pyrE, orotate phosphoribosyltransferase; Validated.	3.1838e-71
NZ_CP023777.1\|WP_098194264.1\|2903060_2904455_+\|arginine-decarboxylase	gnl\|CDD\|143503	cd06830, PLPDE_III_ADC, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Arginine Decarboxylase. This subfamily includes plants and biosynthetic prokaryotic arginine decarboxylases (ADC, EC 4.1.1.19). ADC is involved in the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. It catalyzes the decarboxylation of L-arginine to agmatine, which is then hydrolyzed to putrescine by agmatinase. ADC is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC), which are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. Homodimer formation and the presence of both PLP and Mg2+ cofactors may be required for catalytic activity. Prokaryotic ADCs (biodegradative), which are fold type I PLP-dependent enzymes, are not included in this family.	1.81845e-118
NZ_CP023777.1\|WP_157760797.1\|2899904_2900360_-\|hypothetical-protein	gnl\|CDD\|377000	pfam03168, LEA_2, Late embryogenesis abundant protein. Different types of LEA proteins are expressed at different stages of late embryogenesis in higher plant seed embryos and under conditions of dehydration stress. The function of these proteins is unknown. This family represents a group of LEA proteins that appear to be distinct from those in pfam02987. The family DUF1511, pfam07427, has now been merged into this family.	3.17237e-08
NZ_CP023777.1\|WP_098194267.1\|2907229_2907676_-\|Hsp20/alpha-crystallin-family-protein	gnl\|CDD\|223149	COG0071, IbpA, Molecular chaperone (small heat shock protein) [Posttranslational modification, protein turnover, chaperones].	9.46041e-31
NZ_CP023777.1\|WP_098194263.1\|2902105_2902744_+\|hypothetical-protein	gnl\|CDD\|378083	pfam08889, WbqC, WbqC-like protein family. This family of proteins are functionally uncharacterized. However it is found in an O-antigen gene cluster in E. coli and other bacteria suggesting a role in O-antigen production. Feng et al. suggest that wbnG may code for a glycine transferase.	1.65736e-37
NZ_CP023777.1\|WP_098194254.1\|2896442_2896997_+\|methyltransferase	gnl\|CDD\|223813	COG0742, COG0742, N6-adenine-specific methylase [DNA replication, recombination, and repair].	1.0577e-37
NZ_CP023777.1\|WP_098194268.1\|2907887_2908301_+\|BrxA/BrxB-family-bacilliredoxin	gnl\|CDD\|377667	pfam06491, Disulph_isomer, Disulphide isomerase. This family of proteins has disulphide isomerase activity, EC:5.3.4.1. It has a similar fold to thioredoxin, with an alpha-beta-alpha-beta-alpha-beta-beta-alpha topology. It has a conserved CGC motif in the loop immediately downstream of the first beta strand. This motif is essential for activity.	2.46506e-84
NZ_CP023777.1\|WP_098194255.1\|2897015_2897498_+\|pantetheine-phosphate-adenylyltransferase	gnl\|CDD\|234674	PRK00168, coaD, phosphopantetheine adenylyltransferase; Provisional.	2.46494e-76
NZ_CP023777.1\|WP_098194272.1\|2912216_2914670_+\|TonB-dependent-receptor	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	6.16611e-122
NZ_CP023777.1\|WP_098194256.1\|2897550_2897982_+\|hotdog-fold-thioesterase	gnl\|CDD\|182360	PRK10293, PRK10293, 1,4-dihydroxy-2-naphthoyl-CoA hydrolase.	1.61155e-43
NZ_CP023777.1\|WP_098194273.1\|2914910_2917448_+\|TonB-dependent-receptor	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	1.99736e-124
NZ_CP023777.1\|WP_098194257.1\|2898040_2898667_-\|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.	2.65188e-31
NZ_CP023777.1\|WP_098194261.1\|2900483_2901416_-\|TolB-family-protein	gnl\|CDD\|223893	COG0823, TolB, Periplasmic component of the Tol biopolymer transport system [Intracellular trafficking and secretion].	3.00578e-45
NZ_CP023777.1\|WP_098194259.1\|2899447_2899825_+\|heavy-metal-associated-domain-containing-protein	gnl\|CDD\|225328	COG2608, CopZ, Copper chaperone [Inorganic ion transport and metabolism].	2.36633e-08

>NZ_CP023777.1|WP_098194264.1|2903060_2904455_+|arginine-decarboxylase
MNNTYTDLVNQTFEFPQDGFEVKDNYLQYNGLDIKALIDKYGTPFKLTYLPKIGMQINRAKEMFKEAIKKNRYDGKYYYCYCTKSSHFSFIMEEVLKHDVHIETSSAYDVDIINKLHEKKKLSKSTYIICNGYKTKPYTRAIGKLINSGFENVIPVLDNKEELDHYTRVRSGNPVKIGIRIAAEEEPTFDFYTSRLGIRSRDVLEFYIDKLKDNPKFELKMLHFFMNKGIKDDIYYWSQFNKVLSLYCQLKKISPELTSINIGGGFPIKHSLGFDYDYKYIINELVANIKSVCKKNKVPVPDIYTEFGSFTVGESGSVIYSVVGEKMQNDREIWYMIDSSFITTLPDTWGIGEKFLMLPINKWDNEYQEVHLGGLTCDGYDFYTSEEHINAVFLPKQGKGEPLYIGFFHTGAYQDQLSGYGGIKHCLIPSPKHVIVGYDKNGQLKDWLYAKEQSAQSMLKILGY
>NZ_CP023777.1|WP_098194263.1|2902105_2902744_+|hypothetical-protein
MAGHQFENAILIESQYFPNIFYYKTLINSDILLIERYEHYQKMSFRNRCYVAGPNGRILLSVPLTHGKNQRTVVKDVKISYDEKWQDLHFKTLLSAYRRSPWFEYFEDQLAALFSQKFTYLLDWNMACFEWVNKRINVTTPVSLTESYRGASELEAGITDMRGTLLPANMESYGEQLPGYTQVFGERTGFLPNLSILDLLFNEGKNCLAHLK
>NZ_CP023777.1|WP_098194261.1|2900483_2901416_-|TolB-family-protein
MKHLLFSVACIMSCSLPLQFLMAQQKIISILETVEVSSGQRTVLCRDTSHFEAPNWSRDGKYLLLNKAGKLYQFQIDSKQWNTLPFGAGLKANNDHGFSPNGELLAISSGIVEKDDPAFGKGSVIYIADAQGGNLRRITSLSPSYWHGWSPDGKTLAFVGQRNGEFDIYSIPASGGTEKRLTNTPGLDDGPDYSPDGKYIYYNSYRSGKMEIWRMEADGSNAEQLTDDGYANWFPHPSPDGKQLVFLSFMEDQGQDHPFGKDVRLRIIDLETGETRNLTGIFFGGQGSINVPSWSPDSRYVAFVRYEVIK
>NZ_CP023777.1|WP_157760797.1|2899904_2900360_-|hypothetical-protein
MKLVKTSLLIVLIWAGATACGGIKDLEFVRIADVTLGQMGFTKSTVKMNIAYYNPNGFALKMKDAAFDIFIDDAKVGHSMQDTLLYIPARDTFYFPVKIDLNMANLMKNAANILANKEVTLKAMGNCKVGKSGVFVPFPIKVESKQKFDLF
>NZ_CP023777.1|WP_098194259.1|2899447_2899825_+|heavy-metal-associated-domain-containing-protein
MRILKLIVLLLLVGTGVTMAQAKKGIVTAKIKTPTVQCEMCKNTIERYLKREEGVISSKVDYKKKITTVKFYADRTNIEYVKTAIANAGYDADNVTANPDSYNALPKCCKKPEDGGGGGETKKKH
>NZ_CP023777.1|WP_098194258.1|2898758_2899397_+|orotate-phosphoribosyltransferase
MNTNIREKQVAEKLLQIQAVKLSPNAPFTWASGWKSPIYCDNRKILSYPYVRDFMKSEMCNLVFETYPDAAVIAGVATGGIPLGALVADQLKLPFIYVRSKPKEHGMGNQIEGVLQEGQEVVVIEDLISTGKSSLEAVQAIRAAGGNVIGMVSVFNYGFDAALQAFATADVGFKSMSNYNAMIELAVEKGIVSEADMNILESWRDNPGQWGR
>NZ_CP023777.1|WP_098194257.1|2898040_2898667_-|NUDIX-domain-containing-protein
MNTVFTIYINERPLYIARSAMEALANYHQGNVFDVPSQQDIEAVIARLEKGDLPGAVLTSPNPQSLLDQVKKLYTEFLAAGGLVLKEPGGEILLMFRRGKWDLPKGKLDDGEDLPTCALREVQEETGLQNVRIDSPLMETYHYYPLEGKKILKHTYWYKMKFTGNELTIPQIEEDILDIQWVKPENITKYIPYTYLNIAAVLEQGLGL
>NZ_CP023777.1|WP_098194256.1|2897550_2897982_+|hotdog-fold-thioesterase
MKPIWHSLDISLDQINEYNTGTMGEHIGIEFTEIGPDYLRAIMPVDKRTTQPYGLLHGGASAALAETLGSVASALIIDPAKQICVGLEINANHIRGVKVGYVHGIAKPLHLGSSTHVWDIRILDDDHKLVCASRLTVAILLKK
>NZ_CP023777.1|WP_098194255.1|2897015_2897498_+|pantetheine-phosphate-adenylyltransferase
MARRICLFPGTFDPVTLGHTDVINRAKDLFDELIIGIGINSGKVPMFSVEQRVAWFQEIYKDDPKIKAAAYEGLTVNFCKEVGARYILRGIRYVSDFEYEKAIADMNRMLDHDVETFFLTASAEHATMASTLVRDVLKNGGDVSRFVPGAVAATFKKHFG
>NZ_CP023777.1|WP_098194254.1|2896442_2896997_+|methyltransferase
MRIIGGEMGGRRIQPPSHMPHTRPTTDIAKTGLFNIIENNLEIGSLKTLDIFGGTGAISYELASRGATDQTIVERDSKMADFIQNTAKTLHIDHLKLVRMDVFKYLEQCNETYDFIFAGPPYALEEIDELPKIIFGKGLLKPEGWFVLEHTPRNNYKEFSYYRTERNYGTTIFTIFINRESLKK
>NZ_CP023777.1|WP_157760799.1|2905255_2905426_-|hypothetical-protein
MLQRNCKALAFSLTVAVILIASSCTTSKEYTKPYPAGSVYPFPVPDSVHTDRVSPR
>NZ_CP023777.1|WP_098194265.1|2905699_2906164_+|nuclear-transport-factor-2-family-protein
MIKYFLPAIITLLLTFSPSLKAQQTTADSIKAVINQLFKGMKEKDSTLVSACFSSGAIMQTVASRKDGMNVVRSGSVREFLIAVAADHPEVYDERIRFDGIHIDGDLASVWTPYEFYIGERFWHCGANSFQLARLNGLWKIIYLVDSRHPGPCR
>NZ_CP023777.1|WP_098194266.1|2906182_2907040_-|hypothetical-protein
MLALLKRLRSFAYNSYTTAEQRALKSYMFLGANAYELAKAKLLFDYIFFVLLTSITIFILVIARQDYYNLINCSFFTAIFFGCFISLHIGKKLVHIGMLTAYNTVLYTVAASIINNLDIGPMFTVPMLLGILLAHITNPGKHTFILVGIVFLYLSAVSYAEFKGISLNLTRLEDSQVINNARPFFSAVYILLLLRVFGLHYRDVIILSQQESTEHQKQFSALVNQNLIKQFIIVKGLSRSGKSKYLDGTMELDECFTEIERQCDSAIQYLDHQGYDDPGHNQHTS
>NZ_CP023777.1|WP_098194267.1|2907229_2907676_-|Hsp20/alpha-crystallin-family-protein
MTLVKFNQHPAKSFNGLFNDLFGNHPLNRFWNEDANQFFSALPPVNIVESKDAYKLDVVAPGFEKSDFKINLEGDQLTISVEKKENAIQEGDKQVRREFSFKSFKRSFSLDESVDIEKINAKYENGVLALVLPKKEEKQVANKEITIA
>NZ_CP023777.1|WP_098194268.1|2907887_2908301_+|BrxA/BrxB-family-bacilliredoxin
MYPAELVMPMKAELTDNGFTELLTPGAVDEALKQEGTTLVVINSVCGCSAGTARPGVLLAVANSEKKPDRLTTSFAGFDSAAVQQIRTHLMPYPPSSPSIALFKDGQLVHFIERHMIEGRPAQLIAASLVDAFEEYC
>NZ_CP023777.1|WP_098194269.1|2908491_2909790_+|diacylglyceryl-transferase
MYPNLYYAFQDLFGIELPFLKVVQTFGFFVAMAFLAAAYVLTTELKRRERLGLMQGVKEKQLVGKPATPLELIGVGLVWFIFGYKIFGLFSINATNQDTAYVDFLLSSKGNLLGGIALGGLMAFLRYNSKKKEAAGGTKESEVMIMPHQRVPDFTVLAAIVGFIGAKIFHNLENFGEFLSDPMGSLFSRGGFTFYGGLILASYVIIRYAKKRKISTRHLIDSAAPALMLAYAVGRMGCHFSGDGDWGIYNSAYVTDVKGTVVEVPKAEFQSALEKNKDFFLHQYQSFDNVPHASFAKPDALGFLPDWFFAYSYPHNVINEGAPIPGCEGQYCSVLPIPVFPTPLYEIITCMLMFILLMALRKKITTPGVMFGFYLILVGIERFFVELIRVNTKYEFLPLQPTQAELISLGMVIGGTLFIIYCKKRYQKELAS
>NZ_CP023777.1|WP_098194270.1|2909799_2910222_+|hemerythrin-domain-containing-protein
MQLHSSLVPLIEEHQRLLEACRKSKKDAAGASQHVMSEQEKLDFVVTVFKAVMVPHLQKEDHVFELCMGHDPEIDHCIKALMEEHHHISKMYSRLMDSNQLDEDLHNLATSLEEHINKENDKIYLMIQERLPFILDNVKY
>NZ_CP023777.1|WP_098194271.1|2910305_2911790_+|arylsulfatase
MRKLLLLLCSTLPIIAFAQKANNQRKPNIIYIYADDMGIGELGCYGQQQIKTPHLDQLASEGMKFTKHYSGTAVCAPSRCMLLTGRHSGHSYIRGNYELGGFTDATEGGQMPLPEGTYTIGHMLQNAGYVTGAIGKWGLGMFDNSGNPNKQGFDYFYGYLDQKQAHNYYPTHLWENGHWDTLENEFFLVHSPLKPSDTGQAAYDHFIGKEYSMDKLLEKSVQFIKQHKDQPFFLYLPYTGPHVSLQAPKEAVAKYIGTFDEQPYRGNQGYASTLHPKSTYAAMISYFDHNVGAIMELLQQLGLDDNTVVMFSSDNGPTFHTGGINVDDFNSKLGMRGYKGQLYEGGIRAPFIVRWPGHVKAGTTSDLLSNQFDMMATFAAIAGIKAPENDGINILPTLEGKKQKEHHDFMYFEFPERGGQLAIRVGDMKGIKTGMKKNHDAPWQVYDLSKDPDEKNDIASQNPQFIKQLDDIVKREHLRAHITEWEFIDPKTGQ
>NZ_CP023777.1|WP_098194272.1|2912216_2914670_+|TonB-dependent-receptor
MKTNMKILVVTFIAMTFTSIVNAQTKSSHISGKITDAAKAPVPFATATLLKAQDSSLVKGAIADLNGVYSFENIIPGKYIIAAINMGMAKNYSAVLVVDGNKHIAVPDILLHADTKKLSTVEIIKKKPFIEQRADKTIVNVEKSIVGAGSTAMEVLQKAPGVVVDKDDNISLKGKSGVNVMIDGKMVNMTSQDLAQYLKSMPSSNVEQIELISNPSSKYDASGTAGIINIKLKKNKNYGTNGNFTLSGGKGVKERYNAALFLNHRNKNFNIFGNLSRYYQTQYEHLRLSRDNEEKDRTIHMKQINDLDKKYDNYSGKIGMDYFINKNHTLGFMADGTLSNWIGNGDGSTKIGDLNSFDSTLLTTTDNKANWDRYTVNVNYKGKLDTLGKELNIDLDIARNKNDMKSHIYSLYEKGQMVSDPTFVRNYQPATIDIRTAKLDYTHPLKNGAKFEAGVKLSWVTSDNDVRFDSLRKESWVYDTIRSNHFVYKENVNAAYLNFSKNWKKWSLQAGLRMEQTNISGVSTAHKQHQENDSSYINLFPSIFISYNPSEKNTFGFSYSRRLQRPSYENLNPFELFLDNYTTTAGNPGLKPQYMDNFEISHTFHSFLTTSISYGHTKDGITRIIEPGIDPVSGDTLILRYKYQNVAVRHNYSFNVSAPYEIKKWWNVYTTMSLYYNSFKTNVSGDPLEVSSAAFYAQMQHTFSLPKDYSIQLSGEYISPQVTDEGLMRMHAMGGVELGFKKQLWDKKATITLNVQDIFRTYRFTGDFKNGNRHVILSNTWDSRMVRASFTYRFGNKNVKEARQRSTGAQAELNRAQ
>NZ_CP023777.1|WP_098194273.1|2914910_2917448_+|TonB-dependent-receptor
MYYVMHNTYFCIVVVKERNYIPNNTITPPCMKSFIKILTIIGLVSFAMKTKAQVAPKITGTVIRTDKSPVEFATVILLNAKDSSLVKGAIATIEGKYEFDKVAPGKYLVAGYHAGMPKVFGLPFQWTAQKGLSLDAITLVEKAQQLNAVEVVAKRPFIEQHADKLVVNVESSIVGPGGTAMDVLEKSPSILVDKDDNISLKGKSGVIIMIDGKITNMSSQDLAQLLRSMPSSNLDQIELISNPSAKYDAAGNAGIINLKLKKNKNYGANGNINLSGGMGIYPKVNTGINLNYRNKNVNLYGSYNYSFRQNYQDLHIDRAGTEGDHPIRFDQRTRMSKVSRFQSFKAGADYFIGKNHTVGFMVDGFIRNLNIDNKAVSYIGDNVVVDSVLRTIAYNKPTGDRFNYNLNYRGKLDTLGREINVDIDYSKHRADVTSLFHAAVWDGNEKAITGADTTRSMQPSDIRLKSAKIDYVHPLKDGSKFELGVKSSFVTSDNNAVFDSLKQSDWKVDLNRTNHFIYKENINAAYINYIRQIKKWGIQAGLRAEQTNIETSSYAVKNTFADTSYINLFPSLAVSWNANENNQLAVSYSRRLRRPNYDQLNPFEFYLDRYTKEAGNPYLKPQYSNNFELTHTFRKFLTSSIGYAHTNNTIMRIVEPDIDPATGDTTFVRYKVMNVDNRDNFSLNISAQVPFTKWWSAFVTTSLYYNHYKTFVGKQLVDRGSAGFYGQIQNSFDLPKHFSLQLSYNYISPQIADEGLFRMSAMHGVDFGVRKQVLDKKGTLSLNVQDVFNTRKFRGTYELENQHLEINNKWESRVITLSFSYRFGNMNVKESRKRKGGAEEEQSRL

