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
LS483377	Stenotrophomonas maltophilia strain NCTC10258 genome assembly, chromosome: 1	11 crisprs	csa3,DEDDh,WYL,cas3,Cas9_archaeal,DinG,PD-DExK	0	2	5	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: LS483377_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_1

25720-25865

Orphan

Consensus_repeat	Method
TGCCGGCCAGCGGCCGGCACTACC	CRISPRCasFinder

2 spacers

The CRISPR arrays of LS483377_1

>merge|LS483377|1|25720-25865|CRISPRCasFinder
TGCCGGCCGCTGGCCGGCATCGCTTTGTGTAGGGCAGCCCAGACGTTGCCGGCCAGCGGCCGGCACTACCCCGTAAATCGGGGGCCCTGGCCGGCATCGCGCCGCGCAGGGCGTCAGGAGGCTGCCGGCCAGCGGCCGGCACTACC

>LS483377|1|1|25720-25865|CRISPRCasFinder
TGCCGGCCGCTGGCCGGCATCGCT	TTGTGTAGGGCAGCCCAGACGT
TGCCGGCCAGCGGCCGGCACTACC	CCGTAAATCGGGGGCCCTGGCCGGCATCGCGCCGCGCAGGGCGTCAGGAGGC
TGCCGGCCAGCGGCCGGCACTACC

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG08591.1\|17705_18239_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG08605.1\|32836_33493_-\|cysteine-dioxygenase-type-I	unknown	unknown	gnl\|CDD\|380416
LS483377.1\|SQG08607.1\|34831_35725_-\|phenylalanine-4-hydroxylase	unknown	unknown	gnl\|CDD\|237020
LS483377.1\|SQG08595.1\|21956_22124_-\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG08597.1\|23617_25711_+\|tonB-dependent-receptor-yncD-precursor	unknown	unknown	gnl\|CDD\|238657
LS483377.1\|SQG08588.1\|14936_15680_+\|pyridoxine-5'-phosphate-synthase	unknown	unknown	gnl\|CDD\|235380
LS483377.1\|SQG08592.1\|18590_18773_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG08598.1\|25867_26206_-\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG08590.1\|17012_17621_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG08601.1\|27841_30328_+\|ATP-dependent-DNA-ligase	unknown	unknown	gnl\|CDD\|235658
LS483377.1\|SQG08599.1\|26354_26753_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG08593.1\|19993_20704_-\|Uncharacterised-protein	unknown	unknown	gnl\|CDD\|379309
LS483377.1\|SQG08606.1\|33680_34721_+\|LacI-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380487
LS483377.1\|SQG08604.1\|32084_32723_-\|4-hydroxy-2-ketovalerate-aldolase	unknown	unknown	gnl\|CDD\|235577
LS483377.1\|SQG08600.1\|26917_27838_+\|Ku-domain-containing-protein	unknown	unknown	gnl\|CDD\|238408
LS483377.1\|SQG08602.1\|30399_30792_-\|transmembrane-protein	unknown	unknown	unknown
LS483377.1\|SQG08603.1\|30959_31988_-\|alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|176257
LS483377.1\|SQG08596.1\|22243_23446_-\|aromatic-amino-acid-aminotransferase	unknown	unknown	gnl\|CDD\|181731
LS483377.1\|SQG08594.1\|20812_21829_-\|Fructose-1,6-bisphosphatase,-type-I	unknown	unknown	gnl\|CDD\|236458
LS483377.1\|SQG08589.1\|15781_16873_+\|radical-SAM-protein	unknown	unknown	gnl\|CDD\|275263

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG08607.1\|34831_35725_-\|phenylalanine-4-hydroxylase	gnl\|CDD\|237020	PRK11913, phhA, phenylalanine 4-monooxygenase; Reviewed.	1.37006e-154
LS483377.1\|SQG08606.1\|33680_34721_+\|LacI-family-transcriptional-regulator	gnl\|CDD\|380487	cd01545, PBP1_SalR, ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.	2.01319e-103
LS483377.1\|SQG08597.1\|23617_25711_+\|tonB-dependent-receptor-yncD-precursor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	1.77934e-49
LS483377.1\|SQG08588.1\|14936_15680_+\|pyridoxine-5'-phosphate-synthase	gnl\|CDD\|235380	PRK05265, PRK05265, pyridoxine 5'-phosphate synthase; Provisional.	2.4364e-113
LS483377.1\|SQG08601.1\|27841_30328_+\|ATP-dependent-DNA-ligase	gnl\|CDD\|235658	PRK05972, ligD, ATP-dependent DNA ligase; Reviewed.	0
LS483377.1\|SQG08605.1\|32836_33493_-\|cysteine-dioxygenase-type-I	gnl\|CDD\|380416	cd10548, cupin_CDO, cysteine dioxygenase, cupin domain. This family contains cysteine dioxygenase (CDO; EC 1.13.11.20), which catalyzes the conversion of cysteine to cysteine sulfinic acid, the first step in the biosynthesis of essential oxidized cysteine metabolites such as sulfate, hypotaurine, and taurine. CDO also plays an important role in the regulation of intracellular cysteine levels in mammals; CDO expression is altered in cancer cells, and abnormal or deficient CDO activity has been linked to Parkinson's disease, Alzheimer's disease, and rheumatoid arthritis. CDO is an iron-dependent thiol dioxygenase that uses molecular oxygen to oxidize the sulfhydryl group of cysteine to generate cysteine sulfinic acid. The CDO active site contains an amino acid-derived cofactor. These enzymes are found in prokaryotes as well as eukaryotes and belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.	1.01388e-28
LS483377.1\|SQG08593.1\|19993_20704_-\|Uncharacterised-protein	gnl\|CDD\|379309	pfam13640, 2OG-FeII_Oxy_3, 2OG-Fe(II) oxygenase superfamily. This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.	2.15043e-09
LS483377.1\|SQG08604.1\|32084_32723_-\|4-hydroxy-2-ketovalerate-aldolase	gnl\|CDD\|235577	PRK05718, PRK05718, keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional.	1.12294e-85
LS483377.1\|SQG08600.1\|26917_27838_+\|Ku-domain-containing-protein	gnl\|CDD\|238408	cd00789, KU_like, Ku-core domain, Ku-like subfamily; composed of prokaryotic homologs of the eukaryotic DNA binding protein Ku. The alignment includes the core domain shared by the prokaryotic YkoV-like proteins and the eukaryotic Ku70 and Ku80. The prokaryotic Ku homologs are predicted to form homodimers. It is proposed that the Ku homologs are functionally associated with ATP-dependent DNA ligase and the eukaryotic-type primase, probably as components of a double-strand break repair system.	1.37503e-115
LS483377.1\|SQG08589.1\|15781_16873_+\|radical-SAM-protein	gnl\|CDD\|275263	TIGR04470, hypothetical_protein_ALIPUT_00462, radical SAM mobile pair protein B. Members of this family are the downstream member (B) of a pair of tandem-encoded radical SAM enzymes. Most of these radical SAM gene pairs have an additional upstream regulatory gene in the MarR family. Examples of high sequence identity (over 96 percent) from cassettes in several Treponema species of the oral cavity to those in multiple Firmicutes in the gut microbiome suggest recent lateral gene transfer, as might be expected for antibiotic resistance genes. The function is unknown.	6.63241e-26
LS483377.1\|SQG08596.1\|22243_23446_-\|aromatic-amino-acid-aminotransferase	gnl\|CDD\|181731	PRK09257, PRK09257, aromatic amino acid transaminase.	0
LS483377.1\|SQG08594.1\|20812_21829_-\|Fructose-1,6-bisphosphatase,-type-I	gnl\|CDD\|236458	PRK09293, PRK09293, class 1 fructose-bisphosphatase.	0
LS483377.1\|SQG08603.1\|30959_31988_-\|alcohol-dehydrogenase	gnl\|CDD\|176257	cd08297, CAD3, Cinnamyl alcohol dehydrogenases (CAD). These alcohol dehydrogenases are related to the cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Cinnamyl alcohol dehydrogenases (CAD) reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.	0

>LS483377.1|SQG08597.1|23617_25711_+|tonB-dependent-receptor-yncD-precursor
MNPAARRRCLPLSALLLSPWTAVAEPAPTALPAVQVQAARVPGIDPFALPASQDTVWIDASRAGTGAQLSEALAGVPGLLARDRQNFAQDTQLSIRGFGARSTFGVRGVRVLIDGVPATMPDGQGQLSHASLLGAERIEVLRGPFSALYGNSSGGVLQVWSAQGQAGDPWRLRVNAGADNTLSVGAQLKGAGQVLDYNIAANHFRTDGWRDHSRARRESLNARIGGELGGGRLELLLNALDAPDAQDPLGLTRAQVAADPRQATAVAHQYNTRKTVRQQQAGLRWTRETGAQRWQLMGYAGQRAVRQYLPIPPAPQTNSPLHAGGVIDLQGGYGGLDARWGWHGDLAGRPLDLVAGLSADRQRQHRTGFENFIGSALGVRGRLRRDQIDVVQNVDQFAQAWWQWSPRWSLLAGLRHSAVRFESNDRYIVGANPDDSGHRRYQATTPVAGVSFEASPQWRLHAAVGRGFETPTFNELGYRADGQAGLALDLAAARSRSIEVGSKWHAQDGNQLDISLFRADTDDELAVASNIGGRSTYRNIGRTRRQGLELQYRQPLAEHLELQLAWTWLQAQVRSPYLTSNTLVAAGSRLPGVPRQQAFARLQWSPADWQWALEAMASSDTVVNDVATERAPGYALLHLEAGRRWTLPGGELRAFARLENVLDQAYIGSVIVNDGNGRFYEPGPGRRANVGLQWSWR
>LS483377.1|SQG08596.1|22243_23446_-|aromatic-amino-acid-aminotransferase
MSFFANVELVPGDPILGLTEAYNADSRPTKVNLGVGIYYDESGRIPLLRAVKQIEQQLAAEAKPRGYLPIDGLPAYTQATRELVFGKDSPLLAAGRVTTAQTVGGSGALRVGADVLKKLLPHATVALSNPSWENHRAVFSAAGFDVLDYTYFDPATHGVDFDGMLADLGKLDAGTVVLLHACCHNPTGADLTVTQWKQVAQLLKDKQLFPFIDMAYQGFDKGIEQDGAAVRIIAEAGIDSFIVANSYSKSFSLYGERVGALSMVAPTAADAKAVQSQVKRVIRTIYSSPSTHGAALVAGVLTNPELRAMWEQELTEMRERIHALRQGLVEKLAAAGAPQFGFINEQAGMFSYSGLSREQVERLRDEFGIYAVGTGRICVAALNQNNLEYVAKAVATVAKG
>LS483377.1|SQG08595.1|21956_22124_-|Uncharacterised-protein
MQDRWRHGPEACLGRVGQDAPTPVLPCAQDSAHEQGAIELTWTYLQRVLHRLPLP
>LS483377.1|SQG08594.1|20812_21829_-|Fructose-1,6-bisphosphatase,-type-I
MSRTSLTRFLIQEQHAGRINADLRQLIAVVARACTSISIAVSKGALGGVLGDAGTGNVQGEAQKKLDVISNEILLEANAWGGHLAACASEEMDHSQPVPDIYPRGDFLLLFDPLDGSSNIDVNVSVGTIFSVLRCPTNVELPGDDAFLQPGSKQIAAGYCIYGPSTQLVLTVGHGTHAFTLDREKGEFVLTTENMQIPAATQEFAINMSNQRHWEAPMQAYVGDLLAGKEGTRGKNFNMRWIASMVADVHRILTRGGIFIYPWDKKDPSKAGKLRLMYEANPMGLLVEQAGGAAWTGRERILDIQPDQLHQRVPVFLGSREEVAEAVRYHHAHDDAQG
>LS483377.1|SQG08593.1|19993_20704_-|Uncharacterised-protein
MHEQGPVDFIEVIHNAVPSEVCAAIVERMRAARGLQPGAVGSGVFPELKHSKDLRISGLDGWQDVDHQLQHAVFNGLLTYLRRYPQALIAPLMLQIQDSNGQPRRLSAEDFPDMPQQQLADLARTCLRPGAINLQWYAAGEGGYPYWHCELYPKDAQAETLHRHVLWTLYLNEEFEEGETEFLFQGRKIAPRTGSLLIAPTAFTHTHRGNRPQGGDKFIATSWILFQSAQKLFGGR
>LS483377.1|SQG08592.1|18590_18773_+|Uncharacterised-protein
MKIIYWLGIAFLWMLPLNVLLLTGGKLISGDALGEEELVGFGVAVFGAVAGGMLYRRRPR
>LS483377.1|SQG08591.1|17705_18239_+|Uncharacterised-protein
MEARSIHECIIVPQAAIVTDMPAGLDEFEQRLWVADTGQRVRKGTDTLLLLRLFSDSPGVIDSQQYIKITGSLKRYAPSSEGTPEVVDARLTSGGAGFVHKGDNWLSDSVDVELHQPHERDSRMEVKVTAVGWNSYRKEDRSFYLQFTCQLKEIPVEKLSAWQGGNDDLWGSFGPTR
>LS483377.1|SQG08590.1|17012_17621_+|Uncharacterised-protein
MKRSHAFSCGAFLIFCGTDAEAARAFVVEDAAMRDPTCLTVEPRQRLFACHRIVAGDSRVIGLRRFRTSWRTDRSTFSKLTIQLPADAKAGDRFSVPNDRVRMFHSRGSSAFAGKTGCYAVPVAGQITVVSAGDFGIEVQVDATFRSASPLQWPGECEAPTTVSEHLRAQPLSLEQLDAWTGVHDPEASPFEQAHPSRRSRN
>LS483377.1|SQG08589.1|15781_16873_+|radical-SAM-protein
MGIAIKGRGSTSHLAGRFESTVSEAVDDGWAVDESEEFLAPRLRTEVRAETARSIISRNTSPDVGFSQSVNPYRGCEHGCSYCFARPSHAYLNLSPGLDFETKLFAKTNAPQLLRKELSKPGYVPQPIALGINTDAYQPIERKFKLTRQLIEVMLETKHPFSLITKNALVERDIDLLAPLAAENLVSVHFSVTSLDPHLSAKLEPRASAPHARLRAMKRLHEAGIPVGVMVAPVIPWINDSELEAVLEAAHDAGASTAGYVLLRLPLEVAPLFRDWLDTHHPDRAAHVMSTIQQLRGGKDYDSQFGTRMRGQGVYADLLNNRFKLARKRLGFNAQNSHWPKLDCSRFQKPLPPKKDSPQGSLF
>LS483377.1|SQG08588.1|14936_15680_+|pyridoxine-5'-phosphate-synthase
MTQLSVNVNKIAVLRNSRGGAEPDVVRAAQACLDAGAHGITVHPRPDRRHITAEDVLALSTLTRARGVEFNIEGNPFAPPREGYPGLLPLCAQTRPAQATLVPDGDGQITSDHGFDFERDAERLRPLVAELKAMGCRVSLFVDAGNPLLEQAAEVGADRVELYTGPYAEAHAAGDAAAMLELFATAARRAQAVGLGVNAGHDLSQDNLRDFLAHVPDVLEVSIGHALIGEALYDGLDATVRGYLALL
>LS483377.1|SQG08598.1|25867_26206_-|Uncharacterised-protein
MSRETSRDPLRENHPPIPGEQRGKRDADNADYRGTGAPFFDAEHDHLPVKHEAEQAAQDRKDGGDRHRGGQESPLKRRERKQRASDNQDEALEETFPASDPTSPFVPAKAPD
>LS483377.1|SQG08599.1|26354_26753_+|Uncharacterised-protein
MPRLERPAPSVFNALLDPLGQRTAQRRTRRHEDPQAVAQDYLQYMLSDYEERRGQSHRNWRDLCPVYAFALTTHAADWPRGDAADTCEELAEHWEQMRGQSRLGWSQARPVVEDAWRALDHIPAAAVRPLLQ
>LS483377.1|SQG08600.1|26917_27838_+|Ku-domain-containing-protein
MARPIWTGTLSFGLLNVPVSLMSGERKVDLQFRMLDSRDRKPIRFERVNADTGEEVPWKDIVKAYEYDKGSYVVLEEGDIRSAAPESHEAVEVESFVDAAQIDPRYYEKPYLLVPGKKAEKGYVLLRETLRSTGKVGIARVVVRTREYLCSVMPHEDALVLMILRYPQELVDPEDYKLPTGKLSDYRITSKETAMAEQLIESMAGDWDPSQYHDEFRERLQQVLNKRIKSKGGTTRVDDEPAPREDASTNVVDFMALLQKSLDANKRTPAKKAATRKAAAKSPVKKAVKKTTKKAAKKTAPRRKAG
>LS483377.1|SQG08601.1|27841_30328_+|ATP-dependent-DNA-ligase
MSLHQYRRKRRLGGGAGQTTEPDDTPAPGDPKRRPTFVIQLHHASSRHYDFRLEMDGVLKSWAVPKGPSLRVGEKRLAVEVEDHPLSYAGFEGDIPEGHYGAGHVEVFDHGTWACEGDPLQALAAGRIDFVLHGQRLAGGWKLVRTAMKGRQVQWLLIKRGDGEARDAEADDLLTAPMPKRTPAAKKRSADKTARATPVARTTTRKADVRWHARALQLYGARDAPYPHAFKPQLTDHRDSAPDGDRWLHEIKWDGYRLLADLHDGEVKLRSRNGLDWTDDFPEVVQAVQALPVRDARLDGELVVLDKEGRSDFAALQRVIDGSSKQPLRYIVFDLPGVAGADISRAPLLERKALLKELIGPAPGTLAFSEHVIDHGPQVFVASGKAGFEGIVSKQVDAPYVNTRARSWVKVKHEDTDEFLIVGYTAPKGSRVGFGSLLLATPDKGGLRYVGRVGTGFDDQSLRALLKALQPLAVKTPVLQLPAHVPFRAASVRWVKPVAVAEVAFRGWGKEGLLRQASFKRLRSDKQKEDLGMSTADAETGGEVEITHPERVVFPRQKLRKGDVADYYQRMARWILPEIAGRPLSLLRCPDGVGKACFFQKHHGPGLGDAVHAVPLQQKSGREDYVYVDDARGLLQLVQMNTLELHPWGATVADPEHPDRLVFDLDPGEGVSWAQVKAAARDVRDRLQEVGLQSFVRLSGGKGVHVVVPLQPKAGWDEAKAFCEAFAQAMALEQPDRYVATMSKAKRGGVIFIDWLRNTRGATSVCSWSLRARDAAGVAVPLRWEELARVSAADAFPMAKALARAKRLKGDPWQGIARLKQRLPSLKR
>LS483377.1|SQG08602.1|30399_30792_-|transmembrane-protein
MPGLLKTLFLSIVALIGGVLSLALVSSVAGWLPPLLGLSPDSNSVQLGWDLAFSVLGGVAGISFATYYAPCWSRSHGFSIWSLIALGCGYAMWTAGADFPFWFVISLLASLPLQLLVGWWFGRRPSRDLR
>LS483377.1|SQG08603.1|30959_31988_-|alcohol-dehydrogenase
MQSTMKAAVVREFGKPLVIEEVSVPRPGAGEVLVRIEACGVCHTDLHAAEGDWPVKPNPPFIPGHEGVGHVVAVGGGVGHVKEGDRVGIPWLYSACGHCEHCLGGWETLCETQRNTGYSVNGGFAEYALADANYVGLLPKEVGFVEIAPVLCAGVTVYKGLKVTDTKPGDWVAVSGIGGLGHMAVQYARAMGLNVAAVDVDDNKLALARQLGAQITVNARTTDPAAFLRKEIGGAHGALVTAVSPKAFEQALGMVRRGGTVSLNGLPPGNFPLDIFGMVLNGITVRGSIVGTRLDLQESLQFAAEGKVAATVSTDRLENINDVFARMHAGTIEGRVVLDFAA
>LS483377.1|SQG08604.1|32084_32723_-|4-hydroxy-2-ketovalerate-aldolase
MSSADPRLRALLKLAPVIPVYTPEDVNEAVEVAQALFRGGLPVIEVTLRTPQALDAIKAMVEAVPDAVIGAGTVLNVTQMQAAKQAGARFAVSPGATPALYAAARDADLPYLPGAATASDLILGLEQGTDTFKFFPAVQAGGAALLAAWHGPFADVRFCPTGGISAQTAPQFLHLPNVLCVGGSWLTTPALLQTRDWDAIERLAREASVLAS
>LS483377.1|SQG08605.1|32836_33493_-|cysteine-dioxygenase-type-I
MNAGATRANTNIPLTMLRYSRGMDLQTSPFPAFRGRDRLIAAVDAAMTSGDAGRITADLQLALQEAIADSRIELPECVHRPVSDHYARRPLYHSQEHGYSVIAMSWGPGQGTPLHDHDAMWCVEGVWLGELEITRYELLECAGERWRFRRHAALRGGCGSAGSLIPPHEYHTLRNASDEALAISVHVYEAPMERSAVFDPLGGDWYQRRIQALQADAV
>LS483377.1|SQG08606.1|33680_34721_+|LacI-family-transcriptional-regulator
MSDAALPASKGKAATINDIARLSGVSKKTVSRIINNSPLVRKDTRDKVEALMREVGYVPDPLARGLAFRRSFLIGLVYDDPGAQCIVDLQHGALEALRGTGYELVVHPCDSQDPECAQGVRRFVQQQKLHGVILGPRASESVALAQMLDDIDCRYVRINAHASEEDVQAVVTHDRDGAAAAAGYLLSLGHRDIAVIAGPGDRRAARERTHGFLDRLAQVGLTLPGERVLEAGDTFESGVHAAERLLLGGQRPSAIFAGNDEMAAGVYQVALRAGIAVPQQLSIVSYDDSPLASRLWPPLTSVRRHVSDIGRVAASMLVQADVPDAPTAASVHPQLMVRGSCRAVDA
>LS483377.1|SQG08607.1|34831_35725_-|phenylalanine-4-hydroxylase
MDLAQPRRVEHQQTDKGYVPVYTTALVEQPWDTYTADDHATWSTLYQRQRELLVGRACQEFLDAQDEMGMSAHMIPRFDQLNEVLGAATGWTLVGVEGLLPELDFFDHLANRRFPVTWWIRRPDQIDYIAEPDLFHDLFGHVPLLMNPVFADYMEAYGRGGVKAHAIGPDALQNLTRLYWYTVEFGLIDTPEGLRIYGAGIVSSKGESLYSLESAAPNRIGFDLQRIMRTKYRIDTFQKTYFVIDSFEQLMQATSPDFTPIYAALASQAHLPAGDVQGDDRVFQKGTGDGWADGGDV

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Crispr_ID: LS483377_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_2

751337-751436

Orphan

Consensus_repeat	Method
TTCATCCACGCATGGCGTGGATCT	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483377_2

>merge|LS483377|2|751337-751436|CRISPRCasFinder
TTCATCCACGCATGGCGTGGATCTGCCTCATTGAAAGGCAAACAGAAAAGCCCGGGTGTCTGCACACCCGGGCTTCTTCATCCACGCGTGGCGTGGATCT

>LS483377|2|2|751337-751436|CRISPRCasFinder
TTCATCCACGCATGGCGTGGATCT	GCCTCATTGAAAGGCAAACAGAAAAGCCCGGGTGTCTGCACACCCGGGCTTC
TTCATCCACGCGTGGCGTGGATCT

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG09240.1\|758453_759380_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG09241.1\|759487_762004_-\|inner-membrane-transport-permease	unknown	unknown	gnl\|CDD\|225669
LS483377.1\|SQG09232.1\|749139_750057_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176164
LS483377.1\|SQG09238.1\|755532_757776_+\|TonB-dependent-hemoglobin/transferrin/lactoferrin-family-receptor	unknown	unknown	gnl\|CDD\|273808
LS483377.1\|SQG09244.1\|763455_764169_+\|two-component-system-response-regulator-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223816
LS483377.1\|SQG09224.1\|739806_741522_+\|hemolysin	unknown	unknown	gnl\|CDD\|153248
LS483377.1\|SQG09230.1\|747455_748529_-\|nifR3-family-TIM-barrel-protein	unknown	unknown	gnl\|CDD\|129820
LS483377.1\|SQG09242.1\|762000_762648_-\|polyamine-transporting-ATPase	unknown	unknown	gnl\|CDD\|226647
LS483377.1\|SQG09225.1\|741518_742319_+\|Ser/Thr-protein-phosphatase-family-protein,UDP-2,3-diacylglucosamine-hydrolase	unknown	unknown	gnl\|CDD\|277343
LS483377.1\|SQG09239.1\|757780_758380_+\|hemin-transport-protein	unknown	unknown	gnl\|CDD\|226243
LS483377.1\|SQG09228.1\|744582_746409_-\|transmembrane-protein	unknown	unknown	gnl\|CDD\|287142
LS483377.1\|SQG09223.1\|738269_739481_-\|S-adenosylmethionine-synthetase	unknown	unknown	gnl\|CDD\|235374
LS483377.1\|SQG09243.1\|762723_763368_+\|lysophospholipase	unknown	unknown	gnl\|CDD\|238860
LS483377.1\|SQG09229.1\|746570_747398_-\|methyltransferase	unknown	unknown	gnl\|CDD\|181382
LS483377.1\|SQG09226.1\|742458_743517_+\|YhfP-protein	unknown	unknown	gnl\|CDD\|377294
LS483377.1\|SQG09227.1\|743575_744586_-\|glycosyl-transferase	unknown	unknown	gnl\|CDD\|133022
LS483377.1\|SQG09231.1\|748598_749030_-\|transmembrane-protein	unknown	unknown	unknown
LS483377.1\|SQG09236.1\|753917_754889_+\|aldo/keto-reductase-family-protein	unknown	unknown	gnl\|CDD\|381369
LS483377.1\|SQG09235.1\|752425_753724_-\|nucleoside-permease-NupC	unknown	unknown	gnl\|CDD\|224883
LS483377.1\|SQG09237.1\|755178_755379_+\|hemin-uptake-protein-HemP	unknown	unknown	gnl\|CDD\|378463

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG09241.1\|759487_762004_-\|inner-membrane-transport-permease	gnl\|CDD\|225669	COG3127, COG3127, Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport, and catabolism].	8.2727e-178
LS483377.1\|SQG09232.1\|749139_750057_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176164	cd08475, PBP2_CrgA_like_6, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 6. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	4.50983e-84
LS483377.1\|SQG09238.1\|755532_757776_+\|TonB-dependent-hemoglobin/transferrin/lactoferrin-family-receptor	gnl\|CDD\|273808	TIGR01786, hemoglobin-haptoglobin-binding_protein, TonB-dependent hemoglobin/transferrin/lactoferrin receptor family protein. This model represents a family of TonB-dependent outer membrane receptor/transporters acting on iron-containing proteins such as hemoglobin, transferrin and lactoferrin. Two subfamily models with a narrower scope are contained within this model, the heme/hemoglobin receptor family protein model (TIGR01785) and the transferrin/lactoferrin receptor family model (TIGR01776). Accessions which score above trusted to this model while not scoring above trusted to the more specific models are most likely to be hemoglobin transporters. Nearly all of the species containing trusted hits to this model have access to hemoglobin, transferrin or lactoferrin or related proteins in their biological niche. [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins].	9.59529e-124
LS483377.1\|SQG09244.1\|763455_764169_+\|two-component-system-response-regulator-transcriptional-regulator	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	2.26547e-75
LS483377.1\|SQG09224.1\|739806_741522_+\|hemolysin	gnl\|CDD\|153248	cd07986, LPLAT_ACT14924-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ACT14924. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Pectobacterium carotovorum subsp. carotovorum PC1 locus ACT14924 putative acyltransferase, and similar proteins.	6.33027e-58
LS483377.1\|SQG09230.1\|747455_748529_-\|nifR3-family-TIM-barrel-protein	gnl\|CDD\|129820	TIGR00737, Probable_tRNA-dihydrouridine_synthase, putative TIM-barrel protein, nifR3 family. This model represents one branch of COG0042 (Predicted TIM-barrel enzymes, possibly dehydrogenases, nifR3 family). This branch includes NifR3 itself, from Rhodobacter capsulatus. It excludes a broadly distributed but more sparsely populated subfamily that contains sll0926 from Synechocystis PCC6803, HI0634 from Haemophilus influenzae, and BB0225 from Borrelia burgdorferi. It also excludes a shorter and more distant archaeal subfamily.The function of nifR3, a member of this family, is unknown, but it is found in an operon with nitrogen-sensing two component regulators in Rhodobacter capsulatus.Members of this family show a distant relationship to alpha/beta (TIM) barrel enzymes such as dihydroorotate dehydrogenase and glycolate oxidase. [Unknown function, General].	7.68417e-147
LS483377.1\|SQG09242.1\|762000_762648_-\|polyamine-transporting-ATPase	gnl\|CDD\|226647	COG4181, COG4181, Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport, and catabolism].	3.89092e-97
LS483377.1\|SQG09225.1\|741518_742319_+\|Ser/Thr-protein-phosphatase-family-protein,UDP-2,3-diacylglucosamine-hydrolase	gnl\|CDD\|277343	cd07398, MPP_YbbF-LpxH, Escherichia coli YbbF/LpxH and related proteins, metallophosphatase domain. YbbF/LpxH is an Escherichia coli UDP-2,3-diacylglucosamine hydrolase thought to catalyze the fourth step of lipid A biosynthesis, in which a precursor UDP-2,3-diacylglucosamine is hydrolyzed to yield 2,3-diacylglucosamine 1-phosphate and UMP. YbbF belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	2.73942e-70
LS483377.1\|SQG09239.1\|757780_758380_+\|hemin-transport-protein	gnl\|CDD\|226243	COG3720, HemS, Putative heme degradation protein [Inorganic ion transport and metabolism].	0.00232208
LS483377.1\|SQG09228.1\|744582_746409_-\|transmembrane-protein	gnl\|CDD\|287142	pfam10131, PTPS_related, 6-pyruvoyl-tetrahydropterin synthase related domain; membrane protein. This domain is found in various bacterial hypothetical membrane proteins, as well as in tetratricopeptide TPR_2 repeat protein. The exact function of the domain has not, as yet, been established.	0.000476202
LS483377.1\|SQG09223.1\|738269_739481_-\|S-adenosylmethionine-synthetase	gnl\|CDD\|235374	PRK05250, PRK05250, S-adenosylmethionine synthetase; Validated.	0
LS483377.1\|SQG09243.1\|762723_763368_+\|lysophospholipase	gnl\|CDD\|238860	cd01822, Lysophospholipase_L1_like, Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.	7.13224e-85
LS483377.1\|SQG09229.1\|746570_747398_-\|methyltransferase	gnl\|CDD\|181382	PRK08317, PRK08317, hypothetical protein; Provisional.	2.86608e-27
LS483377.1\|SQG09226.1\|742458_743517_+\|YhfP-protein	gnl\|CDD\|377294	pfam04307, YdjM, LexA-binding, inner membrane-associated putative hydrolase. YdjM is a family of putative LexA-binding proteins. Members are predicted to be membrane-bound metal-dependent hydrolases that may be acting as phospholipases. It is a member of the SOS network, that rescues cells from UV and other DNA-damage. Expression of YdjM is regulated by LexA.	4.11412e-25
LS483377.1\|SQG09227.1\|743575_744586_-\|glycosyl-transferase	gnl\|CDD\|133022	cd04179, DPM_DPG-synthase_like, DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.	4.67475e-43
LS483377.1\|SQG09236.1\|753917_754889_+\|aldo/keto-reductase-family-protein	gnl\|CDD\|381369	cd19143, AKR_AKR6C1_2, AKR6C family of aldo-keto reductase (AKR). Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.	0
LS483377.1\|SQG09235.1\|752425_753724_-\|nucleoside-permease-NupC	gnl\|CDD\|224883	COG1972, NupC, Nucleoside permease [Nucleotide transport and metabolism].	9.89476e-142
LS483377.1\|SQG09237.1\|755178_755379_+\|hemin-uptake-protein-HemP	gnl\|CDD\|378463	pfam10636, hemP, Hemin uptake protein hemP. This is a bacterial family of proteins that are involved in the uptake of the iron source hemin.	2.64857e-16