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Crispr_ID: NZ_CP023777_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_10

3533328-3533452

Orphan

Consensus_repeat	Method
GTCAGGATTCAAACCTGAAACCTTTTGATCCGTAGTCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023777_10

>merge|NZ_CP023777|10|3533328-3533452|CRISPRCasFinder
GTCAGGATTCAAACCTGAAACCTTTTGATCCGTAGTCAAATGCTCTATTCAGTTGAGCTACGGAGCCATCTTAATTTTTGTGACTCTGTCAGGATTCAAACCTGAAACCTTCTGATCCGTAGTCA

>NZ_CP023777|10|10|3533328-3533452|CRISPRCasFinder
GTCAGGATTCAAACCTGAAACCTTTTGATCCGTAGTCA	AATGCTCTATTCAGTTGAGCTACGGAGCCATCTTAATTTTTGTGACTCT
GTCAGGATTCAAACCTGAAACCTTCTGATCCGTAGTCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098194726.1\|3536372_3537056_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098194718.1\|3526487_3526706_-\|YtxH-domain-containing-protein	unknown	unknown	gnl\|CDD\|378938
NZ_CP023777.1\|WP_098194731.1\|3542839_3543901_+\|diguanylate-cyclase	unknown	unknown	gnl\|CDD\|225829
NZ_CP023777.1\|WP_098194722.1\|3529341_3530394_-\|zinc-binding-dehydrogenase	unknown	unknown	gnl\|CDD\|176193
NZ_CP023777.1\|WP_098194730.1\|3541633_3542302_+\|AhpC/TSA-family-protein	unknown	unknown	gnl\|CDD\|239268
NZ_CP023777.1\|WP_098194721.1\|3528675_3529206_-\|DinB-family-protein	unknown	unknown	gnl\|CDD\|378981
NZ_CP023777.1\|WP_098194732.1\|3544088_3544928_+\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|378964
NZ_CP023777.1\|WP_098194729.1\|3540257_3541547_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098194717.1\|3526217_3526469_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098194725.1\|3533550_3534438_-\|mechanosensitive-ion-channel	unknown	unknown	gnl\|CDD\|366370
NZ_CP023777.1\|WP_098194720.1\|3527807_3528170_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098196258.1\|3530558_3531854_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098194727.1\|3537221_3539246_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|225814
NZ_CP023777.1\|WP_098194719.1\|3526724_3527483_-\|DUF1269-domain-containing-protein	unknown	unknown	gnl\|CDD\|377293
NZ_CP023777.1\|WP_098194733.1\|3544986_3545637_-\|NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|225462
NZ_CP023777.1\|WP_098194728.1\|3539251_3540010_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225818
NZ_CP023777.1\|WP_098196257.1\|3528172_3528598_-\|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl\|CDD\|378915
NZ_CP023777.1\|WP_098194724.1\|3532612_3533197_-\|XRE-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_CP023777.1\|WP_098196259.1\|3535020_3536223_+\|alanine-dehydrogenase	unknown	unknown	gnl\|CDD\|240623
NZ_CP023777.1\|WP_098194723.1\|3531874_3532576_+\|phosphonatase-like-hydrolase	unknown	unknown	gnl\|CDD\|274534

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098194718.1\|3526487_3526706_-\|YtxH-domain-containing-protein	gnl\|CDD\|378938	pfam12732, YtxH, YtxH-like protein. This family of proteins is found in bacteria. Proteins in this family are typically between 100 and 143 amino acids in length. The N-terminal region is the most conserved. Proteins is this family are functionally uncharacterized.	0.00424751
NZ_CP023777.1\|WP_098194731.1\|3542839_3543901_+\|diguanylate-cyclase	gnl\|CDD\|225829	COG3292, COG3292, Predicted periplasmic ligand-binding sensor domain [Signal transduction mechanisms].	5.28305e-10
NZ_CP023777.1\|WP_098194722.1\|3529341_3530394_-\|zinc-binding-dehydrogenase	gnl\|CDD\|176193	cd08231, MDR_TM0436_like, Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH). This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, 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.	2.0885e-102
NZ_CP023777.1\|WP_098194732.1\|3544088_3544928_+\|AraC-family-transcriptional-regulator	gnl\|CDD\|378964	pfam12833, HTH_18, Helix-turn-helix domain.	1.48289e-19
NZ_CP023777.1\|WP_098194721.1\|3528675_3529206_-\|DinB-family-protein	gnl\|CDD\|378981	pfam12867, DinB_2, DinB superfamily. The DinB family are an uncharacterized family of potential enzymes. The structure of these proteins is composed of a four helix bundle.	1.11897e-07
NZ_CP023777.1\|WP_098194725.1\|3533550_3534438_-\|mechanosensitive-ion-channel	gnl\|CDD\|366370	pfam00924, MS_channel, Mechanosensitive ion channel. Two members of this protein family of M. jannaschii have been functionally characterized. Both proteins form mechanosensitive (MS) ion channels upon reconstitution into liposomes and functional examination by the patch-clamp technique. Therefore this family are likely to also be MS channel proteins.	1.55746e-19
NZ_CP023777.1\|WP_098196259.1\|3535020_3536223_+\|alanine-dehydrogenase	gnl\|CDD\|240623	cd05199, SDH_like, Saccharopine Dehydrogenase like proteins. Saccharopine Dehydrogenase (SDH) and related proteins, including bifunctional lysine ketoglutarate reductase/SDH enzymes and N(5)-(carboxyethyl)ornithine synthases. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SDH is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure. Bifunctional lysine ketoglutarate reductase/SDH protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases.	3.78638e-179
NZ_CP023777.1\|WP_098194730.1\|3541633_3542302_+\|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.	1.02703e-36
NZ_CP023777.1\|WP_098194727.1\|3537221_3539246_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|225814	COG3275, LytS, Putative regulator of cell autolysis [Signal transduction mechanisms].	6.307e-28
NZ_CP023777.1\|WP_098194719.1\|3526724_3527483_-\|DUF1269-domain-containing-protein	gnl\|CDD\|377293	pfam04306, DUF456, Protein of unknown function (DUF456). This family is a putative membrane protein that contains glycine zipper motifs.	9.91505e-05
NZ_CP023777.1\|WP_098194733.1\|3544986_3545637_-\|NAD(P)-dependent-oxidoreductase	gnl\|CDD\|225462	COG2910, COG2910, Putative NADH-flavin reductase [General function prediction only].	1.98002e-76
NZ_CP023777.1\|WP_098194728.1\|3539251_3540010_+\|response-regulator-transcription-factor	gnl\|CDD\|225818	COG3279, LytT, Response regulator of the LytR/AlgR family [Transcription / Signal transduction mechanisms].	6.06137e-37
NZ_CP023777.1\|WP_098196257.1\|3528172_3528598_-\|nuclear-transport-factor-2-family-protein	gnl\|CDD\|378915	pfam12680, SnoaL_2, SnoaL-like domain. This family contains a large number of proteins that share the SnoaL fold.	2.40014e-14
NZ_CP023777.1\|WP_098194724.1\|3532612_3533197_-\|XRE-family-transcriptional-regulator	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.	8.78098e-12
NZ_CP023777.1\|WP_098194723.1\|3531874_3532576_+\|phosphonatase-like-hydrolase	gnl\|CDD\|274534	TIGR03351, PhnX-like, phosphonatase-like hydrolase. This clade of sequences are the closest homologs to the PhnX enzyme, phosphonoacetaldehyde (Pald) hydrolase (phosphonatase, TIGR01422). This phosphonatase-like enzyme and PhnX itself are members of the haloacid dehalogenase (HAD) superfamily (pfam00702) having a a number of distinctive features that set them apart from typical HAD enzymes. The typical HAD N-terminal motif DxDx(T/V) here is DxAGT and the usual conserved lysine prior to the C-terminal motif is instead an arginine. Also distinctive of phosphonatase, and particular to its bi-catalytic mechanism is a conserved lysine in the variable "cap" domain. This lysine forms a Schiff base with the aldehyde of phosphonoacetaldehyde, providing, through the resulting positive charge, a polarization of the C-P bond necesary for cleavage as well as a route to the initial product of cleavage, an ene-amine. The conservation of these elements in this phosphonatase-like enzyme suggests that the substrate is also, like Pald, a 2-oxo-ethylphosphonate. Despite this, the genomic context of members of this family are quite distinct from PhnX, which is almost invariably associated with the 2-aminoethylphosphonate transaminase PhnW (TIGR02326), the source of the substrate Pald. Members of this clade are never associated with PhnW, but rather associate with families of FAD-dependent oxidoreductases related to deaminating amino acid oxidases (pfam01266) as well as zinc-dependent dehydrogenases (pfam00107). Notably, family members from Arthrobacter aurescens TC1 and Nocardia farcinica IFM 10152 are adjacent to the PhnCDE ABC cassette phosphonates transporter (GenProp0236) typically found in association with the phosphonates C-P lyase system (GenProp0232). These observations suggest two possibilities. First, the substrate for this enzyme family is also Pald, the non-association with PhnW not withstanding. Alternatively, the substrate is something very closely related such as hydroxyphosphonoacetaldehyde (Hpald). Hpald could come from oxidative deamination of 1-hydroxy-2-aminoethylphosphonate (HAEP) by the associated oxidase. HAEP would not be a substrate for PhnW due to its high specificity for AEP. HAEP has been shown to be a constituent of the sphingophosphonolipid of Bacteriovorax stolpii, and presumably has other natural sources. If Hpald is the substrate, the product would be glycoaldehyde (hydroxyacetaldehyde), and the associated alcohol dehydrogenase may serve to convert this to glycol.	1.87525e-64

>NZ_CP023777.1|WP_098194724.1|3532612_3533197_-|XRE-family-transcriptional-regulator
MEDYIVGIGKRIKELRKKNNLTIHNIASSSGVSNGLISRVENGRTIPSLPVLISIIHSLGIDVPGFFQGLPQHEEKKYIITRKSEHSVIEKEDEAIGFEYRYLFGKQFISIGFEAILLDIQPGSKREKVETDAYEMKLILSGDCSYQIGDDEVLLHEGDTLFFDGRVPHVPVNNGKIPCKMLVIYFFNNTLSTT
>NZ_CP023777.1|WP_098194723.1|3531874_3532576_+|phosphonatase-like-hydrolase
MKDIKMVVFDMAGTTVDEDNIVYKTVHKVLVDEGCPVSLQEVLKHAAGKEKFQAIRDVVASVSGLPDPEGIACRAFAQFKITLEQQYDHVQIKGFDGVEQLFAKLRAGGVKVVLNTGYSKMIAHKLLTKLGWETGTHIDALVTADDVARSRPYPDMIFKAMALFDINNPALVLKAGDSDVDIMEGKNAGCGMTVGVLSGAQGRLQLEAAAPDYIFDKLTGIESLLHVHGLPGI
>NZ_CP023777.1|WP_098196258.1|3530558_3531854_+|hypothetical-protein
MFNKIFNFTNSKNWSSAYLIIAVFICYTGMYAVRKSFLAGQFTGLDFGYGLDAKTILVLSQVLGYMLSKFFGIRIVSEMKKEHRVSWLTGLVSFGLLMLAVFAWGPGLVKVAALFLNGLSLGIVFGIVFSFIEGRKNTELLAAALSATFIFSTGLVKTTGLVLMQDFNLGEYQVPFLTGLLFFPLFLLSVWVLNRTGAPDDSDIRERVQRVPMYREDRRQFLIQNGTGYFGLVAIYIVLTVVRDFRDNFVVEFWAEQGFSKAPQVVTLTEIPVAVSVLLVASAGVLIRNNKTAFNVGMWLMMLSALLMLCSTMLFNWGRMNAVVWMIVSGIGVYLPYILFHCLVFERLVALLKFKGNVGFLFYMADAFGYLGSVAVLVLKEVLGFHQSWSVFFVNMNLEAASCILLITVFVTWYFNKKFAKKSAAGVLNYT
>NZ_CP023777.1|WP_098194722.1|3529341_3530394_-|zinc-binding-dehydrogenase
MCNPSPAYATSMVFSDVGKPLEAVTIPIPTTSNEEVLVKIEYTTICTSDVHTYLGRRHGPMPCVLGHEIIGRITAKGTGIDTDFAGENLQVGDLVTWCVYAFDPHGNTMALRGMPQKSPGLYKYGHQEFTLEDGLNGGFSTHCVLKKGTAIFKLPGSLTPREAAPINCTHATIAGALRLAGNVKNKNVLVTGCGMLGLSACAMSKEAAAAKVVAMDINRGRLEMATRFGAENTPVTKEFDIVIDTTGVPAVMERGLSCLNTGGTAVWVGAVYSQPATLVNAEMIVKNLLTIKGLHNYTPDDLAQAINFIKKHRRKYPFDGLVGKEFPLEQIDEALQQATRGQYYRLGICS
>NZ_CP023777.1|WP_098194721.1|3528675_3529206_-|DinB-family-protein
MKIIYTSLLLAFVTFLCSSKAQAQQKDSLLSQLSVKWQNATGYALKMAELMPEEYYDFKPVPEQMSFKEQMVHIAQNIQWLSNSYLMNGGTVPKLDAENLDKAGVIQVLKDAYASGLKAHQQLQASELDDIVKFFAGPKTKRQILILLHDHQSHHLGQVIVYLRLKGIKPPPYIGW
>NZ_CP023777.1|WP_098196257.1|3528172_3528598_-|nuclear-transport-factor-2-family-protein
MTLTFCACNQDRIPAEDTVNTHSALINEYFDNFNQHDWKSMAAMYSDTAAFKDPSLGQGLVYQTHEQIIHKYTALQQGIPDVNDTIINMYPSGDDYMIVEFISRGTLPDSTTFTLPICSIFKIENGKITNDFTYYNNSGEK
>NZ_CP023777.1|WP_098194720.1|3527807_3528170_+|hypothetical-protein
MKLDSTKGGAFWKVYDKYENSRKGIINNRLNILKDYADEYKTLNDAEAINLANRAIKNKLAAEKLNKKYLKRFSKAIGGKGAAKFMQLENYIQTVISSSIQEQLPFIDELQEAQAAALDM
>NZ_CP023777.1|WP_098194719.1|3526724_3527483_-|DUF1269-domain-containing-protein
MENVIVASYAKKESAHDAWQHLKDLQEIHDIIIYRKVLLKVLDGQEIKVLTDTDDPEEGWRTITGTAIGGLVGLLGGPIGVVIGATFGMLVGAYGEVQAFDISEEFVSELKKRANPGSYIIILDADEEEPVFLDSYLEKGAQNVVRMPVDKVYDEYIAKSEEEERNLVEQAEKEFKQALRRDDSEVDDQNRVSLKTQASPELQEKMEYLEGLRKDTRYKLSQVENKIAKTPGNALEKWHRQKERFLPGSNSK
>NZ_CP023777.1|WP_098194718.1|3526487_3526706_-|YtxH-domain-containing-protein
MKSSERKKMIAGIILGASVGAFIGFLLSCDKGRNMVRKMKKLPGMAADELEKFANPIDDKEIHVDTPLEHIP
>NZ_CP023777.1|WP_098194717.1|3526217_3526469_-|hypothetical-protein
MDTKAKILASALVGTAVGTLIGYACTQSDHKKAIKKLKQWIGFAGMNGNDISKSIARLEKMQQQTMNKYKELADNLEKKLKSS
>NZ_CP023777.1|WP_098194725.1|3533550_3534438_-|mechanosensitive-ion-channel
MAKDQATYNKKQTKNDRLIFIVKLIVYIALVYVKLNHVDWFAKYNWVTRVMDGLMFFLGANLVISLSRLVLISWYTRKHNLPPLTRDNFVLGLNRISSVLNTTFIVLSLIIVFGYDLSQFITSITIVAAAIAILSKDYIANMINGLIIMFSDQLSLGDHIRIDDYKGKILDITLVNIVLQNDDDDIVLLPNSVIFTSIITNQSKQNIKKLSIEFELDIKHAQSPEELELQLKKAIAPSIKNNISEQSFSLKTLDIKKDLVKFKVQLLLPNQNKELARTIKRELNTAIMAISKEMA
>NZ_CP023777.1|WP_098196259.1|3535020_3536223_+|alanine-dehydrogenase
MTHIGLIREGKVPSDNRVAFTPQQCAWIMENYPQVSFTVQPSPDRCFSDDEYRQEGVPLSEDLNHCDILMGIKEVPVQQLIPGKKYLFFSHTKKLQEQNKDLLRSIIDKKITLIDYECLVHDDGQRILGFGFFAGVVGAHNGLLAYGQRTGSFTFKRVHQCKDFQELITHYFGVKLPPMKIVVTGSGRVAAGILEVMGLLGIKYVTPDEFLICQYKYPVYTQLKAGELYLKKTDKSYSREDFHRNPGAYECKFLPFATVSDVLMNGIYWDKNIPQLFTWEDLALDNFRIQAIADITDDKFGSVPCNLGDTSIDDPIYGVHKRKREKTEDPFDPDSITMMCVGNLPNELPRDASQYFGDQLMKYVFDDLLMEKSELIRRATIIDAGKLTKKYSYMRDYAGV
>NZ_CP023777.1|WP_098194726.1|3536372_3537056_-|hypothetical-protein
MEASNQSSGATAGIMDKENLKSFYKKQLPGILKTVFLKPVNGTYDLFKQPGEGVYGNALLLMLSTMILYFLTPYILAGKYLREILSFGMLLKCGLVAGLFMLIISTLSFGIKSISGKPVFKQELLTGALCGIGLVLLLVVVLLVKMFGSSVNVYDMMNPAGIIRSIGFMMVFIVYIFLFMINIFQQSLRASGTQETISWYISPIAIMFAFYITGKLAAEFLMPSSPF
>NZ_CP023777.1|WP_098194727.1|3537221_3539246_+|tetratricopeptide-repeat-protein
MKFLLLFLVAFYMIFPLEAQQLQRSIDSLNYLLSRHTEQDTTRLKLLNELAFNYYSVSPDKGLELAMEAEQLAKKLHNINGMAVANSRIGVNYWAKGEYGKAMEYNNRAIAIYKESGNRLSYAKNLNNRGISHFALGDYVASLRDHEEALAAFQSLFYQPGVQHSYNNMGTVFLTLNDYPKALDAFLSALRVKGNDDPYLQASVLSNIGLVYKNWKQYDKALAYEQDALKIYTDFGSKRGMASCYSNIASLYDFMHQPGKAIEQFRKSLEINTEIGNREKVASDLTNLGMVYRDQNKKDSAVQYLKHAIELYREQGNKGDLSIAQISLASAIGGPPAEVLKIQEAALKNARESEIPLRISEALLAISETYEHGGQWAAAMKAFKEHAALKDSIYNQEKDREITRKQMSFDFEKKEAAAKAEIQRQSTMRKATMLAGGGLLCAAMLGFILYKRRRDMISIKKEAAFKTLVAETELKALRSQMNPHFIFNSLNSIGDYILKNDTKAARDYLANFSKLMRLTLENSLYPEISLQEDLKFVEMYLAVERKRLQGKFDYRISCSEAIDAENILLPPMLLQPFIENSIWHGFHGDFENGMIEINIAMQGNKLLCSIEDNGQGRRHADTVGKPASLGMSITRSRLDILNAQHTSGALATLQIIDKLKGVKVELLLPLIQKF
>NZ_CP023777.1|WP_098194728.1|3539251_3540010_+|response-regulator-transcription-factor
MGMNIAIVDDEQHCIDALLELLNHYSEHIASIKTYGNVEAAVKGINSFKPDILFLDIQLQDQTGFDVLKQLRFKDFNLVFCTAFEQYAITAFKFSAMDYLLKPIAGEEFNETMEKLLAKSEKDALNGKMQVLMSHLESSGQQHKKICIPTIDGYVFLKMQEIIRCQADVNYTYIFTADQQKFVVSKTLKHFEDLLKPPHFFRVHNSHLVNMDYIQKYTKGKGGFVTLSDQTVLEVSTRRKDEFLRLCKLLEK
>NZ_CP023777.1|WP_098194729.1|3540257_3541547_+|hypothetical-protein
MNYKNFKWLSFGLLPFFLLSCDKDDDQPKQQKVTISIENILDSRPLVESGTFKNDGAAPVVMPGESISLQFYAAKGQAISFATMYGWSNDLFFAPENPGIKLYSEDGTPIEGDVSSQIKLWDNGTRINQTPGASVTHPGTAETSPKNIMQISGMDEQGNKYEAASNLMKASLHYDGNSQFTLTIENISGGTMNETPFSPGVWAVSYIAGGNLLMPNPLYVNGEVSKNGLTNIAEMGDNSVLGDYIAGQTGIFTPLSPVLVVVYNGIDNPIYKTGENDRGKGLKNLAQKGDASVLAAYLETLPGVKNVYVLPAESSTVLLPMINGAAGSKVSQDLNVSKGDRVAIATMYGLSNDWFFASKDNGVDAMEKGDISNTIGLYDDGTAVNQFPGAGITQFNLAGTPLDESKAIEAVPNPNEFTTLPSIIKVTLE
>NZ_CP023777.1|WP_098194730.1|3541633_3542302_+|AhpC/TSA-family-protein
MLYKLIKMNMLKGILTKGVPVLILLLCSLMPSLKAQQVDQYPSMPEDISPLLNGEKIPALMLRDMAGKSVDLNAEFMNKPTVLVVYRGGWCPFCNKQLSALQEAFPALKEMGYQLIAVSTDSPGNLKMTAEKDQLEYTLLSDADLHAAKSLGIAYMAPKAYHKLLPNSTGGLDKDLLLPVPSVFILDKKGVIHFEYINPDFKQRLDAGLLKTVAAGLYKDLM
>NZ_CP023777.1|WP_098194731.1|3542839_3543901_+|diguanylate-cyclase
MNKSVRLIFLVLILTLNLSCSERISTRKEANKPGLVATSKTDTLKFTSGIRAIFQDREGNYWFGSHEEGVSVYNGISFEYFTTHDGLPGNQIRSIQEDNNDKIWIGTSNGASVYDKGTFTNYSTKANEPKYDWNKTIGDLWFYAVEEGGINRFDGNNMNYLIFPKPKNETPDNSYGVTGISKDKDGNVWIATYAALFNYDGKMVTIFDHKTLKLKDNELLHIRSVLADSKGRIWIGNNGIGVLLMEGNSIINFSEKYNLIHPASTRRGDKSPRGTLEHVFAIEEDSEGNIWFGDRDSGAWKYDGKKLTNYSISEKLSNPMIWSIYEDQDKNLLFGMAAGGVYKFNGKTFVKQF
>NZ_CP023777.1|WP_098194732.1|3544088_3544928_+|AraC-family-transcriptional-regulator
MIREFNDSNTAGRFIMHVNNEFLHGLGMRDEVPQTINTFVYNKGEEQTVTIDEINYKMPSKSILPLVSNQHFSFEHPAALLAWQFNREFYCILDHDAEVGCVGFLFYGIHHPMFILLGEKEVRDMAQLEQTFGDEWQFKDKFQGEMLRTLLKRLIIKATRVAKEQCDDYRDLPDDKLDIVRKFSLILEGNFRKEHGVKFYADGLNKSPKTLTNLFALLNQQSPSKLIQNRIILEAKRYLHYTDKSAKEIAYELGFESPAHFSKFFKSYAGDNISSFRKK
>NZ_CP023777.1|WP_098194733.1|3544986_3545637_-|NAD(P)-dependent-oxidoreductase
MKIALIGASGFVGNTVLNELLNRGHEVTAIARNVDKLGLDSSNLTKVPADVYDTARLAQVLKGHDAVINTFNSGWNNPNIYDDFLRGSGSIQEATKQAGVKRILTVGGAGSLYIDGQQLVDSPGFPEAFKAGALAARDYLNELRKEAVLDWTFLSPAIEMHHGIERKRTGAYRSGLENPVFNDEQRSWITVDDLAVAIVDEIENPKHIRQRFTVAY

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Click the colored protein region to show detailed information

Crispr_ID: NZ_CP023777_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP023777_11

4402527-4402680

Orphan

Consensus_repeat	Method
AAGCTCGGACCCACGCACAATTGTCAACATTTACAATTGTACCGGAAACCAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP023777_11