>LS483377.1|SQG09232.1|749139_750057_-|LysR-family-transcriptional-regulator
MLPTERLRGIEAFVATADAGSFTAAAERLHLTSSAVGKTIARLEARLGARLFERSTRRLRLTEAGEGFYRTCVRVLGELADAESVLVSHADAPVGRLRVDAPATFGRLKVWPLLLQLAAEFPQLHPQVTFSDRFSDLAEDGVDLAVRIGGPEPLPATLGSRLLGYECLRFCASPAYLLRHGQPRSAAELAGHDGVLFGRADGSIGPWQVADGRQRSTPLQARARLVVGSAEAQVAAVEAGFGIAQLATWLVDDALARGSLVSILPSLDCRGLPLRLLWPQGRQRLPRVDVALDRLGAGLQIDPPR
>LS483377.1|SQG09231.1|748598_749030_-|transmembrane-protein
MDGFPWLLVAAAGSAIAALLHIGCIAFGAAWYRYFGAGQRMVRLAQAGHWWPPLMTAGITAVLVAWALYALAAAGWHSPLPASRLVLTGIALLLLLRAAMGFGLALLRPGYNGRRFWVASSLVCLCLGLAFALGTRQAWQSLG
>LS483377.1|SQG09230.1|747455_748529_-|nifR3-family-TIM-barrel-protein
MRSVPIGLNRTAPDAAVPPRAPYNERMQIGPYTIAPNVVLAPMAGVTDKPFRLLCKRLGAGLAASEMTISDPRFWNTRKSIHRMDHDGEPAPISVQIAGTEPQQLAEAARYNVDHGAQIIDINMGCPAKKVCNAWAGSALMRDEQLVARILEAVVNAVDVPVTLKIRTGWDCDHRNGPLIARIAEDSGIAALAVHGRTRDQHYTGQAEYATIGEIKAALRIPVIANGDIDSPQKAAYVLKETGVDAVMIGRSAQGRPWIFREVAHYLATGEELPPPSLAEVRDILLGHLHALHAFYGEPQGVRIARKHLGWYAKDRPENAAFRAVVNRAEDPASQIALTTEYFDRLIAGEPALPSAA
>LS483377.1|SQG09229.1|746570_747398_-|methyltransferase
MTPPISSPTYLHGFSGTEQQRLMTQARLLESSIFGQIDYSGARRLLEVGSGVGAQTEILLRRFPELHVTGVDLSETQLATARENLARTPWCSDRYTLQQADAGELPFEARSFDAAFLCWVLEHVPSPARVLSEVRRVLAPGSPVYITEVMNASFLLDPYSPHIWRYWMAFNDFQYDHGGDPFVGAKLGNLLLAGGFRDVHTEIKTIHLDNREPARRKTMIAFWEQLLLSAADQLLQAGSVDEETVEGMRREFRLVQNDPNAVFFYSFVQGRATVY
>LS483377.1|SQG09228.1|744582_746409_-|transmembrane-protein
MSDSGRTPFSAHDVNLPGGLPPGQTRLLAGIIALLCILYVAFALTPSSYSLAYEYLGLAPQQPLLGTARYIRTDEWMVFTPYIQIAVNNDFGQVNAHSPYHESLRTFQALPLLDWGLLFKPYHWAFFVLPAANAYSFFFMFMAMAFLSGWALFLRQLRMPVPAAVLVSATLFFAPFVQVWWTSNAGAFALAPWAAVAWLGISHRALRIAASAYALAAWLISVSYPPFIISSVLALAVLILAVRRDALTLPRLIDAGIAGALALAVFIGYFHDIIPIVRNTVYPGQRQSAGGGVGLTSLFAHAFPNLMTYRFAPLPLFKASNDCEIAVLGSLLPLFTLVLADGTRLREWARSHRSSVLALAAGVLLIACWIFLPVPVLVGKLTGLSMVPPARALLAFGLLLNIGCAMILVRCGVRLERRRLLLLAALLMAGSVAKFLFGEGQFSRLHSAADAIPYLCLAGLAVAARHPKLSAHAATLVLATAALANLLGNGLFNPVQPAGPIFAMDRAAVLHSLQARGSATTPEGALVAPGGFGALLPGVGIPAVNHVLYLPQMEYFRRYFPLMPDEAFNFTFNRYHHITVAPEGDAPQVLQGDLVELPAKALLAHPAP
>LS483377.1|SQG09227.1|743575_744586_-|glycosyl-transferase
MSPMTTITPSASTPARIAVIIPCYKVTRHVLSVLAAIDDAVTAIYCVDDACPDGSGRLILAEANDPRIAVLFHQHNLGVGGAIKTGYRAAIADGMDILVKVDGDGQMDPALLMDFVAPIADGHADYTKGNRFWNLTHIRRMPPVRRLGNLLLSFMTKASSGYWQVFDPTNGYTAIHAKVASHLKLEAVSDRYFFETDMLFRLNTVRAVVQDVAMDAHYGDETSNLRIGRILGEFSFKHLRNTLKRIAYNYFLRDLSIASLELIAGSSLLAFGGLFGLYHWVRSAQADVATPVGTIMIAMVALISGLQFLLAFVGFDIANVPRQVLNRSIKLNRQPQ
>LS483377.1|SQG09226.1|742458_743517_+|YhfP-protein
MDSLTQIVLGGAVAAAIAPPGHRRAALLAGAALGTLPDLDALWLGFTATDPVANMIEHRSFSHSLLVLPWVAALIWWLFKRFGNGRVAQSPVRWFWAIQLALVTHPVLDAFTVYGTQLWWPLRPHPTMGSSVFIIDLGYTVWLLLGCVLAWFGRARPWAGKVLGVALLVSSGYLGWGLIAKAQVDRAAQQSLAAMGLGDAPRFSVPMPFNTLLWRVVAMTPNGYVVGDRSLVADHGPMQFEGHASNVQALREAGSIPAVQQLTWFNRGFMRAQVVDGRLVLSDLRMGLEPDYTFNFAVAEQVDGQWRPITPEQVRTDYSSPAARADAGRRLAAMWQRIWHEPAASATGAAHP
>LS483377.1|SQG09225.1|741518_742319_+|Ser/Thr-protein-phosphatase-family-protein,UDP-2,3-diacylglucosamine-hydrolase
MSVLANLSPHRRAVFVSDVHLGSRHCHATELARFLSQLRCERLYLVGDIIDLWWMAHRRANWRQSHSEVIQALHALRRAGTEIVYIPGNHDASLRQVCGLMLPAMQVRRRAIHVTADGRRLLVAHGDEYDGVTHFGGLQEKFGDWLYYRILTGNQALNAVRRRLGMRYWSLSEFLKKRSGAAERYIERFVQAGLDDVRRRGLDGIVCGHIHRAALVERDGLVYANDGDWVESLTALVEDHDGALRLLDHNGQTLVELPGARLSQAA
>LS483377.1|SQG09224.1|739806_741522_+|hemolysin
MQELEQRLQQRFPDWFHGRRGQLARPLLRSVGRWSRLDQIEAFLQRSAGLRGFGFVAAGLEFIDGQYQVDPAALAKIPATGRLLIVANHPSGALDALALLDAVGRIRRDVRIVANDLLGAIAPLQDLLLPVRILGGKAQRGSLHAVEEALAAEQCVIVFPAGEVSRLSLRGIRDGRWQRGFVRFARAAGAPVLPVRVEARNSALFYGASTLFKPAGTALLAREMFTRRGRPLRLSIGEPMQLGKGGDPGAQLLSVRRALYALGRNGAAGNAAAFAGPEPLAAPVPPSQVAAGIAAATQLGQTADGKQILLATCTADSPLLLELGRLRELTFRQVGEGTGRSRDLDDYDPQYEHIVIWDAAAQRIAGAYRIMRGAHALARHGLSGLYSASLFRYSDDAITHIAEGLELGRSFVVPDYWGSRSLDYLWQGIGAYLQCRPGIRYLFGAVSISAALPRDAREQLVAYYQRYYGGTAGLAESNRPFQYFAAPPSFGELDAGAAFDVLKANLAALGTGVPTLYRQYTDLCEPGGARFLAFGVDPDFSDSIDGLIEVDLCAIRPNKRKRYLRDAGTPA
>LS483377.1|SQG09223.1|738269_739481_-|S-adenosylmethionine-synthetase
MSSYLFTSESVSEGHPDKVADQISDAVLDAILTQDQRARVACETMVKTGVAIVAGEITTSAWIDLEALTRKVITDIGYDSSDVGFDGATCGVLNLIGKQSPHIAQGVDRKKPEEMGAGDQGLMFGYATNETDSYMPAAIHLSHRLVEQQAKIRKKKNSPLSWLRPDAKSQVTLRYENGVVSAIDAVVLSTQHAPGIKQKDLIEAVREEIIKPVLPAKWLHKGTKFHINPTGKFEIGGPVGDCGLTGRKIIVDTYGGWARHGGGAFSGKDPSKVDRSAAYAARYVAKNVVAAGLADRCEVQVSYAIGVAEPTSISVTTFGTGKISDDKIEKLIRKHFDLRPYGIIKMLDLIHPMYQQTAAYGHFGRKPKEFSYLNGEGETVNATAFSWEKTDRAAALRADAKLK
>LS483377.1|SQG09235.1|752425_753724_-|nucleoside-permease-NupC
MVEGLGRIGFGLFGLAVLIGITWLFSNNKRAVDWKLVATGITLQIAFAALVILVPGGRDVFDALGHGFVKVLSFVNEGSGFIFGSLMDTKNYGFIFAFQVLPTIIFFSALMGVMYHLNIMQAIVRVMAWAITKVMRVSGAETTSVCASVFIGQTEAPLTVRPYIARMTQSELLTMMIGGMAHIAGGVLAAYVGMLGGGDPAQQAFYAKHLLAASIMAAPATLVVAKLLIPETGTPLTRGTVKMEVEKTSSNIIDAAAAGAGDGLKLALNIGAMLLAFIALIALLNAPLTWIGEVTGLAAQIGKPTNLSTIFGYLLAPIAWVIGTPWADATTVGSLIGQKVVINEFVAYTELSQIVNGQVAGVSLSSEGRLIATYALCGFANFSSIAIQIGGIGGLAPERRHDLAKFGLRAVLGGTIATFMTATIAGVLTHFS
>LS483377.1|SQG09236.1|753917_754889_+|aldo/keto-reductase-family-protein
MQYRRLGSTGLPISALSFGAWVTFGDQIPRDEARNLVAAAWDHGVNFFDNAEGYANGRAEQVMGDVIADLRLPRDGFCVSSKVFFGSAKDPRPTQRGLSRKHVTDACHAALKRLRVDYLDLYYCHRPDPDAPIAETVHAMDTLVRQGKILYWGTSEWSAVQIQQALDIAEARNLQGPSMEQPQYNLLHRERVEVEYAPLYAGAGLGTTIFSPLASGLLTGKYDQGIPADARLGREGMEWLQDLVLGADAGARLGQVRRFSEVARALGHAPATLAIAWCLRNPNVSSVILGASRVSQLLQNLQALDVLEQVDAAGWADVEAAFA
>LS483377.1|SQG09237.1|755178_755379_+|hemin-uptake-protein-HemP
MLMNAQPVLLRPETLTLRDRPVRVVPPEEVIDSEALLKGRREILIQHGDRFYRLRHTSNDKLILTK
>LS483377.1|SQG09238.1|755532_757776_+|TonB-dependent-hemoglobin/transferrin/lactoferrin-family-receptor
MTRHTALCLAVWMALPLSAHAAATAAPDAREFDRVQVTATRTERAVSDVAATVDVIDREQMDRHLVQDIKDLVRYEPGLSVTRSATRFGLDGFRIRGLDGNRVRIQTDGIVMPTRFDIGSFASSNRNFTDLDTLKRVEIVRGPASSLYGSDALGGVVAFVTKDPADYLKDGKNSYFGLKFGYDGEWKGLLGGATAAFGGDYWSGLVNVNHHQGQETDNKGTVRSDNDTRTASNPQDRDGRSLLSKLVYAPSEDQRFRLTVEGNEDTTDTNVLSAIASVAPRPGAMAAATGMKSHDTQKRNRVSFAHEMDALDQPFADSLHWQVYAQNSETRQQTDETRTDGTRRHRVFSFDQHAYGLQAQFNKAFTTGSVEHALTYGFEGTRTEIRQKRDGYQVSKAGVVSNTVLPDTFPVRDFPISKTTELGLYAQDEMRFADGRLSLVPGVRVDRYELKPEVDSIFAEDNPTTAVAQLKKTSVSPKLGMVWRFTDEWSLFAGYARGFRSPPYNDVNIGLTNVAFRYTAIANPDLKPETSDGYELGLRFIAPAAYVSVSGYYNDYKDFIQSNVDTGRNAQGLTVFQSQNIADARIYGAEMKAGIEFGELSPALKGWALRSALAWSRGDNRTDDEPLASVDPLRGTLGLMYDTDTWGVELAGTFVQRKKRLPPPAAQTNPNAPAPFVYQPAGYGVLDLMAHWNFAPGATFNVGVFNLADKRYIEWSSITPSLITDRALSDRFSSPGRTFSASLAVSW
>LS483377.1|SQG09239.1|757780_758380_+|hemin-transport-protein
MSRALSARRNDSIAAPNSAAWPTPAQLATLGTVMCLYHADGNELGGWRQAVRVHACQGVDSEGLRESLCFLDGRGRCVWRLYLLPDSDFLAWDRLVAALPPGPEHDSEASVGERLWRRLAGHLGGQRWRLCALRLHAADDGRTLAASLSTLSSLGAATARRIARLEGAEGELAIDDCCCADAARRPAPQIPGDLPLIRL
>LS483377.1|SQG09240.1|758453_759380_+|Uncharacterised-protein
MKLQTASAMLLLAASGVASAQPSDIARDHDSILAMQGEYTVDFAFDETVLLKPGYERAPAMRSGGSEVVIVVEDTPKRIVLQHLLLDEKSGHITKHWRQDWVYEAPNRFEFSADQTWKVRSIPSAVNQGAWTQCVYEVSDAPRYCGTGTWTYTNNVPSWTSDLSWRPLPRREYTKRSDYNALAVVNRHTLTPNGWTHEQFNTKVQRNADGSQVEIAREFGFNDYVKTTEVDFTPARNYWKATAGYWAKVRQRWDGFLTQAPGVHLKTRIDGMAMIIPLFTQAEAIQSGKKVKDKQIDDVFAKYVEKAQ
>LS483377.1|SQG09241.1|759487_762004_-|inner-membrane-transport-permease
MNLLRHAWRALRREALAGDLLTVFAALVLGVAVMTAVGTLVNRVNLALTGSAAEMLGGDLGIAGRDDPPQAFADEAQRRGLAFTRIASFGSVLFNGDASQMASIKAVQAGYPLRGTLRVRSTPGGALIANAGTPPKGQAYADPRLLQGLGLKAGDDLEFGAGTLRIAGIIEAEPDAGGDLLTLSPTLLVNRADVEGTGLLGPGSRINYRLMFAGSADQVAALRQWLLPQVKGLRLLSVDDTQRGVRQAFDLAGRFLGLSALLAVLLAGVATALAANRFALRRIDQVAILRCLGARQRDILLGLALQLLMLAVPACALGIGLGMAAQEGLVQVLGSLVPQRLPLPEAMPALTGAGIGLLLLFGFGLPPLLRLRGVPPMRVLNRSFAALPPASLLAYVAALAASLLLAVQVTGDLKLALWVLGGLAALAVAAGVVGFVLLQLLRGLQHRLHGHWRLGLAALTRRRMLAVMQLVGLSLSLCALLLLAVTGPGLLQQWRERLPADTPNYFLINIQPEQRDSVLGALRGLGANDASIEPMATGRLIAINGKPPLRVDRSPDQSGQPASGEAQRDDDDENRPLNFSWRSSFPPANTLMNGTFWTPDSTAPEASVEIGWAKRYGVYPGDRITIAVGEQEREFTVTSVRKADWNTFRPNFFVLLNPNAVGDTPHNLLSAFHLSAGKAAGLGELIRAQPNLSLLDVDAVISQVRDVMERVAQAVQLVMVFSLLAGVLVLLAALQATAGERRYDSAVLRTLGATRRQLRGAVLVEFGALGTLAALLAVGAAAAIGVAVSQKVFELPLLPPWPGLLIGGVVGIGLSLLAGWWGTRAILHTPPALALREA
>LS483377.1|SQG09242.1|762000_762648_-|polyamine-transporting-ATPase
MQGPEGEVHILDNITLTVHEGTSVAIVGASGSGKTTLLGLLAGLDLPSRGRIALAGQDLSALDEEARAQLRAREVGFVFQSFHLLPALTAAENVALPLELAGREDRARVDEVLAQVGLAHRARHYPRQLSGGEQQRVALARAFVTRPRILFADEPTGSLDHATGQHISDLLFELNAGSGTTLVLVTHDLRLAQRCQYIHRIDNGRLLPVERGAQA
>LS483377.1|SQG09243.1|762723_763368_+|lysophospholipase
MRKTGWSRRAGAMMVLLLGFLLLPGLACAKGPAGTVLVLGDSLSAAHNIPADAGWVSLLQQRVRQQSKTPARIVNASMSGETTAGALTRLPGLLAKEKPTVVVIALGGNDALRGLTPAQVQGNLGRMVQASQKAGAKVLLLGIDVPPNYGPAYRQRLAAAYRALATQYKVPLLPFLLEGVALQPGMMQADGLHPTAQAQPEVLDNVWPLLRPLL
>LS483377.1|SQG09244.1|763455_764169_+|two-component-system-response-regulator-transcriptional-regulator
MRQTKETSGLVLVVEDNRNISEMIGEYLEGRGFEVDYAQDGLDGYRLAAENSYDVVVLDLMLPRLDGIEVCRRLRNDARKSTPVLMLTARDTLDDKLTGLGFGADDYLTKPFAIQELEARLRALIRRERRQVGSEVLKVADLVLDPVSMRATRAGTELQLSPIGLRLLTILMRESPRVVTRQEIEREIWGNGLPDSDTLRSHLYNLRKIIDKPFDRPLLHTVQSAGYRIADIAQPMA

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Crispr_ID: LS483377_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_3

814748-814852

Orphan

Consensus_repeat	Method
TTTGCCGGCCAGCGGCCGGCACTACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483377_3

>merge|LS483377|3|814748-814852|CRISPRCasFinder
TTTGCCGGCCAGCGGCCGGCACTACCGAATCCACGTGTGGCGGCTACATCGGGTAGGTGCGGACCCTGGTCCGCACGCGTTTGCCGGCCAGCGGCCGGCACTACC

>LS483377|3|3|814748-814852|CRISPRCasFinder
TTTGCCGGCCAGCGGCCGGCACTACC	GAATCCACGTGTGGCGGCTACATCGGGTAGGTGCGGACCCTGGTCCGCACGCG
TTTGCCGGCCAGCGGCCGGCACTACC

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG09304.1\|821044_822319_+\|ribonuclease-BN/uncharacterised-domain-fusion-protein	unknown	unknown	gnl\|CDD\|179791
LS483377.1\|SQG09291.1\|810254_811334_+\|NAD(P)-transhydrogenase-subunit-alpha	unknown	unknown	gnl\|CDD\|240629
LS483377.1\|SQG09303.1\|820373_820967_-\|Trp-repressor-binding-protein	unknown	unknown	gnl\|CDD\|179647
LS483377.1\|SQG09300.1\|817613_819356_+\|secreted-serine-protease	unknown	unknown	gnl\|CDD\|173820
LS483377.1\|SQG09296.1\|813242_814703_+\|NAD(P)-transhydrogenase-subunit-beta	unknown	unknown	gnl\|CDD\|376743
LS483377.1\|SQG09289.1\|806968_807655_-\|nitroreductase	unknown	unknown	gnl\|CDD\|380312
LS483377.1\|SQG09301.1\|819476_819971_-\|L-asparaginase	unknown	unknown	gnl\|CDD\|223330
LS483377.1\|SQG09305.1\|822315_822885_+\|Thioredoxin	unknown	unknown	gnl\|CDD\|239264
LS483377.1\|SQG09297.1\|814914_815334_-\|transmembrane-protein	unknown	unknown	unknown
LS483377.1\|SQG09306.1\|823511_824294_-\|transcriptional-regulator	unknown	unknown	gnl\|CDD\|213852
LS483377.1\|SQG09299.1\|816067_817162_+\|branched-chain-amino-acid-aminotransferase	unknown	unknown	gnl\|CDD\|237363
LS483377.1\|SQG09292.1\|811454_811916_-\|Protein-of-uncharacterised-function-(DUF3106)	unknown	unknown	gnl\|CDD\|378633
LS483377.1\|SQG09302.1\|820041_820377_-\|transmembrane-protein	unknown	unknown	gnl\|CDD\|378269
LS483377.1\|SQG09298.1\|815510_816008_+\|FeS-assembly-SUF-system-protein-SufT	unknown	unknown	gnl\|CDD\|213809
LS483377.1\|SQG09294.1\|812242_812827_-\|RNA-polymerase-factor-sigma-70	unknown	unknown	gnl\|CDD\|236367
LS483377.1\|SQG09287.1\|805485_806040_-\|ADP-ribose-pyrophosphatase	unknown	unknown	gnl\|CDD\|239516
LS483377.1\|SQG09295.1\|812925_813246_+\|NAD(P)-transhydrogenase-subunit-alpha	unknown	unknown	gnl\|CDD\|378941
LS483377.1\|SQG09288.1\|806036_806972_-\|5'-3'-exonuclease	unknown	unknown	gnl\|CDD\|235591
LS483377.1\|SQG09290.1\|807881_810203_+\|thymidine-phosphorylase	unknown	unknown	gnl\|CDD\|377917
LS483377.1\|SQG09293.1\|811919_812246_-\|transmembrane-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG09304.1\|821044_822319_+\|ribonuclease-BN/uncharacterised-domain-fusion-protein	gnl\|CDD\|179791	PRK04214, rbn, ribonuclease BN/unknown domain fusion protein; Reviewed.	0
LS483377.1\|SQG09291.1\|810254_811334_+\|NAD(P)-transhydrogenase-subunit-alpha	gnl\|CDD\|240629	cd05304, Rubrum_tdh, Rubrum transdehydrogenase NAD-binding and catalytic domains. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.	0
LS483377.1\|SQG09303.1\|820373_820967_-\|Trp-repressor-binding-protein	gnl\|CDD\|179647	PRK03767, PRK03767, NAD(P)H:quinone oxidoreductase; Provisional.	4.9247e-59
LS483377.1\|SQG09300.1\|817613_819356_+\|secreted-serine-protease	gnl\|CDD\|173820	cd07496, Peptidases_S8_13, Peptidase S8 family domain, uncharacterized subfamily 13. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.	1.39719e-125
LS483377.1\|SQG09296.1\|813242_814703_+\|NAD(P)-transhydrogenase-subunit-beta	gnl\|CDD\|376743	pfam02233, PNTB, NAD(P) transhydrogenase beta subunit. This family corresponds to the beta subunit of NADP transhydrogenase in prokaryotes, and either the protein N- or C terminal in eukaryotes. The domain is often found in conjunction with pfam01262. Pyridine nucleotide transhydrogenase catalyzes the reduction of NAD+ to NADPH. A complete loss of activity occurs upon mutation of Gly314 in E. coli.	0
LS483377.1\|SQG09289.1\|806968_807655_-\|nitroreductase	gnl\|CDD\|380312	cd02135, YdjA-like, nitroreductase family protein similar to Escherichia coli YdjA. A subfamily of the nitroreductase family containing uncharacterized proteins that are similar to nitroreductase YdjA from Escherichia coli. Nitroreductase catalyzes the reduction of nitroaromatic compounds such as nitrotoluenes, nitrofurans and nitroimidazoles. This process requires NAD(P)H as electron donor in an obligatory two-electron transfer and uses FMN as cofactor. The enzyme is typically a homodimer. Members of this family are also called NADH dehydrogenase, oxygen-insensitive NAD(P)H nitrogenase or dihydropteridine reductase.	1.20776e-52
LS483377.1\|SQG09301.1\|819476_819971_-\|L-asparaginase	gnl\|CDD\|223330	COG0252, AnsB, L-asparaginase/archaeal Glu-tRNAGln amidotransferase subunit D [Amino acid transport and metabolism / Translation, ribosomal structure and biogenesis].	1.97276e-30
LS483377.1\|SQG09305.1\|822315_822885_+\|Thioredoxin	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	1.75366e-34
LS483377.1\|SQG09306.1\|823511_824294_-\|transcriptional-regulator	gnl\|CDD\|213852	TIGR03707, PPK2_P_aer, polyphosphate kinase 2, PA0141 family. Members of this protein family are designated polyphosphate kinase 2 (PPK2) after the characterized protein in Pseudomonas aeruginosa. This family comprises one of three well-separated clades in the larger family described by pfam03976. PA0141 from this family has been shown capable of operating in reverse, with GDP preferred (over ADP) as a substrate, producing GTP (or ATP) by transfer of a phosphate residue from polyphosphate. Most species with a member of this family also encode a polyphosphate kinase 1 (PPK1). [Central intermediary metabolism, Phosphorus compounds].	4.55689e-136
LS483377.1\|SQG09299.1\|816067_817162_+\|branched-chain-amino-acid-aminotransferase	gnl\|CDD\|237363	PRK13357, PRK13357, branched-chain amino acid aminotransferase; Provisional.	0
LS483377.1\|SQG09292.1\|811454_811916_-\|Protein-of-uncharacterised-function-(DUF3106)	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.	3.14478e-21
LS483377.1\|SQG09302.1\|820041_820377_-\|transmembrane-protein	gnl\|CDD\|378269	pfam09842, DUF2069, Predicted membrane protein (DUF2069). This domain, found in various prokaryotes, has no known function.	0.000174062
LS483377.1\|SQG09287.1\|805485_806040_-\|ADP-ribose-pyrophosphatase	gnl\|CDD\|239516	cd03424, ADPRase_NUDT5, ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. Like other members of the Nudix hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue Nudix motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the Nudix motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer.	1.2487e-37
LS483377.1\|SQG09294.1\|812242_812827_-\|RNA-polymerase-factor-sigma-70	gnl\|CDD\|236367	PRK09047, PRK09047, RNA polymerase factor sigma-70; Validated.	1.57026e-64
LS483377.1\|SQG09298.1\|815510_816008_+\|FeS-assembly-SUF-system-protein-SufT	gnl\|CDD\|213809	TIGR03406, FeS_long_SufT, probable FeS assembly SUF system protein SufT. The function is unknown for this protein family, but members are found almost always in operons for the the SUF system of iron-sulfur cluster biosynthesis. The SUF system is present elsewhere on the chromosome for those few species where SUF genes are not adjacent. This family shares this property of association with the SUF system with a related family, TIGR02945. TIGR02945 consists largely of a DUF59 domain (see pfam01883), while this protein is about double the length, with a unique N-terminal domain and DUF59 C-terminal domain. A location immediately downstream of the cysteine desulfurase gene sufS in many contexts suggests the gene symbol sufT. Note that some other homologs of this family and of TIGR02945, but no actual members of this family, are found in operons associated with phenylacetic acid (or other ring-hydroxylating) degradation pathways. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	2.13399e-96
LS483377.1\|SQG09295.1\|812925_813246_+\|NAD(P)-transhydrogenase-subunit-alpha	gnl\|CDD\|378941	pfam12769, PNTB_4TM, 4TM region of pyridine nucleotide transhydrogenase, mitoch. PNTB_4TM is the region upstream of family PNTB, pfam02233, that carries four of this transporters transmembrane regions. PNTB is the beta-subunit of pyridine nucleotide transhydrogenase. This family forms part of the Proton-translocating Transhydrogenase (PTH) Family.	2.82782e-33
LS483377.1\|SQG09288.1\|806036_806972_-\|5'-3'-exonuclease	gnl\|CDD\|235591	PRK05755, PRK05755, DNA polymerase I; Provisional.	1.47051e-84
LS483377.1\|SQG09290.1\|807881_810203_+\|thymidine-phosphorylase	gnl\|CDD\|377917	pfam07793, DUF1631, Protein of unknown function (DUF1631). The members of this family are sequences derived from a group of hypothetical proteins expressed by certain bacterial species. The region concerned is approximately 440 amino acid residues in length.	0

>LS483377.1|SQG09296.1|813242_814703_+|NAD(P)-transhydrogenase-subunit-beta
MNISTVELLDWLVKASYLVAATLFLLGLQRMASPLTARSGIRWAGLGMLLATAATFFLPELHNVPLILVALLLGAGLAWWSAGKVAITDMPQMVALYNGMGGGSAAAIGAVELLRYAFLANRDTSHWSAQALADLAARQPSGTVLLLAVVGAAIGAVSLSGSVIAWAKLDGRLDKRVTWPGQQVMNLLVALAVVVLAIIAASTLSTWAIVAFFVLALTLGVLMTLPIGGADMPVVISLYNAFTGLAVSFEGYVLGNEALIIAGMMVGAAGILLTRLMAKAMNRPIRNVLFSNFGGGAGGEAQAISGSQKPIEAADVAAMMAFAERVVIVPGYGMAVAQAQHKIWELAQRLGQRGVKVKFAIHPVAGRMPGHMNVLLAEAGVPYDLIADMDDINPEFANTDVVLVIGANDVVNPVARTDPASPIYGMPVLDVVNARNVVVIKRGKGTGFAGIENALFYADNTRMLYGDGAEAAASLVSELKALDGGH
>LS483377.1|SQG09295.1|812925_813246_+|NAD(P)-transhydrogenase-subunit-alpha
MSDGFVALYIFMLAAIAGHVIISRVPVILHTPLMSGSNFIHGIVLIGAMVVLGHAQTPLEKVLGFLAVVLGAGNAAGGYVVTARMLEMFKPSAPKGGKDEPKEPQA
>LS483377.1|SQG09294.1|812242_812827_-|RNA-polymerase-factor-sigma-70
MVTPSEEPYPVLVSSPVPPSAETDALPASLEAFLASVGPRAFRFAEAGLRQREDAMDAVQDALLRMLDYADKPAAEWAPLFWSILRRRVIDVQRRRRFRLPFWRDNQDAEGGEIDWADPGPDPAQAHEQRQQYQQLVDALRRLPARQREAFTLRVLQDLDGATTARAMGCSEGAVKTHLARARQALQDYLEIHP
>LS483377.1|SQG09293.1|811919_812246_-|transmembrane-protein
MNRSLPSDDTLRSLHAQSLHALSPATLARLRQARHGASATRHGRLRWWLASACSLVVALGIGLQFTGHGTLTGPAPAPVLASVEDNSALYDENPDLYLWLGDTDLAME
>LS483377.1|SQG09292.1|811454_811916_-|Protein-of-uncharacterised-function-(DUF3106)
MPRLHTLPLLMTLLLLPALPALAQSAAPAPAARPAPATPLPVWEQLSEAQRESLLAPLRDRWNSADAGQRQRMLSHGQRWQTMSPEERDKARRGLRRFEHMSPEQREQARALFGQMRELPPAQRDALRERWSQMTPEQRKDWVRDNPPPAKPR
>LS483377.1|SQG09291.1|810254_811334_+|NAD(P)-transhydrogenase-subunit-alpha
MAVALLGIKETAPGERRVALTPETARKLGARGITVWYEAGAGLAAGFTDAAYDDAGARAFDAGRWAEIDILLCVQAPPAAVLEQLKPGATVVGLLTPASDPGLAALAADDRLHLFPLQQLPRTTRAQAMDVLSSQAGMAGYKAALIAAERAPRFFPMLTTAAGTVRPAKVLVIGAGVAGLQAIATARRLGAQVEGFDVRPETREQIQSLGARFLDLGVSAAGEGGYARALTDEERAEQQRRLADHLRSVDVVICTAAVPGRPAPTIVTAAMVEGMATGSVIVDLAAESGGNCALTQPGQCIEHQGVTIDGPLGLASRGATQASEMYARNLLNFVALFVREGQLGFDWEDELLAKTRWQA
>LS483377.1|SQG09290.1|807881_810203_+|thymidine-phosphorylase
MMSAPTPMGSPGRDPAQLQRARDMVLPALCQAFGAALARFDDALFDRAGNAGSSQLLFLDAMRELRRRREDIAGAFSGHLQRAWDALASGEPMSAESTLSGPAEDGLSLLAEHVLESRLAVRNFATVLLRDFKPVLARLDRRLGRLVGGAELDADHNPISPEHLGVAIHEAFAGCELAPEVHLVLIKLCERDLRAPVGRIYEKLDEQLAAAGVMSQMGAPRRPPSAAPDPRMASGLDDLVEQRPGSGLDGEFGDDEQAAPAWAQRFAARWSERRGHMQQHLGAEGSGTGEAHAGQQGMLLEALHELLQQTRHVREDATSAAQVAIGQQRPLSQREMMSVLSLLQATPSATLRAAIGEDGESLAQRLKSEVLSSATRLGVDPGQTRLDPQDEDAIDLVGMLFDVMLDERELEGRSRELIGRLVVPFVKVAMLDRRMFVQKTHPARKLLNSLAEACEGNTGESQAERMLMAKVEEIIERLVAEFNENLAIFLTLEEEFREFLVQHRRRVEIAERRAAETQRGQEKLEMARTRAGAELDRRIGDATLPPAIAEFLRQPWQHHLTLALLREGEEGASVAEALSLGDGLLEEVAEARRQIVGKPWLQAWQPALAKVFASVGVHGDAATGAIDALHDTLQGIAESRPELQRALPELPQVALPTPPVAESPAVELGGQIDADDFDNADADRFRRMEIGNWLDFVDKDGKVQAGKLSWVSPISSRLLFVNRRGVRFCVASPEELAVMVRLGRLRAHVDDGAFDSAMQGVIDRLDPGSATLH
>LS483377.1|SQG09289.1|806968_807655_-|nitroreductase
MTFITVWYSKARRDTDGVFDHPDYNQTSVMTGSDSMPDPAALLALDARRSVPSRQLAEPGPDPATLQRMLASAVRVPDHGKRVPFRFLKIAGDARHTLGDFLAERSRQRDPHAGEAVFEKDRQRFSHAPLVIVVVASPRPDPKVPEQEQLMTAGCVCFALLQAAQALGFGAQWLTAWMAFDPAVHAYLGLAEGEGIAGFIHIGTPKAAVPERERPDPATLLRDWTPPA
>LS483377.1|SQG09288.1|806036_806972_-|5'-3'-exonuclease
MTLPVPPPSLYLVDASIYVFRAWHSLPDQFQDAQGWPTNAVHGFARFLLDLLERERPRHIAIAFDEALDSGFRHRLYPAYKANRDPAPEALKRQFVHCKALCAALGLAVLAHHEYEADDLIGSALHVHRGSHRGVIISADKDLSQLLLDHDEQWDYARNQRWNVAGVKARHGVHAHQIADYLALCGDAVDNIPGISGVGSKSAAVLLAHFGSMDALYERLDEVPFLRLRGAAQMAVRLREQREHAQLWRQLTTIALDAPLEGSQPGLLRQAADPELLGGLCQTLRFGPMTRRRLFDAAGVPDILPTHSEPA
>LS483377.1|SQG09287.1|805485_806040_-|ADP-ribose-pyrophosphatase
MSQRNTEAPRVVYEGKYQRMLVRGTWEYSERTHAGGLAAIIIAVTPEDKVLFVEQFRVPLQAPTIEMPAGLVGDIHAGESIEVSAVRELEEETGWTADHAEVLLIGPTSSGASSEKIAFVRATGLRRVGEGGGDDSEDIIVHEIPRSEAAAWLVQKMGEGYELDAKLWAGLWMIEHHLDGRPRG
>LS483377.1|SQG09297.1|814914_815334_-|transmembrane-protein
MSSNAARARTVTWLWPIMLLLGLVVAPLAWMVLALMTGRQVGWMAVLTALELVFMLRMGTLGPGRLRIVLVVVGTLLVAAVANWTIASAWMGGSIGLDLWDATMRMGPHLAWTLITLANGAVEWLWLAVAVAVGAWLAR
>LS483377.1|SQG09298.1|815510_816008_+|FeS-assembly-SUF-system-protein-SufT
MVPQGDTVTLPAGSYGYITQALGGSYSVFVEGNLFRIAGKDGDAIGKEAPAPLELPADATDEQVEQLVWQQLRTCFDPEIPVNIVELGLVYEVEIKHLDEGQREIDVKMTLTAPGCGMGDILVDDVRSKLEMIPTVAEADVDLVFDPPWNQHMMSEAARLETGML
>LS483377.1|SQG09299.1|816067_817162_+|branched-chain-amino-acid-aminotransferase
MSQSIPSFAVTRSDHPRSAEERAKILEKPGFGLHFTDHMVEVRWDKDAGWHNANVRAYGPLQLDPAAAVLHYGQEIFEGIKAYRHADGSIWTFRPDANGRRLQRSAQRLALPELPVEIFVESLKQLIAVDSDWVPSADESSLYFRPFMIGDEAFLGVRGAHKAGYYVIASPAGPYFAKGVAPVSIWLSTEYARAAKGGTGAAKCGGNYAASLLPQQKAQAQGCSQVLFLDPVEGKYLEELGGMNVFLVYKDGTLVTPELSGSILEGITRESILQLARDRGMKVEERKVSIDEWKQGVASGEIAEVFACGTAAVVTPIGQLKGEGFSVGDINAPAGEVTMSLRKELTDIQYGRLPDRHNWLVKLG
>LS483377.1|SQG09300.1|817613_819356_+|secreted-serine-protease
MSQVTQPRVRRVWVVLGASVLSSLLLATPALAGDVQLSGLQSAPTHQRFIVKYRDGSAAVANTTALASSLKTAAAGLASSQGRALGLQQVRKLAVGPTLVKTDRPLDQAESELLMRKLAADPNVEYVEVDQIMRATLTPNDTRFSEQWGFGTSNAGINIRPAWDKATGTGVVVAVIDTGITNHADLNANILPGYDFISDAAMARDGGGRDNNPNDEGDWYGANECGSGIPASNSSWHGTHVAGTVAAVTNNSTGVAGTAFNAKVVPVRVLGKCGGYTSDIADAIVWASGGTVSGVPANANPAEVINLSLGGGGSCSTTYQNAINGAVGRGTTVVVAAGNSNTNVSSSVPANCPNVIAVAATTSAGARASFSNYGTGIDISAPGQSILSTLNTGTTTPGSATYASYNGTSMAAPHVAGVVALMQSVAPSPLSPAQVESIIKSTARPLPGACSGGCGAGIIDANAAVAAAINGGGNPNPGGNVLQNNVPVTGLGAATGAELNYTVAVPAGSTQLRVAISGGSGDADLYVRQGSAPTDTTYTCRPYLSGNSETCTINSPAAGTWYVRVKAYSTFSGLTLNAQY
>LS483377.1|SQG09301.1|819476_819971_-|L-asparaginase
MHMMEELLVVTTGGTIDKIYFDDKSDYQIGDPQIGMILRELGVTFRFNVIPILRKDSLHINDEDRELIRATIAAQPTRHVLVTHGTDSMVQTGKVLATIPDKTIVMTGALSPARFRGSDAEFNIGCAIGAVQSLPSGVYIAMNGRIFDPQHVRKNVAANRFESV
>LS483377.1|SQG09302.1|820041_820377_-|transmembrane-protein
MSRPPRTVLLLALMGLAALFAGWFINDKHWLATQLVFTAPPLALAFALRLGWRKAGFWASVLALGWFSHGVMSAWSHPETRWLALIEIALALLVIFSASLPGLRARFGKRR
>LS483377.1|SQG09303.1|820373_820967_-|Trp-repressor-binding-protein
MGEILVLYYSRGGSVARLARQIARGIGEVPGMSARLRTVPPVAAVTQTAQPPVPDDGAPYVSVQDLVECQGLLLGSPTRFGNMAAPVKHFLDGLGAEWVNGTLSGKPAGVFTSTASMHGGQESTLLSMQVPLLHHGCVIVGIPFTEPALSHTTSGGTPYGASHVAGAADDPQPTDDEAVLARALGRRVADIAQRLAR
>LS483377.1|SQG09304.1|821044_822319_+|ribonuclease-BN/uncharacterised-domain-fusion-protein
MEPLDTLNLWMERARDRARAISFGRFLWHRFLDDRLFQAAAALAYTTVFALVPLAIVVFGVLSAFPVFDRWSDQLSDYVFSNFVPNAARAAEGYLRQFSASAGQLTAAGFIALVVSLLITLNSVEETFNQIWRVGSTRPKLTRFLVYWTVLTLGAMLAAASLAVSARVFAMPLFGTQEGRWLAELALRLAPILIEFVCITLMFRVVPHHTVKWRHAVPGAILAAVILELVKWGIGAYLGSFQSYQKLYGTVAFVPILLLWIYLCWVAVLLGASLSSSMAAFRYQPVELRLPQGYEFYGLLRLLGRFHHARAKGKGLADDEILRLEPMLTDSLLQDLACNLQEIGLLRRDERGEWLLSRDLDQVSLADLYECTQLRIPVAEQHLPYRDDSLGRAALAALDDLRLPLRERLKRKVSDIYTDSGDMP
>LS483377.1|SQG09305.1|822315_822885_+|Thioredoxin
MTRKTPLLLPLALLLALSACKPAQEPTPASSQPPAQAPTPTAPAPVEETPAERTTAEFPTLKMKAVDGSDYDLAAHRGKWVVVNFWATWCAPCRKEMPELSALHAMRSNIEVVGLAYEDIEVPEMQSFLTKHPVTYPIVIVDPFDPPADFATPRGLPLTHLLDPQGKLSHTFLGPVTAADIEKQIAAAK
>LS483377.1|SQG09306.1|823511_824294_-|transcriptional-regulator
MAKLKRKDYDELLLPLQLELTAMARWVQHSGQRLLVLFEGRDTAGKGGAIQAISQHLNPRQCRVVALPKPTDREATQWYFQRYASHLPAAGEIVLMDRSWYNRAGVERVMGYCSETEYQQFLRQAPVFEQLLVDDGILLFKYWLCVDQEQQEKRFAERHLDPLKGWKLSPVDLKSRSKYSAYTEAREAMLRATHREAAPWTLVDFNDQRLGRLTLVRNLLDRLPDTRVDAPLPELPKLKGKLHREHYDVLKPIEDFPVED

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Crispr_ID: LS483377_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_4

2566281-2566381

Orphan

Consensus_repeat	Method
TTGCCGGCCAGCGGCCGGCACTACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483377_4

>merge|LS483377|4|2566281-2566381|CRISPRCasFinder
TTGCCGGCCAGCGGCCGGCACTACCGAAGATCGCGGGATTGCCGGCCAGCGGCCGGCACTACCGAAGATCACGGGGTTGCCGGCCAGCGGCCGGCACTACC

>LS483377|4|4|2566281-2566381|CRISPRCasFinder
TTGCCGGCCAGCGGCCGGCACTACC	GAAGATCGCGGGATTGCCGGCCAGCGGCCGGCACTACCGAAGATCACGGGG
TTGCCGGCCAGCGGCCGGCACTACC

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG10895.1\|2558512_2560672_+\|TonB-dependent-outer-membrane-protein	unknown	unknown	gnl\|CDD\|238657
LS483377.1\|SQG10908.1\|2575397_2575787_-\|dioxygenase	unknown	unknown	gnl\|CDD\|319923
LS483377.1\|SQG10913.1\|2580883_2581237_-\|Spermidine-export-protein-mdtJ	unknown	unknown	gnl\|CDD\|182471
LS483377.1\|SQG10905.1\|2569218_2570196_+\|oxidoreductase-SMc00968	unknown	unknown	gnl\|CDD\|176252
LS483377.1\|SQG10897.1\|2561250_2561721_-\|Mn-dependent-transcriptional-regulator-MntR	unknown	unknown	gnl\|CDD\|182927
LS483377.1\|SQG10896.1\|2560661_2561210_+\|alkyl-hydroperoxide-reductase	unknown	unknown	gnl\|CDD\|239262
LS483377.1\|SQG10900.1\|2563673_2564123_-\|transposase	unknown	unknown	gnl\|CDD\|376564
LS483377.1\|SQG10901.1\|2564417_2564744_-\|Thioredoxin	unknown	unknown	gnl\|CDD\|239245
LS483377.1\|SQG10898.1\|2561838_2563170_+\|manganese-transport-protein-MntH	unknown	unknown	gnl\|CDD\|234815
LS483377.1\|SQG10909.1\|2575937_2576456_+\|RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|171561
LS483377.1\|SQG10910.1\|2576452_2577403_+\|transmembrane-FecR-family-iron-uptake-regulator-protein	unknown	unknown	gnl\|CDD\|226235
LS483377.1\|SQG10906.1\|2570528_2573156_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
LS483377.1\|SQG10912.1\|2580560_2580884_-\|Spermidine-export-protein-mdtI	unknown	unknown	gnl\|CDD\|224987
LS483377.1\|SQG10907.1\|2573222_2575202_-\|High-affinity-choline-uptake-protein-BetT	unknown	unknown	gnl\|CDD\|236635
LS483377.1\|SQG10899.1\|2563209_2563725_-\|ISStmaD4-Transposase	unknown	unknown	gnl\|CDD\|376773
LS483377.1\|SQG10903.1\|2565208_2566249_-\|ribonucleotide-reductase-of-class-Ia-(aerobic),beta-subunit	unknown	unknown	gnl\|CDD\|236591
LS483377.1\|SQG10902.1\|2564715_2565258_-\|ribonucleotide-reductase-associated-flavodoxin	unknown	unknown	gnl\|CDD\|181744
LS483377.1\|SQG10894.1\|2555864_2558252_+\|autotransporter-protein	unknown	unknown	gnl\|CDD\|237940
LS483377.1\|SQG10904.1\|2566424_2568788_-\|ribonucleotide-diphosphate-reductase-subunit-alpha	unknown	unknown	gnl\|CDD\|181700
LS483377.1\|SQG10911.1\|2577472_2580421_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|273808

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG10895.1\|2558512_2560672_+\|TonB-dependent-outer-membrane-protein	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	5.80533e-61
LS483377.1\|SQG10908.1\|2575397_2575787_-\|dioxygenase	gnl\|CDD\|319923	cd07262, 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.	2.7009e-45
LS483377.1\|SQG10913.1\|2580883_2581237_-\|Spermidine-export-protein-mdtJ	gnl\|CDD\|182471	PRK10452, PRK10452, multidrug/spermidine efflux SMR transporter subunit MdtJ.	6.17282e-25
LS483377.1\|SQG10905.1\|2569218_2570196_+\|oxidoreductase-SMc00968	gnl\|CDD\|176252	cd08292, ETR_like_2, 2-enoyl thioester reductase (ETR) like proteins, child 2. 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the 2-enoyl thioester reductase (ETR) like proteins. ETR catalyzes the NADPH-dependent dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. 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. 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. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.	1.67714e-164
LS483377.1\|SQG10897.1\|2561250_2561721_-\|Mn-dependent-transcriptional-regulator-MntR	gnl\|CDD\|182927	PRK11050, PRK11050, manganese-binding transcriptional regulator MntR.	1.03909e-82
LS483377.1\|SQG10896.1\|2560661_2561210_+\|alkyl-hydroperoxide-reductase	gnl\|CDD\|239262	cd02964, TryX_like_family, Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.	7.57314e-23
LS483377.1\|SQG10900.1\|2563673_2564123_-\|transposase	gnl\|CDD\|376564	pfam01548, DEDD_Tnp_IS110, Transposase. Transposase proteins are necessary for efficient DNA transposition. This family includes an amino-terminal region of the pilin gene inverting protein (PIVML) and of members of the IS111A/IS1328/IS1533 family of transposases. The C-terminus is represented by family pfam02371.	8.55119e-18
LS483377.1\|SQG10901.1\|2564417_2564744_-\|Thioredoxin	gnl\|CDD\|239245	cd02947, TRX_family, TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.	6.37031e-18
LS483377.1\|SQG10898.1\|2561838_2563170_+\|manganese-transport-protein-MntH	gnl\|CDD\|234815	PRK00701, PRK00701, divalent metal cation transporter MntH.	0
LS483377.1\|SQG10909.1\|2575937_2576456_+\|RNA-polymerase-sigma-factor	gnl\|CDD\|171561	PRK12528, PRK12528, RNA polymerase sigma factor; Provisional.	4.47185e-46
LS483377.1\|SQG10910.1\|2576452_2577403_+\|transmembrane-FecR-family-iron-uptake-regulator-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].	2.43037e-48
LS483377.1\|SQG10906.1\|2570528_2573156_+\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.77456e-66
LS483377.1\|SQG10912.1\|2580560_2580884_-\|Spermidine-export-protein-mdtI	gnl\|CDD\|224987	COG2076, EmrE, Membrane transporters of cations and cationic drugs [Inorganic ion transport and metabolism].	1.93171e-21
LS483377.1\|SQG10907.1\|2573222_2575202_-\|High-affinity-choline-uptake-protein-BetT	gnl\|CDD\|236635	PRK09928, PRK09928, choline transport protein BetT; Provisional.	0
LS483377.1\|SQG10899.1\|2563209_2563725_-\|ISStmaD4-Transposase	gnl\|CDD\|376773	pfam02371, Transposase_20, Transposase IS116/IS110/IS902 family. Transposases are needed for efficient transposition of the insertion sequence or transposon DNA. This family includes transposases for IS116, IS110 and IS902. This region is often found with pfam01548. The exact function of this region is uncertain. This family contains a HHH motif suggesting a DNA-binding function.	3.59936e-20
LS483377.1\|SQG10903.1\|2565208_2566249_-\|ribonucleotide-reductase-of-class-Ia-(aerobic),beta-subunit	gnl\|CDD\|236591	PRK09614, nrdF, ribonucleotide-diphosphate reductase subunit beta; Reviewed.	7.18352e-125
LS483377.1\|SQG10902.1\|2564715_2565258_-\|ribonucleotide-reductase-associated-flavodoxin	gnl\|CDD\|181744	PRK09271, PRK09271, flavodoxin; Provisional.	3.68424e-91
LS483377.1\|SQG10894.1\|2555864_2558252_+\|autotransporter-protein	gnl\|CDD\|237940	PRK15313, PRK15313, intestinal colonization autotransporter adhesin MisL.	4.43034e-74
LS483377.1\|SQG10904.1\|2566424_2568788_-\|ribonucleotide-diphosphate-reductase-subunit-alpha	gnl\|CDD\|181700	PRK09209, PRK09209, ribonucleoside-diphosphate reductase subunit alpha.	0
LS483377.1\|SQG10911.1\|2577472_2580421_+\|TonB-dependent-receptor	gnl\|CDD\|273808	TIGR01786, hemoglobin-haptoglobin-binding_protein, TonB-dependent hemoglobin/transferrin/lactoferrin receptor family protein. This model represents a family of TonB-dependent outer membrane receptor/transporters acting on iron-containing proteins such as hemoglobin, transferrin and lactoferrin. Two subfamily models with a narrower scope are contained within this model, the heme/hemoglobin receptor family protein model (TIGR01785) and the transferrin/lactoferrin receptor family model (TIGR01776). Accessions which score above trusted to this model while not scoring above trusted to the more specific models are most likely to be hemoglobin transporters. Nearly all of the species containing trusted hits to this model have access to hemoglobin, transferrin or lactoferrin or related proteins in their biological niche. [Transport and binding proteins, Cations and iron carrying compounds, Transport and binding proteins, Porins].	3.28921e-29

>LS483377.1|SQG10903.1|2565208_2566249_-|ribonucleotide-reductase-of-class-Ia-(aerobic),beta-subunit
MATPLDRIKILEPRHPNRSTGIINGRTSGILNWNDIPYPSFYRAYKELSTNFWIPDEVDMKLDARQYGELNAREKNAYDSIIGLLATLDSPQTRFIYNVAEYITDPAAHANAAIIGQQEVIHNESYSYVLASITDLPNQNRIFEIARTHPTIIKRNAPIMGAYDDFMREKTAETLLKSLIQSSILEGINFYSGFAYFYNMVRQNRMNGTGKIISFINRDELAHTKFISELIRAIIGENPELQTNELTAYVHQSFEHAIELETQWSSEVLDGIDGIDVDEMVRYVKYRANKMAGMLGIERLYSDTTDNVMPWIKAYADNFTETKTDFFEMRNASYKKTNVDNGFDDL
>LS483377.1|SQG10902.1|2564715_2565258_-|ribonucleotide-reductase-associated-flavodoxin
MQVTRRPTSTTASTTSEPSAALSILVVVASLSGNTRELGRQIAERCRAAGHAVHWQEADDLRQAPPLAADEADLVLLGCWTDNAGRTPSEMKAWVAGIAERGERPRQLAVFGTGETQWGQEYYCGAVHRLIRYFRSDYPPLEIEQMPHGQRHAGAIEAWTDAVLAHYWSNTDADHRRRHA
>LS483377.1|SQG10901.1|2564417_2564744_-|Thioredoxin
MQIIDAATPEQFQQLLAEHPRVLVDFHKDQCPGCRMLEMSLHRVANSVAGQGTTLLRVQLEVLGEAFFRELGLRQTPTLSLFRDGDERTRLAGFQSPQQIEAAIALHL
>LS483377.1|SQG10900.1|2563673_2564123_-|transposase
MFGIGIDVSKATLDVAVHGEQFRQFSNDKRGFVRLIRWLKTWPIKQVVLEASGGYERAALDVLHAAGLPMVRINPARARRFAQGTGRAAKTDRLDATVLAQMAHLLPLTRYVPPLLGSSVWLNLRNAAGNWCRCGSVRCSACGDWSIRI
>LS483377.1|SQG10899.1|2563209_2563725_-|ISStmaD4-Transposase
MRVSEMQRLRRLVDPDLIAMKQRHIAQLSDDLKQLDKAIAEQLEGQPGWKNIGALKGVGPILISTLACELPELGSLGSKAIASLVGLAPMNRESGTWQGQRRISGGRAVVREALYMAALTAIRYEPRLRAFYAGLKAKGKASKVALVAVMRKMLVILNARKRDAEVALGCP
>LS483377.1|SQG10898.1|2561838_2563170_+|manganese-transport-protein-MntH
MNTLAPRDPSASTPASLGALNASVAVPDKGHWWFRLLAFLGPGYMISVGYMDPGNWATDLAGGSRFGYLLLSVILISNLMAVILQALSARLGIATGMDLAQACRARYPKPVNLALWALCEAAIIACDLAEVIGTAIALKLLFDLPLLWGAVITALDTLLVLLLMNRGFRALEAFVIALLMVIFGCFMVQIALAAPPVMDVLGGFIPRAQVVTDPHALYIAIGIIGATVMPHNLYLHSSIVQTRAYPRTDEGRRSALRWAVTDSTLALTLALFINASILILAAAVFHANGRFDVEDIEQAHQLLAPMLGMGAAATLFAVALLASGLNSTVTATLAGQIVMEGFLHLRLPPWLRRLITRALAIIPVVVVIMLFGDQGAVKLLVLSQVVLSMQLPFAIIPLVRIVTDKVTMGALVAPRWLGAIAWVIALVIVVLNVKLLVDTFSGG
>LS483377.1|SQG10897.1|2561250_2561721_-|Mn-dependent-transcriptional-regulator-MntR
MGKTDDSTSLKSTPLIEAERQVESFRQVREAHRMELVEDYVELISDLLADGGEARQVDIATRLGVAQPTVAKMLRRLARDGWVVQRPYRGVFLTPEGEALAHASRQRHQTVERFLLALGVDADTARRDAEGIEHHVSEQTLALFEAFVRKAEGGAP
>LS483377.1|SQG10896.1|2560661_2561210_+|alkyl-hydroperoxide-reductase
MRSEALRALLLACAVLVAVPAMAADLHAQVSASLMRPEQRSLRPMQWTPPPKLVALYFGADWCAPCHAFVPTLRSVRDALREAGADTEVVYVSLDESDAALRRYMHAQDMPWPVLDPRRAARMPALQALAGLAPPNLVLIDADGTVLANGWQGRRYEGLQPVLKEWTKRACAQEQARCPPGL
>LS483377.1|SQG10895.1|2558512_2560672_+|TonB-dependent-outer-membrane-protein
MPVATPLFHRLPMAAAIALTLPLPVLAATPKPTELDRVQVKVSTATRSERLLSDVPIRTEVLRKEDIALRAATDFSRAAELINGLRVESNCQNCNTSEVQLLGLPGAYNQLLFDGIPLLSTLGSVYGLEQIPAGFVDRIEVVKGGGSALYGPGAVAGVINLIPPLPARSGGHVQAGVDVLKGTPQKNADVRLDLVAKEADAGLSVIAQRNWNSGIDYNGDGYTEITRKNLKVGGLQAWYAPTPGTRLRLDLQVTDETRRGGNRLDQPEYLANIAESLDTKYRRGSVSWDQEINADVDFRLAYAFADIDRDSFYGGLGDVVTDPSAPGYDPSQLDPNVAGSAASRSWRQYGRTHNPLHYIDSQLNWRLGAHALAFGVQYKHEALRDDNRTGDGQRLAVLEDATFHNLGAFIQDEWSLRDNVDLVLGARVDKSSELDSAVFSPRIALAWQATPNLKWRAGIATGFRAPEIFVEDVHVDTLGGEQVRVRNTDGLKEERALTTLFGFDWRSDPANPVWSWDATASYARIRDTFALGEIQRGDDGQLSQLRYNASGSNVLGAETNLGWQPSPQWRLTAGASWYRSRFREPQRIFDDTGDGGDTVIESRDYLKTPRWTGLAQLSWMPAEPWETFVALRHTGPMSVLNNRLGELHRTRSFLVTDLGARWHRHLGAQAQQEVSVAAGVKNVFDQRQKDLEMGALRDSDYVYGPRFARSWYVNLRYAF
>LS483377.1|SQG10894.1|2555864_2558252_+|autotransporter-protein
MRMMQFTPKFHSPFRPTALGLAVTFGLALASGAHAQTVIVNAGETRTVTAGSSVEGRAFQVLGTLNVDGASTAEITVNRGGQIALDNANLAATNGTFGVRAVNSNATISNSKIVADITRGIGLTTAGGLTTTALPLSQVEVSGSTISGQLIGAQVSGGGTIVSSNSHFTGAQAGTRALAGTVELRSGSRSTGDNTGMHIAFTKQGQPGYADPADWSILIDNSTVEGKAGPAILLARTLSSQDLELARVTVQNGATLIGGNGVLVDAQDGALLDFTARTSTLKGDILIADTATAKISLLDGLDLTGRILGPADVIVDQGGRWTLSGDSNTGNLTLGAGSNIFLGSAGTAAYPQLTVNGNYTGNGGTLHFNTVLAGDDAASSRMHVTGDTSGTTQVTVNNIAGAGAQTVNGIPLVQVDGASNGKFTLQGRAIGGMHEYFLHKGSPGAANGNWYLTSVYTGNPCDINPSLPECTPVDPVDPVDPTDPVDPVPVLRPEPGAYLANQAAAVQMFQLRRHDRGEPGFDRARIGTWVRAGRDQLQANVAGQVDARTHINTLQLGSDVWRWGDGRGQVGVMLGTGEATTQAVSTLSGYGTRGRVKGKSAGVYLGWVQDAQSSAGLYVDGWLQAARFDNEVQGEGIARETYDSRTRSASLEAGYAWAIRSTEASTLYLQPQAQLTWTDYDGDSLVENNGTTVEDGRGGGLNGRLGLRLFGQSTLQGNRVQPFLAANWLRGQRDEAMRFNSESLSAKTPENRYEVQAGAQLQLGQRWSAWGDLRVQRGDSGYRNHGAQVGLRAAW
>LS483377.1|SQG10904.1|2566424_2568788_-|ribonucleotide-diphosphate-reductase-subunit-alpha
MTDSTFRVADLAGAGDALRAGGERVPTWITKEAGNRRLPFEAERLQRSIDAVHAEFPQLDVSDYRRVVQSMVERKPSISADDLVDLLIREAESRVDLVAPEWEQFAARIYLRRLYKRASRNRFYDVGLKYGSYVGLQESLADRGIYSNDILRCYSKEELQQAGEMIDPERDRLFAYNGLYLLATRYLASDRSREVYELPQERWLTIALYLMQEEKPRERRMQLVGEAYWALSNLYMTVATPTLANAGKVGGQLSSCFIDTVDDSLQGIYDSNTDIARVSKHGGGVGAYLGYVRSSGAPIRGVANSSGGVVPWIKQLNNTAVSVDQLGQRKGAVAVYLDIWHRDIEAFMDLRLNNGDQRLRAHDVFTSVCVPDLFMEAVERRADWYLFDPHEVKQAKGWYLQDFYDEKRGSGSFRDRYAELVADERISRRTVKAIDLFKRIMLSQLETGNPFLFYRDEVNRRNPNKHAGMIYSSNLCTEILQNMSPTRMIQEIVSGDQIVTTRRAGDFVVCNLSSINLGRAISAPDDLLATDVLERLIPIQVRMLDNVIDLNALPVPQATITNRKYRAIGLGTFGWHHLLAQQAIQWESPDAEQLADRLYERINFLTIQASAQLAKEKGSYPMFAGSDWHNGRYFRDRDYSGAAWDSLAREVATHGLRNGWLLAVAPNMSTAQIAGSTASIDPIYSAFYYEEKKDFRRPVAAPGLSLETWPYYEKGAYKVDQFASVRQNARRQRHVDQSISFNLYVPSTIRASTLLELHLSAWREGLKTTYYVRSNDIDISECEWCSS
>LS483377.1|SQG10905.1|2569218_2570196_+|oxidoreductase-SMc00968
MRAAQYPSFGDPADVLAIADAALPEPGPGEVRIRTVLASIHNHDLLTVRGLYGYKPTLPAIGGSEALGVIDALGDGVDGLQVGQRVAAASVHGTWAEAFIAPARMVIPMPEAIPDEMAAQLIAMPLSALMLLEFLHVEPGQWIVQNTANGAVGKSLAMLARARGVHVANLVRNADAVAQLQALGIDHVFDTSVDGWKDRVREATGKAQAAAAVDSIGGDASGDLVDLLGHHGTLVSFGVMSGEPMRIPAGGLIYKEAMVKGFWGSKVSQAMAVEGKRRLVGELLKRAASGELTLPVEQIFALDDIAQAAKAGAGSGRNGKVLLRP
>LS483377.1|SQG10906.1|2570528_2573156_+|TonB-dependent-receptor
MYRTTLNLLAGAIALGLTAGAAGAAESAATGKDSTTLGAVLVTGSNIKRSDTAGPNPVQIVSREQIEQTGRSTLTDVLRNLSANAGNSFDEQYTGSFAAGSASIGLRGLSPKNTLVLVNGYRVSNFGFALNTQDTFVDLNALPISAVERIEVLKDGASAVYGSDAIAGVINIILRKNFQGVEVGGGFGTATQGGLNERKASLLAGFGDLEQQGWNVLFGLDLLKRDRLDADQRAYTRSGDFRDKPGGRLAGWSTAGGNWLSNPRAPQPFANCPDGSQLRPYSDFGSTLPGQACAFNAQPFKTLQPGAERLQASLSATYRFNDSVEAFADVLYSHNKADQIFSAPLTVGPGLRAYNPATGTLIDVPAVLPVGHPNNPGSTPLPFEYTFFDLGPRLKDNTQVFYRALAGVRGSGERWDWEVAALTSQSAQREYVDNFVNRYAFEQILRDGSYNFLNPSSTPGALDALRLQTKRPGWYKLHSLNVKASTSLWELPAGAVGFAWGAEFRKESLDARTSAQVLSGTELRPAINVVNGERQVSAAYAELSVPLHRTLELQVAGRGDHYDDFGNAFSPKVALRWQPLDSLLLRGSFSRGFRAPSLPEIAPGQTVSYGSVIDPLDPLQPGGSRGVTNIRTGNPDLKAERSRNFNVGAVWSPDGDTSIGLDWYRIEQDNLVKPDSAQFIVDNPTLFPGRVQRDAQGRIQFITNQYANQGELTTSGLDLEANRTFRTEGWGNFTVAGSWTHLLSFKQPLVAGQAPYEGAGNNRHGALPRTRGTTSLNWAVGDWSSTLSLQYVSGYDQRVATATSNPGLRDRIKPYHQLDLYVAYEGIPNTTLSLSVLNLTDKDPPFDPAGGSNGFDISQYNLRGQFVSLGARYRF
>LS483377.1|SQG10907.1|2573222_2575202_-|High-affinity-choline-uptake-protein-BetT
MDVLEPQQSPVRTLRPVFAFAAIVVVAFALFVSLFPLGAGRLLLKAQDWAALNVGWYYLLAMTLYLVFVVGVALSKYGGIKLGADHDEPEFSYLSWAGMLFAAGISITLFFFCVSEPLTHYLQPPQGDPAAGEAGARQAMQLLFLHWGLHGWGVFALAAMAMAYFAYRHNLPLALRSALYPLIGKRINGPIGYTVDALGIVATVFGIGADMGFGVLHLNAGLAHLFNIPHSNLVQIILVVSMMGAAVAVAVSGVEKGVRWMANINMLLAIALVLFMLFAGPTQYLFSTLMQNLGDYLGSVVGKSFDVYAYGGRPEWLGGWTVFYWAWWIGWAPFVGLFIARISRGRTIREFVFGVLLIPLGFTLAWLSIFGNSALDQVLHHGQQQLAQLAVDDPPTVLYALLDGYPWSRTVIAVTVLVSFIFFVTSADSGAVVLSTLSSHGGAPEDDGPRWLRVFWGTVIAVLTAGLLLAGSIDALKSAVVLASLPFSAILLLMMWGLTRAFSDESHRKRALQYRPSPLIGDDRHHQGWRQRLSQAMHFPVRDQVYRFMDDTVKPAMEAVAEQLRGQGWDVSTRFEAGDMELTVNHGEQQDFLYRVILSGYLTPSFAAQQLRNQRYYRAEVHLFEGSQDYDLVGYSRKQIINDIISQYERHLQFLHLSR
>LS483377.1|SQG10908.1|2575397_2575787_-|dioxygenase
MFSHITVGTNDMDAARRFYDALFAAMGARPGVFDEKGRLLYFKDGRMFGVTAPIDGQPACHANGGTIGFTLDSAEAVRGWQDAGVAHGGTAIEDPAGIRSMAGRQLFLAYLRDPDGNKLCAVHVVHVMS
>LS483377.1|SQG10909.1|2575937_2576456_+|RNA-polymerase-sigma-factor
MAVPAASSTALAGFYREHHGWLLGWLRRRTHNADCAADLTQDTFLRLLSRRVDPSELRLPRAYLSTIAHALLVNHWQRADLERAYLTALAAQPEPVHPSAEECTQALQLLHAIADMLSGLAERPRRAFLLARLSGLGYAEIGQQLGVSERMVKKYMAQAMLHCLRLSGDAAA
>LS483377.1|SQG10910.1|2576452_2577403_+|transmembrane-FecR-family-iron-uptake-regulator-protein
MSAAVAGPALEQAAEWFALRQQGWSDDDQQDWRAWLQADAGHADAWRRVEAVWQSFAPLSAPAAATALDAAGHRRRRALRSLGGALGIGAVSLLGLHGLQAQRHLQTQRTAAGRTGHWTLADGSQLWLNAGSEVTVDIGNGNGNRALHLLRGELLLQTGHHTAFVGLPLSVHVPGARLQPIGTRFAVGREAQHSRLDVFEGVVRCLPMFGAALDVPAGSALQIGPMGGLTTVAADPLRGDWQDGRLQVQDTQLIRVIDELARHHRGYLGCDRALSALNVTAVLPRLDSLQALKLLARALPIRIEQRWPWWTVVRPR
>LS483377.1|SQG10911.1|2577472_2580421_+|TonB-dependent-receptor
MKLPCPSPRPLAIALCLALATPCLLPAAAHAQNAASAFRWQIPAGPLDQALTAFGQQSGLSIAADARLTRGRHSGGVQASLNTEAALAQLLTGTGLSFHRDASGVVLQAAPATDAGVRQIGTLRVTGQASEGASPWGLADADAVYRDSGSRVHLDHQQLERFRGQSIGDVLAGAVGVHTGDVRNGGALDVNIRGLQGQNRVPVIIDGGQQAIDVYRGYAGVQQRSYLDPDLISAISIEKGPSLAANAASAIGGVVYMETLKTDDILNDGQAWGLRLRGGVADNSIDRTRTFKQIARGSDNRNSLRDPRDWNGSVAFAQRGEDWQLVAAYARRRQGNYFAGSNGAHRYDDQHLSSGGTGMSSQAVSKLYHPGDEVLNTHTDNESALLKFTWAPNPDQRLELSHRFFNSSFGEIMPSAIGRVGESNEWVTYVDKANTMFQFEPGKMRVNATSLRHRYRPEAHPWLDLSSTLWFTTATSRMFNSNIANTPLFKEMASDQMPDTLGETYGPGLQSDVKTRRWGLDSSNTTRFSNGLGDWTLRYGASLQHEDTAPNSPVLPVDYNNNRYLRSGTRREASVVASLQWQPWDWLSLTAGGRFIDYRTRDRNRVAFVSECRDLRYTFARLSKGGQLLPGWYKEWYPDAQGNYTYDSLRATPYGDSTLGQTYDFDGFIRDPRGANGFHTKQIPTAWGYKPAIRRSGHGVAPYAEARFNLDADMFFYVKYAQGWKMPSLFESTLGNSTSAPVADLKPEKNRSWDIGFSLLKQDLWRDGDRLAFKVAWFKNDIDNAITRRFDSSNWAFYVDNVDNYTVSGYELQSGYDAGIAYLDLSASYYQRARTCDAATAKRLREDPYAKWSKLDTTPDCVDGGFGTSFVNAQNPPKYSIHSTLGFRLFDKRLDTGIRRTYNSGPTHELDKPWNTTGSTGLQNIYLPTAIYDFYARWQFTPKAEVELVVSNLRNTYYMDTLAMSLMPGPGRTTRLNFTARF
>LS483377.1|SQG10912.1|2580560_2580884_-|Spermidine-export-protein-mdtI
MNTLALFFVICSALIDVAANMMVAKSEGFRRWRWGVGAIVMVWIAFALLGQAVRYMDLATAYAMWGAIGVIGTATCGRLLFGNRLRPIGWVGIALVTVAVLLLSTAK
>LS483377.1|SQG10913.1|2580883_2581237_-|Spermidine-export-protein-mdtJ
MSRTVPARGALVAWACLTVAIVAEVVGTSFMAHAARDGGWTGYLVMAGALALSYFFLAQSVRRIAVGVAYAVWEGLGLTLLTVVGLTVFGESLSLQQLAGLVLAVVGIVCVTLGEAH

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Crispr_ID: LS483377_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_5

2841049-2841148

Orphan

Consensus_repeat	Method
GGTAGATGCCCACCTTGGTGGGC	CRISPRCasFinder

1 spacers

DEDDh,csa3

The CRISPR arrays of LS483377_5

>merge|LS483377|5|2841049-2841148|CRISPRCasFinder
GGTAGATGCCCACCTTGGTGGGCATGGATCCAGGACGGCGCCAACCAAGGTTGGCGACTATCGCGGTACAGCGCTCTGGCAGATGCCCACCTTGGTGGGC

>LS483377|5|5|2841049-2841148|CRISPRCasFinder
GGTAGATGCCCACCTTGGTGGGC	ATGGATCCAGGACGGCGCCAACCAAGGTTGGCGACTATCGCGGTACAGCGCTCT
GGCAGATGCCCACCTTGGTGGGC

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG11146.1\|2840466_2841018_+\|Protein-of-uncharacterised-function-(DUF2939)	unknown	unknown	gnl\|CDD\|378575
LS483377.1\|SQG11141.1\|2834931_2835453_+\|3-hydroxyanthranilate-3,4-dioxygenase	unknown	unknown	gnl\|CDD\|183930
LS483377.1\|SQG11154.1\|2854219_2855137_+\|Uncharacterised-protein	unknown	unknown	gnl\|CDD\|185110
LS483377.1\|SQG11149.1\|2843154_2848131_-\|NAD-glutamate-dehydrogenase	unknown	unknown	gnl\|CDD\|377452
LS483377.1\|SQG11138.1\|2833213_2833528_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG11143.1\|2836921_2838289_+\|kynurenine-3-monooxygenase	unknown	unknown	gnl\|CDD\|223727
LS483377.1\|SQG11139.1\|2833535_2834174_+\|transcriptional-regulator-protein-Pai2	unknown	unknown	gnl\|CDD\|377290
LS483377.1\|SQG11140.1\|2834248_2834911_+\|carbonic-anhydrase	unknown	unknown	gnl\|CDD\|238448
LS483377.1\|SQG11144.1\|2838288_2839728_+\|Exodeoxyribonuclease-I	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|236979
LS483377.1\|SQG11145.1\|2839724_2840411_+\|Uncharacterised-protein	unknown	unknown	gnl\|CDD\|274138
LS483377.1\|SQG11137.1\|2832906_2833206_+\|transmembrane-protein	unknown	unknown	unknown
LS483377.1\|SQG11152.1\|2850321_2853495_+\|RND-efflux-system,-inner-membrane-transporter-CmeB	unknown	unknown	gnl\|CDD\|273335
LS483377.1\|SQG11153.1\|2853648_2853942_-\|transmembrane-protein	unknown	unknown	unknown
LS483377.1\|SQG11142.1\|2835615_2836890_+\|Kynureninase	unknown	unknown	gnl\|CDD\|130873
LS483377.1\|SQG11148.1\|2842190_2842964_-\|NAD-kinase	unknown	unknown	gnl\|CDD\|179876
LS483377.1\|SQG11156.1\|2856484_2857414_+\|ArsR-family-transcriptional-regulator-/-Methyltransferase	csa3	COG0640_csa3_CAS-I-A	gnl\|CDD\|369777
LS483377.1\|SQG11151.1\|2849037_2850306_+\|RND-family-acriflavine-resistance-protein-A	unknown	unknown	gnl\|CDD\|169982
LS483377.1\|SQG11155.1\|2855182_2856331_-\|acyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|173847
LS483377.1\|SQG11147.1\|2841198_2842143_-\|5'-nucleotidase	unknown	unknown	gnl\|CDD\|377624
LS483377.1\|SQG11150.1\|2848381_2849038_+\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|379522

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG11146.1\|2840466_2841018_+\|Protein-of-uncharacterised-function-(DUF2939)	gnl\|CDD\|378575	pfam11159, DUF2939, Protein of unknown function (DUF2939). This bacterial family of proteins has no known function.	7.54732e-30
LS483377.1\|SQG11141.1\|2834931_2835453_+\|3-hydroxyanthranilate-3,4-dioxygenase	gnl\|CDD\|183930	PRK13264, PRK13264, 3-hydroxyanthranilate 3,4-dioxygenase; Provisional.	2.02528e-108
LS483377.1\|SQG11154.1\|2854219_2855137_+\|Uncharacterised-protein	gnl\|CDD\|185110	PRK15188, PRK15188, fimbrial chaperone protein BcfB; Provisional.	0.00608855
LS483377.1\|SQG11149.1\|2843154_2848131_-\|NAD-glutamate-dehydrogenase	gnl\|CDD\|377452	pfam05088, Bac_GDH, Bacterial NAD-glutamate dehydrogenase. This family consists of several bacterial proteins which are closely related to NAD-glutamate dehydrogenase found in Streptomyces clavuligerus. Glutamate dehydrogenases (GDHs) are a broadly distributed group of enzymes that catalyze the reversible oxidative deamination of glutamate to ketoglutarate and ammonia.	0
LS483377.1\|SQG11155.1\|2855182_2856331_-\|acyl-CoA-dehydrogenase	gnl\|CDD\|173847	cd01158, SCAD_SBCAD, Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases. Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.	6.30209e-177
LS483377.1\|SQG11143.1\|2836921_2838289_+\|kynurenine-3-monooxygenase	gnl\|CDD\|223727	COG0654, UbiH, 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme metabolism / Energy production and conversion].	1.39021e-38
LS483377.1\|SQG11139.1\|2833535_2834174_+\|transcriptional-regulator-protein-Pai2	gnl\|CDD\|377290	pfam04299, FMN_bind_2, Putative FMN-binding domain. In Bacillus subtilis, family member PAI 2/ORF-2 was found to be essential for growth. The SUPERFAMILY database finds that this domain is related to FMN-binding domains, suggesting this protein is also FMN-binding.	9.26576e-50
LS483377.1\|SQG11140.1\|2834248_2834911_+\|carbonic-anhydrase	gnl\|CDD\|238448	cd00883, beta_CA_cladeA, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.	4.05054e-108
LS483377.1\|SQG11144.1\|2838288_2839728_+\|Exodeoxyribonuclease-I	gnl\|CDD\|236979	PRK11779, sbcB, exonuclease I; Provisional.	0
LS483377.1\|SQG11145.1\|2839724_2840411_+\|Uncharacterised-protein	gnl\|CDD\|274138	TIGR02453, conserved_hypothetical_protein, TIGR02453 family protein. Members of this family are widely (though sparsely) distributed bacterial proteins about 230 residues in length. All members have a motif RxxRDxRFxxx[DN]KxxY. The function of this protein family is unknown. In several fungi, this model identifies a conserved region of a longer protein. Therefore, it may be incorrect to speculate that all members share a common function.	3.55639e-91
LS483377.1\|SQG11152.1\|2850321_2853495_+\|RND-efflux-system,-inner-membrane-transporter-CmeB	gnl\|CDD\|273335	TIGR00915, Probable_aminoglycoside_efflux_pump, The (Largely Gram-negative Bacterial) Hydrophobe/Amphiphile Efflux-1 (HAE1) Family. Proteins scoring above the trusted cutoff (1000) form a tight clade within the RND (Resistance-Nodulation-Cell Division) superfamily. Proteins scoring greater than the noise cutoff (100) appear to form a larger clade, cleanly separated from more distant homologs that include cadmium/zinc/cobalt resistance transporters. This family is one of several subfamilies within the scope of pfam00873. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate].	0
LS483377.1\|SQG11156.1\|2856484_2857414_+\|ArsR-family-transcriptional-regulator-/-Methyltransferase	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	8.59407e-24
LS483377.1\|SQG11142.1\|2835615_2836890_+\|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].	0
LS483377.1\|SQG11148.1\|2842190_2842964_-\|NAD-kinase	gnl\|CDD\|179876	PRK04761, ppnK, inorganic polyphosphate/ATP-NAD kinase; Reviewed.	2.02836e-157
LS483377.1\|SQG11151.1\|2849037_2850306_+\|RND-family-acriflavine-resistance-protein-A	gnl\|CDD\|169982	PRK09578, PRK09578, MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit.	3.0369e-87
LS483377.1\|SQG11147.1\|2841198_2842143_-\|5'-nucleotidase	gnl\|CDD\|377624	pfam06189, 5-nucleotidase, 5'-nucleotidase. This family consists of both eukaryotic and prokaryotic 5'-nucleotidase sequences (EC:3.1.3.5).	1.21892e-153
LS483377.1\|SQG11150.1\|2848381_2849038_+\|TetR-family-transcriptional-regulator	gnl\|CDD\|379522	pfam14246, TetR_C_7, AefR-like transcriptional repressor, C-terminal region. This family comprises the C-terminal domain of transcriptional regulators of the TetR family. It includes the AefR transcriptional regulator from P. syringae. It is found in association with pfam00440.	9.42099e-15