>merge|NZ_CP023777|11|4402527-4402680|CRISPRCasFinder
AAGCTCGGACCCACGCACAATTGTCAACATTTACAATTGTACCGGAAACCAAACAGTACGTACTCATTGCACGACGAGCCTCCTGGCTGGTTCGAGCTTCCAAGCTCGGACCCACGCACAATTGTCGACATTTACAATTGTACCGGAAACCAAA

>NZ_CP023777|11|11|4402527-4402680|CRISPRCasFinder
AAGCTCGGACCCACGCACAATTGTCAACATTTACAATTGTACCGGAAACCAAA	CAGTACGTACTCATTGCACGACGAGCCTCCTGGCTGGTTCGAGCTTCC
AAGCTCGGACCCACGCACAATTGTCGACATTTACAATTGTACCGGAAACCAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP023777.1\|WP_098195362.1\|4391321_4394552_+\|DNA-polymerase-III-subunit-alpha	unknown	unknown	gnl\|CDD\|235553
NZ_CP023777.1\|WP_098195358.1\|4387682_4388021_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378935
NZ_CP023777.1\|WP_098195367.1\|4399187_4402409_+\|DUF2723-domain-containing-protein	unknown	unknown	gnl\|CDD\|378545
NZ_CP023777.1\|WP_098195361.1\|4389809_4391306_+\|DNA-polymerase-Y-family-protein	unknown	unknown	gnl\|CDD\|176458
NZ_CP023777.1\|WP_098195374.1\|4411179_4412058_+\|nucleoside-phosphorylase	unknown	unknown	gnl\|CDD\|350155
NZ_CP023777.1\|WP_098195360.1\|4389076_4389808_+\|Error-prone-repair-protein-ImuA	unknown	unknown	gnl\|CDD\|226918
NZ_CP023777.1\|WP_098195371.1\|4408025_4409330_+\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP023777.1\|WP_098195363.1\|4395134_4396406_-\|site-specific-integrase	unknown	unknown	gnl\|CDD\|271185
NZ_CP023777.1\|WP_098195376.1\|4412946_4413885_+\|magnesium-transporter-CorA-family-protein	unknown	unknown	gnl\|CDD\|213361
NZ_CP023777.1\|WP_098196313.1\|4396932_4397745_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|235726
NZ_CP023777.1\|WP_098195369.1\|4405259_4406354_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|227204
NZ_CP023777.1\|WP_098195366.1\|4398746_4399064_+\|antibiotic-biosynthesis-monooxygenase	unknown	unknown	gnl\|CDD\|367760
NZ_CP023777.1\|WP_098196314.1\|4402894_4404046_-\|TIGR03364-family-FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|132407
NZ_CP023777.1\|WP_098195365.1\|4397922_4398750_+\|SAM-dependent-chlorinase/fluorinase	unknown	unknown	gnl\|CDD\|376645
NZ_CP023777.1\|WP_098195368.1\|4404270_4405101_-\|sugar-phosphate-isomerase/epimerase	unknown	unknown	gnl\|CDD\|224007
NZ_CP023777.1\|WP_098195375.1\|4412111_4412891_+\|diaminopimelate-epimerase	unknown	unknown	gnl\|CDD\|234768
NZ_CP023777.1\|WP_098195373.1\|4410620_4410848_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP023777.1\|WP_098195370.1\|4406382_4407894_+\|magnesium-chelatase	unknown	unknown	gnl\|CDD\|224160
NZ_CP023777.1\|WP_098195359.1\|4388198_4389002_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|378971
NZ_CP023777.1\|WP_098195372.1\|4409383_4410112_+\|DUF1080-domain-containing-protein	unknown	unknown	gnl\|CDD\|368908

Protein	Function_ID	Function_description	E-value
NZ_CP023777.1\|WP_098195362.1\|4391321_4394552_+\|DNA-polymerase-III-subunit-alpha	gnl\|CDD\|235553	PRK05672, dnaE2, error-prone DNA polymerase; Validated.	0
NZ_CP023777.1\|WP_098195358.1\|4387682_4388021_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378935	pfam12728, HTH_17, Helix-turn-helix domain. This domain is a DNA-binding helix-turn-helix domain.	2.56313e-07
NZ_CP023777.1\|WP_098195367.1\|4399187_4402409_+\|DUF2723-domain-containing-protein	gnl\|CDD\|378545	pfam11028, DUF2723, Protein of unknown function (DUF2723). This family is conserved in bacteria. The function is not known.	5.11786e-90
NZ_CP023777.1\|WP_098195361.1\|4389809_4391306_+\|DNA-polymerase-Y-family-protein	gnl\|CDD\|176458	cd03468, PolY_like, DNA Polymerase Y-family. Y-family DNA polymerases are a specialized subset of polymerases that facilitate translesion synthesis (TLS), a process that allows the bypass of a variety of DNA lesions. Unlike replicative polymerases, TLS polymerases lack proofreading activity and have low fidelity and low processivity. They use damaged DNA as templates and insert nucleotides opposite the lesions. The active sites of TLS polymerases are large and flexible to allow the accomodation of distorted bases. Expression of Y-family polymerases is often induced by DNA damage and is believed to be highly regulated. TLS is likely induced by the monoubiquitination of the replication clamp PCNA, which provides a scaffold for TLS polymerases to bind in order to access the lesion. Because of their high error rates, TLS polymerases are potential targets for cancer treatment and prevention.	3.9215e-68
NZ_CP023777.1\|WP_098195374.1\|4411179_4412058_+\|nucleoside-phosphorylase	gnl\|CDD\|350155	cd00436, UP_TbUP-like, uridine phosphorylases similar to Trypanosoma brucei UP. Uridine phosphorylase (UP) catalyzes the reversible phosphorolysis of uracil ribosides and analogous compounds to their respective nucleobases and ribose 1-phosphate. Trypanosoma brucei UP has a high specificity for uracil-containing (deoxy)nucleosides, and may function as a dimer. This subfamily belongs to the nucleoside phosphorylase-I (NP-I) family, whose members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases, such as purine nucleoside phosphorylase (PNPs, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases, such as AMP nucleosidase (AMN, EC 3.2.2.4), and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.	2.55571e-164
NZ_CP023777.1\|WP_098195360.1\|4389076_4389808_+\|Error-prone-repair-protein-ImuA	gnl\|CDD\|226918	COG4544, COG4544, Uncharacterized conserved protein [Function unknown].	2.49731e-44
NZ_CP023777.1\|WP_098195371.1\|4408025_4409330_+\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	2.92413e-33
NZ_CP023777.1\|WP_098195363.1\|4395134_4396406_-\|site-specific-integrase	gnl\|CDD\|271185	cd01185, INTN1_C_like, Integrase IntN1 of Bacteroides mobilizable transposon NBU1 and similar proteins, C-terminal catalytic domain. IntN1 is a tyrosine recombinase for the integration and excision of Bacteroides mobilizable transposon NBU1 from the host chromosome. IntN1 does not require strict homology between the recombining sites seen with other tyrosine recombinases. This family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	3.42213e-48
NZ_CP023777.1\|WP_098195376.1\|4412946_4413885_+\|magnesium-transporter-CorA-family-protein	gnl\|CDD\|213361	cd12827, EcCorA_ZntB-like_u2, uncharacterized bacterial subfamily of the Escherichia coli CorA-Salmonella typhimurium ZntB family. A uncharacterized subfamily of the Escherichia coli CorA-Salmonella typhimurium ZntB (EcCorA-ZntB_like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes.The EcCorA-ZntB-like family includes the Mg2+ transporters Escherichia coli and Salmonella typhimurium CorAs, which can also transport Co2+, and Ni2+. Structures of the intracellular domain of EcCorA-ZntB-like family members, Vibrio parahaemolyticus and Salmonella typhimurium ZntB, form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA. Natural variants such as GVN and GIN, such as occur in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.	2.51963e-111
NZ_CP023777.1\|WP_098196313.1\|4396932_4397745_+\|SDR-family-oxidoreductase	gnl\|CDD\|235726	PRK06181, PRK06181, SDR family oxidoreductase.	2.3219e-96
NZ_CP023777.1\|WP_098195369.1\|4405259_4406354_+\|hypothetical-protein	gnl\|CDD\|227204	COG4867, COG4867, Uncharacterized protein with a von Willebrand factor type A (vWA) domain [General function prediction only].	5.087e-60
NZ_CP023777.1\|WP_098195366.1\|4398746_4399064_+\|antibiotic-biosynthesis-monooxygenase	gnl\|CDD\|367760	pfam03992, ABM, Antibiotic biosynthesis monooxygenase. This domain is found in monooxygenases involved in the biosynthesis of several antibiotics by Streptomyces species. It's occurrence as a repeat in Streptomyces coelicolor SCO1909 is suggestive that the other proteins function as multimers. There is also a conserved histidine which is likely to be an active site residue.	6.75727e-12
NZ_CP023777.1\|WP_098196314.1\|4402894_4404046_-\|TIGR03364-family-FAD-dependent-oxidoreductase	gnl\|CDD\|132407	TIGR03364, putative_secreted_oxidoreductase, FAD dependent oxidoreductase TIGR03364. This clade of FAD dependent oxidoreductases (members of the pfam01266 family) is syntenically associated with a family of proposed phosphonatase-like enzymes (TIGR03351) and is also found (less frequently) in association with phosphonate transporter components. A likely role for this enzyme involves the oxidative deamination of an aminophosphonate differring slightly from 2-aminoethylphosphonate, possibly 1-hydroxy-2-aminoethylphosphonate (see the comments for TIGR03351). Many members of the larger FAD dependent oxidoreductase family act as amino acid oxidative deaminases.	2.11796e-122
NZ_CP023777.1\|WP_098195365.1\|4397922_4398750_+\|SAM-dependent-chlorinase/fluorinase	gnl\|CDD\|376645	pfam01887, SAM_adeno_trans, S-adenosyl-l-methionine hydroxide adenosyltransferase. This is a family of proteins, previously known as DUF62, found in archaebacteria and bacteria. The structure of proteins in this family is similar to that of a bacterial fluorinating enzyme. S-adenosyl-l-methionine hydroxide adenosyltransferases utilizes a rigorously conserved amino acid side chain triad (Asp-Arg-His) which may have a role in activating water to hydroxide ion. This family used to be known as DUF62.	4.81556e-75
NZ_CP023777.1\|WP_098195368.1\|4404270_4405101_-\|sugar-phosphate-isomerase/epimerase	gnl\|CDD\|224007	COG1082, IolE, Sugar phosphate isomerases/epimerases [Carbohydrate transport and metabolism].	3.80764e-21
NZ_CP023777.1\|WP_098195375.1\|4412111_4412891_+\|diaminopimelate-epimerase	gnl\|CDD\|234768	PRK00450, dapF, diaminopimelate epimerase; Provisional.	4.70364e-79
NZ_CP023777.1\|WP_098195370.1\|4406382_4407894_+\|magnesium-chelatase	gnl\|CDD\|224160	COG1239, ChlI, Mg-chelatase subunit ChlI [Coenzyme metabolism].	7.40283e-65
NZ_CP023777.1\|WP_098195359.1\|4388198_4389002_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|378971	pfam12844, HTH_19, Helix-turn-helix domain. Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.	2.4484e-10
NZ_CP023777.1\|WP_098195372.1\|4409383_4410112_+\|DUF1080-domain-containing-protein	gnl\|CDD\|368908	pfam06439, DUF1080, Domain of Unknown Function (DUF1080). This family has structural similarity to an endo-1,3-1,4-beta glucanase belonging to glycoside hydrolase family 16. However, the structure surrounding the active site differs from that of the endo-1,3-1,4-beta glucanase.	3.60234e-47

>NZ_CP023777.1|WP_098195367.1|4399187_4402409_+|DUF2723-domain-containing-protein
MNFNRINNIVGWLVCIFACVVYLMTMEATGSLWDCGEFISAAYKVQVPHPPGAPLFVLIGRMFTLPFKPTEASLGINIMSALSSGFTILFLFWTITHFARRIVQKAGQTLTGNQVTAIMGAGIVGAAAYTFSDSFWFSAVEGEVYAMSSLFTAVVFWAMLKWEHEADQKYADRWIILIAYLMGLSIGVHLLNLLTIPAMVMIYYFKKNKGATKNWGIFWAFMVGCLLTGLVQKFIIQDTITVSGIMDVFFVNTLGLPFFSGFTFYFLAIFAVMITGYFKPKFGLYAPLILVASVFFIPVLDPGGSGGAKMLKVILGALTLTLPTILKKFDIDLSIHKIKHFVQLTTACIIFLLLGYSTYVTTLIRSSANPSVDMYNVDNPVSLVGYLGREQYGDFPLIYGQVFTASPTDYKETGNVYMRGKDRYEIAGKKMKPVYDSKDMMLFPRVWDASNEQGHADYYRSFLNLGKDEKPNFVDNIKFFLGYQVNFMYIRYFLWNFAGKQNDTQWSGNVRDGNWISGIAPIDNVLYGDQSEMPDSLKNNKAHNKYYFLPLILGLVGFFYQYKRHKKDSLIVSLLFFFTGLAIVLYLNQAGNQPRERDYAYVGSFYAFAIWIGLGVLSISEFIEKKSKFKMSAVLATVLCFVAVPLLMGFQNWDDHDRSQKLLARDVAKDYLESCAPNAILFTVGDNDTYPLWYAQEVEGIRPDVRVINLSLLGVDWYIDQQRRMVNQSPAIPMTWSAATYRGDNRNYVQYVDAGVFPQDRFYNLKEVMQFIASDDNRAKLSTSRGDKMNYLPTQKLFIPVNVEEVIKNGTVSIEDSANITPQVTFQLTKNFLYKNDLALLDIIAANDWKRPIYFTGPTGLGLEDYLRVDGLTYRLVPIRRPQSDEILPGLQDNINIPVMEKNLMTKFDFGGAQTPGTYFDEPNRRMLQVIRNAYTKAGVALSKVDEKERALKLLNRMDTNILDQNFPYAMTSPGNMHNLYSMEVVYAYYLAGDFKKGNEISDKIIRDLSQQLNYYQNLPNSKMTGDLRDDAMRAERFKQMLEQMKQEFAKTPTTSPTSVDGHQQINTMDSSK
>NZ_CP023777.1|WP_098195366.1|4398746_4399064_+|antibiotic-biosynthesis-monooxygenase
MILRIVKMIFDPGKTGEFEALFARQKEAIRNFPGCTHLELWRESPGGNIYFTYSHWNSPADLESYRHSELFRETWAATKILFAGKPEAWSLNRVAGPVAGATTPL
>NZ_CP023777.1|WP_098195365.1|4397922_4398750_+|SAM-dependent-chlorinase/fluorinase
MAIITLTSDIGLQDYLVGAIKGQLLQYCPGHHVMDISHQVSPFNLPQAAYICKSAFRHFPAGTFHLVLINLFDKKPEHMLIVPYDDQFLVCADNGLITMLMGEKPKEVYKIPLADNSPRNTIQIIRILAATLQQLIDGKSLEAVGSKDDNIIEKKNLQPLTGEDYIEGQIIHIDNFENVVVNITREQFEQHRQGRKFAIYFRRDEVINNISESYPDVPEGHKLALFNAAGYLEIAVNKGNAAGLFGLQGFDRGQLIQPTPYTQLSFYQTVRIIFE
>NZ_CP023777.1|WP_098196313.1|4396932_4397745_+|SDR-family-oxidoreductase
MNQFFQHKVVVVTGGTSGIGKAIAEEALKLGAAVAVCGRKQEALDQLQASLQSNRLLTCVADVSKEEDCKRFIEQTLQRFGRLDILVNNAGISMRALFKDAEVKVLQQLMDINFWGTVYCSKFALPEIIKQKGTIVGVSSIAGYRGLPGRTGYSASKFAMQGFLEALRTENLHTGVNVMWVCPGFTASNIRNTALNQHGAAQGDTPLDEGKLMSSEEVAQHTLKAIAKRKRTLVLTGQGKLTVFMSRMFASLADKLVFNHFKKEPGSPLQ
>NZ_CP023777.1|WP_098195363.1|4395134_4396406_-|site-specific-integrase
MSKQDISILFWLKRSVARRSEDGKAPIYIRVTIDGRKAEISLSRKVHPDNWDEKNKQVLGKDPEVKIINRKISQAEVDLDRHFTALQAQYQYVTPEMVKNLYEGRPAIPVDPIEEVSFLEAFDYFITRFEKLVKIKKRSGETLRKWNSNRNKIKVFIKHQFKKENVLLRQLPVSVADDLLDFLMIEQDLANNTAMKLVKDTKQVLKMAKRKGWLLNNPMEEFVCTYEDPGIEELEMDEVLAIYNKELTIDRLVEVRDASIFQCFTGFAYQDIYALGPEHYITVNGEKWLKKPRGKTGEKELLPVLPIAAALIEKYTDHPYCRQRGTLLPINSNSRYNGYLKEIADLCGIKKKLTTHVFRHTFATTIALEQGISLEVVQTMLGHRSIRTTQRYARIKKKRMAREMNGLKDELFDEGGKLRIPAV
>NZ_CP023777.1|WP_098195362.1|4391321_4394552_+|DNA-polymerase-III-subunit-alpha
MHYTELQVTTNFSFLRGGSHPEELVAQAAELGYDALAITDHNTLAGIVRAHAAAREKNIRIIPGCRLDLQDGPSLLAYPTDKAAYARLSGLLTVGNFRTEKGNCLLYKSDVYRYREGLLFIVIPPDSLNLYFDFEETFKAALREYRQVLGQCLYLGMMRSYQADDTKRLFRLSQLAKDLDVPLIATNDIHYHERERRELQDILTCIREKCTIYNAGFRLFQNAERYMKPEPEMLRLFRQNPDAIARTGEIAAACRFSLDSLEYVYPEEITGGDRTPQEELALLTWQGARERYGGQVPEAVCKAIDEELAFISKKNYAAYFLTVHDLVCFARSRQILCQGRGSAANSAVCYCLGITSVDPVKFKLLFARFMSDARDEPPDIDVDFEHERREEVMQYIYGKYGRDRAGIVATVTRVHWKGAIRDVGKAMGLSVDAVDRLSKSGYELTTEWLEGKASSSEGFDPGDPHLLKVLELTQQYIGFPRQLGQHTGGFVITQGKLSDLCPVLNARMENRSNIEWNKDDIEALGFLKVDVLALGMLTCIRKAFDLAQQHYGLELTLASIPQDDPAVYTMISHADTLGVFQIESRAQMSMLPRLRPKCFYDLVIEVAIVRPGPIQGDMVHPYLRRRNGEEPVEYPSKELEDILGRTLGVPLFQEQAMEIAIVAAGFTPAEADGLRRSMATFKAKGKVSDWEKKLVEGMIAKGYKEDFARRVFRQLEGFGSYGFPESHAASFALLVYVSSWLKCYYPDVFAAALLNSMPMGFYQPAQIVIDAQKHGVSVLPVDVNLSTWDHRLDERKGKYYPLRLGLRQVKGLKEEEMQLLVSKRQSPYHSINELCDAGVGMAALEKLADADAFRSLGLDRRQALWDVTALCDHPTGLFEGQPSGSSHEKATLLPAMSAPEHVLQDYSALSLSLKAHPVSFVRRQLYHQGILPTNELNLWPDGTMVKVAGLVLVRQRPATATGVCFITIEDETGTSNLVIFQKLFDKYRKEIVRSTLLMVEGKLQRAGEVTHVIVKSCHDLSGLLSELNIPTLAIPDVQTLSRADEGKDTDYEGSDKHVKKPAVVQGEIFPGGRNFK
>NZ_CP023777.1|WP_098195361.1|4389809_4391306_+|DNA-polymerase-Y-family-protein
MERYLSIWFPRLLTDWKERHEPNLKGKAFVLAELERGRKVIRAVSAAAQPYGIRYGTVVADARAAYPSLLVYDYDPDQSLILLGNIAEWCIHYSPVVGVDSPDGLVLDISGCTHLWGGEIPYLEKITGKFKTTGYSVQGAIADTIGAAWAQARYGNSPFIIPPGRQREALLALPPAALRLEPGLLNRMRKLGFYQVGNFISIPRGTLRRRFGQQLLDRLAQALGEAREALTPVIPVAPYQEHLPSLEPIQSAAGIEIALQRLLETLCRRLFREGVGLRKAVLTVYRIDGKKQQLEIGTNRPSRHTAHLLKLFKLKTQAIAPGLGIELFVLEAPVVEELTQTTETLWKCHDPADEEAVADLLDRMAGRLGASAIRRYLPQEHYWPERATRPAASLSEPCTTGWRSHVPRPVCLLAVPLAIEVMVPLPDYPPIQFRYRGTWHKVKKADGPERIEQEWWMQQGDHRDYYCVEDEPGRRYWIFRLGLYGKDTPEWFLHGFFA
>NZ_CP023777.1|WP_098195360.1|4389076_4389808_+|Error-prone-repair-protein-ImuA
MEIAETKKSIIEKLQRQILELQGIRDTGTSKVKGLGEVEKAFPNGTFPTGVIHEFTSNEYGGYVATHGFIAALLGKLMAQGGPCLWVSRNRRAAPGGLAAFGIPPERVIFIDLDRDKDLLWTIEEALKCPGLSAVVGEVGNLDFNASRRLQLAVEESRVTGFIHCCRPAYLQQTTSVARWRIAPLPSWLPDGMPGIGHPCWRVELLKVRSGKPGTWDIQYAAGQLRHLDRQSVTAATYLENAG
>NZ_CP023777.1|WP_098195359.1|4388198_4389002_-|helix-turn-helix-domain-containing-protein
MKTQKIFFCGNLKFLRERKHKSQEELANILGIKRSKLAALESGQTKSPLPEDFLNISEYFKISVDSLFKIDLSSLSELSLRQLEAGNDVYITGSNMRVLAMTVDKTSKENLEYVPVKAKAGYIAGHRDPEFIAGLPRFSFPSLPKGKTYRMFTITGDSMLPFPDGCDVIGQYLEDWRDIKPQTLCVAILKGEQDFVFKQVTLKGDGLLMESMNKSYQPYTVPFSEVLELWRFHSYHTVEVPEAQDMQSIATLIREVQAEIKVIKGRR
>NZ_CP023777.1|WP_098195358.1|4387682_4388021_-|helix-turn-helix-domain-containing-protein
MKAPPAGSNLTQRDHIYTNQIVTLADLQDLKLELLEEIRKLLREQQGQPGKKWLKTSEVRKLLDASPGTLQRLRNDGTLPHKKIGGIVYYDYEQISKMLAPDQFSQHKSYKK
>NZ_CP023777.1|WP_098196314.1|4402894_4404046_-|TIGR03364-family-FAD-dependent-oxidoreductase
MNKFDLIVVGGGIMGTFHAYHALMMGKKVLLFERDNYPVGATVRNFGQVVPSGMANEWFEYGRQGLEVYKSIQEEMDISIRNNGSVYIASDDDEQLLLHELKAHFDAKNYTSQLLTKDQILQKYPAIKSSYAKEALFFPQEVSVEPDVLIYKIQSWMKERFENFEIHYNVPVVDCEDKGSDVKVLTAGRGMYTAGQVVICSGNEFKLLFPGVFRESGIVVSKLQMMRTVPMPEVALEGNILTGLTIRRYESFETHCPSFHKISIPDHYHELKRWGIHILFKKAADGSIIIGDSHEYAAAFEADDLGFKLNQYINELMLMEAARIVDFDVKQIAQTWAGYYPQHKDNIFHADLGQRIHIRTAIGGKGMTASIGFTAKSTAEIFQ
>NZ_CP023777.1|WP_098195368.1|4404270_4405101_-|sugar-phosphate-isomerase/epimerase
MTKKLANSLFLICFLLMGSMAMAQDKAEQLGWKLGAQAYTFNRFTLAEALDKIDSCGLKYVECYPGQKIGGGIEGTMDFKMDAATRAKVLGLIKSKGLTLVAYGVVVPSSPADWRKLFEFAKAMGIEVINSEPKDSDLDLVSSLCDEFKIHLAMHDHPKPSHYWHPDSVLVAIKGRSQYMGSCADIGHWVRSGLDPIECLKKLKGHVFSMHFKDLNEKSRRAHDVIWNTGTSNIPAIMATMKEIGFKGPISAEYEYHWDNSVPEVKQSVANFRSLL
>NZ_CP023777.1|WP_098195369.1|4405259_4406354_+|hypothetical-protein
MRGIVFSRFDPNENARSPFDRLLSFFTQLLTYTSGDFNEALQWLMELDKQYQLTDKNYGIGDFLNDLKEKGYIQENELSGEITITPKTEQTIRQGALEEIFGKLKKSTQGNHTTRKPGLGDEINAETRPYNFGDPLENIDMTASIRNAQINHGVNIFDMQQDDLEVRETDFKTQTSTVLMIDISHSMILYGEDRITPAKKVAMALGELITTRYPKDTLDIIVFGNDAWQIQIKDLPYLQVGPFHTNTVAGLELAMDILRRRRNPNKQIFMITDGKPTCLKIGSQYYKNSFGLDRKILNRTLNLAAQCKKLKIPITTFMVATDPYLQEFVNEFTETNSGKAFYSGTDNLGKFLFRDFQSGKRKFY
>NZ_CP023777.1|WP_098195370.1|4406382_4407894_+|magnesium-chelatase
MQHIKTLGELKKSGYKSRSVKEEIRENLITHLKSKTPTFPGIIGYEDTVIPETETALLSRHNILFLGLRGQAKTRMARQMIDFLDEFIPVVAGSEVNDDPFAPLSRYAKDLIAEMGDKTPIEWLSREERYGEKLATPDVSVADLIGDIDPIKAAHQKLSYADERAIHFGIIPRSNRGIFVINELPDLQARIQVALFNILQEGDIQIRGFKLRMPLDILFVFTANPEDYTNRGSIVTPLKDRIESQIITHYPKDVESSLLITEQEANLLPAQEKVVHVPDILKRLIEQVAFEARNSELVDKKSGVSARLTIAAYENLVSAAERRSLINKEKTTMTRISDLHGIIPAITGKIELLYEGEQEGAAQVAYNLLEKAIRNLFAQYFPNPDSFKKRKQPIDPASNPYRPIIQWFDQGNSLQVLQHCSDKQWETNLKKVNGLKELIDARFSAANNNEKLLMMEFVLHGLAAYSLISKKSMDNSTTFSDLLGTIMNFGSDIEEDEDDPYNI
>NZ_CP023777.1|WP_098195371.1|4408025_4409330_+|Gfo/Idh/MocA-family-oxidoreductase
MTGFSRRNFIRSASTILAGTALPGALHAIPRISANDKINVAAIGINGMGWTDLSAMLKHPEAQCVALCDVDKNVLDKRVAELATKGIKVKAYHDYRDLLSNKDIDAVIIGTPDHWHCLQMTDACAAGKSVYVEKPIGNSIVECRTMEAAQQKYNSVVQVGQWQRSQQHFADAIDFVHSGKLGQIRLVKAWAYMGWMKSIPVVADAAAPAGVDYTTWLGPATKRPFNANRFHFNFRWYWDYAGGLMTDWGVHLLDYALYGMKAQFPKSIMAAGGKFAYPDDAAETPDTLTTVYEFDGFNLQWEHATGIDGGPYGRDHGIAFIGNKGTLVLDRGGWEVIPEGNKMEAVPRQKKMDDGVFLHTKNFLDVIKSKNLGQLHAPIQVGAHVAVNAQMGNIAFKTNQKIHWDAANDRFQEQAANEYLAAKYHNGYSIPRIS
>NZ_CP023777.1|WP_098195372.1|4409383_4410112_+|DUF1080-domain-containing-protein
MRKITFTAALALVTFMVQAQDKPEDTEVWKPVPKVIQPGTSTNTAPSDAIILFDGKNLNHWESEKGGPAQWTISGGAMTVKKGTGVIKSKEKFEDFQLHIEFRTPEKVVGEGQGRGNSGIFMQSYYELQVLDNYNNVTYSNGQAGSFYKQRIPLVNACKKPGEWQTYDVIWTAPRFNEDGSLKSPARATVLQNGVLVQNNVSLDGETLYIGKPSYKAHGAMPFILQDHGNPVSYRNIWVRRL
>NZ_CP023777.1|WP_098195373.1|4410620_4410848_-|hypothetical-protein
MKNSRPKPSYYIGLIVFFFAGAGFLIAGFNTSPEKMTDGGAMRSSNVYYLLGSAFVLLAFIGLIAGIKMKERNKS
>NZ_CP023777.1|WP_098195374.1|4411179_4412058_+|nucleoside-phosphorylase
MDRIAESELILNSRGAIYHLDLKPGELADTVITVGDPDRVANVSKHFDKLEGKFQHREFVTHTGYVGDKRISVVSTGIGTDNIDIVLNELDALVNIDFDSRTIKQALQSLKIIRLGTAGALQADIPVDECVVSAFGLGLDNLLPFYSLENSATEQQVLADFKLQVPLKDGTANPYIAGANTGLQNHFKNGFHQGITVTCPGFYGPQGRILRGALSHPELIDQLTGFQSGEHRITNFEMETAGIYGLGKVLGHQCLSISAIVANRVSKQFSKDGAAAVEQLIQKALTVIEKIN
>NZ_CP023777.1|WP_098195375.1|4412111_4412891_+|diaminopimelate-epimerase
MQLHFHKYQGTGNDFVIIDNRQGIYNELSQPTVEKLCDRRFGIGGDGLMLLNGSKDYDFEMIYYNADGRPGSMCGNGGRCLSAFAKKLGIQQNAAKFIASDGPHEVVYAENGWVQLKMQDVDYVEIGPGYFFLDTGSPHFVRYVTGIEEMDVYTEGSNIRYNERFAEEGTNVNFVQETDNGIFVRTYERGVEDETYSCGTGVTAASLTFAKGAPGAYTVPVQTLGGPLEVRFTKVDDRTYNNIWLCGPAEWVFEGDIKI
>NZ_CP023777.1|WP_098195376.1|4412946_4413885_+|magnesium-transporter-CorA-family-protein
MIQFFKNIDAATVEINSPEHDAWVNVAPPLKQSEFEQLSEELDIPLDFLTDSLDIDERSRFELEDNVKLIVIKTPTENNSINESDAYYITIPIVIILTHNQIVTVNSFDNAAIKKFLNTFHNRHPEKRNMMVLKIFEKVTVNFLDYLKEINQRRNALEQKLYDSNRNEELLYLMQIQKSLVYFVTALRSNELLLMKLERTNFLGLNEDEKEFLNDLIVDTSQALEMANVYTNILSSTMDAFASIISNNLNQVMKRLTSITIVLSFPMLVASIYGMNVHIPYAEVPHAFYVPVILSIVISVLMSWYFMKKKWF