>LS483377.1|SQG11146.1|2840466_2841018_+|Protein-of-uncharacterised-function-(DUF2939)
MKKLTALAVLLVLALAAWWFGGPYMAVHGLSKAIEERDTARLERYVDFPRVRSSLRAQLNDYLVRQAGPDVAASPFGALLYGLGDQLGGAAVETMVTPTGIGAMLQGHVLWKRGRNELQGGDAFGATEPARPLKNAEHHFEALDRFVIDVDRGPDQPPMKVVLEPQGLRWKVVDLQLGMSATP
>LS483377.1|SQG11145.1|2839724_2840411_+|Uncharacterised-protein
MSTYFSDASFKFLRSLARHNDKAWFNDHRQQYEDHVRQPFLRLLGDLQPALAEVSEHFRADTRGVGGSLFRIHRDARFSNDKSPYKTWQGARLFHERRREVAAPSFYVHLQPGESFVGAGLWHPEPETQRRVRHFILDNPGSWKAAAHAPALRKRFDFEESEKLVRPPRGFPADFEFIDDLKHRNWVMWRSLDDATMTGPRLLSTLGKDLAGLGPFVDYLCAALDLEF
>LS483377.1|SQG11144.1|2838288_2839728_+|Exodeoxyribonuclease-I
MADSFLFYDLETFGQDPRRTRISQFAAIRTDADLNEIDTPVSFFVRPADDLLPSPMATLVTGITPQQALAEGISEAEAFDRINEQLSRPGTCALGYNTLRFDDEFVRYGLFRNFHDPYEREWRNGNSRWDLLDMLRLMRAMRPDGIQWPLREDGATSFKLEHLAEANHVREGDAHEALSDVRATIGMARLFKQSQPRLWDYALKLRDKRFVGGLLDVAAMKPVLHISMRYPASRLCAAPVLPLAVHPTINNRVIVFDLEGEIDDLLELPAEVIAQRLYMRASELPEGVAWVPLKEVHLNKVPALIAWNHLRADDHARLGLDVAAIEAKVERLRAFAPQLAEKARQVYNQPRAATVADVDASLYDGFLGNGDKPLLALARTTAPEQLAALEGRFRDPRLPELLFRYRARNHPDSLAPPERQRWQDYRRQRLLGDGGLGELNLPQYQQQLDALAAEAPDDTRRQALLQSLRDWGQHLQETL
>LS483377.1|SQG11143.1|2836921_2838289_+|kynurenine-3-monooxygenase
MIAHASRSLSIIGAGLAGSLLAILLSRQGWRITLYERRGDPRVADYESGRSINLALAERGRNALRQAGVEDEVMARAVMMRGRMVHPREGEPQLQRYGRDDSEVIWSIHRSDLNTTLLELAEQAGATVHFHRRLHTVDFDAGYARFIDDRDDSPHDIRFDTLIGADGAGSALRAAMNRRAPLGEDIAFLDHSYKELEIPPAADGSFRIERNALHIWPRGHYMCIALPNHEGTFTVTLFLPNQGDPSFATINTGAQAEALFAREFADTLPLIPNLRADWEQHPPGLLGTLTLDRWHQQGRAVLIGDAAHAMVPFHGQGMNCAFEDCVALARHLMEADDLEGAFAAFEAERKPNARAIQQMALENYLEMRDRVADPAFLLQRELEQELQRRWPTRFVPHYTMVTFLHTPYAEALRRTELQRDMLVAATTGHDSLDNIDWAALEAQIHAQLPVLEGAH
>LS483377.1|SQG11142.1|2835615_2836890_+|Kynureninase
MSDLLSRTHAIALDAADPLRPLRNEFLIPRHGGVEQTYFVGNSLGLQPRGAQAAVQEVMKQWGELAVEGHFTGPTQWLSYHRLVSAQLARVVGALPSEVVAMNTLSVNLHLMMVSFYRPTAQRPVILMEAGAFPTDRHAVEAQIRFHGFDPAECLVEVQPDEANGTISLTAIERAIAEHGPRLALVLWPGVQYRTGQAFDLDAITRAARLQGARIGFDLAHSVGNLPLRLHDVAPDFAVWCHYKYLNSGPGAVAGAFVHERHHRDTTLPRFAGWWGHEEATRFQMAPQFTPAIGAEGWQLSNPPILGLAPLRASLDLFERAGMEALRNKSLALTGMLEALVRARLSGVLDIITPAEPQRRGCQLSLRVIGGRERGRALFEHLRGIGVLGDWREPDVIRISPTPLYNRYLDVHHFVEEVEAWAGL
>LS483377.1|SQG11141.1|2834931_2835453_+|3-hydroxyanthranilate-3,4-dioxygenase
MLASPINLHAWIEENRHLLKPPVGNKMIDNGDFIVMVVGGPNSRTDYHYDEGPEWFYQLEGEMVLKVQEDGAVRDIPIRAGEIFLLPARVPHSPRRPPGGIGLVVERKRLPHEKDGVIWHCERCNHKLHEEFFPLQNIETDLPKVFARYHASLELRTCSQCGHVDPLPVPAAG
>LS483377.1|SQG11140.1|2834248_2834911_+|carbonic-anhydrase
MKDIHRLLQNNRDWADRIAKEDPEFFQQLSKQQHPEYLWIGCSDSRVPANQIIGMAPGEVFVHRNVANVVAHTDLNCLSVVQYAVDQLKVKHILIVGHYGCGGVHACLHNTRVGLADNWLRHVGDVVQKHQSILDAIEDDELKHARLCELNVIEQVANLCRSTIVEDAWARGQKLMVHGWVYSLKNGRVSEMGIDVGGPEELKPAYEKALSYVPRQGRRD
>LS483377.1|SQG11139.1|2833535_2834174_+|transcriptional-regulator-protein-Pai2
MFTPRAFAETDLLWLDRLLARDPFVTVLTPGSDGLPELTRMPVLYRRDGDQIELRGHWARANPQSRHSGAAKVLVDGPHGYVSASWYPDKEPAARVPTWNYAAAELRGQLQTFDDADALAELVGAISDRFEASVGQAWRFDAARAEHGPELRAIVGFRFQVEHVQLKLKLSQNHPDANQQAVIAALEALASPSSHELAQWMRWHREQSASSG
>LS483377.1|SQG11138.1|2833213_2833528_+|Uncharacterised-protein
MNDITASRDSWWLASLGNTLIWARLRVRPAGTAEVLDSDGNTLSYDSEDTARSQLFDAEFVEYDGLDEEDALVRGFSLHEVQPPQADSDEGLRGRMVQSLGGRA
>LS483377.1|SQG11137.1|2832906_2833206_+|transmembrane-protein
MTLFFALCFVGVAVAGFSAFVIFWPLTLVHVRDRHPALAARFGSGAFLKPDALAWLLRRDYRQQPDRSLSGLATPAWVSLLTLLAGLGMAALLWLASLW
>LS483377.1|SQG11147.1|2841198_2842143_-|5'-nucleotidase
MGDNSPRLLTVAVTSRALFDLEESHALFESDGVAAYAEFQRQHEDDILGPGVAFPVVRKLLALNQGASPENPRVEVILLSRNSADTGLRIFNSIQHYGLGIIRATFTAGEPTWPYVKPFGTDLFLSANPESVRSALRHGIAAATILPKPPGETAAAAADQIDTGRPAGQLRIAFDGDAVIFGDESERISREQGVEAFGRHERERAREPLSGGPFRGFLSALHTLQEVFPAGESAPIRTALVTARSAPAHERVIRTLREWGVRLDEALFLGGRHKGPFLQAFGADIFFDDSQHNIDSAREHVAAGHVPHGVANEG
>LS483377.1|SQG11148.1|2842190_2842964_-|NAD-kinase
MSDTPRIAFLASTAEPAQMARAAMISRYGDHAPEQADVLCPLGGDGFMLQTLHRHGHLGKPVFGMKLGTVGFLMNQYRGDDDVQARIARAEPANLRPLEMVALTESGTSTGSLAYNDVSLLRQTRQAAHIGIDLNGQERVAELIGDGVLVATPAGSTAYNYSAHGPVLPLGSHTIALTPLAPYRPRRWRGAILKADTEVRFRVLDPYKRPVSVTADSHETRDVVEVTIRESKDRRVTLLFDPEHNLEDRILSEQFVF
>LS483377.1|SQG11149.1|2843154_2848131_-|NAD-glutamate-dehydrogenase
MKPQKTAAKTVKNKTKPAESEVAVTAGFSLEPVYTALRKRYPAAAQAEAVAFATDFYKRMESDEFPHHSAEEWAALAAETLEFARARKAGKANVRVFNPTAKANGWESPHTVLQIVNDDMPFLVDTVTMSLAEQGVGVHVLGHPVLRFTRDKAGKLVKVGEGDAESVMLLEIDRQPAEAMAAIEQAINKALDEVRAIVRDWQPMKDKALALADDLGKRQLPVDDASRKEAQEFLRWAADNHFTFFGYREYRVEKQGKEDVLAPLNDTGLGLMRGKDKSAARPVKTLAAQGLNATSGLKDALILTKTNARSRVHRAGYMDYIGVLEFDAKGKIIGEQRFLGLFTSSAYNRRPWEIPLVRQRHEHVMKQSGLAPASHSGKALRHILETLPREELFQSSEDELFRTAMGVLGLQERVRSRLFLRRDKYSRFISALVYLPRERFNTDVRLRIEAMLKDALHGEYVDSSVVLGESPLAQVHLIVRPKPGEMLDVDTAELEQKLAQVLRNWQDDLREALVARHGETEGLRIAARIGKALPAGYIEDNSTAVAANDVSQLDALTGPDDLRLSLQAVPRESGDGLRLKLYRQLDDIPLSDALPMMENMGLRVIAERPYRLSVDNAPVYVQDFEVESTAGAIDAASVDEAFGETFARVWHGDAENDGFNRLVLAAGLHWRQVAMLRGYCKYLLQTGVPFSQAYVEGTFARYPLLARLLVELFEARFDPATGHESKDDIAAGQAQLKAHFDVLAAGDDATLKVLKTVVDARKGDRDAQMQAARDALLKLMDRVSSLDEDRILRSFMGVIDATLRTSYYQTDANGQHGHVISFKFDSALVPDLPKPRPYREIFVYGPRVEGTHLRFGAVARGGLRWSDRREDFRTEVLGLVKAQMVKNTVIVPVGAKGGFFAKTPPVNGDRDAIFANGVACYKLFIQGLLDITDNIVNNKIVPPVDVVRHDMDDPYLVVAADKGTATFSDIANGLAIAHGFWMGDAFASGGSVGYDHKGMGITARGAWESVKRHFRALGRDSQTQDFTAVGVGDMSGDVFGNGMLLSRHIRLVAAFDHRHIFLDPNPDAATTFVERERLFTVPRSSWADYDAKLISKGGGVYPRSLKSIEITPQVREALGLDDNVKALSPNDLMSAILKAPVDLLWNGGIGTYVKAASEQHSDVGDRANNALRVNGGELRCKVVGEGGNLGMTQLGRIEAAQAGVLLNTDFIDNSAGVDTSDHEVNIKILLNDVVRAKKLTVEQRNKLLASMTDEVAELVLNDNYRQNQALSLMERMAVKRLGSKQHFIRTLEQQGLLDRQIEFLPSDAELSQRKARGQGLTRPELSVLLSYSKLVAFAQLLESDIPEDPYLSKELQRYFPTPLQKKYADAMERHRLKREIIATAVTNQTINRMGATFLMRMQEDTGRSIAEVAKAYTISRETLDARALWAQIDALDGKVPESVQIDALEVIWKLQRSFVRWLLSRPGAMPGITEAVNRYQGPFNDIRVASGVLPDSQRPTYEALVAEWKEKGLPSALAQQLAELHFLEPAFDIIELARTRKLKPVDVSKVHFRLGDALQLPWLFEQVDALEVNGRWHAVARGVLRDELAANHRNLAGQVLGTKGSSAEAKVAAWMGRDDNSLRFTLAMLAELAEQKTLDYPTVSVAVQRLGQLAAHGA
>LS483377.1|SQG11150.1|2848381_2849038_+|TetR-family-transcriptional-regulator
MNPAYLPVALDARDERVFDAVRELLAQQGMQMSMEAVAQHAGCSKQTLYSRYGSKQELLRRVMQRHVGHATGAMVRALRTDDLRASLLQFATDFLEHFNQPHVGQACRLIAADAAQFPEEARTLYRHGAGALTLHLAEWIETVCMRGQLRHDDPHFMAELLLSMIAGQDFDKQRFHTPHRDDARLRRRWAEFSVDSFLRAFAPQPSPAPSSNQPRSSS
>LS483377.1|SQG11151.1|2849037_2850306_+|RND-family-acriflavine-resistance-protein-A
MTAPLRTLALTCAVAVALAACKKPEQQTPPPPEVGVIDAKPQTLPLQRELVGRLSPFRSADVRARVPGVLLKRVYQEGSQVKQGQTLFLIDPAPLRASLNASEAQLASARATYANAKVAADRARSLAPQQFVSKSDLDNAESAERTALAAVKQAEAAVTSSRISLGYTEVTAPISGVANKQQVTEGALVGQGDVTLLTTVDQLDPLYVNFSLSVDELTQLRAQQAKGALALSGDGKATVNVKLADGSTYSEPGTLDFSSTTVDPATGAVSLRALLPNPQQILLPGAFVSFQANLGERNNAFLVPQQALLRDTTGGYVMVVGADGKVARKNVKTDGAQNGNWLVSDGLAAGDKVIVAGVQKVKEGAPAVAKPWTPGQDANGKPAAGGAAPAGTAPAAGKAPADAAKPEQADAAKPAATDSNKQ
>LS483377.1|SQG11152.1|2850321_2853495_+|RND-efflux-system,-inner-membrane-transporter-CmeB
MPKFFIEHPVFAWVVAILISLSGVIAILNLGVESYPNIAPPQVTVSATYPGASADTTEKSVTQVIEQQLTGIDHLLYFSSSSSSNGRAQITLTFETGTDPDIAQVQVQNKVSLATPRLPSEVTQQGVVVAKANAGFLMVVALQSDTPTINRDALNDIVGSRVLDQVSRIPGVGSTQQFGSEYAMNIWLNPEKMQGYGLSASQVLAAVRAQNVQFAAGALGSDPSPEGQHFTATVSAEGRFSSPQEFENIILRANADGSRVLLKDIARVAFGANNYGFDTQYNGKPTGAFAIQLLPGANALNVAEAVRAKMDELQPSFPAGVTWFSPYDSTTFVKISIQEVVKTLFEAVFLVFLVMLIFLQNFRATLIPTLVIPVALLGTFLGMWMIGFTINQLTLFAMVLAIGIVVDDAIVVIENVERIMTEEGLAPKPATQKAMTQITGAVVAITVVLAAVFIPSALQGGAAGEIYKQFALTIAISMAFSAFLALGFTPALCATFLKPTHNDNPNIVYRTFNKYYDKISHTYVGHITSAVRHAPRWMILFVVLTALCGFLFTRMPGSFLPEEDQGYALAIVQLPPGSTKGQTNEVFAQMRGILEKQDGYEGMLQVAGFSFVGSGENVGMGFIRLKPWEERKFTAPEFIQNMNGAFYGIKEAQIFVVNLPTVQGLGQFGGFDMWLQDRSGAGYEQLTQARNILLGQAAQKPDHLVGVRPNGLENAPQLQLHVDRVQAQSMGMSVSDVYSTIQLMLAPVYVNDFFYEGRIKRVTMQADGPYRTGQESLKSFYSPSSLTKNADGTNSMIPLNTVVKSEWVSAPPSLSRYNGYSAINIVGSQAPGTSSGEAMQTMESIVNDDLPAGFGYDWSGMSYQEILAGNAATLLLVLSIVVVFLCLAALYESWSIPVAVLLVVPLGVLGALGLSMLRGLPNDLFFKIGLITVIGLAAKNAILIVEFAVEQRAAGKNLRDATIEAARLRFRPILMTSFAFIMGVIPMAISTGAGANSRHAIGTGVIGGMLFATLLGLLMIPVFFVVVRRMLGDKLDEPSKEFMERQRDADAAHRPDR
>LS483377.1|SQG11153.1|2853648_2853942_-|transmembrane-protein
MLIYRGAGLLTLLTPIAAVLLILILFPDPAVGRGNTSLSQVLLAFGLGSAINTVLGFVLNRKPRAPGQHAPHHFFFLPMQWPALAIVAACVVIAVLR
>LS483377.1|SQG11154.1|2854219_2855137_+|Uncharacterised-protein
MERAPLRRFSRPALLLGALFAASSVQDAHAAGVLVCDNCRDPRALALSSGTGPTIVADFQQRRLHGFDVEYDRELRRYRATRAQIPGPINASFNRIMGMLDNNVPTVQFAPRQWAGRGVQYEVHPDDPQYANGIGFPEEHKNLNAYDVVQMATERFRLESAMGKAFTGATTSSRAWNSMAIFLSSIGLSFVSKALGIDGAIYRITWRDGSKTTLVIVSSSVDTARYVQGQSKDANGNMIPDGAATSPGLAQHFAGTYNFNSRDDLDRWIDSGRLYGMNMFPGAPPESLQIVCEWNGTDIVCRLPR
>LS483377.1|SQG11155.1|2855182_2856331_-|acyl-CoA-dehydrogenase
MDFSFTEEQLMLQDVARRIAQEKIAPSAEHHDRTGEFPLDNIRLLGENGLMGIEVPTEYGGAGMDPVAYVLAMVEVAAADAAHSTIMSVNNSLFCNGILTHGTEQQKQTYVRAIAEGEAIGAFALTEPQSGSDATAMRCRAVKQADGTFVINGKKSWITSGPVARYIVLFAMSEPDKGARGITAFLIDTDKAGFGRGKTEPKLGIRASATCEIEFNDYVAKAEDVLGQEGEGFKIAMSVLDAGRIGIASQAIGIARAAYEATLEYVKERKAFGAAIGTFQMTQAKIADMKCKLDAALLLTLRAAWVKGQGKRFSTEAAVAKLTASEAAMWITHQAVQIHGGMGYSKEMPLERYFRDAKITEIYEGTSEIQRLVIARNETGLR
>LS483377.1|SQG11156.1|2856484_2857414_+|ArsR-family-transcriptional-regulator-/-Methyltransferase
MDLEDWSTRLKVFADATRVRLLALLEQEELTVAELSAITRLAQPRVSTHLARLKEAGLVRDRRAGVSAYYRFDEAQLDPAQRALWHALSNGSDDPLLRQDAERVAAVLAHRASDQNWADSVAGDMERHYSPGRTWEALARTALPLLETGDVLDIASGDGVLAELVAPHAKRYICIDTSARVVAAASERLRRLPNVEVREGDMHALPFKDNSFDLVVLMHALTYASKPAQAVTEGARVLRPGGRLLLCSLARHEHKAAVEAYGHVNLGFSDKELRRFVDKAGLQVSSLETVTREKRPPHFEVISLIAHKP

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Crispr_ID: LS483377_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_6

3293413-3293516

Orphan

Consensus_repeat	Method
CGGTCGTGCCGGCCGCTGGCCGGCAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483377_6

>merge|LS483377|6|3293413-3293516|CRISPRCasFinder
CGGTCGTGCCGGCCGCTGGCCGGCAACGCCAACCAAGGTTGGCATCCACCAGAGCCGGGCCATGCATGTGAACGCAGGCGGTAGTGCCGGCCGCTGGCCGGCAA

>LS483377|6|6|3293413-3293516|CRISPRCasFinder
CGGTCGTGCCGGCCGCTGGCCGGCAA	CGCCAACCAAGGTTGGCATCCACCAGAGCCGGGCCATGCATGTGAACGCAGG
CGGTAGTGCCGGCCGCTGGCCGGCAA

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG11548.1\|3291887_3293180_-\|adenylosuccinate-synthetase	unknown	unknown	gnl\|CDD\|234904
LS483377.1\|SQG11558.1\|3302255_3307163_-\|alpha-2-macroglobulin-domain-containing-protein	unknown	unknown	gnl\|CDD\|225248
LS483377.1\|SQG11557.1\|3299809_3302179_-\|penicillin-binding-protein	unknown	unknown	gnl\|CDD\|227289
LS483377.1\|SQG11556.1\|3299161_3299737_+\|Bacterioferritin	unknown	unknown	gnl\|CDD\|225104
LS483377.1\|SQG11554.1\|3297495_3298389_-\|curved-DNA-binding-protein	unknown	unknown	gnl\|CDD\|182347
LS483377.1\|SQG11549.1\|3293551_3293737_-\|inner-membrane-protein-YjeT-(clustered-with-HflC)	unknown	unknown	gnl\|CDD\|225782
LS483377.1\|SQG11555.1\|3298649_3299132_+\|peroxiredoxin	unknown	unknown	gnl\|CDD\|239311
LS483377.1\|SQG11541.1\|3285353_3286094_-\|BioH-protein	unknown	unknown	gnl\|CDD\|223669
LS483377.1\|SQG11547.1\|3291107_3291770_-\|transmembrane-protein	unknown	unknown	unknown
LS483377.1\|SQG11551.1\|3294664_3295798_-\|HflK-protein	unknown	unknown	gnl\|CDD\|130988
LS483377.1\|SQG11542.1\|3286234_3286774_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG11552.1\|3295951_3296947_+\|alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|176183
LS483377.1\|SQG11539.1\|3282742_3284833_+\|catalase	unknown	unknown	gnl\|CDD\|236886
LS483377.1\|SQG11546.1\|3290494_3291172_+\|endopeptidase/peptidoglycan-hydrolase	unknown	unknown	gnl\|CDD\|366703
LS483377.1\|SQG11553.1\|3297035_3297407_+\|twitching-motility-protein-PilH	unknown	unknown	gnl\|CDD\|381093
LS483377.1\|SQG11544.1\|3287168_3289295_-\|methyl-accepting-chemotaxis-protein	unknown	unknown	gnl\|CDD\|185001
LS483377.1\|SQG11543.1\|3286788_3287079_+\|transmembrane-protein	unknown	unknown	unknown
LS483377.1\|SQG11545.1\|3289527_3290490_+\|ErfK/YbiS/YcfS/YnhG-family-protein	unknown	unknown	gnl\|CDD\|341130
LS483377.1\|SQG11540.1\|3284855_3285344_+\|Uncharacterised-protein	unknown	unknown	gnl\|CDD\|237855
LS483377.1\|SQG11550.1\|3293804_3294668_-\|HflC-protein	unknown	unknown	gnl\|CDD\|259803

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG11548.1\|3291887_3293180_-\|adenylosuccinate-synthetase	gnl\|CDD\|234904	PRK01117, PRK01117, adenylosuccinate synthetase; Provisional.	0
LS483377.1\|SQG11558.1\|3302255_3307163_-\|alpha-2-macroglobulin-domain-containing-protein	gnl\|CDD\|225248	COG2373, COG2373, Large extracellular alpha-helical protein [General function prediction only].	0
LS483377.1\|SQG11557.1\|3299809_3302179_-\|penicillin-binding-protein	gnl\|CDD\|227289	COG4953, PbpC, Membrane carboxypeptidase/penicillin-binding protein PbpC [Cell envelope biogenesis, outer membrane].	0
LS483377.1\|SQG11556.1\|3299161_3299737_+\|Bacterioferritin	gnl\|CDD\|225104	COG2193, Bfr, Bacterioferritin (cytochrome b1) [Inorganic ion transport and metabolism].	1.51554e-34
LS483377.1\|SQG11549.1\|3293551_3293737_-\|inner-membrane-protein-YjeT-(clustered-with-HflC)	gnl\|CDD\|225782	COG3242, COG3242, Uncharacterized protein conserved in bacteria [Function unknown].	6.77277e-12
LS483377.1\|SQG11555.1\|3298649_3299132_+\|peroxiredoxin	gnl\|CDD\|239311	cd03013, PRX5_like, Peroxiredoxin (PRX) family, PRX5-like subfamily; members are similar to the human protein, PRX5, a homodimeric TRX peroxidase, widely expressed in tissues and found cellularly in mitochondria, peroxisomes and the cytosol. The cellular location of PRX5 suggests that it may have an important antioxidant role in organelles that are major sources of reactive oxygen species (ROS), as well as a role in the control of signal transduction. PRX5 has been shown to reduce hydrogen peroxide, alkyl hydroperoxides and peroxynitrite. As with all other PRXs, the N-terminal peroxidatic cysteine of PRX5 is oxidized into a sulfenic acid intermediate upon reaction with peroxides. Human PRX5 is able to resolve this intermediate by forming an intramolecular disulfide bond with its C-terminal cysteine (the resolving cysteine), which can then be reduced by TRX, just like an atypical 2-cys PRX. This resolving cysteine, however, is not conserved in other members of the subfamily. In such cases, it is assumed that the oxidized cysteine is directly resolved by an external small-molecule or protein reductant, typical of a 1-cys PRX. In the case of the H. influenza PRX5 hybrid, the resolving glutaredoxin domain is on the same protein chain as PRX. PRX5 homodimers show an A-type interface, similar to atypical 2-cys PRXs.	3.28546e-78
LS483377.1\|SQG11541.1\|3285353_3286094_-\|BioH-protein	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	3.3085e-07
LS483377.1\|SQG11551.1\|3294664_3295798_-\|HflK-protein	gnl\|CDD\|130988	TIGR01933, Protein_HflK, HflK protein. HflK and HflC are paralogs encoded by tandem genes in Proteobacteria, spirochetes, and some other bacterial lineages. The HflKC complex is anchored in the membrane and exposed to the periplasm. The complex is not active as a protease, but rather binds to and appears to modulate the ATP-dependent protease FtsH. The overall function of HflKC is not fully described.//Regulation of FtsH by HflKC appears to be negative (SS 8/27/03].	8.29771e-117
LS483377.1\|SQG11554.1\|3297495_3298389_-\|curved-DNA-binding-protein	gnl\|CDD\|182347	PRK10266, PRK10266, curved DNA-binding protein.	1.98574e-74
LS483377.1\|SQG11539.1\|3282742_3284833_+\|catalase	gnl\|CDD\|236886	PRK11249, katE, hydroperoxidase II; Provisional.	0
LS483377.1\|SQG11550.1\|3293804_3294668_-\|HflC-protein	gnl\|CDD\|259803	cd03405, SPFH_HflC, High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily. This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.	3.90151e-107
LS483377.1\|SQG11553.1\|3297035_3297407_+\|twitching-motility-protein-PilH	gnl\|CDD\|381093	cd17538, REC_D1_PleD-like, first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains. PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	3.3106e-35
LS483377.1\|SQG11545.1\|3289527_3290490_+\|ErfK/YbiS/YcfS/YnhG-family-protein	gnl\|CDD\|341130	cd16913, YkuD_like, L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD. Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.	9.68896e-27
LS483377.1\|SQG11544.1\|3287168_3289295_-\|methyl-accepting-chemotaxis-protein	gnl\|CDD\|185001	PRK15041, PRK15041, methyl-accepting chemotaxis protein.	1.75207e-79
LS483377.1\|SQG11552.1\|3295951_3296947_+\|alcohol-dehydrogenase	gnl\|CDD\|176183	cd05280, MDR_yhdh_yhfp, Yhdh and yhfp-like putative quinone oxidoreductases. Yhdh and yhfp-like putative quinone oxidoreductases (QOR). QOR catalyzes the conversion of a quinone + NAD(P)H to a hydroquinone + NAD(P)+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR 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.	1.34182e-163
LS483377.1\|SQG11540.1\|3284855_3285344_+\|Uncharacterised-protein	gnl\|CDD\|237855	PRK14900, valS, valyl-tRNA synthetase; Provisional.	1.16853e-13
LS483377.1\|SQG11546.1\|3290494_3291172_+\|endopeptidase/peptidoglycan-hydrolase	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	3.31464e-25

>LS483377.1|SQG11548.1|3291887_3293180_-|adenylosuccinate-synthetase
MGQSVVVLGAQWGDEGKGKIVDLLTEEIGAVVRFQGGHNAGHTLVINGKKTVLHLIPSGILRDDALCLIGNGVVISPAALQKEIAELEASGVEVRSRLKISPAAPLIMPYHIALDQARERAAGGKAIGTTGRGIGPAYEDKVARRGIRIADLHYPKQLEELLRTALDYHNFVLTKYLNTDAVDFQKTFDEALAFGEYVQPMKSDVAGILHDLRKQGKRVLFEGAQGALLDIDHGTYPYVTSSNTTVGGALAGSGVGADSIDYVLGIAKAYATRVGGGPFPTELDDEVGQGIRDRGAEYGASTGRPRRCGWMDIVALKRAVAINGISGLCITKLDVLDGMAKLKVCIAYEYNGKRTEYAPLDAQGWEECTPVYLEFPGWSENTHGITNWDDLPPAARAYLRSLEELAGCPISIVSTGPDRDHTMVLQDPFA
>LS483377.1|SQG11547.1|3291107_3291770_-|transmembrane-protein
MKGETVVRITLWVLWSLWGIACLVLVLGAAANTLASRTQTVPLVLSPGATAQITVYRLIDDQLRLRLRYAADGTDADPEVLLRIETPTDHGDFRAGERSGVAGQGINRGLASVESSGLMASYFGYGRGDALPRGRSWVRVTVLEVDPALADRAATVELQPPLDLLKLTDLDYVWLWPFFFWKVAALLLLIPGAALAVFTFTLRRWQHRASKQADSAVGTD
>LS483377.1|SQG11546.1|3290494_3291172_+|endopeptidase/peptidoglycan-hydrolase
MRLSQLIVLGVLLGLGAGWWLRRDAGEPVAASLPEAQPAAAVAPAKGSVAPLGTAPAPAATVPSAARTADAPSGLLLPVQGVLASQLRDTFTDARSEGRVHDAIDIMADAGTPVLAVADGTVEKLFDSERGGLTIYQFEPSGRWCYYYAHLQRYADGLTEKQVIRRGEVIGYVGSTGNASAEAPHLHFEVHVLGPEKQWWKGESINPYPLLNPPASKPGAASAAR
>LS483377.1|SQG11545.1|3289527_3290490_+|ErfK/YbiS/YcfS/YnhG-family-protein
MPLPVYRSTLLALSLLASPAFAQAPPPGLPAPIAEKAGPDTAARSALHAQVLLDRANFSPGQIDGEVGSNQRRAVSGFQAAHGLAVTGELDDATWQALQADTVPPLASYTLTSEDVAGPFQAVPKGPAAQAKLKSLGFNNVEESLGERFHASPELLKLLNPGVDLSKAGNRIQVPNVAPSPLPKAAKVVVDKSDSSLQLLDAQGKVIAQVPVSSGSQHDPLPIGEWKILGVYRDPPFHYNPKLFWDARKGEKKATLPPGPNNPVGRVWIDLSKPHYGLHGTPEPGHVGKTESHGCVRMTNWDALRVADAVDTSVPVVMQE
>LS483377.1|SQG11544.1|3287168_3289295_-|methyl-accepting-chemotaxis-protein
MNYLRNVRVAWRLGLGFGLLLLLVAAVVATGATASVVQKRAMQQVVDVSVAKVRLLSQMLDANNQMMVVRREMLIRQGGDRGHDEQRIADLVKRYEASWTAYQALPSDAEGKAIAETIAAKRAIARPLNKQTSELMEQGDYPGAVALTLGPVQEAANGWNKALSDGVDFEEKESREAAAEAIRLGERSLLQLLVLGGVALLVGIGASVMIGRSLTGPLARAVNLAERLSRGQLDQEFRLGGRDELTQLGEAMASVRQSVQAAIGAQLQMAEQHEAGAIRYRMDASAFPGDFGRMVQATNSLVESHVQVELLMAEVMQRYAIGDLSRDLPDYPGEKGTLTRTLAAVKQSLMAINAQIDALARAARAGDFSMRGDAAAFQFQFKAMVEHLNGMMASSQASIADVSDVLRAISHGDLTARMDGEYDGVFARMRDDANTTTAQLTGIVRGIQVAADSINNAAQELAAGNNDLSRRTEQQAANLEEAAASMEELTSTVRQNAELARQADSEAHAAGAAVRETEQAMAQMASVMGEIDQSSARISEISTVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVASEVRTLAQRAGVAAKEIKELIEDAAAKVKSGLAVTVESEAAIARVAQASSRTTQLMSDIAAASKEQAAGIEQVNQVVVQMDQVTQQNAALVEEATAASRALEEQAHALTTSVAVFKVEQGARMPIVPAQAA
>LS483377.1|SQG11543.1|3286788_3287079_+|transmembrane-protein
MKMRRLLSWTGLALCVVYLLLTAWLVHGAQSDADPKGAYILMSLPITLQSAALDAIGAGSLLYGKPWSTAYAVLVPPTLLLLYAAGWLIERAARGR
>LS483377.1|SQG11542.1|3286234_3286774_+|Uncharacterised-protein
MRWTYALAMMAMMLPLNSSANDGWINGAGKAMPETDAMKSSGGFAASLLVTSDADWQAKWETPPETTPGFTQADEVHPGGELFLLTFLSNPQLDENRVPKVHCDLRMLRPDGTTSIDESDVPCFTAALPGPPTLLYMTNLHLKFVAEASDPKGTWTAQVVVRDLLRNVSLPLQAHFDVR
>LS483377.1|SQG11541.1|3285353_3286094_-|BioH-protein
MGIGSEEKPGCDSASPTPQHVLMLPGLDGSGRLSIPFLSALQAHGLTTQAITLPAQGGQDHATLAQRLWSQLPGHPFILLAESFSGPLAVELAMRQPAGLRGLVLAATFACRPVPLPAASAALLTPAWPLPPVALLARLLLGRWRTREHLSMLRDALARIPAATLRRRAAATLRVDVRALVPAIDVPTLCLHACHDRLLWPPSVAELQALLPDARHVSLEGPHLLLQARADAAAAEVAAWMRTLSP
>LS483377.1|SQG11540.1|3284855_3285344_+|Uncharacterised-protein
MPRGDKSAYSDKQKRQAEYIEESERERGASEGTAERIAWATVNKQDGGGKRSGSARKGTKKATSKKAAKKAPARKSGTKKATTKATAAKKAPAKKTTARKAAKKAPARKTATKKTAKKTAARKAGTAASRSAAAKKAAKTRAAKKTVRKVAAKKAARTRARG
>LS483377.1|SQG11539.1|3282742_3284833_+|catalase
MAASKPTGKRATTHAENHHRGSGDELHQQAGGSHPAMTTDQGIPVADNQNSLRQGPRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFELTRSLKAHTRARILTEVGVKTPVFTRFSTVAGGAGSVDTPRDVRGFAVKFYTREGNWDLVGNNIPVFFIQDAMKFPDLVHAVKMEPDRAFPQAASAHDTFWDFISLMPESMHMIMWAMSDRAIPRSLRMIEGFGVHSFRLLNEAGESTFVKFHWRPKLGIQSTVWDEALKLQSADNDFHRRDLFEAIQRGDFPEWELAVQLFTEEDADAFPFDHLDPTKIIPESLVPLQVIGRMVLDRWPDNFFAETEQVAFCPANVPPGIDFSNDPLLQGRLFSYLDTQLLRLGGPNFHQIPVNAPKCPFANHQRDGHMQMQVPKGRVAYDPSSLQEDTPRETPAGFRSHASADDGRKGRTRAESFADHYSQARMFFRSLEKPEQAHLASALVFELSKVETLKVRVRTVSHLRNIDDSLAQRVADGLALPALPDPAPTATPVRDMPPAPEVRVIGRNKPTLQGRCIGILFDEGSDARIIASLSKAARKAGADVKLVAPKVGGATLSDGALQAADGQLAGTPSAVFDAVAVVLSPEAAKALSKESAAIEFVSQAWAHLKAIASDAGGQTLLKAARVGNDAGIVEAEDAKAFLAAAATRQWAREPKLRLLA
>LS483377.1|SQG11549.1|3293551_3293737_-|inner-membrane-protein-YjeT-(clustered-with-HflC)
MKDLFAAVCLVAVLEGLFLFVAPFAWKRMAERLLDLPSPALRSFGGLVLLAGLSLLWWVRH
>LS483377.1|SQG11550.1|3293804_3294668_-|HflC-protein
MKSPIWIAVIVAVVLGLLGSVYVVREDQTAMVLNLGKVVRSDIKPGLHFKVPVVETVKVFDRRFQVLDTAPARYFTAEQKDVSVDFFAIGYISNVGDYFRATGGDPRIANARLAPIITDSLRNQINSRTLQQLVSGDRSELIAEQLKGINEAVAGLGMQMIDLRIKQVDLPTDSQVINDVYERMRAQRKQEAAKLRAEGEEQSLTIRAQADRDSTVLIAEAERDAQRLRGEGDAEAARIYGKAGSADPSFYAFYRSLEAYRGSMTDGNGVIVLDKNDPFLQYLKNDR
>LS483377.1|SQG11551.1|3294664_3295798_-|HflK-protein
MAWNTPGGNKGGQGPEDNRRGPFGSRGGGNGGGWGGLPGPLKDLFDGGIVRWVVAAVVLLVLFSSFQLIGEQQRGVVLRFGQFSRILQPGPNFKLPWPIESVTKVNATEIKTFSIQVPVLTRDENIVNVSLNVQYRIDDPQQYLFGTVDANQVLEQSAQSAVREEVGRADLNAVLNNRGPLAVAAEERLQALLKAFKTGLTVTGLTLQDARPPEEVKPAFDEVNGAQQVKERLINEAQAYAAKVVPEARGQASRARTTAEGYKQAVVSKAEGDAQRFSLLQAQYKDAPEVTRKRLWLETVQQVLSENRKVIGGDGRQLIYVPMTGDTRPSTSAPAAVANPDVVMPSLPGAAAEASRDPGRPVGRPTGRPSGREEGSR
>LS483377.1|SQG11552.1|3295951_3296947_+|alcohol-dehydrogenase
MAPTTPFTAFRIENDDAGYRSGLVRLGVDDLNPGQVLIRAHWSSVNYKDALAGTGKGKILRRFPLVGGIDVAGTVVASTDPDWREGDAVLATGCGLSETRDGGYSQYVRLESRAVIAQPAGLTPREAMVLGTAGFTAALALLRMQDNRQTPELGPLAVTGASGGVGALALSIFSRAGYSVHAVSGKPDQAGFLRSIGATEVLPRDALADTGALQSARFGGGLDNAGGDMLASLLAQTVPYGSVVSAGLAASPTLDMTVMPFILRGVSLLGVSSANAPRGLREEVWSRLGSDWKPQHLDRICTAEVGLDGLPAVFERMLAGGSLGRTVVRID
>LS483377.1|SQG11553.1|3297035_3297407_+|twitching-motility-protein-PilH
MARILIVDDSPSQLLGIQRIVEKLGHQILTATDGAAGVETAKAELPDLVLMDVVMPNLNGFQATRTLARDEATRHIPVILVTTKDQDTDRMWGMRQGAKAYITKPFSEDELSEVLERVFAGQG
>LS483377.1|SQG11554.1|3297495_3298389_-|curved-DNA-binding-protein
MEFKDYYATLGVEPSAGEAEIKTAYRRLARKYHPDVSKEAGAEDKFKAVNEAYEALRDPEKRAAYDQLRAQGYRPGEEFNVPPNYGGAGGFNFEEVFGGGGPNGGFSDFFESLFARQRGGAGAGAGPGFSSQGHAPNRDTRAKLSVPLEAAYSGDSLRITVNGKQLDVRVPKGIRPGQVIRLAGQGNHGGNLLLEVEYAAHPQFEVDGRNILYTLPLTPWQAALGTSISVPTLGGAVELKIPADSDAGRKLRLRGRGLPGNPDGDQIVEIEIVAPAATDEAQKKAYRNLAKAFGETI
>LS483377.1|SQG11555.1|3298649_3299132_+|peroxiredoxin
MTIHVGDRIPEVTLKRIREGIETLDTHSLFDARKVVLFAVPGAFTPTCSARHLPGYVEKFEAFRQRGIDVYCMAVNDPFVMKAWAADQSVPDGLLMLSDGNAELTRALGLELDASASGMGIRSRRFALYVDDGVVREAWVEQPGQFEVSSAEYVLEHLPT
>LS483377.1|SQG11556.1|3299161_3299737_+|Bacterioferritin
MSSKPAKTSKPAVNVPGISDRATLRERARRNLEDGAITDSYSADREVVIKLLNDALATEYVCVLRYYRHYFMAKGMLADAVKAEFLEHAQQEQAHAGKLAERIVQLGGEPDLNPDTLTARSHAEYKEGSDLRDMVRENLVAERIAIDSYREMINFIGDRDTTTKRILEEILAQEEEHADEFADLLDGWIGE
>LS483377.1|SQG11557.1|3299809_3302179_-|penicillin-binding-protein
MTTRLAALRRRLRPLWPWLRWGTAATLALLLVLDFAFPPPLPKQRDTSTLVVAADGTPLRAFADAEGVWRYPASTDSVSPLYLQALLTYEDRWFWRHPGINPLAILRASGQLLRGGRIVSGGSTLTMQVARILDPHTRTPWGKLKQMLRAVQLEVHLSKQQILALYLERAPYGGTIEGVEAASWAYLGKPAAQLSHAEAALLAVLPQAPSRLRPDRHPEAAQKARDKVLSRMAELGAWTAEEVEDARIENVVARSLRPPLHAALLAQRLHSAHPGQARIQSSIDIGLQRTLEERVASYFSTLPERTSAALLVVDNQTLQARAYVGTLAFGDRQRLGHVDMVQAWRSPGSTLKPFLYAMALDDGLIHSESLLVDAPQSFGSYRPGNFDMAFNGPIGASSALRLSLNVPSVDLLQRVGPARFAARLSHSGIQLRFPPGSTPNLSLILGGTGARLEDLVGAFAALNRNGIAGRVRYTDEEPMIERRLASPGASWIVREMLESNPRPGYSVGTFDVGGRPRVAWKTGTSYGYRDAWAIGSTRHYTVGVWVGRPDGTPLPGQYGAVTALPLMFEVVDSLPRQRGDSAAAPMPASVSQEDICWPTGERAEGLPAALCQRLMPAYLLEGAAPPTFPEREARRWQPGRQRYLADARTGLRVSADCRLPHEEVAREIARWPALLSPWLSKATREASQLPALSPDCRDDGREASVALHIDGLNDGATLARAPNSEHGVRLQLRALGSEQAVDWLLDGRWIAQTHGAQLMQREFVEPGAHTLTALAADGAWTQVRFNVLR
>LS483377.1|SQG11558.1|3302255_3307163_-|alpha-2-macroglobulin-domain-containing-protein
MSGPARRKRWGWAAAVLAGGLLLGLAGCRNDSGQLPKASGEAITTKAEQVKEFTLLRTYPDQKNDGLSLALEFSRPLVGTQDFDKLVRFEEKVGTDDSSWTLSDDGLTLRYPFVEAGKEFSLVVSPDLLAADGSRLGKELKQKVFSGELKPVVGFASQGSVLPAKDSRGLPVVSVNVPEVDVEFLRVREKDLPTFFSQYQRGGRRGSWELSSDYERSPINKLAEPVYVNRFILGGKKNERVLTYLPTQDIKELQEPGLYFALLKRTGDYEGEFDTAFFSVSDIGLHTRAYKDKLFVHTAGLKDGAPLKGIDLRVLDAKGEVVLKGSTDGNGNALLNYTLDATHVLVASTGKDTSFLPFNQPALDLSEFAVAGRDNAWFDVYAWSGRDLYRPGETVRLSALLRDNDGKPVKAQPVFLRLKQPDGKTFRETRLQPGDQGYINFEQVIPAEAPTGRWQVEFRTDPASKEAIQGMTLRIEEFLPERMKLDLDSAQKTLKPGEDLRLQANGAYLYGAPADGNRFTARMAVAAEQKPVEGLPGYFFGDPTQQLPREAKDVIDTTLPGNGQLREDVALPEEAAKAKAPIAVVLSGSLYETGGRTVTRTLKRVMWPANALVGVRPLFNPEDGADSNGNARFELMRVDAAGTPQPAKGLKITLVRELRDYHWTFNDNRWDYDFTRRFENKETRTVDAGSSAVAFDFPVEWGEYRVDVFDPSTGLTSRYPFRAGWSWGDDNRGLDARPDKIKLGLDKTGYKAGDTLEVTVTPPHAGKGILMVETDRMLYVQDIDAKPGSTFKIPVTADWERHDVYITALVFRGGSAPSKITPARAVGVVHVPMDRKGRTVAVGLAAPKQMRPEQDLPVTVSAPQLAGKMAHVTVSAVDVGILNITRFPVPDAGAHFFAQRRLGIDAYDIYSRVIESFDGGAGKLKFGGDMALQALPQAKRPTARVQTVDLFSGPVQLDAKGIARIRLKVPDFNGTLRVSALVYSDDQYGKRDVETVVRAPILAEASMPRVLAPGDRSTVTLDVQNFTGKPGQFNVKVESEGPLNLGEGSRSVQLNADAKTTLSFPLSAREGHSVAKVRVRVDGNGFKADRRYDLPVRAAWPQVLRSQVRTLDPLAAVSLDNSLTDGLMAESVNARLLVSPLPPIPFASALQGALNYPYGCAEQTTSKGYAALILDQATSSMLGADGLDAKTRRERMEGAFGRLASMQVANGNFSMWGDDGYVNPWLTPYITEFLLDAKDAGFAVPDNVLQKALNRLSEDLLSGGNQFYGQDDREKLKFANQAYSGYVLARVNRAPLGTLRTLYDNERSKAVGGLSLVHLGVALSLQGDAKRGQAALAAAFAKSSSERPSYFGDYGSAIRDDALMIALTHENKLAKPAWDARAVDLGRGLDARRNAGWMWLSTQEQVAIARLGKALAANQKALVAGELVIGGNTEAIGERKLFGRNFSANELASGVRFTPQGQPPMFASIDVAGIPRSAPAPDNSVLGVERSYYGTDGKPWSPRPLKEGEALIVRVTVTADTTMPDALLTDLLPAGLEIENFNLGDAKQWADVVVDGITISDRGEAADTKHEEFRDDRYVAALKLSRGSKANVFYLVRAVTPGTYSVPPPLVEDMYRPQLRGVGRSNPTTITVVQP

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Crispr_ID: LS483377_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_7

3560936-3561089

Orphan

Consensus_repeat	Method
GCTCTGGTGGGTGCCAACCGTTGGTTGGCACC	PILER-CR

2 spacers

The CRISPR arrays of LS483377_7

>merge|LS483377|7|3560936-3561089|PILER-CR
GGTCCGGTGGGTGCCAACCGTTGGTTGGCACCAATGCATCCGCCGGGCACAGCCCCGCGCTGCTCTGGTAGATGCCAACCTTGGTTGGCGCCCCGTGCCGACCAAGGTCGGCACCTGCCAAAGCGTTGGTGGGTGCCAACCGTTGGTTGGCATC

>LS483377|7|1|3560936-3561089|PILER-CR
GGTCCGGTGGGTGCCAACCGTTGGTTGGCACC	AATGCATCCGCCGGGCACAGCCCCGCGCT
GCTCTGGTAGATGCCAACCTTGGTTGGCGCCC	CGTGCCGACCAAGGTCGGCACCTGCCAAAGCGT
TGGTGGGTGCCAACCGTTGGTTGGCATC

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG11780.1\|3574498_3575776_-\|Citrate-synthase-(si)	unknown	unknown	gnl\|CDD\|180164
LS483377.1\|SQG11764.1\|3551022_3551952_-\|Uncharacterized-conserved-protein-(some-members-contain-a-von-Willebrand-factor-type-A-(vWA)-domain)	unknown	unknown	gnl\|CDD\|224635
LS483377.1\|SQG11769.1\|3556356_3557229_-\|type-4-fimbrial-biogenesis-protein-PilN	unknown	unknown	gnl\|CDD\|225707
LS483377.1\|SQG11776.1\|3568177_3569311_-\|CblD-family-pilus-biogenesis-initiator-protein	unknown	unknown	gnl\|CDD\|284778
LS483377.1\|SQG11763.1\|3550576_3551026_-\|transmembrane-protein	unknown	unknown	gnl\|CDD\|379552
LS483377.1\|SQG11762.1\|3549575_3550580_-\|BatA-(Bacteroides-aerotolerance-operon)	unknown	unknown	gnl\|CDD\|238744
LS483377.1\|SQG11781.1\|3576072_3576315_-\|50S-ribosomal-protein-L31	unknown	unknown	gnl\|CDD\|234969
LS483377.1\|SQG11765.1\|3551960_3552986_-\|ATPase	unknown	unknown	gnl\|CDD\|223786
LS483377.1\|SQG11778.1\|3572097_3572595_-\|alpha-fimbriae-major-subunit	unknown	unknown	gnl\|CDD\|367947
LS483377.1\|SQG11766.1\|3553184_3555152_-\|type-IV-pilus-secretin-PilQ	unknown	unknown	gnl\|CDD\|274173
LS483377.1\|SQG11774.1\|3562795_3567391_-\|YadA-domain-containing-protein	unknown	unknown	gnl\|CDD\|240612
LS483377.1\|SQG11771.1\|3558506_3560930_+\|multimodular-transpeptidase-transglycosylase	unknown	unknown	gnl\|CDD\|227342
LS483377.1\|SQG11770.1\|3557228_3558287_-\|type-4-fimbrial-biogenesis-protein-PilM	unknown	unknown	gnl\|CDD\|378558
LS483377.1\|SQG11768.1\|3555703_3556360_-\|type-IV-pilus-biogenesis-protein-PilO	unknown	unknown	gnl\|CDD\|225708
LS483377.1\|SQG11775.1\|3567452_3568160_-\|alpha-fimbriae-chaperone-protein	unknown	unknown	gnl\|CDD\|237939
LS483377.1\|SQG11773.1\|3561982_3562726_-\|transmembrane-protein	unknown	unknown	unknown
LS483377.1\|SQG11772.1\|3561161_3561806_+\|Predicted-nucleotidyltransferase	unknown	unknown	unknown
LS483377.1\|SQG11777.1\|3569307_3572037_-\|outer-membrane-usher	unknown	unknown	gnl\|CDD\|185210
LS483377.1\|SQG11779.1\|3573113_3574133_-\|transmembrane-protein	unknown	unknown	gnl\|CDD\|236090
LS483377.1\|SQG11767.1\|3555173_3555707_-\|type-IV-pilus-biogenesis-protein-PilP	unknown	unknown	gnl\|CDD\|377322

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG11764.1\|3551022_3551952_-\|Uncharacterized-conserved-protein-(some-members-contain-a-von-Willebrand-factor-type-A-(vWA)-domain)	gnl\|CDD\|224635	COG1721, COG1721, Uncharacterized conserved protein (some members contain a von Willebrand factor type A (vWA) domain) [General function prediction only].	1.6771e-23
LS483377.1\|SQG11769.1\|3556356_3557229_-\|type-4-fimbrial-biogenesis-protein-PilN	gnl\|CDD\|225707	COG3166, PilN, Tfp pilus assembly protein PilN [Cell motility and secretion / Intracellular trafficking and secretion].	5.05466e-50
LS483377.1\|SQG11776.1\|3568177_3569311_-\|CblD-family-pilus-biogenesis-initiator-protein	gnl\|CDD\|284778	pfam07434, CblD, CblD like pilus biogenesis initiator. This family consists of several minor pilin proteins including CblD from Burkholderia cepacia which is known to CblD be the initiator of pilus biogenesis. The family also contains a variety of Enterobacterial minor pilin proteins.	2.56544e-45
LS483377.1\|SQG11763.1\|3550576_3551026_-\|transmembrane-protein	gnl\|CDD\|379552	pfam14316, DUF4381, Domain of unknown function (DUF4381). This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 158 and 180 amino acids in length.	1.08203e-19
LS483377.1\|SQG11762.1\|3549575_3550580_-\|BatA-(Bacteroides-aerotolerance-operon)	gnl\|CDD\|238744	cd01467, vWA_BatA_type, VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.	3.45172e-76
LS483377.1\|SQG11781.1\|3576072_3576315_-\|50S-ribosomal-protein-L31	gnl\|CDD\|234969	PRK01678, rpmE2, type B 50S ribosomal protein L31.	3.97798e-51
LS483377.1\|SQG11765.1\|3551960_3552986_-\|ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	2.41494e-92
LS483377.1\|SQG11778.1\|3572097_3572595_-\|alpha-fimbriae-major-subunit	gnl\|CDD\|367947	pfam04449, Fimbrial_CS1, CS1 type fimbrial major subunit. Fimbriae, also known as pili, form filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometres. They enable the cell to colonise host epithelia. This family constitutes the major subunits of CS1 like pili, including CS2 and CFA1 from Escherichia coli, and also the Cable type II pilin major subunit from Burkholderia cepacia. The major subunit of CS1 pili is called CooA. Periplasmic CooA is mostly complexed with the assembly protein CooB. In addition, a small pool of CooA multimers, and CooA-CooD complexes exists, but the functional significance is unknown. A member of this family has also been identified in Salmonella typhi and Salmonella enterica.	4.65191e-26
LS483377.1\|SQG11766.1\|3553184_3555152_-\|type-IV-pilus-secretin-PilQ	gnl\|CDD\|274173	TIGR02515, Putative_DNA_transport_protein_HofQ, type IV pilus secretin (or competence protein) PilQ. A number of proteins homologous to PilQ are involved in type IV pilus formation, competence for transformation, type III secretion, and type II secretion (also called the main terminal branch of the general secretion pathway). Members of this family include PilQ itself, which is a component of the type IV pilus structure, from a number of species. In Haemophilus influenzae, the member of this family is associated with competence for transformation with exogenous DNA rather than with formation of a type IV pilus; the surface structure required for competence may be considered an unusual, incomplete type IV pilus structure. [Cell envelope, Surface structures].	0
LS483377.1\|SQG11774.1\|3562795_3567391_-\|YadA-domain-containing-protein	gnl\|CDD\|240612	cd12820, LbR_YadA-like, YadA-like, left-handed beta-roll. This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.	1.01122e-09
LS483377.1\|SQG11771.1\|3558506_3560930_+\|multimodular-transpeptidase-transglycosylase	gnl\|CDD\|227342	COG5009, MrcA, Membrane carboxypeptidase/penicillin-binding protein [Cell envelope biogenesis, outer membrane].	0
LS483377.1\|SQG11770.1\|3557228_3558287_-\|type-4-fimbrial-biogenesis-protein-PilM	gnl\|CDD\|378558	pfam11104, PilM_2, Type IV pilus assembly protein PilM;. The type IV pilus assembly protein PilM is required for competency and pilus biogenesis. It binds to PilN and ATP.	8.46083e-170
LS483377.1\|SQG11768.1\|3555703_3556360_-\|type-IV-pilus-biogenesis-protein-PilO	gnl\|CDD\|225708	COG3167, PilO, Tfp pilus assembly protein PilO [Cell motility and secretion / Intracellular trafficking and secretion].	2.37744e-74
LS483377.1\|SQG11775.1\|3567452_3568160_-\|alpha-fimbriae-chaperone-protein	gnl\|CDD\|237939	PRK15308, PRK15308, fimbrial protein TcfA.	1.95009e-46
LS483377.1\|SQG11780.1\|3574498_3575776_-\|Citrate-synthase-(si)	gnl\|CDD\|180164	PRK05614, gltA, citrate synthase.	0
LS483377.1\|SQG11777.1\|3569307_3572037_-\|outer-membrane-usher	gnl\|CDD\|185210	PRK15310, PRK15310, fimbrial outer membrane usher protein TcfC; Provisional.	5.16582e-180
LS483377.1\|SQG11779.1\|3573113_3574133_-\|transmembrane-protein	gnl\|CDD\|236090	PRK07764, PRK07764, DNA polymerase III subunits gamma and tau; Validated.	0.000333094
LS483377.1\|SQG11767.1\|3555173_3555707_-\|type-IV-pilus-biogenesis-protein-PilP	gnl\|CDD\|377322	pfam04351, PilP, Pilus assembly protein, PilP. The PilP family are periplasmic proteins involved in the biogenesis of type IV pili.	1.15922e-67

>LS483377.1|SQG11771.1|3558506_3560930_+|multimodular-transpeptidase-transglycosylase
MTRLRRWLRWIFLIVLVLALIGAAAVGGLYYAVSSKLPDVQTLRDVEMQEPMYVYAADGKLMAVFGETRRTPITMKDVPERLKQAFLATEDARFYEHGGVDYMGIGRAVWLLATTNDKRVPGGSTITQQVARQFFLSSEYSYTRKLAEILLARKIESELSKDEIFELYLNKSFFGNRAYGVAAAAEFYYGKKLNELDLDEMASLAGIPKFPSSGNPISNPERARQRRDNYVLQRMADLKFVSQAEADAAKAVPMHATAHEPPVQVDAPYVAELVRQEMIARFGGDVVNKGYHVTTTIDSTLQTAANQSVRDGLLLYDHRHGWHGVEKQVQVGAGEDAAALAEHLRGMYGQAGLLPAIVASTGADGSATVVLANRSEIVLPAGAAKWTNKTPGKLVQRGDIVRVRAGAKEGEWLLDQIPRGQSALVSLDAHNGALKALVGGFSFSGNKFNRATQARRQPGSSFKPFIYAAAFDKGYNPASIVLDAPVVFRDRRGKTWAPQNDGGGFRGPMRLREALVQSRNLVSVRLLDGMGVDYARKYISEFGFAESELPPNLSMSLGTASLTPLSVARGYAVFANGGSRVDTWLIDQVNDRDGNLVFKENPALACRDCAGSSDQPVNQVVDGFNFGAPAPKVDPAAATKAEAKTETPAAPANPDARTAPRAIDARTAYQLVSMMRDVVQRGTGVQAKVLGREDVGGKTGSTNDHRDAWFSGFGGPYVTTVWVGRDDFRSLGYREYGGKAALPIWIDYMRTALKDTPVAQNEPPSGMVQATLNGATEWVKVEDMDRLTDYDLNLNTPQADAAAFDIF
>LS483377.1|SQG11770.1|3557228_3558287_-|type-4-fimbrial-biogenesis-protein-PilM
MGLIPKSQSPLVGVDISSTAVKLLQLSRSGNRFRVEHYAVEPLPPNAVVEKNIVEVEAVGEAIRRAMNRSGSKAKLAAAAVAGSAVITKVIPMPAELDENDMEAQIELEAVNYIPYPIEEVNLDFEVIGAIPNNPEMVQVLLAASRSENVELRQSALELGGLQAKVMDVEAFAVENAYALVASELPVSIDGVVALVDIGATMTTLNVLRGGRSLYSREQVFGGKQLTDEIMRRYGLSYEEAGLAKRQGGLPESYEMEVLEPFKEATVQQISRLLQFFYAGSEFNRVDHIVLAGGCAVLGGLPEMVEEQLGVPTVVANPLAQMTLGPKVNAHALAQDAPALMIATGLALRSFD
>LS483377.1|SQG11769.1|3556356_3557229_-|type-4-fimbrial-biogenesis-protein-PilN
MARINLLPWRAERRKQRQREFYAMLGMAAISGLLLSLLIWFYYDRQVSGQMDRNAYLEAEIEKVKEQNKEIDRLDAQKDRLLARKKVIEELQAKRSQMVHLFDALVRTIPDGVVLTALQQEGDMLTLEGRTQSNARVSAYMRNLETSGWMTNPELSIIQASAGDKSAAGPVSDIKALPYMFKVTVKLPAQSEETGTAGLNADGSVAAAPAATPAVAPLAAGPDAAAPAAAPAPAPAQPAAAPAAAPASAPAPAPAKPNQPAAPAPAARPEGSRLAQPPQASYAPLQGDRA
>LS483377.1|SQG11768.1|3555703_3556360_-|type-IV-pilus-biogenesis-protein-PilO
MSQKIDLKNLDFNDIGNWPQKAKIVFCSLLALVIMFVAWMLLISGKRDELASLESKESDLRTEFSKQQERAVNLGPLKQQLAQMEQVLQQMLRQLPSKTEMPDLIIDISQTALSSGLTSQLFEPEQEQVKEFYAEKPIKLKMVGSYHQFGAFVSGVASLPRVVILTMHDINLKPADKAGGGSRAGALELSGTVKTYRYLDETEVQEQQKAEAGKEGSK
>LS483377.1|SQG11767.1|3555173_3555707_-|type-IV-pilus-biogenesis-protein-PilP
MIRSFFARCGMAAAVLLLAACGRGVTSTPGDAPNLEKWVEGERARPAQPLEPLPVMQQFETFEYSAQGLRDPFTDAWTNPQGNGGLRPDPNRRKEPLEGFPLDALDMVGTIGTGGGTVALVMGPDKVTYRVRPGGYLGQSDGRVTAVFEDRVELIELVPDGAGGWLERPATLSLEDQ
>LS483377.1|SQG11766.1|3553184_3555152_-|type-IV-pilus-secretin-PilQ
MTFHQAKGLRPNRRSTLNRVSALGVALMLACAPALAAAPAEKPVGTTVAPAAAPAGLSVAKIDFKRGDDGAGRLIVQFDGQGAIPDLRTQGNSVVVDVGNARLPANLQKPLNVVDFATPVQRIDAKPSGTGTQLVLSTGGAVESLAYQSGNEYVVEISARQAPAAVGAVTAGSVTQAAKAVGQRGFTGKPVTFNFQDVPVRTVLQLIAEESNLNVVASDSVQGNVTLRLVNVPWDQALDIVLRAKGLDKRRDGSVIWVGPQAELAKFEQEKEDARIAIENREDLVTDYVQINYHSATQIFKALTEAKGIGGGGGGGAGGGGGGSSQEESGFLSGRGRIVADERTNTLMISDIPKKIARMRELINVIDRPVDQVLIESRIVIATDTFARELGARFGISGSRDNAYFSGNLEANEATRKSQVEANATNAKAYRDWLAGGSTGPAPVPVGSAITRGLNWAMPAASTNPAGSLALSILNAGYLLDVELSAMQEESRGEVISNPRVVTTNQREALIKQGKEIGYVTISAGAGGVATPNVQFKEVVLELKVTPTITNDNRVFLNMQVKKDEVDRLIQLEGYGTVPSINRREVNTAVLVEDGQTVVIGGVYEFTDRNSISKVPFLGDVPFLGNLFKKRGRSKDKAELLVFVTPKVLRVARQN
>LS483377.1|SQG11765.1|3551960_3552986_-|ATPase
MNLPPPMPETVSPPPAPAASRLHGAFNQLRDALSAEIVGQAALVERLLIALLADGHLLVEGAPGLAKTTAIRALASRLEADFARVQFTPDLLPADLTGTEIWRPQEGRFEFVPGPIFHPILLADEINRAPAKVQSALLEAMGERQVTVGRHTYALPPLFLVMATQNPIEQEGTFPLPEAQLDRFLMHVRIGYPDQAAESEILRLARERARGALGEAAPAPAKLPMQDVFDARREVLDLHMAPALERYLVELVLASRDPSRYDAGLGRRIAWGASPRGSIALERCARARAWLAGRDFVTPDDVRAVAADVLRHRVLPSYEATAEGWDGERLVQELLARVPAP
>LS483377.1|SQG11764.1|3551022_3551952_-|Uncharacterized-conserved-protein-(some-members-contain-a-von-Willebrand-factor-type-A-(vWA)-domain)
MTDPSLEAASTVSDGDGLRPHLSELVALRRLAQRPPPPRRGRAGNAGQAPSPLRGRGMEYAESREYVAGDDARHIDWRVTARTGRAHTKLFQAERERVSLIVADTSPALYFGTRVRFKSVQAARAGAVAAWSAQRRGDRVGALRGSDREAPIAPAGGPRGVLRVLDALTRWYTQPPADDLGLERALDHAARVLRPGARMLVLADPQQAARIPVVRWSALAQHHDLSLVLLVDPLELQPPSAALQFQTAQQRIGLDLRRSEVQAHWQAHFVEPLQALRRQLGARRVDVQVLSTDAPSDAWLAPPVTEVPA
>LS483377.1|SQG11763.1|3550576_3551026_-|transmembrane-protein
MSANLPLRDVQLPPAPSWWPPAPGYLMVGGAVLLVILALALLWWQRRRRRQRWLQAFDQELATTADATAELAAIAGLLRRAARQAQPGSESLRDDAWWQRVDPKGTLPDARRSLLAEGAYRPSVDASEVAAVRSWARERYLAMLLERRR
>LS483377.1|SQG11762.1|3549575_3550580_-|BatA-(Bacteroides-aerotolerance-operon)
MNLLASYWPWPDLQLAWPLALLALPLPLLMRWWKRRADPGAALRVPYAATELEALAGGGRVDVSWLRTLLLWLGWCALCVALARPQQLGEAITPPQQGRQMMLAMDVSGSMGEGDMVLGGQAVDRLTAAKAVLADFLDRRAGDRIGLLIFGDRAYTLTPLTADLASVRDQLRDSVVGLAGRETAIGDAIGLAVKRLRSQPEGQRVLILLTDGVSNAGVLEPLRAAEVAQAEGVRIHTVAFGGDGSMRFLGIPISADQDPVDEATLKKIASLTGGQFFRARDTAQLAGIYAELDRLEPIAAKGPSLRPREERYAWPLGLALLLGALAWVWPERRR
>LS483377.1|SQG11772.1|3561161_3561806_+|Predicted-nucleotidyltransferase
MHRARQHAASQTRERRHRLAHEAARLMAEGGIRDYHQAKLKAASRLGIHDDASLPRNTEIEDALREYQRLFSGPQHGNELQRRREAAMRALEFLHGFAPRLAGPVLEGTADANSPVQLHLHSDDPEAVHRFLDEHGIPAESRTRRLRMDRERSLDVPVWVFSAEELTFDLAVLPYDALRQAPLSPVDEKPMRRASVTQLRQLLAEAEITAYIGG
>LS483377.1|SQG11773.1|3561982_3562726_-|transmembrane-protein
MYRWVSGIVSYRTFYIWRARYRYYTRNLDMWTLMSGLCIAGLLLVLWYLWQMLGVPPPRVHPQAAALRIDGVTREAIHRIVLVRHAGSTPGAPFTTPEEVRASTLRTMRVRQVMDSEVVWRLKADMLADIADYITATGGCFPYNCRRVLDRLDYVRQAGVENAQINAALSTVLEVPLDQMPPLEADEHERVKSGWSDGFDDIYYQSWLLRDLQVMHAQMMREYPQRAPAPWLPRLFSDPLRDTRFVW
>LS483377.1|SQG11774.1|3562795_3567391_-|YadA-domain-containing-protein
MNHVYRRIWSAAKRCWVVGSELTKRGPAARRSVSVAMSAAMLALSANAMAIEGAEKENPGEETETIWNEQEDSRYSGMPMDLFAMTGGLNAGLSLTSIAPQSTHYQLAIVNDVAYRDSTATGDDTVVVGSRSTISGKRSVGYGNGIRSTGERNVAIGTNVKIEHWYATAVGDGAYAGGGWGATAYGNDSRADGGNAIAIGSGSRVATGGGIGGIALGGDARAGTSGYSGAIAVGNKSNASYDAMAIGYESSASASGAVALGRGSVASEANSVSVGNSSTKRRVVNVADARLNSTSSDAVTGKQLNATNSNVTAARSVADSAKTNADSALAKANTLSGLLSQTSASGNVRIGASNSGTVLDVRNSASANRKVTGVADGTLSTTSTDAVSGKQLNATNSNVTAARSVADSAKTSADSALAKANTLSGLLSQTSASGNVRIGASNSGTVLDVRNSASANRKITGVADATLSTASTDAVSGKQLNSTNSNVAAARAVADSAKTNADSALAKANTLSGLLSETSASGNVRLGVSNSGTVLDVRNSAGANRRITGVADATLSSTSTEAVTGRQLNTTNSNVSTAMSDASSAKTTANTALTQVGTLNGLLSQVSASGNVRVGEKNSGTVVDVRNSANASRKLTGVADGVVSASSYEAVNGRQLNATNDKVTTVEGVARSAGADAAVAKTDAARALVETAALGGLVAQVSASGDVRLGEKNSGTTLDVRNSANANRKITGVADGILSASSADAVSGRQLYSSNARIAALEDTTQFLSIGTAPVSERAEAGPVGVAVGNSAKTGNDGGTAVGTHAKALGRNSVAIGRASVVHEDSDSGFALGAGAEVGIAGSGARGGVAIGAGAKVGKGADGSLAIGEGSQANEAGVASFGSATTYRRLVNIARGTADHNATTVSQLKDSLATLGGGAGMVANGTIIAPTYAVQGGTQSTVEDALMALDGAVITAGRRAEKVEGQLSSIFQDSPSIRAGGMNQIALNGVNGMVLTNLADGRVAPGSRDAVTGSQLYAAEQKISQNRNDLEAMRKEREMGEQAMRGLDASVIDYGGARLTGVAEAKLSADSSDVVRGSQLYETNSRVSELEDVAHFVSIGSAPFSERAEAGVAGVAVGNSAKTGLEGGTAVGTFAGAMGKNSTAIGRAATVSVDSANGFAMGVGAQVGGDAGGANEGVAIGAGARVGSGAHGSLALGNGSQADEEGVASFGGVGIKRRLVNIANGTANHNAATVGQLRGALSALGGEVDANGNIVGPSFNVQGQSQSTLNGALEALDGAVVSTTSRVNQVESQLRSVFQENPSVRADGIHQLTLAGANGMVISNVANGLIAAGSRDAVNGGQLHSMQQQLNGRMDGLEQRIDDQPQARAMAAASTPSPSTEEIAPTPETSGSPQIASTGEGDKPTPQPKSKQDDTPKPQVDTADLEKMLARANEYTDGAISNFERRLDKMDKRFNRMAAMSSAQSAMAMNTAGLATYNRLGAGVGYSEGESAMAVGYQRVLNEKGSATFSLNGAFTNSGERSMGVGVGIGW
>LS483377.1|SQG11775.1|3567452_3568160_-|alpha-fimbriae-chaperone-protein
MKKLLFCLLPLSALLAPPAHANLSIHPMRAAVDGKRGTQIRVYSHSTRPQYVQARLLRISNPAQVGEEEVEMEAADAAVAITPGKFALSGGGNRLIRVIPLRTVEKEAAYRVYFEGVRGPDGTLLEDDEQAAQANVGVSLVWGALVNVLPTNGSVDLQLQGDTLRNVGTLRVGITGLAECSASGACTTHDFAKSLYPDAELKLPFLPQPGNTVQLHYRLSKDGYREHTTTLAPSA
>LS483377.1|SQG11776.1|3568177_3569311_-|CblD-family-pilus-biogenesis-initiator-protein
MSRRWMCVLMLVCALVLVMPRAWAQWPPETHPTDQSRDIVMTWDRSAVPGDVELWAPRTVLGFSHDLAFKYGQIHVVCGSASVSEFGRCAVDGEPGQSLGISNVALLFVEQRTGLRTELRAEGYLQRIMSDWICASDYWDTARRHLNASFWFECGSGQPAGTGANLGLPSAALSRLVAGHWKATMRLNIKADPAAAPVATATFNFDFTVTDYDAISIYFPGFDGISPLVNMDLRYDPIRKMVGGRKEVDMCLYDGVGSQSEFLGVTVRDSGPRPPPGRDYAVWHGDGGSDDTQRLDYQVGLKYGGNLLAMKHGEEQLLRGIDSAQLRLVMLPGISQPVYCVPTPLTLETPPTPIASKRPGLYDGELTVELRVPTAKP
>LS483377.1|SQG11777.1|3569307_3572037_-|outer-membrane-usher
MIPHAPAVTRLAVALALAMAAPLVAAHGVPAGFEDLIEGQTEQLDIQLFGRSAGLSPVRVTLEHVQLEDPARVLQALDLPAEAQAALLPTLSQPLPRNSHLACRFGGATAGCGYLDPPEDPTAARALYDEGEGAVRLFVARQWIPGEPAAERYHTVTANAENAFLHQQTLNVSGGRDYQALSARGMGTLGLFDRGHLSADWYYTQQRYRSRGSNDDFQFDNVYYRHDLGQAHYLQAGRMDRLNLSSPQGGTFSFSMLPLDRFRGARVGTTQAYVDTDAAVQATPLTVLLARDARVDVFDGERLLQTFYLQAGINQIDTRNFPFGNYLVRMRIYEDGVLVRTEEAPFDKGGDWTNSQWQWFVQGGRRNERRSDRFDGERVAMAGLRVPLGRDAALTAGVANLGGHSYGELRVDLRRVLATHEMRATLSGMRGSDGSNGQQHQLSYRRKASWNLYQQRMRGKACQFEADARDQLGCTNSLSGSMSLPLAGGNAYVGYTRRQTWRTGWHRPEFDQDPLFGLDPLLPPGPLEPRREPVLSRTWQASFSRSHRWQDFSVSTRVGLWQQRSADSVRGSNERDRGIYFNLSLTRLQRNHDSSGQRRYAVDVRQPQHQRPTIDYSVGQSLRQDRDTHYREFNAELRANNNDRYSASLSGQLQNGIGNTTASIAHYEQRGRGETGYSGSHSSGFALGRRGVYWSGAHGAEAGLAVQVDGSDDVDLRGVAAELQVGGLRRQRLQIGERRLLPLSSYQSHRAEVQDASTLDSIAAIRVTGVGGARPMFLTPGKLMRMPVPIEVTYTFIGNAKDLAGSPLGGARILNAPVPGTSANGSFVADFPRRETTLYLLQDDRLLHCPLQVRERRQVVLLVGAVHCEPLAVAQLPPEIRQQVRVTRLLQERALIAATPQTAAAGGTP
>LS483377.1|SQG11778.1|3572097_3572595_-|alpha-fimbriae-major-subunit
MHAILKKAALAAALATASLSAHALETKITVYADVDPTLALLLEDGTPLPDTVQMTHDPLRGLLPSTQQVRIHSNDIDKDIEVRLGHDPVLLNGSTRVPLAVSLNTDALTTAVTEFKAADLFNGASSTPGASISMPLTIAQAGAGGPLTVNGRYEGMVYIVMNQKP
>LS483377.1|SQG11779.1|3573113_3574133_-|transmembrane-protein
MSTRFDPPERGPLGPDVAAVVTAPIVAPPSESAVSWGAIFAGATAAAALSLILLILGVGLGLSSVSPWSFEGVSKETFGWSSIIWLTFTALAASGLGGYLAGRLRTKWTQIHGDETYFRDTAHGFVSWAVATLLTAGLLTSAIGGVLGAGAKVAGAAAGAAASTASVAAAGAGSTAAAAPEGDLNYWVDSLFRSTTSAGPTAPAAPPPGAPMDPNAAPPPRPMPGNGPMGDRREVRAEVNRIIVNSLQGDGLDPDDTQYLAQLIARETGMSPAEAQARVTDVQTRMRAALEKARKTAKQAADDARKATAYAALWLFITLLIGAFFASLSATWGGRRRDL
>LS483377.1|SQG11780.1|3574498_3575776_-|Citrate-synthase-(si)
MSDLDQVTLNAGDKSVVLPVIKPTLGNDCVDIAKLTKETGFFTYDSGFTATASCKSAITYIDGDKGVLLYRGYPIEQLSEKSSYVEVAYLLINGERPSAEQLKAFTDELTAEANVDESINTLIGSFAKDAHPMAILAAAIAQLSAIYHDSLDLSDAEQRRQAAVRLIAKVPTLSALIYRHGKGLPANKPDTSLDYVSRFLKQTFESADGQYDLNPDVVKALDLLFILHADHEQNASTSTVRLVGSTGANPYASVAAGVTALWGPAHGGANEAVLKMLEEIGSADNVESAVVKAKDKTSGFRLMGFGHRVYKNFDPRAKVIGEMTSKVLKQLGVQDPLLDVAVKLEQAALQDEYFVARKLYPNVDFYSGIIYKALQIPTEMFTVMFALGRTSGWVSHWLEQQVDPEMKIGRPRQVYTGSDVRDYQG
>LS483377.1|SQG11781.1|3576072_3576315_-|50S-ribosomal-protein-L31
MKADIHPNYRDVVFHDVTSDFKILTRSTMATKETIQWEDGNEYPLVKVEISSASHPFYTGKHKVIDTSGRIDKFQKRYAR

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Crispr_ID: LS483377_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_8

3574247-3574359

Orphan

Consensus_repeat	Method
GCGTGCCAACCAAGGTTGGCACCTACCGAAGGCGGGTGCGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483377_8

>merge|LS483377|8|3574247-3574359|CRISPRCasFinder
GCGTGCCAACCAAGGTTGGCACCTACCGAAGGCGGGTGCGGCGGTAGATCCACGCCGTGCGTGGATGGGAAAGCGTGCCAACCAAGGTTGGCACCTACCGAAGGCGGTTGCGG

>LS483377|8|7|3574247-3574359|CRISPRCasFinder
GCGTGCCAACCAAGGTTGGCACCTACCGAAGGCGGGTGCGG	CGGTAGATCCACGCCGTGCGTGGATGGGAAA
GCGTGCCAACCAAGGTTGGCACCTACCGAAGGCGGTTGCGG

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG11786.1\|3582648_3582948_-\|DNA-directed-RNA-polymerase-subunit-omega	unknown	unknown	gnl\|CDD\|234744
LS483377.1\|SQG11784.1\|3579845_3580232_-\|endoribonuclease-L-PSP	unknown	unknown	gnl\|CDD\|129116
LS483377.1\|SQG11787.1\|3583058_3583724_-\|guanylate-kinase	unknown	unknown	gnl\|CDD\|234719
LS483377.1\|SQG11774.1\|3562795_3567391_-\|YadA-domain-containing-protein	unknown	unknown	gnl\|CDD\|240612
LS483377.1\|SQG11778.1\|3572097_3572595_-\|alpha-fimbriae-major-subunit	unknown	unknown	gnl\|CDD\|367947
LS483377.1\|SQG11785.1\|3580380_3582543_-\|GTP-pyrophosphokinase	unknown	unknown	gnl\|CDD\|223394
LS483377.1\|SQG11789.1\|3588008_3588656_+\|formate-dehydrogenase-O-subunit-gamma	unknown	unknown	gnl\|CDD\|225419
LS483377.1\|SQG11776.1\|3568177_3569311_-\|CblD-family-pilus-biogenesis-initiator-protein	unknown	unknown	gnl\|CDD\|284778
LS483377.1\|SQG11788.1\|3587094_3588012_+\|formate-dehydrogenase-O-subunit-beta	unknown	unknown	gnl\|CDD\|273705
LS483377.1\|SQG11781.1\|3576072_3576315_-\|50S-ribosomal-protein-L31	unknown	unknown	gnl\|CDD\|234969
LS483377.1\|SQG11783.1\|3577726_3579838_-\|ATP-dependent-DNA-helicase-RecG	unknown	unknown	gnl\|CDD\|236794
LS483377.1\|SQG11779.1\|3573113_3574133_-\|transmembrane-protein	unknown	unknown	gnl\|CDD\|236090
LS483377.1\|SQG11771.1\|3558506_3560930_+\|multimodular-transpeptidase-transglycosylase	unknown	unknown	gnl\|CDD\|227342
LS483377.1\|SQG11770.1\|3557228_3558287_-\|type-4-fimbrial-biogenesis-protein-PilM	unknown	unknown	gnl\|CDD\|378558
LS483377.1\|SQG11782.1\|3576403_3577342_-\|inosine-uridine-preferring-nucleoside-hydrolase	unknown	unknown	gnl\|CDD\|239115
LS483377.1\|SQG11775.1\|3567452_3568160_-\|alpha-fimbriae-chaperone-protein	unknown	unknown	gnl\|CDD\|237939
LS483377.1\|SQG11773.1\|3561982_3562726_-\|transmembrane-protein	unknown	unknown	unknown
LS483377.1\|SQG11772.1\|3561161_3561806_+\|Predicted-nucleotidyltransferase	unknown	unknown	unknown
LS483377.1\|SQG11777.1\|3569307_3572037_-\|outer-membrane-usher	unknown	unknown	gnl\|CDD\|185210
LS483377.1\|SQG11780.1\|3574498_3575776_-\|Citrate-synthase-(si)	unknown	unknown	gnl\|CDD\|180164

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG11786.1\|3582648_3582948_-\|DNA-directed-RNA-polymerase-subunit-omega	gnl\|CDD\|234744	PRK00392, rpoZ, DNA-directed RNA polymerase subunit omega; Reviewed.	1.39874e-21
LS483377.1\|SQG11784.1\|3579845_3580232_-\|endoribonuclease-L-PSP	gnl\|CDD\|129116	TIGR00004, RutC_family_protein, reactive intermediate/imine deaminase. This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other].	1.07399e-58
LS483377.1\|SQG11787.1\|3583058_3583724_-\|guanylate-kinase	gnl\|CDD\|234719	PRK00300, gmk, guanylate kinase; Provisional.	5.54639e-121
LS483377.1\|SQG11774.1\|3562795_3567391_-\|YadA-domain-containing-protein	gnl\|CDD\|240612	cd12820, LbR_YadA-like, YadA-like, left-handed beta-roll. This group contains the collagen-binding domain virulence factor YadA an adhesion proteins of several Yersinia species, and related cell surface proteins, including Moraxella catarrhalis UspA-like proteins. The collagen-binding portion is found in the hydrophobic N-terminal region. YadA forms a matrix on the bacterial outer membrane, which mediates binding to collagen and epithelial cells. YadA inhibits the complement-activating pathway with the coating of the cell surface with factor H, which impedes C3b molecules. These domains form a left handed beta roll made up of a series of short repeated elements. UspA1 and UspA2 are part of a class of pathogenicity factors that act as cell surface adhesion molecules, in which N-terminal head and neck domains extend from the bacterial outer membrane. The UspA1 head domain of Moraxella catarrhalis, is formed from trimeric left-handed parallel beta-helices of 14-16 amino acid repeats. The UspA1 head domain connects to a neck region of large extended, charged loops that maybe be ligand binding, which is in turn connected to an extended coiled coil domain that tethers the head and neck region to the cell surface via a transmembrane region.	1.01122e-09
LS483377.1\|SQG11778.1\|3572097_3572595_-\|alpha-fimbriae-major-subunit	gnl\|CDD\|367947	pfam04449, Fimbrial_CS1, CS1 type fimbrial major subunit. Fimbriae, also known as pili, form filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometres. They enable the cell to colonise host epithelia. This family constitutes the major subunits of CS1 like pili, including CS2 and CFA1 from Escherichia coli, and also the Cable type II pilin major subunit from Burkholderia cepacia. The major subunit of CS1 pili is called CooA. Periplasmic CooA is mostly complexed with the assembly protein CooB. In addition, a small pool of CooA multimers, and CooA-CooD complexes exists, but the functional significance is unknown. A member of this family has also been identified in Salmonella typhi and Salmonella enterica.	4.65191e-26
LS483377.1\|SQG11785.1\|3580380_3582543_-\|GTP-pyrophosphokinase	gnl\|CDD\|223394	COG0317, SpoT, Guanosine polyphosphate pyrophosphohydrolases/synthetases [Signal transduction mechanisms / Transcription].	0
LS483377.1\|SQG11789.1\|3588008_3588656_+\|formate-dehydrogenase-O-subunit-gamma	gnl\|CDD\|225419	COG2864, FdnI, Cytochrome b subunit of formate dehydrogenase [Energy production and conversion].	2.88434e-72
LS483377.1\|SQG11776.1\|3568177_3569311_-\|CblD-family-pilus-biogenesis-initiator-protein	gnl\|CDD\|284778	pfam07434, CblD, CblD like pilus biogenesis initiator. This family consists of several minor pilin proteins including CblD from Burkholderia cepacia which is known to CblD be the initiator of pilus biogenesis. The family also contains a variety of Enterobacterial minor pilin proteins.	2.56544e-45
LS483377.1\|SQG11788.1\|3587094_3588012_+\|formate-dehydrogenase-O-subunit-beta	gnl\|CDD\|273705	TIGR01582, Formate_dehydrogenase_iron-sulfur_subunit, formate dehydrogenase, beta subunit, Fe-S containing. This model represents the beta subunit of the gamma-proteobacterial formate dehydrogenase. This subunit contains four 4Fe-4S clusters and is involved in transmitting electrons from the alpha subunit (TIGR01553) at the periplasmic space to the gamma subunit which spans the cytoplasmic membrane. In addition to the gamma proteobacteria, a sequence from Aquifex aolicus falls within the scope of this model. This appears to be the case for the alpha, gamma and epsilon (accessory protein TIGR01562) chains as well. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport].	7.07461e-156
LS483377.1\|SQG11783.1\|3577726_3579838_-\|ATP-dependent-DNA-helicase-RecG	gnl\|CDD\|236794	PRK10917, PRK10917, ATP-dependent DNA helicase RecG; Provisional.	0
LS483377.1\|SQG11779.1\|3573113_3574133_-\|transmembrane-protein	gnl\|CDD\|236090	PRK07764, PRK07764, DNA polymerase III subunits gamma and tau; Validated.	0.000333094
LS483377.1\|SQG11771.1\|3558506_3560930_+\|multimodular-transpeptidase-transglycosylase	gnl\|CDD\|227342	COG5009, MrcA, Membrane carboxypeptidase/penicillin-binding protein [Cell envelope biogenesis, outer membrane].	0
LS483377.1\|SQG11770.1\|3557228_3558287_-\|type-4-fimbrial-biogenesis-protein-PilM	gnl\|CDD\|378558	pfam11104, PilM_2, Type IV pilus assembly protein PilM;. The type IV pilus assembly protein PilM is required for competency and pilus biogenesis. It binds to PilN and ATP.	8.46083e-170
LS483377.1\|SQG11782.1\|3576403_3577342_-\|inosine-uridine-preferring-nucleoside-hydrolase	gnl\|CDD\|239115	cd02649, nuc_hydro_CeIAG, nuc_hydro_CeIAG: Nucleoside hydrolases similar to the inosine-adenosine-guanosine-preferring nucleoside hydrolase from Caenorhabditis elegans. Nucleoside hydrolases cleave the N-glycosidic bond in nucleosides generating ribose and the respective base. These enzymes vary in their substrate specificity. This group contains eukaryotic, bacterial and archeal proteins similar to the purine-preferring nucleoside hydrolase (IAG-NH) from C. elegans and the salivary purine nucleosidase from Aedes aegypti. C. elegans IAG-NH exhibits a high affinity for the substrate analogue p-nitrophenylriboside (p-NPR). .	1.64895e-119
LS483377.1\|SQG11775.1\|3567452_3568160_-\|alpha-fimbriae-chaperone-protein	gnl\|CDD\|237939	PRK15308, PRK15308, fimbrial protein TcfA.	1.95009e-46
LS483377.1\|SQG11781.1\|3576072_3576315_-\|50S-ribosomal-protein-L31	gnl\|CDD\|234969	PRK01678, rpmE2, type B 50S ribosomal protein L31.	3.97798e-51
LS483377.1\|SQG11777.1\|3569307_3572037_-\|outer-membrane-usher	gnl\|CDD\|185210	PRK15310, PRK15310, fimbrial outer membrane usher protein TcfC; Provisional.	5.16582e-180
LS483377.1\|SQG11780.1\|3574498_3575776_-\|Citrate-synthase-(si)	gnl\|CDD\|180164	PRK05614, gltA, citrate synthase.	0