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP023777_6	6.18\|1729370\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1729370-1729399	30	MH572378	Microviridae sp. isolate SD_SC_96, complete genome	1022-1051	4	0.867
NZ_CP023777_6	6.3\|1728143\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728143-1728172	30	MK250029	Prevotella phage Lak-C1, complete genome	188019-188048	5	0.833
NZ_CP023777_6	6.4\|1728220\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728220-1728249	30	NC_028683	Edwardsiella phage PEi20 DNA, complete sequence	42222-42251	5	0.833
NZ_CP023777_5	5.6\|1726339\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726339-1726367	29	NZ_CP028348	Novosphingobium sp. THN1 plasmid pTHN, complete sequence	1093527-1093555	6	0.793
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	CP021183	Sphingomonas wittichii DC-6 plasmid pDC02, complete sequence	99721-99750	6	0.8
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	KM659093	Paracoccus yeei strain LM20 plasmid pLM20P1, complete sequence	3681-3710	6	0.8
NZ_CP023777_6	6.3\|1728143\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728143-1728172	30	NC_015418	Clostridium botulinum BKT015925 plasmid p3BKT015925, complete sequence	2302-2331	6	0.8
NZ_CP023777_6	6.3\|1728143\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728143-1728172	30	NC_012040	Campylobacter lari RM2100 plasmid pCL2100, complete sequence	16853-16882	6	0.8
NZ_CP023777_6	6.3\|1728143\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728143-1728172	30	NZ_CP032288	Acinetobacter lwoffii strain ED9-5a plasmid pALWED3.3, complete sequence	4411-4440	6	0.8
NZ_CP023777_6	6.5\|1728297\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728297-1728326	30	MK448388	Streptococcus satellite phage Javan259, complete genome	11870-11899	6	0.8
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	NC_014719	Caldicellulosiruptor kristjanssonii I77R1B plasmid pCALKR01, complete sequence	15143-15172	6	0.8
NZ_CP023777_6	6.21\|1729141\|30\|NZ_CP023777\|PILER-CR	1729141-1729170	30	MN693713	Marine virus AFVG_250M788, complete genome	33669-33698	6	0.8
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_KY888886	Acinetobacter pittii strain IHIT24944 plasmid pAP24944-OXA-58, complete sequence	27131-27159	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_KT965093	Acinetobacter towneri strain G295 plasmid pNDM-GJ02, complete sequence	118-146	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_CP033131	Acinetobacter wuhouensis strain WCHAW010062 plasmid pOXA58_010062, complete sequence	25467-25495	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_CP042558	Acinetobacter baumannii strain E47 plasmid pE47_002, complete sequence	39228-39256	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NC_007103	Bacillus cereus E33L plasmid pE33L466, complete sequence	338737-338765	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	CP040057	Acinetobacter baumannii strain VB35435 plasmid unnamed1, complete sequence	45190-45218	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_CP038502	Acinetobacter baumannii strain CIAT758 plasmid unnamed2, complete sequence	4108-4136	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_CP026416	Acinetobacter sp. ACNIH2 plasmid pACI-3569, complete sequence	33581-33609	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_CP038646	Acinetobacter baumannii strain ACN21 plasmid unnamed2, complete sequence	23018-23046	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_CP039147	Acinetobacter sp. 10FS3-1 plasmid p10FS3-1-4, complete sequence	34094-34122	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_CP009967	Bacillus cereus E33L plasmid pBCO_1, complete sequence	449653-449681	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NC_021734	Acinetobacter baumannii BJAB0715 plasmid pBJAB0715, complete sequence	32506-32534	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_CP032133	Acinetobacter chinensis strain WCHAc010005 plasmid pOXA58_010005, complete sequence	4484-4512	7	0.759
NZ_CP023777_5	5.4\|1726186\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726186-1726214	29	NZ_CP053657	Bacillus cereus strain CTMA_1571 plasmid p.1, complete sequence	85978-86006	7	0.759
NZ_CP023777_5	5.6\|1726339\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726339-1726367	29	NC_014389	Butyrivibrio proteoclasticus B316 plasmid pCY360, complete sequence	239618-239646	7	0.759
NZ_CP023777_5	5.6\|1726339\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726339-1726367	29	MN180248	UNVERIFIED: Wolbachia phage WO isolate Seq1WORi_AMD1 genomic sequence	22678-22706	7	0.759
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP052758	Cellulosimicrobium sp. BI34T plasmid pCPRO01, complete sequence	118641-118670	7	0.767
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP027025	Streptomyces sp. WAC00288 plasmid p3, complete sequence	44451-44480	7	0.767
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_012586	Sinorhizobium fredii NGR234 plasmid pNGR234b, complete sequence	627007-627036	7	0.767
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_011368	Rhizobium leguminosarum bv. trifolii WSM2304 plasmid pRLG201, complete sequence	339767-339796	7	0.767
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	MN813686	Mycobacterium phage BirdsNest, complete genome	10923-10952	7	0.767
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	MK059749	Mycobacterium phage CRB2, complete genome	12694-12723	7	0.767
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP027026	Streptomyces sp. WAC00288 plasmid p4, complete sequence	3095-3124	7	0.767
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_016624	Azospirillum lipoferum 4B plasmid AZO_p5, complete sequence	349973-350002	7	0.767
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP024310	Sinorhizobium fredii strain NXT3 plasmid pSfreNXT3c, complete sequence	380076-380105	7	0.767
NZ_CP023777_6	6.3\|1728143\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728143-1728172	30	NZ_CP040856	Lactobacillus johnsonii strain G2A plasmid unnamed2, complete sequence	71176-71205	7	0.767
NZ_CP023777_6	6.3\|1728143\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728143-1728172	30	NZ_LR214986	Mycoplasma cynos strain NCTC10142 plasmid 13	972163-972192	7	0.767
NZ_CP023777_6	6.3\|1728143\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728143-1728172	30	LC425517	Uncultured phage DNA, contig: NODE382	516-545	7	0.767
NZ_CP023777_6	6.6\|1728374\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728374-1728403	30	NC_004565	Clostridium tetani E88 plasmid pE88, complete sequence	61583-61612	7	0.767
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	NZ_CP019234	Bacillus thuringiensis strain YGd22-03 plasmid pYGD83, complete sequence	67108-67137	7	0.767
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	MN693728	Marine virus AFVG_250M561, complete genome	25024-25053	7	0.767
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	KX373685	Lactococcus phage D4410, complete genome	18981-19010	7	0.767
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	NZ_AP018442	Undibacterium sp. YM2 plasmid pUYM01, complete sequence	17761-17790	7	0.767
NZ_CP023777_6	6.13\|1728913\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728913-1728942	30	AP013980	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C7-MedDCM-OCT-S31-C4, * SEQUENCING IN PROGRESS *	13205-13234	7	0.767
NZ_CP023777_6	6.17\|1729294\|29\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1729294-1729322	29	NZ_CP046399	Bacillus sp. A260 plasmid unnamed11, complete sequence	42323-42351	7	0.759
NZ_CP023777_5	5.5\|1726262\|30\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726262-1726291	30	NZ_CP007453	Peptoclostridium acidaminophilum DSM 3953 strain al-2 plasmid EAL2_808p, complete sequence	504608-504637	8	0.733
NZ_CP023777_5	5.5\|1726262\|30\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726262-1726291	30	GU071095	Synechococcus phage S-SM2, complete genome	79275-79304	8	0.733
NZ_CP023777_5	5.6\|1726339\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726339-1726367	29	NC_014824	Ruminococcus albus 7 = DSM 20455 plasmid pRUMAL01, complete sequence	199547-199575	8	0.724
NZ_CP023777_5	5.6\|1726339\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726339-1726367	29	MN812219	Flavobacterium phage vB_FspS_morran9-1, complete genome	14862-14890	8	0.724
NZ_CP023777_5	5.6\|1726339\|29\|NZ_CP023777\|PILER-CR,CRISPRCasFinder	1726339-1726367	29	MN180248	UNVERIFIED: Wolbachia phage WO isolate Seq1WORi_AMD1 genomic sequence	23974-24002	8	0.724
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP014516	Frondihabitans sp. PAMC 28766 strain SR6 plasmid 3, complete sequence	56927-56956	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP021082	Deinococcus ficus strain CC-FR2-10 plasmid pDFI1, complete sequence	491965-491994	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_006362	Nocardia farcinica IFM 10152 plasmid pNF1, complete sequence	38019-38048	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_004320	Corynebacterium efficiens YS-314 plasmid pCE3, complete sequence	27745-27774	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP018229	Rhizobium leguminosarum strain Vaf-108 plasmid unnamed1, complete sequence	657649-657678	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP025431	Paracoccus zhejiangensis strain J6 plasmid pPZ01, complete sequence	209710-209739	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP017563	Paraburkholderia sprentiae WSM5005 plasmid pl1WSM5005, complete sequence	333629-333658	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP054022	Rhizobium sp. JKLM12A2 plasmid pPR12A201, complete sequence	85449-85478	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_020553	Corynebacterium callunae DSM 20147 plasmid pCC2, complete sequence	9973-10002	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP006990	Rhizobium sp. IE4771 plasmid pRetIE4771d, complete sequence	716468-716497	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP048642	Streptomyces aureoverticillatus strain HN6 plasmid unnamed, complete sequence	18964-18993	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_023285	Streptomyces sp. F8 plasmid pFRL5, complete sequence	145186-145215	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_019789	Deinococcus peraridilitoris DSM 19664 plasmid pDEIPE01, complete sequence	508737-508766	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP048281	Rhizobium leguminosarum bv. viciae 248 plasmid pRle248e, complete sequence	330061-330090	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP021127	Rhizobium sp. Kim5 plasmid pRetKim5c, complete sequence	643657-643686	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP054028	Rhizobium sp. JKLM19E plasmid pPR19E01, complete sequence	1419592-1419621	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_012848	Rhizobium leguminosarum bv. trifolii WSM1325 plasmid pR132501, complete sequence	83733-83762	8	0.733
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	CP007644	Rhizobium etli bv. phaseoli str. IE4803 plasmid pRetIE4803c, complete sequence	699124-699153	8	0.733
NZ_CP023777_6	6.6\|1728374\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728374-1728403	30	KY942057	Dickeya phage XF4, complete genome	8363-8392	8	0.733
NZ_CP023777_6	6.6\|1728374\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728374-1728403	30	MG266157	Dickeya phage PP35, complete genome	8363-8392	8	0.733
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	MK433577	Klebsiella phage ST512-KPC3phi13.6, complete genome	28943-28972	8	0.733
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	NC_049453	Klebsiella phage ST13-OXA48phi12.1, complete genome	32071-32100	8	0.733
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	MK433581	Klebsiella phage ST258-KPC3phi16.1, complete genome	28943-28972	8	0.733
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	MK416011	Klebsiella phage ST437-OXA245phi4.1, complete genome	28942-28971	8	0.733
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	MN693705	Marine virus AFVG_250M220, complete genome	7005-7034	8	0.733
NZ_CP023777_6	6.9\|1728605\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728605-1728634	30	KP007359	Enterobacteria phage vB_EcoM_VR5, complete genome	136888-136917	8	0.733
NZ_CP023777_6	6.10\|1728682\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728682-1728711	30	NZ_AP018259	Calothrix sp. NIES-4071 plasmid plasmid4 DNA, complete genome	7987-8016	8	0.733
NZ_CP023777_6	6.10\|1728682\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728682-1728711	30	MH884508	Bacillus phage vB_BcoS-136, complete genome	8928-8957	8	0.733
NZ_CP023777_6	6.14\|1728990\|29\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728990-1729018	29	JQ823122	Persicivirga phage P12024S, complete genome	32597-32625	8	0.724
NZ_CP023777_6	6.14\|1728990\|29\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728990-1729018	29	NC_018272	Persicivirga phage P12024L, complete genome	33395-33423	8	0.724
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP029358	Azospirillum sp. CFH 70021 plasmid unnamed3	399040-399069	9	0.7
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_CP053567	Pseudonocardia sp. Gen01 plasmid unnamed3, complete sequence	20506-20535	9	0.7
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NC_023284	Streptomyces sp. F2 plasmid pFRL4, complete sequence	103282-103311	9	0.7
NZ_CP023777_5	5.9\|1726569\|30\|NZ_CP023777\|CRISPRCasFinder	1726569-1726598	30	NZ_AP018921	Pseudonocardia autotrophica strain NBRC 12743 plasmid pPA12743CP, complete sequence	230218-230247	9	0.7
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	MN694758	Marine virus AFVG_250M853, complete genome	13078-13107	9	0.7
NZ_CP023777_6	6.7\|1728451\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728451-1728480	30	MN694077	Marine virus AFVG_250M852, complete genome	13082-13111	9	0.7
NZ_CP023777_6	6.10\|1728682\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728682-1728711	30	NZ_MG205643	Paeniclostridium sordellii strain S0804018 plasmid pCS1-5, complete sequence	11595-11624	9	0.7
NZ_CP023777_6	6.12\|1728836\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728836-1728865	30	NZ_CP034477	Pantoea agglomerans strain CFSAN047154 plasmid pCFSAN047154_3, complete sequence	153640-153669	9	0.7
NZ_CP023777_6	6.12\|1728836\|30\|NZ_CP023777\|CRISPRCasFinder,PILER-CR	1728836-1728865	30	NZ_CP034472	Pantoea agglomerans strain CFSAN047153 plasmid pCFSAN047153_3, complete sequence	27393-27422	9	0.7

1. spacer 6.18|1729370|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MH572378 (Microviridae sp. isolate SD_SC_96, complete genome) position: , mismatch: 4, identity: 0.867

cgatcg-ctgtgttggggtgttttcctattt	CRISPR spacer
-gatcgactgtgttgggttgttctcctattc	Protospacer
 ***** ********** ****.*******.