>LS483377.1|SQG11779.1|3573113_3574133_-|transmembrane-protein
MSTRFDPPERGPLGPDVAAVVTAPIVAPPSESAVSWGAIFAGATAAAALSLILLILGVGLGLSSVSPWSFEGVSKETFGWSSIIWLTFTALAASGLGGYLAGRLRTKWTQIHGDETYFRDTAHGFVSWAVATLLTAGLLTSAIGGVLGAGAKVAGAAAGAAASTASVAAAGAGSTAAAAPEGDLNYWVDSLFRSTTSAGPTAPAAPPPGAPMDPNAAPPPRPMPGNGPMGDRREVRAEVNRIIVNSLQGDGLDPDDTQYLAQLIARETGMSPAEAQARVTDVQTRMRAALEKARKTAKQAADDARKATAYAALWLFITLLIGAFFASLSATWGGRRRDL
>LS483377.1|SQG11778.1|3572097_3572595_-|alpha-fimbriae-major-subunit
MHAILKKAALAAALATASLSAHALETKITVYADVDPTLALLLEDGTPLPDTVQMTHDPLRGLLPSTQQVRIHSNDIDKDIEVRLGHDPVLLNGSTRVPLAVSLNTDALTTAVTEFKAADLFNGASSTPGASISMPLTIAQAGAGGPLTVNGRYEGMVYIVMNQKP
>LS483377.1|SQG11777.1|3569307_3572037_-|outer-membrane-usher
MIPHAPAVTRLAVALALAMAAPLVAAHGVPAGFEDLIEGQTEQLDIQLFGRSAGLSPVRVTLEHVQLEDPARVLQALDLPAEAQAALLPTLSQPLPRNSHLACRFGGATAGCGYLDPPEDPTAARALYDEGEGAVRLFVARQWIPGEPAAERYHTVTANAENAFLHQQTLNVSGGRDYQALSARGMGTLGLFDRGHLSADWYYTQQRYRSRGSNDDFQFDNVYYRHDLGQAHYLQAGRMDRLNLSSPQGGTFSFSMLPLDRFRGARVGTTQAYVDTDAAVQATPLTVLLARDARVDVFDGERLLQTFYLQAGINQIDTRNFPFGNYLVRMRIYEDGVLVRTEEAPFDKGGDWTNSQWQWFVQGGRRNERRSDRFDGERVAMAGLRVPLGRDAALTAGVANLGGHSYGELRVDLRRVLATHEMRATLSGMRGSDGSNGQQHQLSYRRKASWNLYQQRMRGKACQFEADARDQLGCTNSLSGSMSLPLAGGNAYVGYTRRQTWRTGWHRPEFDQDPLFGLDPLLPPGPLEPRREPVLSRTWQASFSRSHRWQDFSVSTRVGLWQQRSADSVRGSNERDRGIYFNLSLTRLQRNHDSSGQRRYAVDVRQPQHQRPTIDYSVGQSLRQDRDTHYREFNAELRANNNDRYSASLSGQLQNGIGNTTASIAHYEQRGRGETGYSGSHSSGFALGRRGVYWSGAHGAEAGLAVQVDGSDDVDLRGVAAELQVGGLRRQRLQIGERRLLPLSSYQSHRAEVQDASTLDSIAAIRVTGVGGARPMFLTPGKLMRMPVPIEVTYTFIGNAKDLAGSPLGGARILNAPVPGTSANGSFVADFPRRETTLYLLQDDRLLHCPLQVRERRQVVLLVGAVHCEPLAVAQLPPEIRQQVRVTRLLQERALIAATPQTAAAGGTP
>LS483377.1|SQG11776.1|3568177_3569311_-|CblD-family-pilus-biogenesis-initiator-protein
MSRRWMCVLMLVCALVLVMPRAWAQWPPETHPTDQSRDIVMTWDRSAVPGDVELWAPRTVLGFSHDLAFKYGQIHVVCGSASVSEFGRCAVDGEPGQSLGISNVALLFVEQRTGLRTELRAEGYLQRIMSDWICASDYWDTARRHLNASFWFECGSGQPAGTGANLGLPSAALSRLVAGHWKATMRLNIKADPAAAPVATATFNFDFTVTDYDAISIYFPGFDGISPLVNMDLRYDPIRKMVGGRKEVDMCLYDGVGSQSEFLGVTVRDSGPRPPPGRDYAVWHGDGGSDDTQRLDYQVGLKYGGNLLAMKHGEEQLLRGIDSAQLRLVMLPGISQPVYCVPTPLTLETPPTPIASKRPGLYDGELTVELRVPTAKP
>LS483377.1|SQG11775.1|3567452_3568160_-|alpha-fimbriae-chaperone-protein
MKKLLFCLLPLSALLAPPAHANLSIHPMRAAVDGKRGTQIRVYSHSTRPQYVQARLLRISNPAQVGEEEVEMEAADAAVAITPGKFALSGGGNRLIRVIPLRTVEKEAAYRVYFEGVRGPDGTLLEDDEQAAQANVGVSLVWGALVNVLPTNGSVDLQLQGDTLRNVGTLRVGITGLAECSASGACTTHDFAKSLYPDAELKLPFLPQPGNTVQLHYRLSKDGYREHTTTLAPSA
>LS483377.1|SQG11774.1|3562795_3567391_-|YadA-domain-containing-protein
MNHVYRRIWSAAKRCWVVGSELTKRGPAARRSVSVAMSAAMLALSANAMAIEGAEKENPGEETETIWNEQEDSRYSGMPMDLFAMTGGLNAGLSLTSIAPQSTHYQLAIVNDVAYRDSTATGDDTVVVGSRSTISGKRSVGYGNGIRSTGERNVAIGTNVKIEHWYATAVGDGAYAGGGWGATAYGNDSRADGGNAIAIGSGSRVATGGGIGGIALGGDARAGTSGYSGAIAVGNKSNASYDAMAIGYESSASASGAVALGRGSVASEANSVSVGNSSTKRRVVNVADARLNSTSSDAVTGKQLNATNSNVTAARSVADSAKTNADSALAKANTLSGLLSQTSASGNVRIGASNSGTVLDVRNSASANRKVTGVADGTLSTTSTDAVSGKQLNATNSNVTAARSVADSAKTSADSALAKANTLSGLLSQTSASGNVRIGASNSGTVLDVRNSASANRKITGVADATLSTASTDAVSGKQLNSTNSNVAAARAVADSAKTNADSALAKANTLSGLLSETSASGNVRLGVSNSGTVLDVRNSAGANRRITGVADATLSSTSTEAVTGRQLNTTNSNVSTAMSDASSAKTTANTALTQVGTLNGLLSQVSASGNVRVGEKNSGTVVDVRNSANASRKLTGVADGVVSASSYEAVNGRQLNATNDKVTTVEGVARSAGADAAVAKTDAARALVETAALGGLVAQVSASGDVRLGEKNSGTTLDVRNSANANRKITGVADGILSASSADAVSGRQLYSSNARIAALEDTTQFLSIGTAPVSERAEAGPVGVAVGNSAKTGNDGGTAVGTHAKALGRNSVAIGRASVVHEDSDSGFALGAGAEVGIAGSGARGGVAIGAGAKVGKGADGSLAIGEGSQANEAGVASFGSATTYRRLVNIARGTADHNATTVSQLKDSLATLGGGAGMVANGTIIAPTYAVQGGTQSTVEDALMALDGAVITAGRRAEKVEGQLSSIFQDSPSIRAGGMNQIALNGVNGMVLTNLADGRVAPGSRDAVTGSQLYAAEQKISQNRNDLEAMRKEREMGEQAMRGLDASVIDYGGARLTGVAEAKLSADSSDVVRGSQLYETNSRVSELEDVAHFVSIGSAPFSERAEAGVAGVAVGNSAKTGLEGGTAVGTFAGAMGKNSTAIGRAATVSVDSANGFAMGVGAQVGGDAGGANEGVAIGAGARVGSGAHGSLALGNGSQADEEGVASFGGVGIKRRLVNIANGTANHNAATVGQLRGALSALGGEVDANGNIVGPSFNVQGQSQSTLNGALEALDGAVVSTTSRVNQVESQLRSVFQENPSVRADGIHQLTLAGANGMVISNVANGLIAAGSRDAVNGGQLHSMQQQLNGRMDGLEQRIDDQPQARAMAAASTPSPSTEEIAPTPETSGSPQIASTGEGDKPTPQPKSKQDDTPKPQVDTADLEKMLARANEYTDGAISNFERRLDKMDKRFNRMAAMSSAQSAMAMNTAGLATYNRLGAGVGYSEGESAMAVGYQRVLNEKGSATFSLNGAFTNSGERSMGVGVGIGW
>LS483377.1|SQG11773.1|3561982_3562726_-|transmembrane-protein
MYRWVSGIVSYRTFYIWRARYRYYTRNLDMWTLMSGLCIAGLLLVLWYLWQMLGVPPPRVHPQAAALRIDGVTREAIHRIVLVRHAGSTPGAPFTTPEEVRASTLRTMRVRQVMDSEVVWRLKADMLADIADYITATGGCFPYNCRRVLDRLDYVRQAGVENAQINAALSTVLEVPLDQMPPLEADEHERVKSGWSDGFDDIYYQSWLLRDLQVMHAQMMREYPQRAPAPWLPRLFSDPLRDTRFVW
>LS483377.1|SQG11772.1|3561161_3561806_+|Predicted-nucleotidyltransferase
MHRARQHAASQTRERRHRLAHEAARLMAEGGIRDYHQAKLKAASRLGIHDDASLPRNTEIEDALREYQRLFSGPQHGNELQRRREAAMRALEFLHGFAPRLAGPVLEGTADANSPVQLHLHSDDPEAVHRFLDEHGIPAESRTRRLRMDRERSLDVPVWVFSAEELTFDLAVLPYDALRQAPLSPVDEKPMRRASVTQLRQLLAEAEITAYIGG
>LS483377.1|SQG11771.1|3558506_3560930_+|multimodular-transpeptidase-transglycosylase
MTRLRRWLRWIFLIVLVLALIGAAAVGGLYYAVSSKLPDVQTLRDVEMQEPMYVYAADGKLMAVFGETRRTPITMKDVPERLKQAFLATEDARFYEHGGVDYMGIGRAVWLLATTNDKRVPGGSTITQQVARQFFLSSEYSYTRKLAEILLARKIESELSKDEIFELYLNKSFFGNRAYGVAAAAEFYYGKKLNELDLDEMASLAGIPKFPSSGNPISNPERARQRRDNYVLQRMADLKFVSQAEADAAKAVPMHATAHEPPVQVDAPYVAELVRQEMIARFGGDVVNKGYHVTTTIDSTLQTAANQSVRDGLLLYDHRHGWHGVEKQVQVGAGEDAAALAEHLRGMYGQAGLLPAIVASTGADGSATVVLANRSEIVLPAGAAKWTNKTPGKLVQRGDIVRVRAGAKEGEWLLDQIPRGQSALVSLDAHNGALKALVGGFSFSGNKFNRATQARRQPGSSFKPFIYAAAFDKGYNPASIVLDAPVVFRDRRGKTWAPQNDGGGFRGPMRLREALVQSRNLVSVRLLDGMGVDYARKYISEFGFAESELPPNLSMSLGTASLTPLSVARGYAVFANGGSRVDTWLIDQVNDRDGNLVFKENPALACRDCAGSSDQPVNQVVDGFNFGAPAPKVDPAAATKAEAKTETPAAPANPDARTAPRAIDARTAYQLVSMMRDVVQRGTGVQAKVLGREDVGGKTGSTNDHRDAWFSGFGGPYVTTVWVGRDDFRSLGYREYGGKAALPIWIDYMRTALKDTPVAQNEPPSGMVQATLNGATEWVKVEDMDRLTDYDLNLNTPQADAAAFDIF
>LS483377.1|SQG11770.1|3557228_3558287_-|type-4-fimbrial-biogenesis-protein-PilM
MGLIPKSQSPLVGVDISSTAVKLLQLSRSGNRFRVEHYAVEPLPPNAVVEKNIVEVEAVGEAIRRAMNRSGSKAKLAAAAVAGSAVITKVIPMPAELDENDMEAQIELEAVNYIPYPIEEVNLDFEVIGAIPNNPEMVQVLLAASRSENVELRQSALELGGLQAKVMDVEAFAVENAYALVASELPVSIDGVVALVDIGATMTTLNVLRGGRSLYSREQVFGGKQLTDEIMRRYGLSYEEAGLAKRQGGLPESYEMEVLEPFKEATVQQISRLLQFFYAGSEFNRVDHIVLAGGCAVLGGLPEMVEEQLGVPTVVANPLAQMTLGPKVNAHALAQDAPALMIATGLALRSFD
>LS483377.1|SQG11780.1|3574498_3575776_-|Citrate-synthase-(si)
MSDLDQVTLNAGDKSVVLPVIKPTLGNDCVDIAKLTKETGFFTYDSGFTATASCKSAITYIDGDKGVLLYRGYPIEQLSEKSSYVEVAYLLINGERPSAEQLKAFTDELTAEANVDESINTLIGSFAKDAHPMAILAAAIAQLSAIYHDSLDLSDAEQRRQAAVRLIAKVPTLSALIYRHGKGLPANKPDTSLDYVSRFLKQTFESADGQYDLNPDVVKALDLLFILHADHEQNASTSTVRLVGSTGANPYASVAAGVTALWGPAHGGANEAVLKMLEEIGSADNVESAVVKAKDKTSGFRLMGFGHRVYKNFDPRAKVIGEMTSKVLKQLGVQDPLLDVAVKLEQAALQDEYFVARKLYPNVDFYSGIIYKALQIPTEMFTVMFALGRTSGWVSHWLEQQVDPEMKIGRPRQVYTGSDVRDYQG
>LS483377.1|SQG11781.1|3576072_3576315_-|50S-ribosomal-protein-L31
MKADIHPNYRDVVFHDVTSDFKILTRSTMATKETIQWEDGNEYPLVKVEISSASHPFYTGKHKVIDTSGRIDKFQKRYAR
>LS483377.1|SQG11782.1|3576403_3577342_-|inosine-uridine-preferring-nucleoside-hydrolase
MTHKIPLLIDTDPGVDDALALLMAFADERHDVVALTIAAGNVGLQYTVRNALKLCDIVGRTDVPVFAGSPDPLLHPSVDAAHVHGRDGYGDVDLPPPSRQAEAEHAALAILRLSHEHAGELMLVMLGPLTNLALALKLDPTLPERIKRIVVMGGAVTCHGNITPAAEFNIAFDPEAAHVVFTSFKHLLVSDWEATVAHGLPLQDAEKWLQADSDRARFYELISRKTRGLSEDSKGGRWYTADAVAMAWALNPEGQLRVESRPLNVELNGTFSRGATIVDWNRQTGQPDNCDLLMAYDQQRFEALVRQALGAD
>LS483377.1|SQG11783.1|3577726_3579838_-|ATP-dependent-DNA-helicase-RecG
MARKAAVTPVLSPSGEASLAMLAGVGPAVAAKLQARGLATLQDLWLHLPLRYEDRTRLTRIEDLRNGVPAQVEGRVVAVERGMRYRPMLKVAVEDEGRGTLVLRFFHFRQQQVGQFAVGNRLRCFGTPKPGQLGLEIVHPSYQVLGRNDDPELGDRLDPVYPTVEGVGPMTMRKLIGQALDRLPEESALELLPSGWLDGLGLPSLRSALLTVHRPPPDADLAALAAGTHPAQRRLAMEELLAHHLSLRRQRIALQAHHAPPLAGPGKLAKALLKQLPFALTGAQARVFKQIREDLARPSPMLRLVQGDVGSGKTVVAALAAMLAVEQGKQVALAAPTELLAEQHLNNLRGWLEPLGVRIAWLAGKVTGKARAKVMEQVASGEAQVVVGTHALMQEAVVFQDLALAIVDEQHRFGVHQRLALRDKGAGGNSVPHQLVMTATPIPRTLAMSEYADLDVSAIDELPPGRTPVQTVALNNDRRPELIERIALACQEGRQVYWVCTLIEESEELDATPAQATYESLQALLPGVRVGLVHGRLKAAEKLATMVAFKAGDIDLLVATTVIEVGVDVPNASLMVIENAERLGLAQLHQLRGRVGRGSAVSRCVLLYQAPLSQMARERLQTMRETNDGFVIAEKDLELRGPGELLGTRQTGLAGFRIADLARDAGLLPGVHDLAERLLDQQPALADRVVQRWIGTAVRYASA
>LS483377.1|SQG11784.1|3579845_3580232_-|endoribonuclease-L-PSP
MSRQIINTEKAPAAIGPYSQAVRAGNTVYFSGQIPLDPATGDIVGAGDVEAQARRAFDNLKAVAEAAGGSLDKVVRLGLYLTDLGEFAKVNAVMQDYFQAPYPARSTIEVSGLPKGANFEVDAVMVID
>LS483377.1|SQG11785.1|3580380_3582543_-|GTP-pyrophosphokinase
MNPGPTAKVAAAPAAAVPDYVLQLERAAHYLPPEQLPLLRRAWEVGASAHAGQTRKSGEPYITHPVAVAQVLAELGLDVEALIAAILHDTIEDTPLTREALAAEFGEAVAELVDGVTKLDKLKFRDRQEAAAESFRKMLLAMSRDLRVIMIKLADRLHNMRTLGAQSREARGRIARETLEIYAPIAQRLGMSLVKSELQNLGFKALYPWRHAIIEKHIRSQPVVRREAMAQVEVQLSQRLAKEGIEHRLISRIKTPWSIYNKMRDENKSFDQVMDVFGFRLVVRSVPSCYHALGSVHATFKPLDGRFRDFIAIPKANGYQSLHTVLFGPYGSPIEVQIRTEEMDLIAERGVAAHWTYKFGGDSPNSAQSRAHAWIVELIDSQRAAGSSLEFLDNVKVDLFPDEVYLFTPKGKILALPRNSTALDFAYAVHTDVGNMAVASRVDKKLVPLRTKLVSGQSVEIITARSATPKPQWLEFVVTSKARTAIRHQLKQLEHEDAVQLGHRMLDRALEAMDSSLERLPKGRLDAFLAEHRFPRLEALLAEVALGNWMPTQAAQALMAYAELRGGPHSRHHSQEKILINGSERGVVTFAGCCQPIPGDEIMGYHTAGKGIVVHRMDCPNLAELRKSPERWVPIGWDTTVSGDYDTSLVVEVENGTGVLAQLAAAIAQSHSNIERVDYLDRDFNAAVLAFNIQVRDRNHLAEVMRRLRRLSVVQSVRRQ
>LS483377.1|SQG11786.1|3582648_3582948_-|DNA-directed-RNA-polymerase-subunit-omega
MARITVEDCLEVVNNRFELVMMASKRARQLANGVQATLDNSETEDKPTVLALREIAARKIDNALIDEVEKAERERAEREALEWAAAEVVADEDMSKNDD
>LS483377.1|SQG11787.1|3583058_3583724_-|guanylate-kinase
MSAPSKPSDAVARGTLYIVAAPSGAGKSSIVNATLARDPQIALSISFTSRAMRPGEVNGQHYHFVSAEKFEQMIAAGDFFEHAWVHGDWKGTARQSVEPQLAAGQDVLLEIDWQGAQQVRQLVPGTVTVFILPPSKQALQDRMRKRGQDSEAVIAQRLGAARDEMLHFNEFDYVIVNEVFDTAVDELCAIFTASRLRREAQKVRHAGLIQALLTPDPGATD
>LS483377.1|SQG11788.1|3587094_3588012_+|formate-dehydrogenase-O-subunit-beta
MSLQSLDIIRRSATTTPSPEARGAHTGQVAKLIDVSKCIGCKACQVACMEWNDLRDEVGSCVGSYDNPPDLSDQSWTVMKFREYEDEKGKLEWLIRKEGCMHCSDPGCLKACPSPGAIIQYANGIVDFQEENCIGCGYCVTGCPFDVPRISKKDHKAYKCTLCSDRVAVGQEPACVKTCPTGAITFGSKQAMTEHAAGRVEDLKSRGYENAGLYDPQGVGGTHVMYVLQHVDKPELYADLPKDPRISPMVEVWKGVAKPLGVLAIAATAFAGFLHYIGIGRNTVNDEEEEEAEHEAKKIEEEQRP
>LS483377.1|SQG11789.1|3588008_3588656_+|formate-dehydrogenase-O-subunit-gamma
MKYAPHPRQIIRYRAPTRINHWIVAICFVLTALSGLALFHPALFPLTQLFGGGPWTRILHPFIGLAMVVGFALLAFRMWRDNLPTADDRAWMRGMRDVLRNEDEKLPPVGRFNAGQKLLFWAIIGCLSALLLTGFVIWRQYFSHFFPIGVIRFSVLAHALFGWVLVCAIVVHIYAAIWIKGSVRAMTQGKVTYGWAYKHHRQWFRDILRGRREEG

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Crispr_ID: LS483377_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_9

3667202-3667310

Orphan

Consensus_repeat	Method
CAGTGCCAACCAAGGTTGGCACCTACCAGGGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483377_9

>merge|LS483377|9|3667202-3667310|CRISPRCasFinder
CAGTGCCAACCAAGGTTGGCACCTACCAGGGCAAAGACCAGCTGCTGTAGATCCACACCATGCGTGGATGCATGCGTCAGTGCCAACCAAGGTTGGCACCTACCAGGGC

>LS483377|9|8|3667202-3667310|CRISPRCasFinder
CAGTGCCAACCAAGGTTGGCACCTACCAGGGC	AAAGACCAGCTGCTGTAGATCCACACCATGCGTGGATGCATGCGT
CAGTGCCAACCAAGGTTGGCACCTACCAGGGC

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG11863.1\|3666268_3667174_+\|LysR-family-transcriptional-regulator-PA2877	unknown	unknown	gnl\|CDD\|176161
LS483377.1\|SQG11856.1\|3658753_3660340_+\|2-isopropylmalate-synthase	unknown	unknown	gnl\|CDD\|234864
LS483377.1\|SQG11857.1\|3660350_3661130_+\|SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|369777
LS483377.1\|SQG11868.1\|3674673_3675891_-\|cationic-amino-acid-transporter	unknown	unknown	gnl\|CDD\|129987
LS483377.1\|SQG11858.1\|3661190_3662609_+\|3-isopropylmalate-dehydratase-large-subunit	unknown	unknown	gnl\|CDD\|235490
LS483377.1\|SQG11866.1\|3672563_3673211_+\|protein-L-isoaspartate-O-methyltransferase	unknown	unknown	gnl\|CDD\|225316
LS483377.1\|SQG11862.1\|3665377_3666151_-\|dehydrogenase	unknown	unknown	gnl\|CDD\|183716
LS483377.1\|SQG11869.1\|3676107_3677406_-\|3-deoxy-D-manno-octulosonic-acid-transferase	unknown	unknown	gnl\|CDD\|235589
LS483377.1\|SQG11864.1\|3667332_3670494_-\|RND-efflux-transporter	unknown	unknown	gnl\|CDD\|223911
LS483377.1\|SQG11867.1\|3673227_3674586_+\|type-I-secretion-outer-membrane-protein,-TolC-precursor	unknown	unknown	gnl\|CDD\|273829
LS483377.1\|SQG11873.1\|3681392_3681590_-\|Uncharacterized-protein-conserved-in-bacteria	unknown	unknown	gnl\|CDD\|226826
LS483377.1\|SQG11872.1\|3680252_3681377_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340846
LS483377.1\|SQG11865.1\|3671746_3672427_+\|TetR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|379522
LS483377.1\|SQG11870.1\|3677466_3678384_+\|lipid-A-biosynthesis-lauroyl-acyltransferase	unknown	unknown	gnl\|CDD\|181542
LS483377.1\|SQG11859.1\|3662608_3663187_+\|3-isopropylmalate-dehydratase-small-subunit	unknown	unknown	gnl\|CDD\|179314
LS483377.1\|SQG11861.1\|3664296_3665304_-\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG11860.1\|3663176_3664238_+\|3-isopropylmalate-dehydrogenase	unknown	unknown	gnl\|CDD\|234832
LS483377.1\|SQG11855.1\|3657665_3658757_+\|threonine-dehydratase	unknown	unknown	gnl\|CDD\|236339
LS483377.1\|SQG11854.1\|3657565_3657679_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG11871.1\|3678940_3680272_-\|O-antigen-polymerase	unknown	unknown	gnl\|CDD\|225844

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG11863.1\|3666268_3667174_+\|LysR-family-transcriptional-regulator-PA2877	gnl\|CDD\|176161	cd08472, PBP2_CrgA_like_3, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding fold. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 3. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	2.473e-95
LS483377.1\|SQG11856.1\|3658753_3660340_+\|2-isopropylmalate-synthase	gnl\|CDD\|234864	PRK00915, PRK00915, 2-isopropylmalate synthase; Validated.	0
LS483377.1\|SQG11857.1\|3660350_3661130_+\|SAM-dependent-methyltransferase	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	3.65828e-22
LS483377.1\|SQG11872.1\|3680252_3681377_-\|glycosyltransferase	gnl\|CDD\|340846	cd03819, GT4_WavL-like, Vibrio cholerae WavL and similar sequences. This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.	3.49014e-47
LS483377.1\|SQG11858.1\|3661190_3662609_+\|3-isopropylmalate-dehydratase-large-subunit	gnl\|CDD\|235490	PRK05478, PRK05478, 3-isopropylmalate dehydratase large subunit.	0
LS483377.1\|SQG11866.1\|3672563_3673211_+\|protein-L-isoaspartate-O-methyltransferase	gnl\|CDD\|225316	COG2518, Pcm, Protein-L-isoaspartate carboxylmethyltransferase [Posttranslational modification, protein turnover, chaperones].	1.35392e-64
LS483377.1\|SQG11862.1\|3665377_3666151_-\|dehydrogenase	gnl\|CDD\|183716	PRK12744, PRK12744, SDR family oxidoreductase.	1.16492e-176
LS483377.1\|SQG11869.1\|3676107_3677406_-\|3-deoxy-D-manno-octulosonic-acid-transferase	gnl\|CDD\|235589	PRK05749, PRK05749, 3-deoxy-D-manno-octulosonic-acid transferase; Reviewed.	0
LS483377.1\|SQG11864.1\|3667332_3670494_-\|RND-efflux-transporter	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
LS483377.1\|SQG11867.1\|3673227_3674586_+\|type-I-secretion-outer-membrane-protein,-TolC-precursor	gnl\|CDD\|273829	TIGR01844, Proteases_secretion_protein_PrtF, type I secretion outer membrane protein, TolC family. Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa). [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins].	1.66583e-106
LS483377.1\|SQG11873.1\|3681392_3681590_-\|Uncharacterized-protein-conserved-in-bacteria	gnl\|CDD\|226826	COG4391, COG4391, Uncharacterized protein conserved in bacteria [Function unknown].	3.15077e-15
LS483377.1\|SQG11865.1\|3671746_3672427_+\|TetR-family-transcriptional-regulator	gnl\|CDD\|379522	pfam14246, TetR_C_7, AefR-like transcriptional repressor, C-terminal region. This family comprises the C-terminal domain of transcriptional regulators of the TetR family. It includes the AefR transcriptional regulator from P. syringae. It is found in association with pfam00440.	4.76636e-27
LS483377.1\|SQG11870.1\|3677466_3678384_+\|lipid-A-biosynthesis-lauroyl-acyltransferase	gnl\|CDD\|181542	PRK08733, PRK08733, LpxL/LpxP family Kdo(2)-lipid IV(A) lauroyl/palmitoleoyl acyltransferase.	0
LS483377.1\|SQG11859.1\|3662608_3663187_+\|3-isopropylmalate-dehydratase-small-subunit	gnl\|CDD\|179314	PRK01641, leuD, 3-isopropylmalate dehydratase small subunit.	2.58314e-93
LS483377.1\|SQG11871.1\|3678940_3680272_-\|O-antigen-polymerase	gnl\|CDD\|225844	COG3307, RfaL, Lipid A core - O-antigen ligase and related enzymes [Cell envelope biogenesis, outer membrane].	7.96855e-20
LS483377.1\|SQG11860.1\|3663176_3664238_+\|3-isopropylmalate-dehydrogenase	gnl\|CDD\|234832	PRK00772, PRK00772, 3-isopropylmalate dehydrogenase; Provisional.	0
LS483377.1\|SQG11855.1\|3657665_3658757_+\|threonine-dehydratase	gnl\|CDD\|236339	PRK08813, PRK08813, threonine dehydratase; Provisional.	0
LS483377.1\|SQG11868.1\|3674673_3675891_-\|cationic-amino-acid-transporter	gnl\|CDD\|129987	TIGR00909, putative_amino_acid_transporter, amino acid transporter. [Transport and binding proteins, Amino acids, peptides and amines].	4.60478e-08

>LS483377.1|SQG11863.1|3666268_3667174_+|LysR-family-transcriptional-regulator-PA2877
MDRIDRFRIFTRVVECASFTRAADQLGLPRSTVSAAIAELEQRLGTRLLQRSTRRVSTTHDGDVFHARCLRLIAEVEDAESLFRQDDAQPVGLLKIDVPSRIGRRIIAPALPDFFARHPQVEVDLGMTDRAVNLIEDGCDAVLRVGQLGDSSLVARTLGQLDFVNVAAPAYLREYGVPQQPADLQQHRAVNYASPTTARVEPWEWQEGTQLRTLPMPGWVRVNSAEASIACCVAGLGLLQIPRYDVQAELQSGALVEVMPQHVAQPLPVTLLQPHRQHRAQRVQVFIEWLLPVLRSGLQLQ
>LS483377.1|SQG11862.1|3665377_3666151_-|dehydrogenase
MTDHSLKGKTVLIAGGAKNLGGLIARDFASQGAKAIVIHYNSAATQADAEATVAAVQAAGSKAVALQGDLTSAAAMERLFADAVAAVGRPDIAINTVGKVLKKPLLEISEAEYDEMSAVNAKAAFFFLKEAGRHVNDGGRICTLVTSLLGAFTPFYSSYAGTKAPVEHFTRAASKEFGERGISVTAIGPGPMDTPFFYPAESADAQAYHKTAAALSAFTRTGLTDIADIVPWIRFLVTDGWWMTGQTILVNGGYTTK
>LS483377.1|SQG11861.1|3664296_3665304_-|Uncharacterised-protein
MFIRTTCALALLLTACSGSARAQTAETDAVLFQNDLREVLECSAGPDLQQRVVSRLRAARYTDVAERTAELRDWRFKEKGADDDHRMTVITLPQPMTVHGIDARQVVADPFGFSIALDTVQRERVIAAHGLRLQSSTLREPFALWSAPTTSVIVRSAGDGYRLGCSPQATGKDAAARPAMAVQDLQEASECRADEATIRRLQAFWQGISERSQLEWPQEVRSVSEVSYTVGDAELPLLVIGLQSPIQVHGVATRTITLAFGGFFGADLGDVAVAPVLAQAGMGTSHQVGKATWQRALPPMTFSGGHWIPQHLVMRTDEGHVIAGCASDYVRSRPR
>LS483377.1|SQG11860.1|3663176_3664238_+|3-isopropylmalate-dehydrogenase
MHAEIVVLPGDGIGPEVAAAAVAVLKSVATRFNHTFTFSEHDIGGIAIDRHGEPLPASTLTACQAANAVLLGAVGGPKWSDPNAKVRPEQGLLAIRKALGLYANLRPVRTHEAALHASPIKAELLQGVDFVVVRELTGGIYFGDKTRDADSASDLCRYTVAEIERVLRSAFRLARQRRGKVTSVDKANVLETSRLWRDVAARIGREEFPDVALEHQLVDSMAMHLLAKPREYDVIVTENMFGDILTDEASMLAGSLGLLPSASLGEPGAVGIYEPIHGSAPDIAGKGIANPYATIFSAAMLLRHSLGLEDEAAAVEAAVHAVLDDGVFTADLAARGSAVSTAAATDAVLAKLG
>LS483377.1|SQG11859.1|3662608_3663187_+|3-isopropylmalate-dehydratase-small-subunit
MAGFRTLTSASVVLRQTNIDTDQIIPARFLSTTERAGLGRNAFNDWRWQADGSPVADFAFNQPHNAGRSILLAGRNFGCGSSREHAPWALTDLGLRAIVSSEIADIFRGNSLKNGLLPIVLDEADVQALMRRPDDELTIDVAARELRTPDGRVYSFPLDGFSQTCLLEGVDQLGYLLGRVPEIERYESEHAR
>LS483377.1|SQG11858.1|3661190_3662609_+|3-isopropylmalate-dehydratase-large-subunit
MTSAPRTLYDKLWDAHVVVPETDSAPAVLYIDLHLIHEVTSPQAFTELRERGLSPRHPDRTKATMDHSTPTLPPAADGTLPYASAASEAQVATLARNCAEHGIELFDMASDNRGIVHVIAPEQGFTQPGMTIVCGDSHTSTHGAFGSLAFGIGTSEVGHVLATQCLLQRKAKTFAITVDGPLAPGVGAKDVVLHIIGVIGVNGGTGHVIEFRGSTIEAMDMEQRMTLCNMSIEAGARAGMVAPDQVTFDFVAATPRGPKGADFDAAVARWQQLRSDDGARFDSEVHIDAADIRPTLTWGTHPGTAIAVDAPIPAANDAAAQKGLDYMHFQAGKALAGTPVDVVFVGSCTNGRLSDMREVAQVLRGRRVADRVRMLVVPGSEIVKREAEAEGIHEIVRAAGAEWREPGCSMCIAMNGDLVAPGQLAVSTSNRNFEGRQGPGSRTLLASPMSAAWAAVNGHVADTRELFAQEVA
>LS483377.1|SQG11857.1|3660350_3661130_+|SAM-dependent-methyltransferase
MSAFDTFTPASAAGQQWNAQDYAIDAGFVPLLGGAVSRLLDPRAGERILDLGCGDGVLSTELALSGARIHGVDASPELVVAARARGVDAQVMDGHALSFDSEFDAVFSNAALHWMTTPDRVLEGVRRALRPGGRFVAEFGGHGNVATIIAAVQAARVAHGHGASTFQWYFPTADAYADRLRQHGFQVQLIECTPRPTALPTGVAGWLRVFAAPLLDDLPAEARATVREAATALLAELPRNAAGQPLADYVRLRVLARRR
>LS483377.1|SQG11856.1|3658753_3660340_+|2-isopropylmalate-synthase
MTTIERITTPRIRIFDTTLRDGEQSPGCSMSPPQKLVMARALDELGVDIIETGFPASSQSDREAMALIGRELRRPSLTLAVLSRCLQADIETSARALEAAANPRLHVFLSTSPLHREHKLRMTREQVLESVRKHVALARSYIDDVEFSAEDATRTELDYLIEVARVAIAAGATTINLPDTVGFTTPEEIRAMFQQVIAGVADVPNAANVIFSAHCHNDLGLAVANSLAAIEGGARQVECTINGIGERAGNCSLEEIAMVLKVRQAFYEQDSSINTPRIVGTSQLLQRLVGMPVQRNKAIVGANAFAHESGIHQHGMLRHRGTYEIMRPEDVGWEDSQMVLGRHSGRAAVEARLRALGFWLDEDELKLVFEQFKGLCEQQRVVTDADLQTLMQGGSNAQGYRLASMTISDVGSRANALVELSDPDGNRVAETAQGDGPVDALFGALSAATGVQLMLDSYHVHSVGIGADARGEANLSVRHEGVEYDGTGTSKDIIEASALAWLDVANRLLRQRQATAHNSTDVPTPATA
>LS483377.1|SQG11855.1|3657665_3658757_+|threonine-dehydratase
MPAADTSQESDVGDVSVADVLAAQARLRRFLPPTPLHHAERFGTWLKLENLQRTGSYKVRGALNALLAGRERGDTRPVICASAGNHAQGVAWAAYRLDVPAITVMPHGAPATKIAGVAHWGATVRQHGNSYDEAYAFAVELAQRHGYRFLSAFDDADVIAGQGTVGIELAAHAPDVVIVPIGGGGLASGVALALKSQGVRVVGAQVEGVDSMARAIRGDVREIAPVASLADGVRVKIPGFLTRRLCTSLLDDVVIVREAELRETLVRLALEEHIIAEGAGALALAAGRRVAGRRKCAVVSGGNIDAGVLAGLLTDIRPRPPRKPRRRRSETPRSPAKASAPPSPMPSPSHLQAATPAVEEISL
>LS483377.1|SQG11854.1|3657565_3657679_+|Uncharacterised-protein
MNTRTVATTVPVRRRLLRRPCPHAGVFRTALVAHAGR
>LS483377.1|SQG11864.1|3667332_3670494_-|RND-efflux-transporter
MRRFNLSEWALANRPLVLFAMLAFALIGAWSYKHLGQSEDPPFTFKAMVVRTLWPGATAEQVSRQVTEPIEKALMNTGEYEFIRSYSRPGESQVIFMARDSLRSRQIPDLWYQVRKRVGDIRATLPREIVGPFFNDEFGDTYGNIYALTGKGFDYAVMRDYADRIQLELQRVPDVGKIDLVGLQDEKVWIELSNTRLATLGVSMQQVQQALADQNAVTGTSFFETATDRVQLRVTGQFNDIEAIRQFPIRAGDRTVHLGDIAEVKRGFADPASPKMRFMGEEAIGLAVAMKDGGDILKLGANLDAEFERLQKTLPAGMQLRKVSDQPQSVEESVGEFVQVLTEAVVIVLLVSFFSLGLRTGLVVGVTIPLVLAMTFFVMHYFDIGLHKISLGALVLALGLLVDDAIIAVEMMATKMEQGYDRLRAASFAWESTAFPMLTGTLITAAGFLPIATAASSTGEYTRSLFQVVTIALVVSWIAAVLFIPYLGDKMLPDLFNPQPPKPGSVSARWHAKRQQWADRYPALANLIGPPQHGHDHDPYQRPFYRSFRRFLDGCLRHRWWVIAATIALFVFSLMMFRFVPQQFFPDSTRPELMVDIELAEGASLRSTQAQAEKLEKLLSSREGIANYVSYVGTGSPRFYLPLDQQLPATNFAQFVVLAKDIKARESTRDWLLHEVIPKFPDVQMRVTRLENGPPVGYPVQMRISGEHIEKVQAIARQVEAKVRENPHVMNVNLDWSEPSKVVRLVIDQERARALGVSSAQVSQFLSSSLAGQSVSVYREGNRQIEMLLRGPADERNQLELLSSLSMPTANGGSITLSQVATMEYGFEDGIIWHRNRLPTVTVRADISDGMQPLDVVHQILPTLDGIRAELPNGYLLETGGTVEDSARGQNSIKAGMPLFLVVVATLLMLQLRSFSRAAMVLVTAPLGIIGATLFLLLFRAPFGFVALLGTIALAGMIMRNSVILIDQIQQDIDAGHDRWHSIIDATVRRFRPIVLTALAAVLAMIPLSRSAFYGSMAISIMGGLIVGTVLTLVFLPALYAAWFRVKPDESGA
>LS483377.1|SQG11865.1|3671746_3672427_+|TetR-family-transcriptional-regulator
MSSSTSRKPSAKPAAKAAGPGRPKDLGKRAAILEAAKVLFIEQGYTGVSMDAIAAQAGVSKLTVYSHFGDKETLFSEAVQSKCIEMLPDALFVADADGPLRDQLIGIGLAFFELITSDAAISIQRMMMAPETDERLRELFWKAGPERTCEALADFLRARAERGELEITDYSLAGEQFLTLVKGEVHMHMMCGMPLSPVECDPLAHVTASIDFFLRAYAPRGTGTAE
>LS483377.1|SQG11866.1|3672563_3673211_+|protein-L-isoaspartate-O-methyltransferase
MTIDYAHARELMVEQQIRPWDVLDIKVLDVLARLPREAFVADAHRALAYADVELPIGHGQKMMKPVIEGRTLQALDLQPGDEVLEIGTGSGFLSACIGALARDVLSLEIDPELATAARARLDASGLGTNVRVEVADALSWQTERRFDVICVTGAVDVVPSQFASWLRPGGRLFVIHGRSPAMEALLVKADGSTESLFETDIDYLRGAAPAPQFHL
>LS483377.1|SQG11867.1|3673227_3674586_+|type-I-secretion-outer-membrane-protein,-TolC-precursor
MIRRSLAVALATALLPLSAHAADLLQVYEMARNGDPQLSAAESTRLVDKEGAVQARAALLPQINGQATLNRTRSEPNADINSGSFTNKRRNYTIDGSQTLFNWTQINNLRSQRELSKAADFTLESANDSLIVRTSAAYFNVLVAIESLNAAQTNEAAAKKQFDFADKRLEVGLAPITDVHEARAQYDQARANTIVAQNTLADNYQALTELTGQPVVNLRGLPADFRPEVPANRGNIDELVHQATTQNPALKAQELKVSAAEAGVQAARGGHYPTLSLGGSWGKTATWGDSTGSGSLSPDARTNSIGLTLNVPIFAGGATQSGVRQALAQRDIAQDGYEQQKRALDRNTRNAYQTLVQGISEVEARRLAVVSAQSAYDASQVGLEVGTRTVLDVIQNQRILFSAQLDYAQARYTFLQNRLLLSQSLGALDVAELQDVNRLLTQDAGNPATTTH
>LS483377.1|SQG11868.1|3674673_3675891_-|cationic-amino-acid-transporter
MDSDSSPGIDEPGYGDRLVVVALTLLLGGGVVALVGQHTAAQAGPAIVLSLLLAALGTGPLLYCLHVLNQQRPAADGLHGVVRDCWGGVPAVLLGGALLLELVVTAAGVAQSVANHLHVLLAGCGIEASNGMPGQLMAAASLLLLAVVGLLRPHRVVLVACVLLTVKVGAGLLLLVLATRHVHYAYWIPWLPPATAPYRFGIGGVLAASVPLYGVFATVGLALGFPGIGRQARARPPLLPACVLLAMVLLIVLAALQAGLVEFPALASTRPLSVALQHHPQLYWVMPLLPLAGVAGAVALILVLLMLAARVAMQLWPTAGDRSLEFRERLVPVAVVLSAALLALWAPMGSLPVLPGPATLLVMGAVCVAVLRGRAPRSRALPVLAPVAIALCLLAAVERMRVWPG
>LS483377.1|SQG11869.1|3676107_3677406_-|3-deoxy-D-manno-octulosonic-acid-transferase
MRKDPVEWILRGLYSVVLYILLPITVYHLVWRGFRVREYFRRWDERYASYPQPTGQPRVWLHAVSVGEVNAAAPLVNALRKERPDIRWVITTITPTGSERVRALWGDALDHVYLPYDVPGSVNRFLGHFQPSLALILETELWPNMLFGCRDRGIPVYILNARLSARSLRGYRLLAALIRRALRTVTCVAAQSQDDAERFVQLGAAPEQVQALGNLKFDITTPDVQGFVEQFHARVPARRPVWIAASTHDGEEQAVIDLHRRLRRQHPDLLLLWAPRHPERFPKVEALAREQGWNVATRRAKQWPEVGTDVFVVDTLGELMPFYACAQVAFVGGSLQPIGGHNLLEPAAMGTAAVTGPHLHNFSEISRRMREAGALLIGEDVQAVGELLQHLLEDPQAREDMARAGCTLISNGRGALQRTLALVGPHLPPPCR
>LS483377.1|SQG11870.1|3677466_3678384_+|lipid-A-biosynthesis-lauroyl-acyltransferase
MSDATTAVRPSLRDPRNWPMFAAMLGAFAIARLPWMLQRALGRGVGWITWRLLGSRRRAAEVNLQLCFPEKDEAWRQRLVRDSFDALGVGVFECIRAWWGSIDSIRPQVQIEGLEHLRQMQAEGRGVLLVSGHFMTLEMCGRLLCDYVDLSGMYRKHKNPVYEWAVKFGRLRYAKAMFANEDIRATVRHLKKGGFLWYAPDQDMRGKDTVFVPFFGHTASTITATHQLARMTGCAVIPYFHRREGGKYFLKIGAPLENFPSDDVEADTTRVNQAIEEMVREAPDQYLWIHRRFKRQPGGRSDFYK
>LS483377.1|SQG11871.1|3678940_3680272_-|O-antigen-polymerase
MPTSPADPTVIVRDDRAGRWAPWWVLAYVAMWPLPGIAETVLGLGALYAAARMVTRRLQRRPHLLSTAAWALTSILFLGYWLPQAFSAFDAIDPAASWTKAAAGLRYLPFMWLVAIAVATPERRRLTFAGLALITGAWTLDALVQAVAGTSPWFWSLEHLKLAVSGHALCPADEAALADRLSGALGPCNLKFGQVLASLSPFLLLPTARRFGNTGWLLAAAALGSVLLLAGSRASWITFALVLAYSGVRQFGWKRLAALALVAVLGAGALTASVPQLRERFARTAMALEGGERGVDEALSGRARIWEAAACMIEEHPINGVGARGFRDAYPACVAEEGPAVWGNAPALHAHQIVLEILAETGVIGLLLWLAAVAQAWRAWRYAPAMARERARPAMLALAVTVFPLNTHLAFYSAFWGGLTVLLAALFAGSLLARDADDTPTAV
>LS483377.1|SQG11872.1|3680252_3681377_-|glycosyltransferase
MRRLTVVQLLPALHSGGVERSTLEIAAALVAAGHRALVVSAGGRLVQPLLDSGAEHLTLDIGRKSLLTLRHLPTLRRLFAEVGADIVHARSRLPAWLGLYAIRALPAAQRPHWVTTVHGLNSPSRYSAVMTSGERVICVSNTVRDYVQRHYPTVPEQALQVIPRGVDVAQFPRVARADRRPRMALAAEYPWLAQVEGPLLLLPGRGTRLKGHAHALQLLADVRAAGVPAQLWMLGTDEPGREAYVADLRRQAAALGVAEAVHISTPTARIAQAYAASDLVLQLSDKPEAFGRTVVEALSVGRPVLGWDHGGVGELLRQLQPAGAVPLGDARALGERALALLALLAQPPSLPTRIPFTLQAMQRDTLRLYADLAG
>LS483377.1|SQG11873.1|3681392_3681590_-|Uncharacterized-protein-conserved-in-bacteria
MSHTATAPANAEKRYTVHRSDLPLSCPTPEMALWNSHPRVYLPIEDEPNGEAQCPYCGSVFVLAD