2. spacer 6.3|1728143|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MK250029 (Prevotella phage Lak-C1, complete genome) position: , mismatch: 5, identity: 0.833

aaagatgtttttgatattttagacctaaat	CRISPR spacer
aaagatgttgttgatattgtagacaataat	Protospacer
********* ******** *****   ***

3. spacer 6.4|1728220|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NC_028683 (Edwardsiella phage PEi20 DNA, complete sequence) position: , mismatch: 5, identity: 0.833

-tatctcatttatttgccttgatgataaatt	CRISPR spacer
ttatcgt-tttatttgccttgatggtacatt	Protospacer
 **** . ****************.** ***

4. spacer 5.6|1726339|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP028348 (Novosphingobium sp. THN1 plasmid pTHN, complete sequence) position: , mismatch: 6, identity: 0.793

tgataaagtaaaggaagaaagcgataggt	CRISPR spacer
acagacagtaaagcaagaaagcgattggt	Protospacer
  * * ******* *********** ***

5. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to CP021183 (Sphingomonas wittichii DC-6 plasmid pDC02, complete sequence) position: , mismatch: 6, identity: 0.8

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
aggccagggcggcgatgaccggcccggtga	Protospacer
..*  ***************.*****.***

6. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to KM659093 (Paracoccus yeei strain LM20 plasmid pLM20P1, complete sequence) position: , mismatch: 6, identity: 0.8

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
ggcgcagggcgacgttgaccagcccgatca	Protospacer
*. * ******.** ************* *

7. spacer 6.3|1728143|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NC_015418 (Clostridium botulinum BKT015925 plasmid p3BKT015925, complete sequence) position: , mismatch: 6, identity: 0.8

aaagatgtttttgatattttagacctaaat	CRISPR spacer
gtaattgtttttgatatttttgacgtaaat	Protospacer
. *. *************** *** *****

8. spacer 6.3|1728143|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NC_012040 (Campylobacter lari RM2100 plasmid pCL2100, complete sequence) position: , mismatch: 6, identity: 0.8

aaagatgtttttgatattttagacctaaat	CRISPR spacer
aaagatatttgtgatattttagaaatacaa	Protospacer
******.*** ************  ** *

9. spacer 6.3|1728143|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_CP032288 (Acinetobacter lwoffii strain ED9-5a plasmid pALWED3.3, complete sequence) position: , mismatch: 6, identity: 0.8

aaagatgtttttgatattttagacctaaat	CRISPR spacer
aaagatatttttgatattttaaagatacag	Protospacer
******.**************.*  ** *

10. spacer 6.5|1728297|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MK448388 (Streptococcus satellite phage Javan259, complete genome) position: , mismatch: 6, identity: 0.8

gctccattcaaccaatttgccgctttgctc	CRISPR spacer
ggttcattcaaccaatttccctctttgtcc	Protospacer
* *.************** ** *****..*

11. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NC_014719 (Caldicellulosiruptor kristjanssonii I77R1B plasmid pCALKR01, complete sequence) position: , mismatch: 6, identity: 0.8

gacaattaaatgataaaaactatgttagag	CRISPR spacer
gacaatctaatgataaaaactatcattgac	Protospacer
******. ***************  * **

12. spacer 6.21|1729141|30|NZ_CP023777|PILER-CR matches to MN693713 (Marine virus AFVG_250M788, complete genome) position: , mismatch: 6, identity: 0.8

aatacgcagtagaggtatatccattgctcc	CRISPR spacer
gctacgcaggaaaggtatatccattggacc	Protospacer
. ******* *.**************  **

13. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_KY888886 (Acinetobacter pittii strain IHIT24944 plasmid pAP24944-OXA-58, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

14. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_KT965093 (Acinetobacter towneri strain G295 plasmid pNDM-GJ02, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

15. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP033131 (Acinetobacter wuhouensis strain WCHAW010062 plasmid pOXA58_010062, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

16. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP042558 (Acinetobacter baumannii strain E47 plasmid pE47_002, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

17. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NC_007103 (Bacillus cereus E33L plasmid pE33L466, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
taaagctccttaaaatgaatttctatatg	Protospacer
  ****.********* ********   *

18. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to CP040057 (Acinetobacter baumannii strain VB35435 plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

19. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP038502 (Acinetobacter baumannii strain CIAT758 plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

20. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP026416 (Acinetobacter sp. ACNIH2 plasmid pACI-3569, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

21. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP038646 (Acinetobacter baumannii strain ACN21 plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

22. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP039147 (Acinetobacter sp. 10FS3-1 plasmid p10FS3-1-4, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

23. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP009967 (Bacillus cereus E33L plasmid pBCO_1, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
taaagctccttaaaatgaatttctatatg	Protospacer
  ****.********* ********   *

24. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NC_021734 (Acinetobacter baumannii BJAB0715 plasmid pBJAB0715, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

25. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP032133 (Acinetobacter chinensis strain WCHAc010005 plasmid pOXA58_010005, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
tcaagccacttaaaatcaatttgagcaag	Protospacer
 ****** **************  .  **

26. spacer 5.4|1726186|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP053657 (Bacillus cereus strain CTMA_1571 plasmid p.1, complete sequence) position: , mismatch: 7, identity: 0.759

gcaagccccttaaaatcaatttctagcag	CRISPR spacer
taaagctccttaaaatgaatttctatatg	Protospacer
  ****.********* ********   *

27. spacer 5.6|1726339|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NC_014389 (Butyrivibrio proteoclasticus B316 plasmid pCY360, complete sequence) position: , mismatch: 7, identity: 0.759

tgataaagtaaaggaagaaagcgataggt	CRISPR spacer
agataaagaaaaggaagaaaacgaaggaa	Protospacer
 ******* ***********.*** .*.

28. spacer 5.6|1726339|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to MN180248 (UNVERIFIED: Wolbachia phage WO isolate Seq1WORi_AMD1 genomic sequence) position: , mismatch: 7, identity: 0.759

tgataaagtaaaggaagaaagcgataggt	CRISPR spacer
gaaacaagtaagggaagaaagagataggc	Protospacer
 .*  ******.********* ******.

29. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP052758 (Cellulosimicrobium sp. BI34T plasmid pCPRO01, complete sequence) position: , mismatch: 7, identity: 0.767

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tccggcccgcggcgatgatcagcccgatga	Protospacer
   **   **********.***********

30. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP027025 (Streptomyces sp. WAC00288 plasmid p3, complete sequence) position: , mismatch: 7, identity: 0.767

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
gcacgatgacggcgatgaccagcccgagca	Protospacer
* . ** *.******************  *

31. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_012586 (Sinorhizobium fredii NGR234 plasmid pNGR234b, complete sequence) position: , mismatch: 7, identity: 0.767

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
cgaggtcggcggcgacgaccggcccgatga	Protospacer
 ..**  ********.****.*********

32. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_011368 (Rhizobium leguminosarum bv. trifolii WSM2304 plasmid pRLG201, complete sequence) position: , mismatch: 7, identity: 0.767

gagggag-----ggcggcgatgaccagcccgatga	CRISPR spacer
-----agtccttggcggcgatgccgagcccgatga	Protospacer
     **     ********** * **********

33. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to MN813686 (Mycobacterium phage BirdsNest, complete genome) position: , mismatch: 7, identity: 0.767

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
caacgagggcggcgaaggccagcccgaggg	Protospacer
 *. *********** *.********* *.

34. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to MK059749 (Mycobacterium phage CRB2, complete genome) position: , mismatch: 7, identity: 0.767

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
caccgagggcggcgagggccagcccgacgg	Protospacer
 *  *********** *.*********.*.

35. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP027026 (Streptomyces sp. WAC00288 plasmid p4, complete sequence) position: , mismatch: 7, identity: 0.767

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
gcacgatgacggcgatgaccagcccgagca	Protospacer
* . ** *.******************  *

36. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_016624 (Azospirillum lipoferum 4B plasmid AZO_p5, complete sequence) position: , mismatch: 7, identity: 0.767

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tcggccgggcggcgatgcccagcacgatgc	Protospacer
  **  *********** ***** *****

37. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP024310 (Sinorhizobium fredii strain NXT3 plasmid pSfreNXT3c, complete sequence) position: , mismatch: 7, identity: 0.767

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
ggagcagggcggcgatgaacagcccgccgc	Protospacer
*..* ************* ******* .*

38. spacer 6.3|1728143|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_CP040856 (Lactobacillus johnsonii strain G2A plasmid unnamed2, complete sequence) position: , mismatch: 7, identity: 0.767

aaagatgtttttgatattttagacctaaat	CRISPR spacer
aaagatgtttttgagattttaaaggaatac	Protospacer
************** ******.*   * *.

39. spacer 6.3|1728143|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_LR214986 (Mycoplasma cynos strain NCTC10142 plasmid 13) position: , mismatch: 7, identity: 0.767

aaagatgtttttgatattttagacctaaat	CRISPR spacer
aaaaatgtttttgatgttttagatgaagaa	Protospacer
***.***********.*******.  *.*

40. spacer 6.3|1728143|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to LC425517 (Uncultured phage DNA, contig: NODE382) position: , mismatch: 7, identity: 0.767

aaagatgtttttgatattttagacctaaat	CRISPR spacer
taaactgtttttgaaattttagaactaagc	Protospacer
 **. ********* ******** ****..

41. spacer 6.6|1728374|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NC_004565 (Clostridium tetani E88 plasmid pE88, complete sequence) position: , mismatch: 7, identity: 0.767

tactgagttcaatgaatatttcttgccaac	CRISPR spacer
acataagttcaatgaatatttgtttccaaa	Protospacer
   *.**************** ** ****

42. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_CP019234 (Bacillus thuringiensis strain YGd22-03 plasmid pYGD83, complete sequence) position: , mismatch: 7, identity: 0.767

gacaattaaatgataaaaactatgttagag	CRISPR spacer
tcaaattaaatgataaaaacgctgttagct	Protospacer
   *****************  ******

43. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MN693728 (Marine virus AFVG_250M561, complete genome) position: , mismatch: 7, identity: 0.767

gacaattaaatgataaaaactatgttagag	CRISPR spacer
tggatataaataataagaactatgttagag	Protospacer
 . *  *****.****.*************

44. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to KX373685 (Lactococcus phage D4410, complete genome) position: , mismatch: 7, identity: 0.767

gacaattaaatgataaaaactatgttagag	CRISPR spacer
gacaattaaacgatgaaaactatgagctat	Protospacer
**********.***.*********    *

45. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_AP018442 (Undibacterium sp. YM2 plasmid pUYM01, complete sequence) position: , mismatch: 7, identity: 0.767

gacaattaaatgataaaaactatgttagag	CRISPR spacer
gaagattcaatgatataaactatgttatca	Protospacer
** .*** ******* ***********  .

46. spacer 6.13|1728913|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to AP013980 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C7-MedDCM-OCT-S31-C4, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 7, identity: 0.767

acggaagcatcaggcacgtctagtacaatt	CRISPR spacer
attacaccatcaagcacgtctagtaaaatt	Protospacer
*. . * *****.************ ****

47. spacer 6.17|1729294|29|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_CP046399 (Bacillus sp. A260 plasmid unnamed11, complete sequence) position: , mismatch: 7, identity: 0.759

caacgcctttaatgcccaggatgttaatt	CRISPR spacer
tgctgccctaaatgcccaggatgttaatc	Protospacer
.. .***.* ******************.

48. spacer 5.5|1726262|30|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NZ_CP007453 (Peptoclostridium acidaminophilum DSM 3953 strain al-2 plasmid EAL2_808p, complete sequence) position: , mismatch: 8, identity: 0.733

tatgtctgtatatgcaattaatgtaagcgc	CRISPR spacer
gctgtctgtagatgcaattaatgaattttc	Protospacer
  ******** ************ *  . *

49. spacer 5.5|1726262|30|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to GU071095 (Synechococcus phage S-SM2, complete genome) position: , mismatch: 8, identity: 0.733

tatgtctgtatatgcaattaatgtaagcgc	CRISPR spacer
taagtctgtatatgcaactaatgatggtaa	Protospacer
** **************.*****  .*..

50. spacer 5.6|1726339|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to NC_014824 (Ruminococcus albus 7 = DSM 20455 plasmid pRUMAL01, complete sequence) position: , mismatch: 8, identity: 0.724

tgataaagtaaaggaagaaagcgataggt	CRISPR spacer
gcgcaaagaaaaggaaggaagcgatagta	Protospacer
  ..**** ********.*********

51. spacer 5.6|1726339|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to MN812219 (Flavobacterium phage vB_FspS_morran9-1, complete genome) position: , mismatch: 8, identity: 0.724

tgataaagtaaaggaagaaagcgataggt	CRISPR spacer
ccgtaaactaaaggaagaaagcgaacgca	Protospacer
. .**** ****************  *

52. spacer 5.6|1726339|29|NZ_CP023777|PILER-CR,CRISPRCasFinder matches to MN180248 (UNVERIFIED: Wolbachia phage WO isolate Seq1WORi_AMD1 genomic sequence) position: , mismatch: 8, identity: 0.724

tgataaagtaaaggaagaaagcgataggt	CRISPR spacer
attctaagtaagggaagaaagagataggc	Protospacer
   . ******.********* ******.

53. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP014516 (Frondihabitans sp. PAMC 28766 strain SR6 plasmid 3, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tgctcagggcggcgatgaacagcgcgatgg	Protospacer
 .   ************* **** *****.

54. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP021082 (Deinococcus ficus strain CC-FR2-10 plasmid pDFI1, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
aggtcagggcggcgatgaccagcacgaccg	Protospacer
..*  ****************** ***. .

55. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_006362 (Nocardia farcinica IFM 10152 plasmid pNF1, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
ccgggagtgcggcgatgaccagcaccgcca	Protospacer
  ***** *************** * .. *

56. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_004320 (Corynebacterium efficiens YS-314 plasmid pCE3, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tgcggatggcggcgttgaccagcccggaaa	Protospacer
 . *** ******* ***********. .*

57. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP018229 (Rhizobium leguminosarum strain Vaf-108 plasmid unnamed1, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
agtcgttggcggcgatgccgagcccgatga	Protospacer
..  *  ********** * **********

58. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP025431 (Paracoccus zhejiangensis strain J6 plasmid pPZ01, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tgccaacgacggcgatgaccagcacgatga	Protospacer
 .  .* *.************** ******

59. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP017563 (Paraburkholderia sprentiae WSM5005 plasmid pl1WSM5005, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tcacgctggcggcgatgaccagcccaaaga	Protospacer
  . *  ******************.* **

60. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP054022 (Rhizobium sp. JKLM12A2 plasmid pPR12A201, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
agtcgttggcggcgatgccgagcccgatga	Protospacer
..  *  ********** * **********

61. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_020553 (Corynebacterium callunae DSM 20147 plasmid pCC2, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tgcggatggcggcgttgaccagcccggaca	Protospacer
 . *** ******* ***********.  *

62. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP006990 (Rhizobium sp. IE4771 plasmid pRetIE4771d, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
actcgttggcggcgatgccgagcccgatga	Protospacer
.   *  ********** * **********

63. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP048642 (Streptomyces aureoverticillatus strain HN6 plasmid unnamed, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
agacggcggcggcgaagaccagcccgaaga	Protospacer
... *. ******** *********** **

64. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_023285 (Streptomyces sp. F8 plasmid pFRL5, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tgccgcgggcggcgatgaccaggccgaggc	Protospacer
 .  * **************** **** *

65. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_019789 (Deinococcus peraridilitoris DSM 19664 plasmid pDEIPE01, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tctgacgggcggcgagtaccagcccgatgg	Protospacer
   *. *********  ************.

66. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP048281 (Rhizobium leguminosarum bv. viciae 248 plasmid pRle248e, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
agtcgttggcggcgatgccgagcccgatga	Protospacer
..  *  ********** * **********

67. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP021127 (Rhizobium sp. Kim5 plasmid pRetKim5c, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
actcgttggcggcgatgccgagcccgatga	Protospacer
.   *  ********** * **********

68. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP054028 (Rhizobium sp. JKLM19E plasmid pPR19E01, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
agtcgttggcggcgatgccgagcccgatga	Protospacer
..  *  ********** * **********

69. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_012848 (Rhizobium leguminosarum bv. trifolii WSM1325 plasmid pR132501, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
agtcgttggcggcgatgccgagcccgatga	Protospacer
..  *  ********** * **********

70. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to CP007644 (Rhizobium etli bv. phaseoli str. IE4803 plasmid pRetIE4803c, complete sequence) position: , mismatch: 8, identity: 0.733

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
actcgttggcggcgatgccgagcccgatga	Protospacer
.   *  ********** * **********

71. spacer 6.6|1728374|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to KY942057 (Dickeya phage XF4, complete genome) position: , mismatch: 8, identity: 0.733

tactgagttcaatgaatatttcttgccaac	CRISPR spacer
ttctgagtccaatgaatttttcttggattg	Protospacer
* ******.******** *******

72. spacer 6.6|1728374|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MG266157 (Dickeya phage PP35, complete genome) position: , mismatch: 8, identity: 0.733

tactgagttcaatgaatatttcttgccaac	CRISPR spacer
ttctgagtccaatgaatttttcttggattg	Protospacer
* ******.******** *******

73. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MK433577 (Klebsiella phage ST512-KPC3phi13.6, complete genome) position: , mismatch: 8, identity: 0.733

gacaattaaatgataaaaactatgttagag	CRISPR spacer
tctgattgaatgataaaaactattttacaa	Protospacer
  ..***.*************** *** *.

74. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NC_049453 (Klebsiella phage ST13-OXA48phi12.1, complete genome) position: , mismatch: 8, identity: 0.733

gacaattaaatgataaaaactatgttagag	CRISPR spacer
tctgattgaatgataaaaactattttacat	Protospacer
  ..***.*************** *** *

75. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MK433581 (Klebsiella phage ST258-KPC3phi16.1, complete genome) position: , mismatch: 8, identity: 0.733

gacaattaaatgataaaaactatgttagag	CRISPR spacer
tctgattgaatgataaaaactattttacaa	Protospacer
  ..***.*************** *** *.

76. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MK416011 (Klebsiella phage ST437-OXA245phi4.1, complete genome) position: , mismatch: 8, identity: 0.733

gacaattaaatgataaaaactatgttagag	CRISPR spacer
tctgattgaatgataaaaactattttacaa	Protospacer
  ..***.*************** *** *.

77. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MN693705 (Marine virus AFVG_250M220, complete genome) position: , mismatch: 8, identity: 0.733

gacaattaaatgataaaaactatgttagag	CRISPR spacer
tacaattaaatgataaaatatatgaggaat	Protospacer
 *****************  ****  ..*

78. spacer 6.9|1728605|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to KP007359 (Enterobacteria phage vB_EcoM_VR5, complete genome) position: , mismatch: 8, identity: 0.733

ctagctacgtggatttatgttacaaattgt	CRISPR spacer
accattacgtggatttatgttacggattga	Protospacer
 . ..******************..****

79. spacer 6.10|1728682|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_AP018259 (Calothrix sp. NIES-4071 plasmid plasmid4 DNA, complete genome) position: , mismatch: 8, identity: 0.733

ggcgcctgtatttcctaaaataaaaattaa	CRISPR spacer
ggcgcctgtatttcctaacatgtcacccga	Protospacer
****************** **.  * ...*

80. spacer 6.10|1728682|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MH884508 (Bacillus phage vB_BcoS-136, complete genome) position: , mismatch: 8, identity: 0.733

ggcgcctgtatttcctaaaataaaaattaa	CRISPR spacer
tatggaggtctttcttaaaataaaaattaa	Protospacer
 ..*   ** ****.***************

81. spacer 6.14|1728990|29|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to JQ823122 (Persicivirga phage P12024S, complete genome) position: , mismatch: 8, identity: 0.724

aaagtttcgaattagaatcaaatgaccac	CRISPR spacer
ttagtttcgaattaaaatcaaataaaatg	Protospacer
  ************.********.*

82. spacer 6.14|1728990|29|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NC_018272 (Persicivirga phage P12024L, complete genome) position: , mismatch: 8, identity: 0.724

aaagtttcgaattagaatcaaatgaccac	CRISPR spacer
ttagtttcgaattaaaatcaaataaaatg	Protospacer
  ************.********.*

83. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP029358 (Azospirillum sp. CFH 70021 plasmid unnamed3) position: , mismatch: 9, identity: 0.7

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
cgaaggcggcggcgatggccagcccgatcc	Protospacer
 ...*. **********.**********

84. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_CP053567 (Pseudonocardia sp. Gen01 plasmid unnamed3, complete sequence) position: , mismatch: 9, identity: 0.7

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
ccaccagggcggcgatgcccagcacgatcc	Protospacer
  .  ************ ***** ****

85. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NC_023284 (Streptomyces sp. F2 plasmid pFRL4, complete sequence) position: , mismatch: 9, identity: 0.7

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
tgccgcgggcggcgatgaccaggccgagtc	Protospacer
 .  * **************** ****

86. spacer 5.9|1726569|30|NZ_CP023777|CRISPRCasFinder matches to NZ_AP018921 (Pseudonocardia autotrophica strain NBRC 12743 plasmid pPA12743CP, complete sequence) position: , mismatch: 9, identity: 0.7

gagggagggcggcgatgaccagcccgatga	CRISPR spacer
ccaatggggcggcgatgagcagcccgaagg	Protospacer
  .. .************ ******** *.

87. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MN694758 (Marine virus AFVG_250M853, complete genome) position: , mismatch: 9, identity: 0.7

gacaattaaatgataaaaactatgttagag	CRISPR spacer
ataaattaaatgaaaaaaattatgtttatc	Protospacer
.  ********** *****.****** .

88. spacer 6.7|1728451|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to MN694077 (Marine virus AFVG_250M852, complete genome) position: , mismatch: 9, identity: 0.7

gacaattaaatgataaaaactatgttagag	CRISPR spacer
ataaattaaatgaaaaaaattatgtttatc	Protospacer
.  ********** *****.****** .

89. spacer 6.10|1728682|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_MG205643 (Paeniclostridium sordellii strain S0804018 plasmid pCS1-5, complete sequence) position: , mismatch: 9, identity: 0.7

ggcgcctgtatttcctaaaataaaaattaa	CRISPR spacer
tataaaagtattttctaaaataaaaattta	Protospacer
 ...   ******.************** *

90. spacer 6.12|1728836|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_CP034477 (Pantoea agglomerans strain CFSAN047154 plasmid pCFSAN047154_3, complete sequence) position: , mismatch: 9, identity: 0.7

agccgtcacgaagcagtaatcgctaaaatt	CRISPR spacer
ggccgtcacgaagcagttatcgaaccggtc	Protospacer
.**************** ****    ..*.

91. spacer 6.12|1728836|30|NZ_CP023777|CRISPRCasFinder,PILER-CR matches to NZ_CP034472 (Pantoea agglomerans strain CFSAN047153 plasmid pCFSAN047153_3, complete sequence) position: , mismatch: 9, identity: 0.7

agccgtcacgaagcagtaatcgctaaaatt	CRISPR spacer
ggccgtcacgaagcagttatcgaaccggtc	Protospacer
.**************** ****    ..*.

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

2167456 : 2176517

Klosneuvirus(16.67%)

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_098193695.1\|2167456_2168932_-	IMP dehydrogenase	A0A1V0SHK8	Klosneuvirus	5.0e-99	42.6
WP_098193696.1\|2169045_2170146_-	DNA-protecting protein DprA	S6BFL3	Thermus_phage	1.3e-27	33.2
WP_098196157.1\|2170228_2171044_+	5'-nucleotidase, lipoprotein e(P4) family	NA	NA	NA	NA
WP_098193697.1\|2171199_2173095_-	OmpA family protein	G3M9Z0	Bacillus_virus	4.4e-07	40.0
WP_098196158.1\|2173159_2173741_-	radical SAM protein	A0A142F2D5	Mycobacterium_phage	1.4e-12	39.2
WP_098193698.1\|2173899_2174787_-	bifunctional methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase FolD	A0A249XZQ2	Enterococcus_phage	2.1e-36	39.3
WP_098193699.1\|2174912_2176517_-	phosphoenolpyruvate carboxykinase (ATP)	A0A2H4PQN1	Staphylococcus_phage	2.8e-159	51.8

DBSCAN-SWA_2

2235916 : 2242619

Enterobacteria_phage(28.57%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_098193740.1\|2235916_2236567_+	ABC transporter ATP-binding protein	G9BWD6	Planktothrix_phage	1.3e-30	38.1
WP_098193741.1\|2236605_2237466_-	dTDP-4-dehydrorhamnose reductase	I7HXC9	Enterobacteria_phage	2.3e-35	36.0
WP_098193742.1\|2237471_2238035_-	dTDP-4-dehydrorhamnose 3,5-epimerase	I7HJC4	Enterobacteria_phage	3.0e-36	44.9
WP_098193743.1\|2238071_2239127_-	dTDP-glucose 4,6-dehydratase	A0A1D7XFE8	Escherichia_phage	5.0e-85	49.4
WP_098196166.1\|2239216_2240161_-	SDR family oxidoreductase	A0A2K9KZK0	Tupanvirus	9.7e-72	44.4
WP_098193744.1\|2240173_2241484_-	UDP-glucose/GDP-mannose dehydrogenase family protein	A0A127AXI2	Bacillus_phage	3.1e-84	39.6
WP_098193745.1\|2241491_2242619_-	DegT/DnrJ/EryC1/StrS family aminotransferase	A0A0F7LAY0	uncultured_marine_virus	5.0e-22	32.9

DBSCAN-SWA_3

3547144 : 3591711

Arthrobacter_phage(20.0%)

tail

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_098194735.1\|3547144_3547738_+\|tail	phage tail protein	NA	NA	NA	NA
WP_098194736.1\|3547775_3548360_+\|tail	phage tail protein	A0A222ZG41	Arthrobacter_phage	1.6e-19	34.6
WP_098194737.1\|3548378_3549548_+	ABC transporter substrate-binding protein	NA	NA	NA	NA
WP_098194738.1\|3549559_3557887_+	T9SS type B sorting domain-containing protein	NA	NA	NA	NA
WP_098194739.1\|3557916_3558888_+	type IX secretion system membrane protein PorP/SprF	NA	NA	NA	NA
WP_098196260.1\|3559109_3561068_-	M1 family metallopeptidase	NA	NA	NA	NA
WP_098194740.1\|3561424_3568915_-	hypothetical protein	NA	NA	NA	NA
WP_098194741.1\|3569653_3570193_+	hypothetical protein	NA	NA	NA	NA
WP_098194742.1\|3570155_3571487_-	ATP-binding protein	A0A0R6PCP6	Moraxella_phage	9.0e-31	37.3
WP_098194743.1\|3571499_3571952_-	hypothetical protein	NA	NA	NA	NA
WP_098194744.1\|3571982_3573332_-	hypothetical protein	NA	NA	NA	NA
WP_098194745.1\|3573345_3577881_-	hypothetical protein	NA	NA	NA	NA
WP_098194746.1\|3577913_3580646_-	hypothetical protein	NA	NA	NA	NA
WP_098194747.1\|3580642_3583915_-	hypothetical protein	NA	NA	NA	NA
WP_098194748.1\|3583921_3584338_-	GPW/gp25 family protein	NA	NA	NA	NA
WP_098194749.1\|3584355_3584646_-	type VI secretion protein	NA	NA	NA	NA
WP_098194750.1\|3584655_3586404_-	type VI secretion system tip protein VgrG	NA	NA	NA	NA
WP_098194751.1\|3586409_3587066_-	hypothetical protein	NA	NA	NA	NA
WP_098194752.1\|3587068_3587254_-	hypothetical protein	NA	NA	NA	NA
WP_098194753.1\|3587243_3587759_-\|tail	phage tail protein	NA	NA	NA	NA
WP_098194754.1\|3587761_3588193_-\|tail	phage tail protein	T2KSM5	uncultured_phage	5.0e-31	56.7
WP_098194755.1\|3588223_3590260_-\|tail	phage tail protein	J9PVC2	Bacillus_phage	3.6e-23	31.4
WP_098194756.1\|3590286_3591711_-\|tail	phage tail sheath family protein	A0A2I7QP51	Vibrio_phage	9.1e-05	25.5

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_CP023777

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

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