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Crispr_ID: LS483377_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_10

3765600-3765680

Orphan

Consensus_repeat	Method
CGACCAAGGTCGGCACCCACCAGAGCGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483377_10

>merge|LS483377|10|3765600-3765680|CRISPRCasFinder
CGACCAAGGTCGGCACCCACCAGAGCGGATCATGGCGTCGATTGGCCCTGTGTCGACCAAGGTCGACACCCACCAGAGCGG

>LS483377|10|9|3765600-3765680|CRISPRCasFinder
CGACCAAGGTCGGCACCCACCAGAGCGG	ATCATGGCGTCGATTGGCCCTGTGT
CGACCAAGGTCGACACCCACCAGAGCGG

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG11954.1\|3776220_3778929_+\|TonB-dependent-outer-membrane-receptor-protein	unknown	unknown	gnl\|CDD\|273804
LS483377.1\|SQG11948.1\|3769031_3770099_-\|transmembrane-protein	unknown	unknown	gnl\|CDD\|226749
LS483377.1\|SQG11950.1\|3771246_3772275_-\|glucosamine-6-phosphate-deaminase-[isomerizing],alternative	unknown	unknown	gnl\|CDD\|225132
LS483377.1\|SQG11947.1\|3765702_3768732_-\|autotransporter-protein	unknown	unknown	gnl\|CDD\|238654
LS483377.1\|SQG11952.1\|3773389_3774679_-\|N-acetyl-D-glucosamine-permease	unknown	unknown	gnl\|CDD\|340952
LS483377.1\|SQG11940.1\|3758700_3759921_+\|tRNA-nucleotidyltransferase	unknown	unknown	gnl\|CDD\|182810
LS483377.1\|SQG11939.1\|3756510_3758496_+\|lytic-murein-transglycosylase	unknown	unknown	gnl\|CDD\|183236
LS483377.1\|SQG11943.1\|3761759_3763244_+\|hemolysin-related-protein	unknown	unknown	gnl\|CDD\|238287
LS483377.1\|SQG11951.1\|3772282_3773350_-\|LacI-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380487
LS483377.1\|SQG11956.1\|3781503_3781896_-\|VanZ-family-protein	unknown	unknown	gnl\|CDD\|227939
LS483377.1\|SQG11944.1\|3763324_3763660_-\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG11949.1\|3770098_3771247_-\|N-acetylglucosamine-6-phosphate-deacetylase	unknown	unknown	gnl\|CDD\|224733
LS483377.1\|SQG11953.1\|3775057_3776077_+\|N-acetylglucosamine-kinase	unknown	unknown	gnl\|CDD\|237092
LS483377.1\|SQG11941.1\|3760000_3760435_-\|Uncharacterised-protein	unknown	unknown	gnl\|CDD\|377787
LS483377.1\|SQG11945.1\|3763656_3764700_-\|nisin-resistance-protein	unknown	unknown	gnl\|CDD\|367567
LS483377.1\|SQG11955.1\|3779040_3781398_+\|beta-hexosaminidase	unknown	unknown	gnl\|CDD\|119333
LS483377.1\|SQG11942.1\|3761124_3761763_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG11946.1\|3765111_3765546_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG11937.1\|3752770_3755632_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
LS483377.1\|SQG11938.1\|3755902_3756313_-\|biopolymer-transport-protein-ExbD/TolR	unknown	unknown	gnl\|CDD\|223917

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG11954.1\|3776220_3778929_+\|TonB-dependent-outer-membrane-receptor-protein	gnl\|CDD\|273804	TIGR01782, TonB-dependent_receptor, TonB-dependent receptor. This model represents a family of TonB-dependent outer-membrane receptors which are found mainly in Xanthomonas and Caulobacter. These appear to represent the expansion of a paralogous family in that the 22 X. axonopodis (21 in X. campestris) and 18 C. crescentus sequences are more closely related to each other than any of the many TonB-dependent receptors found in other species. In fact, the Crescentus and Xanthomonas sequences are inseparable on a phylogenetic tree using a PAM-weighted neighbor-joining method, indicating that one of the two genuses may have acquired this set of receptors from the other. The mechanism by which this family is shared between Xanthomonas, a gamma proteobacterial plant pathogen and Caulobacter, an alpha proteobacterial aquatic organism is unclear. [Transport and binding proteins, Porins].	2.95974e-172
LS483377.1\|SQG11948.1\|3769031_3770099_-\|transmembrane-protein	gnl\|CDD\|226749	COG4299, COG4299, Uncharacterized protein conserved in bacteria [Function unknown].	2.91654e-50
LS483377.1\|SQG11939.1\|3756510_3758496_+\|lytic-murein-transglycosylase	gnl\|CDD\|183236	PRK11619, PRK11619, lytic murein transglycosylase; Provisional.	4.93293e-72
LS483377.1\|SQG11947.1\|3765702_3768732_-\|autotransporter-protein	gnl\|CDD\|238654	cd01344, PL2_Passenger_AT, Pertactin-like passenger domains (virulence factors), C-terminal, subgroup 2, of autotransporter proteins of the type V secretion system of Gram-negative bacteria. This subgroup includes the passenger domains of the nonprotease autotransporters, Ag43, AIDA-1 and IcsA, as well as, the less characterized ShdA, MisL, and BapA autotransporters.	1.39564e-37
LS483377.1\|SQG11940.1\|3758700_3759921_+\|tRNA-nucleotidyltransferase	gnl\|CDD\|182810	PRK10885, cca, multifunctional CCA addition/repair protein.	0
LS483377.1\|SQG11950.1\|3771246_3772275_-\|glucosamine-6-phosphate-deaminase-[isomerizing],alternative	gnl\|CDD\|225132	COG2222, AgaS, Predicted phosphosugar isomerases [Cell envelope biogenesis, outer membrane].	1.67347e-114
LS483377.1\|SQG11943.1\|3761759_3763244_+\|hemolysin-related-protein	gnl\|CDD\|238287	cd00519, Lipase_3, Lipase (class 3). Lipases are esterases that can hydrolyze long-chain acyl-triglycerides into di- and monoglycerides, glycerol, and free fatty acids at a water/lipid interface. A typical feature of lipases is "interfacial activation," the process of becoming active at the lipid/water interface, although several examples of lipases have been identified that do not undergo interfacial activation . The active site of a lipase contains a catalytic triad consisting of Ser - His - Asp/Glu, but unlike most serine proteases, the active site is buried inside the structure. A "lid" or "flap" covers the active site, making it inaccessible to solvent and substrates. The lid opens during the process of interfacial activation, allowing the lipid substrate access to the active site. .	3.73197e-11
LS483377.1\|SQG11951.1\|3772282_3773350_-\|LacI-family-transcriptional-regulator	gnl\|CDD\|380487	cd01545, PBP1_SalR, ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.	8.65071e-119
LS483377.1\|SQG11956.1\|3781503_3781896_-\|VanZ-family-protein	gnl\|CDD\|227939	COG5652, COG5652, Predicted integral membrane protein [Function unknown].	0.00215079
LS483377.1\|SQG11949.1\|3770098_3771247_-\|N-acetylglucosamine-6-phosphate-deacetylase	gnl\|CDD\|224733	COG1820, NagA, N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism].	7.43016e-163
LS483377.1\|SQG11953.1\|3775057_3776077_+\|N-acetylglucosamine-kinase	gnl\|CDD\|237092	PRK12408, PRK12408, glucokinase; Provisional.	0
LS483377.1\|SQG11941.1\|3760000_3760435_-\|Uncharacterised-protein	gnl\|CDD\|377787	pfam07179, SseB, SseB protein N-terminal domain. This family consists of several SseB proteins which appear to be found exclusively in Enterobacteria. SseB is known to enhance serine-sensitivity in Escherichia coli and is part of the Salmonella pathogenicity island 2 (SPI-2) translocon. This entry contains the presumed N-terminal domain of SseB.	1.24916e-09
LS483377.1\|SQG11945.1\|3763656_3764700_-\|nisin-resistance-protein	gnl\|CDD\|367567	pfam03572, Peptidase_S41, Peptidase family S41.	1.2597e-10
LS483377.1\|SQG11955.1\|3779040_3781398_+\|beta-hexosaminidase	gnl\|CDD\|119333	cd06563, GH20_chitobiase-like, The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.	0
LS483377.1\|SQG11938.1\|3755902_3756313_-\|biopolymer-transport-protein-ExbD/TolR	gnl\|CDD\|223917	COG0848, ExbD, Biopolymer transport protein [Intracellular trafficking and secretion].	3.51553e-15
LS483377.1\|SQG11937.1\|3752770_3755632_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	2.4377e-29
LS483377.1\|SQG11952.1\|3773389_3774679_-\|N-acetyl-D-glucosamine-permease	gnl\|CDD\|340952	cd17394, MFS_FucP_like, Fucose permease and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of L-fucose permease (also called L-fucose-proton symporter) and similar proteins such as glucose/galactose transporter and N-acetyl glucosamine transporter NagP. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. Glucose/galactose transporter functions in the uptake of of glucose and galactose. The FucP-like subfamily belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	2.48111e-120

>LS483377.1|SQG11946.1|3765111_3765546_+|Uncharacterised-protein
MNTPHPTYPRLQALLGAALPGLQLPTTAAEALEDALAEANEQAPPSAFFARLRGIAHSHAADGQAWRERQLSEGRGRELAEATRCLAALSACGGVLLAAQSARETDDAQAQCPPQVEEGLLHAMVVLADHAGALVEPDACAPLL
>LS483377.1|SQG11945.1|3763656_3764700_-|nisin-resistance-protein
MQVRKGVRRIGALMLVLLATGAMADMPGAVEVPSPEAQAEILNLLERQALYRDRVDWAATRVRLQSAQGDPAQRLAVLREAIAVSTGNHGGWTTTQRQSESLARAQQAGAAAVDRAKAADAVDMRIGWVVIEGYASTPGATPQEKFRQDIQRAARWQQVIRSKDDGARCGWIVDLRDNSGGNMWPMLLGMAPLLRTSVVNNEDVGSFETAQGPERWTLTATAVQRAGKSVLDFGQSGYVLRQPGAPVAVLFGPRTGSSGEASVLAWRGRPQTRSFGQPTAGVSTGNVVQTLADGSRLLLTTTVMRDRNDRGDGLKIEPDQRIEGDAATLATAEAWLLAQPACQAADP
>LS483377.1|SQG11944.1|3763324_3763660_-|Uncharacterised-protein
MILIGQQERVVVVGPTEAHHCLRCQTETEFAPQLRYKMARIDLLFGLTYQRRYELACTRCGHGWVLDTETMDQQLGGVPIPWRHRFGLPLMLVVVVGLAVAGWMWRNLYSS
>LS483377.1|SQG11943.1|3761759_3763244_+|hemolysin-related-protein
MRPLTNAALANAAYSPPSHPAPGDKESLRVDGEDFEVLGRRDAVSGYQGVVYRNIKTNEIIIAHRGTEFDRQAMLDGGVDAAMVSARVNAQIDDALVLTKQAIKQAEENGYGPVYVTGHSLGGALAQITAYHYNLPGDAFNPYGAAGLAYRLPEGQPANAAPFTNHVMAGDLVSAAGPHYGKVEMYALPKELGVLRDAEQGQRIASLVSLGMKSGHVMSAAVAVQLGDSHRMVHFIDRITDKGPVQSVLDDPGARITDAEDLRRIAEYRKDIHQLRLGATVLVGGGPGLLRDGVNYLLGTGEAGAYARREAEAVQHAESALKAGERSVQEATEKGSPSLSNPGFAPKSPLQESIESTLDKAGLDPRKEGHPDHALYRQIRDGVSAVDARHGRGFDETSERVTAGLLATAKRSGLERVDHVVLGNPPSDGSGPRMFVVQGALDNPAHLRASIAVSEAVNTPVDQSLAKVEQISQAQQVAQQEQTQEQTRTAMRMG
>LS483377.1|SQG11942.1|3761124_3761763_+|Uncharacterised-protein
MLKPSPSLTHVALIALITLAVSGCNKERSYPVYRENPAPKDALPIVIRVHDAPVELTLPKVFVSYEIDPLCLPPINNYEGVQYAPQRHSVEFPVQRVSATEFSSTVFEDGMAVADYYGRGPCEWKPSIIRASFPVISEGREGFISVAVHHLELKKLLTSVSYADSQMTLQTKSSTPGWVRTQSQYSYNRLSDIEKQKYFAIEISSPSKGIVP
>LS483377.1|SQG11941.1|3760000_3760435_-|Uncharacterised-protein
MDHDTPFEPLNDLEVRLLQAQDGTLTASQFLDGLLTSTAFVLLDKAIGEDGAWDESISPLVLTSESGEPMFAVFTAPERAGLWHEQLPQFAHAMPIAVHALLAGIGDGVGLVLNPGLDVGMEMIPDAVAQLKQRAAAITRGMAH
>LS483377.1|SQG11940.1|3758700_3759921_+|tRNA-nucleotidyltransferase
MKIYLVGGAVRDRLLQRPAGDHDWVVVGATPAQMEAQGYTAVGRDFPVFLHPKTGEEYALARTERKSGRGYRGFVVDADPGVTLEEDLQRRDFTINAIACDEDSGALVDPYGGVRDIEQRVLRHVGPAFVEDPLRVLRAARFMARFAPLGFTVAEETMALMREIAASGELDALVPERVWQELRKALVSEQPSAFLRTLHDAHALGPILPELEALYGVPQRAEFHPEVDTGIHQEMVSDMAAKLAPGDDLVGFAALTHDLGKGLTPPEEWPRHIMHEQRGIKPLKALCARLKIPAEHQQLAEAVCREHLNVHRIDELRDATVLELLGRCDALRRPERVARIALCCEADKRGRLGFEDADYPQGETLKRLHQAALSVQARDLNTTHLKGPAIGEALAKARVKAIAAAR
>LS483377.1|SQG11939.1|3756510_3758496_+|lytic-murein-transglycosylase
MLGAMTRRSSTALSLLPLATTLLIGCANAQSLDAQNAQLKAAIAAAERGQFDPGQAAALSRHPAYGWLEYANLRRNIDTVDTAQAQAFLKRYDGQAVANTFRSVWLPSVARRQDWPTLLANWAPTDNVGLRCAQLTARQVTGKVDPQWISEAQDLWRKNGKSLPDGCDAVFAVLQAQGGLSDALRWERIDAAADAQQPAVMRSAARGLPAADLAQANSYAAFVDKPNASALNWPRNERSRRIATDGLAKLAKADPAATEQQLPQYAQALGLSAEQQGQVLYQIALWTVASYLPDSARRLNAVPESAYDERLHEWRVREAMSRGDWPAALTAIRKMASKQRSDPRWRYFEGRMLEKTGQAQQAQPLFREAARAPTFHGFLAADKLQQGYTLCPWRPNDSAQAQAVIARDPAIQRAMALYQIDRTGWAVAEWNSALSRFDDTQRRLAVRVAQDNGWFDRAVFALGKQPQEQRLYDLRFPLHHDATIRRESARNAIDPAWVAAEIRAESTFTPRARSPANAMGLMQVLPATGAGVAKSIGLTGYGGADSLYDPDTNIAIGTAYLRQLMNKYDGLPYVTIAAYNAGPTPTARWQSQRPGFDPDLWIETISYKETREYVARVLAFSVIYDWRLNGDALPLSDRLMGRLVDKRKNFSCAANAEQGGD
>LS483377.1|SQG11938.1|3755902_3756313_-|biopolymer-transport-protein-ExbD/TolR
MRYASVHARALMSGINLAPLVDVLLVLLALVVTTLPMAQTTAVRTFQQRTVCPPGPGHTSPASIALHLDAAGGVYWNDRPLDDPSLQHALAQLQQLPPALQPSLHLTTADSTDYGDMARVLSAIEGRGLRVTAQGY
>LS483377.1|SQG11937.1|3752770_3755632_-|TonB-dependent-receptor
MIHLHHRPLAVAVALCVTALAPLGAAAQSTTNLDAVEVTGTRIKRAEVEGQAPIQTLTRGDIERTGLTSIGEVLQQLTGSGSALNAKFNSSGNFGFPPDGSGVGAGSAQVDLRHLGAKRVLVLVDGIRWVNESSASGVGSATDLNTIPLAIVERIEVLEDGASSLYGSDAIAGVVNIITRRDFDGGQVTLNYGEYSKGDGTQKGVDLAWGKSGDRFSLFLGASWTKQDPVFAKDREQSRFPIPGTGLAFGSGGIPQGRFMFTDPNTGAVQNIVPNTGVSNPRYDGSAGCSRTDDYHCFTTADRFNFAEYNMVLTPSERKGLFGQFRFDITDNVQWYVKALGNRRESTNQAGPEPLFFGPDGATGNPLADNIVVSRLNPYNPFGFDLVSGDNMSLIGRRPVEGGARVFKQKVDTTYFATGLVGDFHAADRSWYWDVNGMYSKNKAEQTNHGSYDIYKVNMALGDPSICAATPGCVPLNIFGGVGSITPDMLKWIQPVVRDRSQNELSLFTANLSSELFSLPAGPVSFATGFEYRKYKGSYQPDPLTVIGHYNGVPSQPTSGSYDVNEAYLELSVPIFADSSFGKKLDLSLAGRYSDYSTFGGEFTPKYGLRWQVTDDFVLRTTYAEGFRAPSIGELYGSAARADLQLFDPCSVGLGGTPPRGSAANCAALGVPAGFQQANSQISVTTGGNRELEPERSRSFSAGFVWSPWFGNNASWSERFDVEVTFYRHAIDGAIQAINAQTQLDLCVDTLDPVYCDGITRASTGAVSSFNNRLTNLGSIKTDGWDVDLFWTLPQTSIGQFKLAWKNTFVGRYEATGAVGQKQPQKPGVEVADSSIPEWTSNASIGWTMDRWSANWTVRHISELTENCGDAAAFPVCSNQAAGTNTLSATTFHDMQVGYKIDWMKGLQLTAGLNNVFDKDPPICLSCSLNGYDASTYDIPRGRYWYLRADLRF
>LS483377.1|SQG11947.1|3765702_3768732_-|autotransporter-protein
MYRAVPRAFRPRRLAVSVLQALAVPSLLLTTASVAWAGCNSPAPTAGQTVTCDTNAPNPQTTPVAANGAAGITVNVAAGAQLQQSGGGSAIALVGAGGHLLSNQGAISSVGGVTVQLGGGSRVDNTGSISTGNNTALQFVGAGDSVLVNRGAISGRTGVQFDAGNDRLEMQSGSITGGVLQGDGNDVLLLSDGTIDSVDQGGGDDQMTVTGGAVTGVVAQGSGRDDFIMSGGTIGALQQGDNIDTFRMSGGRIIGAFEDGDQAWMTAGRIGRVNMKLDKNLWDQSGGTVDGNVVTGFDTDTIIISGTAYIGGNISVSGGNDSVTITDGTVRGQVLLSTGSDTFNWSGGGIVYGAIDMGPDNDVANLSSLNQGNLGAVPLFDGGSGIDQLNFNNVKTTGVARFQNWEAISLANSTELTFDGDLVLGDSATGTGTLTVDDTSTLYAGSGGHAIRPFNSAALVEMVNAGRIDLTGTGAGDVFTVRGNYRGDGGGLYLRTVLGADNSTSDRLVIDGGSATGTTGIGVLNAGGIGAATLADGILVVQALNGGRTAPGAFSLFAPVAAGAYEYFLFKGGVSAGTSENWYLRSTLVAGPAPAPNGSGINGVPPPPTPPVAPPPPITPAPPPPPEGATDPDLTAGETAPPPPPPEPAPVAPPSDPAVPDVPVAGGSLPGTGAPPTPGARPAEGAVVPLYRVETAAYAVVPPLLRETSLASLGTFHERQGEQRLLYNQGAFRTAWGRLVGQSSEIHWKGDAQPGFDGDVMGLQAGLDVWAAASDNHRNQIGVFVGRTRAQGKTSGLALGWENVQVGQNRLDDKHVGLYWAFTDSSGGYIDAVAMQSRYDGRVRSSRGLGFGIKGDGTSVSVEAGKPLLHFGQSAWWLEPQVQVIWQRTSLDDRRDAVSSVRFDNDNAWTGRVGLRLAGDYQLADNGWQPYFKLNYWHGRSGEDRIRFDDDVIFNSQRSRALEAGVGVVGRFNRTISAYAVADYTRELGGDRNEKRRIIEGNIGLRADW
>LS483377.1|SQG11948.1|3769031_3770099_-|transmembrane-protein
MNSSPPRRLGSIDALRGITVAAMLLVNNPGDWSAVFAPLRHSEWHGCTPTDLVFPFFLFLVGVSMAFSVAPRAQDAAARPALARGVLERALRILMAGALLHLLIWWALDTHHFRIWGVLQRIAVCAALVGVLAVYARPRVQVGALIALLVGYTLLLLGIGDLAPWTNPASRLDTALFAPWIYQWHADTGLGHDPEGLLSTLGALASTVLGLLAGGLLRNGRSAALAGLGVATAVLGLLLAVVLPLNKQLWTPSYVLWTGGLAALALWLGHVLIDQKGWPALGRRFGVNAITAYLGASVMSVVLMATGIWGWIWQQLATAMPQALELASMLQALVFVALWWGVAWWLDKRKIYLKI
>LS483377.1|SQG11949.1|3770098_3771247_-|N-acetylglucosamine-6-phosphate-deacetylase
MVTVLRNARILAGDDFRDDLALVIENGRISALLPDAAPQLGHAAEQVDLGGGWLLPGFIDVQVNGGGGALFNNTPDVAALRTIAQAHRRFGTTAMLPTLISDDVAVMREAIAAMREAITQGVPGVIGIHLEGPYIAPARKGTHDASKFRVPDEGEIALAASLDNGVTVLTLAPERVPLETIRALVERGVIVAAGHTAGTYEAIRAGLDAGVRGFTHLYNAMSPLQGREPGAVGAALEDRDSWIGIIVDGVHVHPASLRVALAAKPRGRLLLVTDAMPPVGADDPSYVLYGETITAVDGVVRNAAGSLAGSALDMATAVRNTVQLLGQPLAEAARMASTYPAQFLNVDDRLGHIAEGYQADLVLLDDALQVRGTWIAGQYEAA
>LS483377.1|SQG11950.1|3771246_3772275_-|glucosamine-6-phosphate-deaminase-[isomerizing],alternative
MSLSDPTSTLMFAEAAEAADVVARQFSRNHATMETLAASLRAAPPPFVVTCARGSSDHAATYGKYLLETQLGLVVASASPSVGSVYAAPLQLRGALFIVISQSGKSPDLLRNAEAAKAAGARVIALVNVEDSPLAQLADTVIPLHAGAEKSVAATKSYLASLAALLQLAAYWKQDSSLRAALDLLPDALREAWQCDWSAVTEGLVEATNLFVLGRGLGLGAAQEAALKFKETCSLHAEAYSSAEVKHGPMALVDRGFPVLAFAQPDETGAGTRAVVEEFTARGAQVWMAGAGGNLPVAAAPHPLCAPLLTVQSFYRAINALALRRGFNPDLPPHLNKVTETV
>LS483377.1|SQG11951.1|3772282_3773350_-|LacI-family-transcriptional-regulator
MRRATIKDVAEKAKVSLKTVSRVINNEPSVMQATRARVLRAIAELDYEPDPSARNLRSGTTFVIGLVYDNPNPYHIIGVQNGVLAACRETGFGLQIHPCDSSSPLLADELADWVQRSRLAGLVLTAPMSERRDLIQALTARGIKLVRIIAATEDPADGACVFVDDREAAYEITEHLIQLGHQRIGFLWGGSSHRSSGERYAGYEAALKDYGMTVDKHLVVQGDYTFDDGFRGARRLLALREPPTAIFGSNDEIAAGVLAAAKSAGMNVPYDLSIAGFEDSPFSRQSWPPLTTAKQATEDIARHAARLLIAQLRSDAYDDAPAPLHNQGFVPQLVVRGSTAPMRPAGARPLPSDPA
>LS483377.1|SQG11952.1|3773389_3774679_-|N-acetyl-D-glucosamine-permease
MSAVSAASVRPNVATSIAIVGVLFFLIGFFTWLNGPLITFVKLAFELSEVGAFLVLMVFYLSYFFLALPSSWILRRTGMKKGLSLSLLVMAGGAALFGEFATQRWYPGALGGLFVIGSGLALLQTAINPYISILGPIETAARRIALMGICNKIAGILAPILIGTVVLHGIGDLDVQVQAADAATKAVLLNQFAAKIHAPYLAMAALLVVLAVAILFSPLPEIKSSEANATPVAAGAVERRSIFQFPHLWLGVLCLFVYVGVEVMAGDAIGTYGHGFNLPLDETKMFTAFTLGAMLVGYVVGLLVIPRVVSQSRYLTISAVLGVVFCLGAWATHGYVSVAFVALLGFANAMMWPAIFPLAIRGLGRFTETGSALLVMGIAGGAIIPQLFALLKQHIDFQLTFVLLMVPCYLYILFYSVIGHRAGLPQDKA
>LS483377.1|SQG11953.1|3775057_3776077_+|N-acetylglucosamine-kinase
MTASHPAPAHVLSRIAPSFLAADVGGTHVRVARVQASGDAAHPVQVLEYRKYRNADHAGLSAILSDFLGEGPRPTHCVVASAGYAREDGTVITANLPWPLSARQVEADVGLQRVFIVNDFEAVAYAAAQVDASGVLHLCGPETAARGPTLVVGPGTGLGAALWIPTAHGPVVLPTEAGQPTLAASTELEMAIVRHMQRDRAHVSIEHAISGPGLMNLYRAVCALQGQAPTLASPDAVTAAAMADSDAHARQALDVFCGLLGSTIGDMALFYGAHGGVYLAGGILPQIREYLHASTFVERYLQKGPMGEALARIPVKVVEHGQLGVVGAASWYLQQQSAA
>LS483377.1|SQG11954.1|3776220_3778929_+|TonB-dependent-outer-membrane-receptor-protein
MNTRKTLLSAAIVSCIAFSAHAQQAAQTATDLDTVQVTGIRGSMEKSLDTKREANARVEVVTAEDVGKLPAHNVADTLQRLPGVNISSSSADEGGFDEADRVSLRGTSPSLTQTLINGHTVGTADWFVLSQGNNVGRSVSYSLLPSELVRSVEVNKSSQAKLQDGGTTGTVNILTRKPLEFSKQLTAEGSIGMVRSDQAKSNDPQLSALFNYKNDEGNFGVMVQAFSQKRELRREAQEIPGGFFQIDPNGTVAKSNPDLAGVYAPGLLGSTLFEQTRERKGGLVSLQFKPMDNLTLGLEGFSSELKANNYNRNFMLWGGRILNDRTVEDANGNKILIPGQAPNPGYVIKDGVLSNATFAGQADRDYAVYDMIYRESKAKTNYITFDADWQISDNLGMKFQAGSTKGTGETPRQYIAEVNLARGGGATWATHGNGSPIDWNVGGNIGPSGVTDFGTWGNQQVTAIDKEKWATLDFNQYFADAGVLNSIDFGARFGDHKREAKSPEGATPGAIWNALKNGATANFPGGFANGIGGSFPRDLWYFTPGALKEAVTNNSTWLSGNDGPTGRHNYGAEWKVSEKNFAAYVQGNFSGDRWSGNVGLRYVNIKQDIDTYAAATGSTVPDVSSLFGAWTREAFENKHNRVLPSANFKYDLRDDLVLRVAASQTQTLPDFSALGASSYGSDLNRTGGGGNPKLKPVVSTNFDANLEWYFMPRGMLSIGAYSMRLKDYVAFSTEKEMLFSELTNRLEEYNISRPRNADGKVRGIEVAYEQPIGEYFGVNANYTYADGSTDHTWADGSDNLLGTSKNTYNVGAYFENDTFGARVSYTRRSSFLIGLSGANPYYQDDFGTLSASLSYKATDWLSISFDALNLNNPTYKYYQTAAIPTSFYSNGRQYYLNFRFKY
>LS483377.1|SQG11955.1|3779040_3781398_+|beta-hexosaminidase
MVKPSRARMRSAVLLGSLLALLPALPALAADPTPATEAPGPLLRAGSLMLIPAPATVQRGQGSGITVRADTVLQAEGEAAQRVASQFADLLARSGGPRLAPASGKAAGTSGSIRFQIVPTFRDSGESYTLESTAQGVLIQAGNETGLFYGATTLAQLATGGSNGVLPAVQIQDAPRFSWRGFMLDSARHFQSLDEIKRVLDAMAAHKLNTFHWHLTDDQGWRMEIKRYPKLTDVGSCRLPAGDGGVDPASGQEHPYCGFYTQDQIREVIAYAAKLHIQVIPEIDVPGHATAAIAAYPELGTIDTPLKPISEWGVFPNLFNTEDSTVTFLENVLEEVIDLFPAKYVHVGGDEAVKDQWEASKQVQQRMRALGIKDEMAMQSHIIKRLETFLEEHDRRLIGWDEILEGGLPPQATVMSWQGIEGGLAAASAGHDVIMSPVGYLYLDYLQTASPNEPPGRPTQVNLGKLYNFEPVPAELAADKRGHILGLQANMFTEHTRSYARLQHNLFPRLAAVAETGWSTSEHRDFRDFLARLPSQLRRYRAWGLAYAQTPFEVGVDYTDNRADNTVTVSLANPLGYEVRYSTDGQPVSAQSPLYQQPLTGKLPTTVQAAAFYQGQMLAAKPTIATFTAQSLLSRRSDELLSCVGKKGLVLRLEDDGPREGNRAVFNVDIFQPCWRWPQAQLDGIGSLEVRAGRIPYYFQLAHDEPKRRFEKAKRPHGEMQVRRGDCSGKVLAEVPLPAKPDADGFVTLRAALPKGTQGSGDLCINFTGDTRPAMWVLDEMTLGK
>LS483377.1|SQG11956.1|3781503_3781896_-|VanZ-family-protein
MSEVLPAIKPLRRPRLWAGLWATAVLLVIVVCLIPPPPIPLPENSDKGEHFLAYFILAGSAVQLFRRGRPLLWVGVGLVLMGIGIEFAQGALTSNRMADPMDAIANTVGVLAGMATALTPLRDLLLRWRG

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Crispr_ID: LS483377_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483377_11

3797069-3797179

Orphan

Consensus_repeat	Method
GGCGAAGGCGTGCGGACCAACGGTCCGCACCCACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483377_11

>merge|LS483377|11|3797069-3797179|CRISPRCasFinder
GGCGAAGGCGTGCGGACCAACGGTCCGCACCCACCAGGAGGGTGGTGACACCCATTGGCAGCGCCAGGCCATGGCTGGCGAAGGCGTGCGGACCAACGGTCCGCTCCCACC

>LS483377|11|10|3797069-3797179|CRISPRCasFinder
GGCGAAGGCGTGCGGACCAACGGTCCGCACCCACC	AGGAGGGTGGTGACACCCATTGGCAGCGCCAGGCCATGGCT
GGCGAAGGCGTGCGGACCAACGGTCCGCTCCCACC

Protein	Signature genes	Signature genes Name	Protein_function
LS483377.1\|SQG11965.1\|3789854_3790238_-\|Osmotically-inducible-protein-OsmY	unknown	unknown	gnl\|CDD\|225379
LS483377.1\|SQG11961.1\|3785667_3785850_-\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG11978.1\|3805585_3806680_-\|Rod-shape-determining-protein-RodA	unknown	unknown	gnl\|CDD\|274033
LS483377.1\|SQG11962.1\|3785849_3787361_-\|Histidine-kinase/response-regulator-hybrid-protein	unknown	unknown	gnl\|CDD\|237526
LS483377.1\|SQG11972.1\|3798207_3798918_-\|Octanoate-[acyl-carrier-protein]-protein-N--octanoyltransferase	unknown	unknown	gnl\|CDD\|237681
LS483377.1\|SQG11973.1\|3798905_3799184_-\|lipoate-regulatory-protein-YbeD	unknown	unknown	gnl\|CDD\|179161
LS483377.1\|SQG11976.1\|3802186_3803452_-\|lipoprotein-A	unknown	unknown	gnl\|CDD\|223868
LS483377.1\|SQG11977.1\|3803448_3804570_-\|lytic-murein-transglycosylase-B	unknown	unknown	gnl\|CDD\|274066
LS483377.1\|SQG11980.1\|3807925_3810001_-\|penicillin-binding-protein-2-(PBP-2)	unknown	unknown	gnl\|CDD\|274573
LS483377.1\|SQG11967.1\|3791741_3792647_-\|6-phosphogluconate-dehydrogenase	unknown	unknown	gnl\|CDD\|236582
LS483377.1\|SQG11969.1\|3793910_3794501_-\|lipoprotein	unknown	unknown	gnl\|CDD\|378349
LS483377.1\|SQG11979.1\|3806816_3807929_-\|Rod-shape-determining-protein-RodA	unknown	unknown	gnl\|CDD\|274033
LS483377.1\|SQG11970.1\|3794745_3796923_-\|tail-specific-protease	unknown	unknown	gnl\|CDD\|236873
LS483377.1\|SQG11974.1\|3799535_3800594_+\|outer-membrane-protein	unknown	unknown	gnl\|CDD\|378338
LS483377.1\|SQG11966.1\|3790408_3791452_+\|Oxidoreductase	unknown	unknown	gnl\|CDD\|183212
LS483377.1\|SQG11968.1\|3792657_3793914_-\|Uncharacterised-protein	unknown	unknown	unknown
LS483377.1\|SQG11964.1\|3787802_3789620_-\|two-component-system-sensor-protein	unknown	unknown	gnl\|CDD\|226702
LS483377.1\|SQG11981.1\|3810004_3810490_-\|Rod-shape-determining-protein-MreD	unknown	unknown	gnl\|CDD\|225444
LS483377.1\|SQG11975.1\|3800868_3802086_-\|D-alanyl-D-alanine-carboxypeptidase	unknown	unknown	gnl\|CDD\|224600
LS483377.1\|SQG11963.1\|3787365_3787806_-\|two-component-system-response-regulator	unknown	unknown	gnl\|CDD\|381108

Protein	Function_ID	Function_description	E-value
LS483377.1\|SQG11965.1\|3789854_3790238_-\|Osmotically-inducible-protein-OsmY	gnl\|CDD\|225379	COG2823, OsmY, Predicted periplasmic or secreted lipoprotein [General function prediction only].	5.08321e-17
LS483377.1\|SQG11978.1\|3805585_3806680_-\|Rod-shape-determining-protein-RodA	gnl\|CDD\|274033	TIGR02210, Rod_shape-determining_protein_RodA, rod shape-determining protein RodA. This protein is a member of the FtsW/RodA/SpoVE family (pfam01098). It is found only in species with rod (or spiral) shapes. In many species, mutation of rodA has been shown to correlate with loss of the normal rod shape. Note that RodA homologs are found, scoring below the cutoffs for this model, in a number of both rod-shaped and coccoid bacteria, including four proteins in Bacillus anthracis, for example. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division].	1.96029e-141
LS483377.1\|SQG11969.1\|3793910_3794501_-\|lipoprotein	gnl\|CDD\|378349	pfam10001, DUF2242, Uncharacterized protein conserved in bacteria (DUF2242). This domain is found in various hypothetical bacterial proteins, and has no known function.	3.9445e-62
LS483377.1\|SQG11972.1\|3798207_3798918_-\|Octanoate-[acyl-carrier-protein]-protein-N--octanoyltransferase	gnl\|CDD\|237681	PRK14342, PRK14342, lipoyl(octanoyl) transferase LipB.	8.74975e-140
LS483377.1\|SQG11974.1\|3799535_3800594_+\|outer-membrane-protein	gnl\|CDD\|378338	pfam09982, DUF2219, Uncharacterized protein conserved in bacteria (DUF2219). This domain, found in various hypothetical bacterial proteins, has no known function.	1.33614e-109
LS483377.1\|SQG11976.1\|3802186_3803452_-\|lipoprotein-A	gnl\|CDD\|223868	COG0797, RlpA, Lipoproteins [Cell envelope biogenesis, outer membrane].	1.99888e-51
LS483377.1\|SQG11977.1\|3803448_3804570_-\|lytic-murein-transglycosylase-B	gnl\|CDD\|274066	TIGR02282, Membrane-bound_lytic_murein_transglycosylase_B, lytic murein transglycosylase B. This family consists of lytic murein transglycosylases (murein hydrolases) in the family of MltB, which is a membrane-bound lipoprotein in Escherichia coli. The N-terminal lipoprotein modification motif is conserved in about half the members of this family. The term Slt35 describes a naturally occurring soluble fragment of MltB. Members of this family never contain the putative peptidoglycan binding domain described by pfam01471, which is associated with several classes of bacterial cell wall lytic enzymes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	1.31815e-137
LS483377.1\|SQG11980.1\|3807925_3810001_-\|penicillin-binding-protein-2-(PBP-2)	gnl\|CDD\|274573	TIGR03423, pbp2_mrdA, penicillin-binding protein 2. Members of this protein family are penicillin-binding protein 2 (PBP-2), a protein whose gene (designated pbpA or mrdA) generally is found next to the gene for RodA, a protein required for rod (bacillus) shape in many bacteria. PBP-2 acts as a transpeptidase for cell elongation (hence, rod-shape). [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	0
LS483377.1\|SQG11967.1\|3791741_3792647_-\|6-phosphogluconate-dehydrogenase	gnl\|CDD\|236582	PRK09599, PRK09599, NADP-dependent phosphogluconate dehydrogenase.	0
LS483377.1\|SQG11962.1\|3785849_3787361_-\|Histidine-kinase/response-regulator-hybrid-protein	gnl\|CDD\|237526	PRK13837, PRK13837, two-component system VirA-like sensor kinase.	3.07469e-47
LS483377.1\|SQG11979.1\|3806816_3807929_-\|Rod-shape-determining-protein-RodA	gnl\|CDD\|274033	TIGR02210, Rod_shape-determining_protein_RodA, rod shape-determining protein RodA. This protein is a member of the FtsW/RodA/SpoVE family (pfam01098). It is found only in species with rod (or spiral) shapes. In many species, mutation of rodA has been shown to correlate with loss of the normal rod shape. Note that RodA homologs are found, scoring below the cutoffs for this model, in a number of both rod-shaped and coccoid bacteria, including four proteins in Bacillus anthracis, for example. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division].	1.19066e-144
LS483377.1\|SQG11970.1\|3794745_3796923_-\|tail-specific-protease	gnl\|CDD\|236873	PRK11186, PRK11186, carboxy terminal-processing peptidase.	0
LS483377.1\|SQG11966.1\|3790408_3791452_+\|Oxidoreductase	gnl\|CDD\|183212	PRK11579, PRK11579, putative oxidoreductase; Provisional.	4.22314e-131
LS483377.1\|SQG11963.1\|3787365_3787806_-\|two-component-system-response-regulator	gnl\|CDD\|381108	cd17557, REC_Rcp-like, phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains. This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	3.4568e-62
LS483377.1\|SQG11964.1\|3787802_3789620_-\|two-component-system-sensor-protein	gnl\|CDD\|226702	COG4251, COG4251, Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms].	5.42392e-57
LS483377.1\|SQG11981.1\|3810004_3810490_-\|Rod-shape-determining-protein-MreD	gnl\|CDD\|225444	COG2891, MreD, Cell shape-determining protein [Cell envelope biogenesis, outer membrane].	7.1233e-30
LS483377.1\|SQG11975.1\|3800868_3802086_-\|D-alanyl-D-alanine-carboxypeptidase	gnl\|CDD\|224600	COG1686, DacC, D-alanyl-D-alanine carboxypeptidase [Cell envelope biogenesis, outer membrane].	7.03159e-149
LS483377.1\|SQG11973.1\|3798905_3799184_-\|lipoate-regulatory-protein-YbeD	gnl\|CDD\|179161	PRK00907, PRK00907, hypothetical protein; Provisional.	1.56476e-63

>LS483377.1|SQG11970.1|3794745_3796923_-|tail-specific-protease
MKFKAPAFLMALALVAPLALAAKADSPALPAAATADQVTTSKLVYGLLSDSRYAYRPRALDEATSKDVFKRYLETLDGGKQYFTQADVARFAPFEANIASAIRGGELEPAFQVFAVYKQRVGERVAYARKLLKQEPDFTTDERFEYDRKKVPWAASSAELDELWRKSVKNDWLRLKLAGKKPDDIRKTLDKRYATLEKSVNELKGEDVFQFFMNSYTSAVDPHTDYFTPRTAENFNQAMSLSLEGIGAQLQRQDDVVVIREIIAGGPAAVDGTLKPGDRIVGVGQGKSGLVEDVIGWRIDDVVAKIRGAKDTQVKLEFIPAAEGADGKHHTLVLTRQKVRLAEQAAKGETMTIPAANGEPARRIGVIKLPTFYQDFEGRRRNAADYASATRDVAKLLAGFKNDKLDGVVLDLRNNGGGSLDEAIELTGLFIEQGPVVQVRESGGRVTVNSDRNQGVAWDGPLAVLINRGSASASEIFAGAIQDYGRGLVIGETSFGKGTVQNIVDLDRWPSGETQRFGQVKLTIAQFFRISGSSTQHKGVVPDLAFPASVDATEFGESTYDNALPWTRIAAVPHTQYGNFAPLLPKLETRHDARIATDKEFQWWNEDVQQFRTEAAKKYISLNEATRRAERERQDTQRKARQVQRKELGLALDPLADDSSDDGLTGNERDIVKDAAREKAAEKRPDPLLRESASILADAVNLLANDRPLSAQVLPQSTGAGRWAD
>LS483377.1|SQG11969.1|3793910_3794501_-|lipoprotein
MRAFRLSSVAVALASALILSACGGRAADSTLLRESFDSGDTFSRTVDGRPGDACEAARRTLLSQGYAIARSDAAQVEGNKNFQPREDDHEQLVLRISCAPRGSQTLVFVSAVQDRYALKKSPTSASVGVGALGSVSLPFGSNDDSLVKVASSTVTDAEFYRRFFQRLQQYLPAEAGKPVPPVVTTPEPAPASTDQD
>LS483377.1|SQG11968.1|3792657_3793914_-|Uncharacterised-protein
MNVRGRWMGVALLLPALGAAATPLDCTQGLLQRLGWHFETRAIGAPQVHGGPVCTRASLPEAQAAGDLRVQWPADMPAAARKALLQQVLDDPATVCAYAFQLGAATQRAAAALQGNAGFRFSGLQLGWIGFGLHGAHAQGWQRTRSFGRGFVPIKGNSQALQAFYSGNVRAECGVGRQVAQLATQRELYGDAAFDAGFSAEELSIGTFLALHDTDSILLGAHAGDFSADGKAVRTSAMGRQAFVGVPGFIEHVYDKGMLDDLSNQAENFVVVSVGEEAAQALAAHGGLAWYDQRNAELWALAQDIPRIGRRYFERLLFERDPDLRARLEPRYHATLARMDRLLDDPFYQQFVIYVHPRGIRPIGYHIARLLDRNPRTPFSIDLAVHNLHTTLYRRWREAQLRHCAATGRPGSLTLDPN
>LS483377.1|SQG11967.1|3791741_3792647_-|6-phosphogluconate-dehydrogenase
MDIAMIGLGRMGANMAQRLHRGGHRVVGYDPGEGARQRAAEAGLEVVDSLAAAVAALPVPRVVWLMVPAGETVDQTLGQLTPHLAEGDILIDGGNSNYQDSIRRAKALAEDELGYVDCGTSGGVWGLQEGYSLMVGGEAAVVEQIAPLLRTLAPAEDRGWGRVGPSGAGHFTKMVHNGIEYGMMQAYAEGFALMERKQEMELDLAQVAEVWRHGSVVRSWLLDLSTEALKRNPSLDGIAPYVEDSGEGRWTVAEAIALDVPAPVITLSLLERLRSRESNSFTDRLLSAMRNEFGGHAIKKS
>LS483377.1|SQG11966.1|3790408_3791452_+|Oxidoreductase
MRPDLQLALIGYGLAGRVFHAPLIQHTPGLVLHSIVSSQRDTLLRAFSDVHVRATPQEVFDDPAVDAVVIATPNEQHAPLAIAALAAGKHVLVDKPFALDVAEAEAVLAAARDAGRIATVFQNRRFDADFLTLQALLADGTLGDIAECHVHFDRYRPQVRDRWREQDGPGSGLWYDLGPHLLDQMLVLFGWPEAIDADLAVQRDGGSAIDYFHAVLHYPRHRAIVHSGSLVAAPTPHFSVHGSKASWTKHGLDVQEAQLRRGVAPGAPGWGIDPRHGELVRCDAEDNVQRGTVDNLPGDYRRLYAQFAAAMHGDCEATVDPVQALQLMRLLQAGMDSAREGRRIALG
>LS483377.1|SQG11965.1|3789854_3790238_-|Osmotically-inducible-protein-OsmY
MSNTTRTLIASALTLGLALSSSAAFAKDPAAKSPPTSAHPATHADRHDSNEPVTDTWITTKVKADLLASSNVPGTEIKVETVNGVVSLSGAVASQAEKDKAVTTAKGIKGVTRVDAAALKVSAAAKR
>LS483377.1|SQG11964.1|3787802_3789620_-|two-component-system-sensor-protein
MALVFSDDIWDRWRLPALALAAAAIIVVPWLTLRKLQQDNEQAMAWVNHTQAVGVALQQLQADVRDVESAALTLSKGVDAPGLRERMAAANDIPGRLAELGRMTRDNPDQLIRIGRIESMLEGRMALARELARSEPNSDQRELVKDLSTRYPIRGLVEELQASEQQLLTLRAEQAARQRKQTELVSWSSLVIQLGLLGLVLWLLQRQIGRRLHAERQSLRSAARAASVLQTVREPIVLLDRDLRVQLHNPAFAELYGLQDERADGLLLENVGDGAWKDAVVRQRLSDVLLRGRELWDFEHEQRTADGMARYMLLNARRMPLPDTDDEVVLLTVSDVTMQRAVQLRVEELNRQLEGKVAQVSEVNRELEAFSYSVSHDLRAPLRHVAGFSDKLSRHLGDAADDKSRHYLDVISSSARRMAALIDDLLVYSRLGRAAMRQQAVDMQSLVADTRAMLDSNLQAEAENSGHVHQVEWSIAPLPIVVGDENMIRQVWLNLLGNAVKYSGNREPAKIRVDYQPQPDGGHQFTVSDNGAGFDMAYAGKLFGVFQRLHKASDYPGTGIGLASVRRVLTRHGGRIWAEAEPDVGATFHFYLPPAIDADKQGPSA
>LS483377.1|SQG11963.1|3787365_3787806_-|two-component-system-response-regulator
MTTLRTILLAEDSPADAEMAIDALEEARLANPIVHVEDGVEVMDYLLRRGAFANREEGLPAVLLLDIKMPRMDGLEVLRQIREHEELKRLPVVILSSSREESDLARSWDMGVNAYVVKPVDVDQFFGAVQTLGKFWALINQAPELE
>LS483377.1|SQG11962.1|3785849_3787361_-|Histidine-kinase/response-regulator-hybrid-protein
MPLTGPALGALRILLVEDSPEDAELMSEQMLEAGLEARFERVESEAELRQALAAFQPDIVLSDLSMPGFSGDDALRIVRETSPEVPFIFVSGTMGEENAVAALQKGANDYIIKHQPARLPSAVARAIRDARSAIERARVETELMRAQRLESLSLLAAGLSHDLRNILQPLLIMPDLLKARTDDPQLHHLADVIAECGRRGHEMAESMLSFVRGSRKPSERIEIDGLFDAVALLLRSNVPDAVRLELQVQDEGLVVDANYTELQQVMLNLALNAIQAMPNGGRLSLTASHAGHRDGVDWMHIRVADEGIGMDADTLSHLFNPFFTTKADGTGLGLISCKRIVEGAGGSIHVSSQPGQGTCFELRLPMHDAIDGSEPIEQLVALGSGQSILVVDGEATRLSLLGNALSSQGYQLQLASDGPAALRWMQQEAMPALVIADAGSKLLPASQLLGEMATLGYRGPALVLEDPAVPVAADAFPDGVEVHVLHKPLQMQQVFRAVAEALG
>LS483377.1|SQG11961.1|3785667_3785850_-|Uncharacterised-protein
MPGSAGRWPASLCGGINAVAGQRPALPFGSLPGEAWQGVHRLLQPLQMQLVFRAVAEALG
>LS483377.1|SQG11972.1|3798207_3798918_-|Octanoate-[acyl-carrier-protein]-protein-N--octanoyltransferase
MDAVADSCPAEAAPEDRAPRPALVRDLGRQAYEPVWRAMQRFTDQRSDTDADELWVVEHDPVFTLGQAGKDEHVLAPGDIPVLHVDRGGQVTYHGPGQIVVYPLLRLPRLGIGVRDYVCRIEQAIIDTLGEWNIGAERREGAPGVYVGGAKIAALGIRVRRGCTFHGLAFNVAMDLEPFHRINPCGYQGLQVTSVVDLGGPSGMEAVKPVLLDHLARQFGLLLQHTPELPDLSAAA
>LS483377.1|SQG11973.1|3798905_3799184_-|lipoate-regulatory-protein-YbeD
MEIKSDNPDHGFQFPGQFELSAMGPANRGLEHELPRLLLAAGIDVVNERISWKHSSNGKYVSVRIVFKAESREQYDLAHQALRDHPEVKWTL
>LS483377.1|SQG11974.1|3799535_3800594_+|outer-membrane-protein
MRSVAALGLAGLLASALPLAAQAAEQCGPDAMRDHPPQINFRVDNDLFGGRHQDQGYTNGALLTLVSPNLVDYTDDPCLPRMARWVNQYLEGLHPGRFEQQNMIFSIGQGIFTPTDFSRRDLIEDDRPYAGVLIANFGFNARSGDRLQTTQLTLGVVGPWAQGKQVQNAVHEVLGDEKFKGWDNQLHNEPLFMLTHERMRRWPGDASVNADGWGWDAISHYGGSIGNLETKANLGGEVRFGWKLPDDFGSTPLRPAGENTAPTRGGRPNGWSWHLFATSDAAWVIRDITLDGNTFRNSHSVDKRHVVAYGGYGVAVMYGRWKFAAARYHSTREFNGQREAPVFGSFTISRSL
>LS483377.1|SQG11975.1|3800868_3802086_-|D-alanyl-D-alanine-carboxypeptidase
MNFRSAATALAATLVVGLASAQTPLPTPATPAPAAAAAPATVATPPAPAPSVSKAWVLMDYATGQVLAGENIHEQLAPASITKVMTSYVIAAEVKNGKVRADDQVMMSERAWREGGAGTDGSYSGFPVNQTARLEDMEKGMAIQSGNDAAIALAEHVAGSEEAFASLMNSYAAKIGMKDSHFVNAHGLTAQGHHSTAYDLALLGRAMVRDYPETYAYNKIKEFQVGNIKQPNRNLLLWRDGSVDGIKTGHTSEAGYCLMSSAQRGDQRLIAVVLGGASEKQRADDSLALLNWGFRFFETHRLYEPGKAVAEHKVWKGTTDKVQLGVAQPMLVSVPRGRYNDLKPSIDVPKTLEAPFTAGQQIGTVKVTLDGKVIAEAPLVAVAAVEQAGFFKRLWDSFWMWWESE
>LS483377.1|SQG11976.1|3802186_3803452_-|lipoprotein-A
MNIRWLVPSLIVFALAACSSAPKKPATAGHGGKSSGTLVQGRGSRPAHCPEGSPYAAAKEDLSTRGNYTAGGLYKPGVRDSTPDYIPNVACIPEPEVTAEERSAIGNKSPYVVLGKSYKVLDDTHDYVERGTASYYGAKFHGRLTSNREVYDMYQFTAAHKTLPLPSFARVTNLDNGESVIVRVNDRGPFHDGRVVDLSYAAAVRLGITQRGTGNVEVRALQPGESNLMAQKPSRRERRAAEAAAATAVASARPAPPRASTDSDIDRLVNRLPTDGAPARGQPATTRGVASTAPDVAVSSLPPSAPVVRNSAPAPAVVASTAPRAVAPAPVRAAAAAPSLSQQMVGAVMVQVASFSNRDNANRAMGQLSAAGIVGATISDIAAGGRTLFRLRVPASDHASAAELAGRIAGLGLGSPQIVKD
>LS483377.1|SQG11977.1|3803448_3804570_-|lytic-murein-transglycosylase-B
MLTLGLVACATQPKSPPSSPQASSTPRQPATKAHGPAEAAPEATAATAPPVDLTPVPFEVARARFIADTAKRYGLKPEQISSVLDQAQVRQPIIAAMSRPAERVKPWNEYRPMFISKARIDGGRAFLAEHRAELDRVQQRTGVPAEVIVAIIGVETSYGKNAGSHRVLDALYTLAFYYPRSGDPAKLEREVRRELFFRDELAKLFELGREEKLDITTLKGSYAGAMGMGQFMPSSYLDYAVDGNGDGRRDLFNSYDDVFSSIANYFVKKGGWVRGGQVAVPATLAPGREEFNPTEWMPTWSLADLAQRGYQPSTPVQPGATATPITLEGSTGKQYWLGFQNYYAITRYNLSKMYAMAVFQLSQAIAGQELPPA
>LS483377.1|SQG11978.1|3805585_3806680_-|Rod-shape-determining-protein-RodA
MEWKRLLGGCREVARTIDLPLLIALLILMGAGLAVLHSVSGPVAGQAARFAGGLTSMWLLSRVSLLRLRAWTPAIYALSLLPLMAVYVIGTGKYGQRWLNLGVFYLQPSELLKLSLPLMMAWYLHRQPLPPSPRTVLTTTVLIGVPAVLILMQPNLGTATLVTASGVFALLLAGLHWGWVATGATGLAVAAPLAWFGLLRQYQKDRVLTFLDPSADPLGTGWNILQSRIAIGSGGWDGRGWGQGTQATLDFLPEYTTDFAFSVLAEEFGWIGVATVFALYLFVVGRCLWIAVHARDTHARLLAGSLGLAFFVYVLVNGGMISGLLPVVGIPMPLISYGGTSAVSLLAGIGLVMAVRGHRPVHGG
>LS483377.1|SQG11979.1|3806816_3807929_-|Rod-shape-determining-protein-RodA
MKVFLRWAGDMLRRFFSTLDWVLCLALGALMVIGLATLKSAGGDGLVMAQGARFAVGMAALWGISRVPILRIRSATPMIYAISMIPLLAVFVLGTGKYGRQWLDLKFFYLQPAELLKVSLPMMVAWYLHKMPLPPRFNTVLVALIIIGVPTGLVMLQPDFGTGVLIAASGVFVLLLAGLPWWWVGLGVGGVAAVAPVAWFWLLRPYQKDRIMMFLDPEMDALGAGWNIIQSKIAIGSGGFDGKGWGEGSQSHLNFIPEQTTDFAFSVLSEEFGWMGVALVLTLYLVVIGRCLWIASQSRDSYSRLLAGATGLAFFVYVLVNGGMISGLLPVVGVPMPLISYGGTSAVSLLAGFGLVMAVRSHNPVHGGYG
>LS483377.1|SQG11980.1|3807925_3810001_-|penicillin-binding-protein-2-(PBP-2)
MIPRRQVKNPHAEAEQFRRRAALGFLGVLVCLLGLGGWYFKLQVLDHDVYATRSEANRIKPRPVVPGRGMIYDRNGRLLAENVPAFRLDVTPDKVKDMDATLEGLAKIISISPEELEAFNKSRKARRKFLPVTLKLRMSDEEMARFAVDRWRFPGVELEPYLTRRYPYGDLFAHIIGYVGRVDDKDLEILGEGNAALTHIGKSGLERYYEQQLRGKVGYEQVETNVQGRAIRTIGRVAAQSGADLRLSIDADLQRAMVAAFGDQEGSAVAMDPRTGEVLAMVSLPSYDPNLFVNGISHADFKALNENPSRPQFNRLVLGGVAPGSTLKPLIGLAGLDSGVRRPEDKVLSTGMFYLPGTSRGWGDAHRGGHGWTDLRKSIAESVNTYYYKLALDLGIERFDHYMEYYGFGQPTGIDLTGEIGGILPSPAYKRKTRKEAWYPGDTVNISIGQGDWKVTPLQLARGVSALADGQLRTPHLVIQQRDGFDSDWTATPPGESKPVSPNPNNVQAVREGMMATMRPGGSGWRVAVGAPYVMAGKTGTAQVISRKGTAAVNPKSLPMHLRHRALFVGFAPVENPVIAIAVAVEGGGYGGSAAAPIARKVFDAYLLGKMPEGMQPLDSERGTTAIGAIAFDNEDAGARQAGDLAAAQLGEHPVQVGAPAPEPAPAPQPGTPAAAAVPATPRPTVAEPAR
>LS483377.1|SQG11981.1|3810004_3810490_-|Rod-shape-determining-protein-MreD
MSRLRDNPWVLPASLVVALLLGLLPLPALLQPLRPYWLALVLAYWVIETPERVGLGIAFASGVVADLLYGGVLGEQALRLVMLAFILQRFRARIRFFPMSQQMLAIGGLLFNDRIVSALVHILVGEPTLPWSYWWAPLLGMGLWPLVFVLLDAVRFGKRGR

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

Click the colored protein region to show detailed information

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
LS483377_7	7.1\|3560968\|29\|LS483377\|PILER-CR	3560968-3560996	29	MN234214	Arthrobacter phage Amelia, complete genome	25754-25782	7	0.759
LS483377_7	7.2\|3561029\|33\|LS483377\|PILER-CR	3561029-3561061	33	NZ_CP035508	Haematobacter massiliensis strain OT1 plasmid pOT1-8, complete sequence	40207-40239	8	0.758
LS483377_7	7.2\|3561029\|33\|LS483377\|PILER-CR	3561029-3561061	33	NZ_CP029362	Streptomyces globisporus strain TFH56 plasmid pTFSG1, complete sequence	62538-62570	9	0.727
LS483377_7	7.2\|3561029\|33\|LS483377\|PILER-CR	3561029-3561061	33	NZ_CP013739	Streptomyces globisporus C-1027 plasmid SGLP1, complete sequence	58536-58568	9	0.727
LS483377_7	7.2\|3561029\|33\|LS483377\|PILER-CR	3561029-3561061	33	NZ_CP014942	Rhodococcus sp. BH4 plasmid, complete sequence	632003-632035	10	0.697

1. spacer 7.1|3560968|29|LS483377|PILER-CR matches to MN234214 (Arthrobacter phage Amelia, complete genome) position: , mismatch: 7, identity: 0.759

aatgcatccgccgggcacagccccgcgct	CRISPR spacer
ttcgcgtccgccggccacagccccgcgag	Protospacer
  .**.******** ************

2. spacer 7.2|3561029|33|LS483377|PILER-CR matches to NZ_CP035508 (Haematobacter massiliensis strain OT1 plasmid pOT1-8, complete sequence) position: , mismatch: 8, identity: 0.758

gccccgtgccgaccaaggtcggcacctgccaaa	CRISPR spacer
ggcagtcgcagacgaaggtcggcacctgccaga	Protospacer
* *   .** *** *****************.*

3. spacer 7.2|3561029|33|LS483377|PILER-CR matches to NZ_CP029362 (Streptomyces globisporus strain TFH56 plasmid pTFSG1, complete sequence) position: , mismatch: 9, identity: 0.727

gccccgtgccgaccaaggtcggcacctgccaaa	CRISPR spacer
cctccgtgctgacccaggtcggcacctacatgc	Protospacer
 *.******.**** ************.*  .

4. spacer 7.2|3561029|33|LS483377|PILER-CR matches to NZ_CP013739 (Streptomyces globisporus C-1027 plasmid SGLP1, complete sequence) position: , mismatch: 9, identity: 0.727

gccccgtgccgaccaaggtcggcacctgccaaa	CRISPR spacer
cctccgtgctgacccaggtcggcacctacatgc	Protospacer
 *.******.**** ************.*  .

5. spacer 7.2|3561029|33|LS483377|PILER-CR matches to NZ_CP014942 (Rhodococcus sp. BH4 plasmid, complete sequence) position: , mismatch: 10, identity: 0.697

gccccgtgccgaccaaggtcggcacctgccaaa	CRISPR spacer
ctcccgggccgatcaaggtcggcacccattcac	Protospacer
 .**** *****.*************.... *

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

7438 : 58061

Bacillus_phage(18.18%)

transposase,protease

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
SQG08579.1\|7438_8284_+\|protease	transmembrane protease	NA	NA	NA	NA
SQG08580.1\|8355_9162_+\|protease	Zn-dependent protease with chaperone function	NA	NA	NA	NA
SQG08581.1\|9294_10482_+	TPR domain-containing protein	NA	NA	NA	NA
SQG08582.1\|10625_11294_+	TonB family protein	NA	NA	NA	NA
SQG08583.1\|11388_12150_+	motA/TolQ/ExbB proton channel family protein	NA	NA	NA	NA
SQG08584.1\|12212_12638_+	biopolymer transport protein ExbD/TolR	NA	NA	NA	NA
SQG08585.1\|12641_13055_+	biopolymer transport protein ExbD/TolR	NA	NA	NA	NA
SQG08586.1\|13123_14617_+	phospholipase D/transphosphatidylase	NA	NA	NA	NA
SQG08587.1\|14657_14927_+	Uncharacterised protein	NA	NA	NA	NA
SQG08588.1\|14936_15680_+	pyridoxine 5'-phosphate synthase	NA	NA	NA	NA
SQG08589.1\|15781_16873_+	radical SAM protein	NA	NA	NA	NA
SQG08590.1\|17012_17621_+	Uncharacterised protein	NA	NA	NA	NA
SQG08591.1\|17705_18239_+	Uncharacterised protein	NA	NA	NA	NA
SQG08592.1\|18590_18773_+	Uncharacterised protein	NA	NA	NA	NA
SQG08593.1\|19993_20704_-	Uncharacterised protein	V5UTP7	Synechococcus_phage	1.7e-15	46.4
SQG08594.1\|20812_21829_-	Fructose-1,6-bisphosphatase, type I	A0A1V0SKX4	Klosneuvirus	2.4e-47	36.1
SQG08595.1\|21956_22124_-	Uncharacterised protein	NA	NA	NA	NA
SQG08596.1\|22243_23446_-	aromatic-amino-acid aminotransferase	NA	NA	NA	NA
SQG08597.1\|23617_25711_+	tonB-dependent receptor yncD precursor	A0A1B0VCF0	Salmonella_phage	8.8e-73	41.0
SQG08598.1\|25867_26206_-	Uncharacterised protein	NA	NA	NA	NA
SQG08599.1\|26354_26753_+	Uncharacterised protein	NA	NA	NA	NA
SQG08600.1\|26917_27838_+	Ku domain-containing protein	NA	NA	NA	NA
SQG08601.1\|27841_30328_+	ATP-dependent DNA ligase	A0A068CDF3	Rhizobium_phage	1.6e-49	38.4
SQG08602.1\|30399_30792_-	transmembrane protein	NA	NA	NA	NA
SQG08603.1\|30959_31988_-	alcohol dehydrogenase	A0A2K9L339	Tupanvirus	4.4e-33	29.2
SQG08604.1\|32084_32723_-	4-hydroxy-2-ketovalerate aldolase	NA	NA	NA	NA
SQG08605.1\|32836_33493_-	cysteine dioxygenase type I	NA	NA	NA	NA
SQG08606.1\|33680_34721_+	LacI family transcriptional regulator	C6ZCU4	Enterobacteria_phage	9.5e-28	26.1
SQG08607.1\|34831_35725_-	phenylalanine-4-hydroxylase	NA	NA	NA	NA
SQG08608.1\|35850_36336_+	AsnC family transcriptional regulator	NA	NA	NA	NA
SQG08609.1\|36375_37368_-\|protease	Serine protease	A0A1X7QFZ0	Faustovirus	2.8e-05	25.9
SQG08610.1\|37801_38818_-	Protein of uncharacterised function DUF124	NA	NA	NA	NA
SQG08611.1\|38975_41246_+	TonB-dependent receptor	NA	NA	NA	NA
SQG08612.1\|41358_42198_-	Nonspecific acid phosphatase precursor	NA	NA	NA	NA
SQG08613.1\|42460_43339_+	Uncharacterised protein	NA	NA	NA	NA
SQG08614.1\|43350_44553_+	Uncharacterised protein	NA	NA	NA	NA
SQG08615.1\|44704_45649_-\|transposase	transposase	NA	NA	NA	NA
SQG08616.1\|45868_46699_-	ABC transporter-like protein	NA	NA	NA	NA
SQG08617.1\|46789_47668_-	Uncharacterised protein	NA	NA	NA	NA
SQG08618.1\|47884_49087_+	fatty acid desaturase	NA	NA	NA	NA
SQG08619.1\|49083_49416_+	calcium-binding protein	NA	NA	NA	NA
SQG08620.1\|49435_50248_+	formamidopyrimidine-DNA glycosylase	A0A127AWE5	Bacillus_phage	1.3e-16	27.2
SQG08621.1\|50449_51958_+	glucans biosynthesis protein D precursor	NA	NA	NA	NA
SQG08622.1\|52509_53130_-	thymidine kinase	A0A289ZTU3	Serratia_phage	1.3e-51	52.4
SQG08623.1\|53139_53871_-	Sel1 domain-containing protein repeat-containing protein	NA	NA	NA	NA
SQG08624.1\|53910_54639_-	Sel1 domain-containing protein repeat-containing protein	NA	NA	NA	NA
SQG08625.1\|54687_56715_+	ATP-dependent DNA helicase Rep	A7KV33	Bacillus_phage	3.8e-113	38.1
SQG08626.1\|56910_57204_+\|transposase	ISXac3 like transposase	NA	NA	NA	NA
SQG08627.1\|57458_58061_+\|transposase	transposase	U5P429	Shigella_phage	1.5e-33	44.9

DBSCAN-SWA_2

578454 : 587008

Escherichia_phage(25.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SQG09090.1\|578454_579513_+	dTDP-glucose 4,6-dehydratase	A0A1D7XFE8	Escherichia_phage	6.6e-77	44.7
SQG09091.1\|579527_580415_+	glucose-1-phosphate thymidylyltransferase	I7I009	Enterobacteria_phage	1.6e-95	58.2
SQG09092.1\|580411_580969_+	dTDP-4-dehydrorhamnose 3,5-epimerase	I7HJC4	Enterobacteria_phage	3.0e-44	49.4
SQG09093.1\|580965_581883_+	dTDP-4-dehydrorhamnose reductase	A0A1D7XFA3	Escherichia_phage	4.9e-28	36.9
SQG09094.1\|581947_582934_-	Uncharacterized protein conserved in bacteria	A0A2H4JA46	uncultured_Caudovirales_phage	4.8e-21	29.8
SQG09095.1\|583056_584460_-	mannose-1-phosphate guanylyltransferase	A0A1V0SH58	Hokovirus	2.9e-40	27.5
SQG09096.1\|584471_585818_-	phosphoglucomutase	A0A127AWJ1	Bacillus_phage	5.9e-30	26.7
SQG09097.1\|585946_587008_+	NAD-dependent epimerase/dehydratase	A0A2K9KZK0	Tupanvirus	7.5e-89	48.1

DBSCAN-SWA_3

952297 : 1033106

Escherichia_phage(18.52%)

tail,transposase,plate,integrase,protease

attL 981696:981714|attR 1040256:1040274

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SQG09419.1\|952297_952924_+\|protease	ATP-dependent Clp protease proteolytic subunit	A0A223W000	Agrobacterium_phage	7.7e-57	57.4
SQG09420.1\|953050_954340_+\|protease	ATP-dependent Clp protease ATP-binding subunit ClpX	G3M9Z9	Bacillus_virus	2.9e-135	58.0
SQG09421.1\|954483_956931_+	anti-sigma H sporulation factor LonB	A0A0R6PGP8	Moraxella_phage	1.9e-220	51.9
SQG09422.1\|957148_957421_+	DNA-binding protein HU-alpha	A7KV42	Bacillus_phage	4.5e-22	62.9
SQG09423.1\|958262_960218_+	peptidyl-prolyl cis-trans isomerase ppiD	NA	NA	NA	NA
SQG09424.1\|960430_961630_-	lytic transglycosylase	NA	NA	NA	NA
SQG09425.1\|961626_962391_-	Hydroxyacylglutathione hydrolase	NA	NA	NA	NA
SQG09426.1\|962402_963053_+	SAM-dependent methyltransferase	NA	NA	NA	NA
SQG09427.1\|963066_963519_+	ribonuclease HI	J9Q745	Salmonella_phage	1.0e-42	53.4
SQG09428.1\|963523_964255_+	DNA polymerase III subunit epsilon	A0A1B2LRV5	Wolbachia_phage	3.8e-07	42.4
SQG09429.1\|964366_965071_-	protein phosphatase	NA	NA	NA	NA
SQG09430.1\|965746_968761_-	autotransporter	NA	NA	NA	NA
SQG09431.1\|969052_969457_+	Uncharacterised protein	A0A1C9C5K8	Heterosigma_akashiwo_virus	1.3e-17	35.3
SQG09432.1\|969535_970561_-	ADP-heptose--lipooligosaccharide heptosyltransferase II	NA	NA	NA	NA
SQG09433.1\|970575_971352_+	3-deoxy-D-manno-octulosonic acid kinase	NA	NA	NA	NA
SQG09434.1\|971351_972119_+	beta-lactamase domain-containing protein	NA	NA	NA	NA
SQG09435.1\|972115_972505_+	Uncharacterized protein conserved in bacteria	NA	NA	NA	NA
SQG09436.1\|972980_973298_+	quaternary ammonium compound-resistance protein sugE	NA	NA	NA	NA
SQG09437.1\|973656_984561_+	glycine-rich autotransporter protein	NA	NA	NA	NA
981696:981714	attL	NA	NA	NA	NA
SQG09438.1\|984617_985274_-	acetyltransferase	NA	NA	NA	NA
SQG09439.1\|985400_985811_+	Protein of uncharacterised function (DUF3592)	NA	NA	NA	NA
SQG09440.1\|986384_988436_+	DNA polymerase III subunits gamma and tau	A0A1U9WR94	Streptococcus_virus	2.1e-47	41.4
SQG09441.1\|988442_988763_+	DNA-binding protein, YbaB/EbfC family	NA	NA	NA	NA
SQG09442.1\|988874_989474_+	Recombination protein RecR	NA	NA	NA	NA
SQG09443.1\|989541_989901_+	bis(5'-nucleosyl)-tetraphosphatase	NA	NA	NA	NA
SQG09444.1\|989981_990509_-	Starvation lipoprotein Slp	NA	NA	NA	NA
SQG09445.1\|990505_992455_-	transmembrane transglutaminase	NA	NA	NA	NA
SQG09446.1\|992447_993392_-	transmembrane protein	NA	NA	NA	NA
SQG09447.1\|993394_994348_-	ATPase	NA	NA	NA	NA
SQG09448.1\|994390_996232_+	transmembrane protein	NA	NA	NA	NA
SQG09449.1\|996405_997350_+\|transposase	transposase	NA	NA	NA	NA
SQG09450.1\|997490_998060_-	Maf-like protein	NA	NA	NA	NA
SQG09451.1\|998212_998683_+	characterised ACR protein	NA	NA	NA	NA
SQG09452.1\|998790_998985_+	50S ribosomal protein L32	NA	NA	NA	NA
SQG09453.1\|999076_1000054_+	3-oxoacyl-[acyl-carrier-protein] synthase,KASIII	NA	NA	NA	NA
SQG09454.1\|1000132_1000915_+	Mn2-dependent serine/threonine protein kinase	NA	NA	NA	NA
SQG09455.1\|1001171_1002116_+	malonyl CoA-ACP transacylase	NA	NA	NA	NA
SQG09456.1\|1002198_1002942_+	3-oxoacyl-ACP reductase	Q06VL0	Trichoplusia_ni_ascovirus	4.7e-13	32.3
SQG09457.1\|1003094_1003334_+	acyl carrier protein	B2ZXV3	Ralstonia_phage	4.6e-10	44.6
SQG09458.1\|1003477_1004740_+	3-oxoacyl-ACP synthase	NA	NA	NA	NA
SQG09459.1\|1004919_1006284_+	Para-aminobenzoate synthase, aminase component	NA	NA	NA	NA
SQG09460.1\|1006482_1007544_+	protein YceG like	NA	NA	NA	NA
SQG09461.1\|1007540_1008206_+	thymidylate kinase	W8D0J5	Erwinia_phage	1.6e-20	35.0
SQG09462.1\|1008202_1009159_+	DNA polymerase III subunit delta'	NA	NA	NA	NA
SQG09463.1\|1009155_1009509_+	type IV pilus assembly protein PilZ	NA	NA	NA	NA
SQG09464.1\|1009785_1010076_+	Uncharacterised protein	NA	NA	NA	NA
SQG09465.1\|1010150_1010345_+	Uncharacterised protein	NA	NA	NA	NA
SQG09466.1\|1010692_1010872_+	Uncharacterized small protein	NA	NA	NA	NA
SQG09467.1\|1010996_1011572_+	Uncharacterised protein	NA	NA	NA	NA
SQG09468.1\|1011587_1011716_-\|tail	phage tail assembly protein I	NA	NA	NA	NA
SQG09469.1\|1012079_1012643_-	Uncharacterised protein	NA	NA	NA	NA
SQG09470.1\|1012695_1013103_-	Uncharacterised protein	NA	NA	NA	NA
SQG09471.1\|1013663_1014044_+	4-oxalocrotonate tautomerase	NA	NA	NA	NA
SQG09472.1\|1014074_1015148_-	late control D family protein	D5LGY1	Escherichia_phage	8.4e-96	52.2
SQG09473.1\|1015138_1015354_-\|tail	phage tail protein	A0A193GYC8	Enterobacter_phage	1.6e-14	54.3
SQG09474.1\|1015337_1015805_-\|tail	phage tail protein	A0A218M4I2	Erwinia_phage	1.1e-15	35.2
SQG09475.1\|1015807_1018255_-\|tail	bacteriophage tail protein	A0A1W6JT50	Escherichia_phage	9.4e-26	22.8
SQG09476.1\|1018375_1018666_-	Uncharacterised protein	A0A193GYZ8	Enterobacter_phage	1.5e-18	58.5
SQG09477.1\|1018746_1019250_-\|tail	major tail tube protein	A0A193GYM4	Enterobacter_phage	1.4e-40	51.2
SQG09478.1\|1019252_1020455_-\|tail	bacteriophage major tail sheath protein	A0A088FVH5	Escherichia_phage	6.1e-127	54.2
SQG09479.1\|1020561_1021221_-	Uncharacterised protein	V9IQM3	Stenotrophomonas_phage	6.2e-17	30.4
SQG09480.1\|1021222_1023424_-\|tail	phage tail protein	V9IQX0	Stenotrophomonas_phage	1.5e-115	40.2
SQG09481.1\|1023431_1024211_-\|tail	bacteriophage tail protein I	V9IQK7	Stenotrophomonas_phage	7.1e-44	51.1
SQG09482.1\|1024203_1025100_-\|plate	phage baseplate assembly protein	V5YTH6	Pseudomonas_phage	3.2e-80	56.1
SQG09483.1\|1025102_1025441_-\|plate	phage baseplate assembly protein	A0A193GYY8	Enterobacter_phage	7.8e-32	62.2
SQG09484.1\|1025493_1026084_-\|plate	baseplate assembly protein	A0A193GYL5	Enterobacter_phage	3.6e-24	37.7
SQG09485.1\|1026080_1026635_-	phage-like protein	NA	NA	NA	NA
SQG09486.1\|1026988_1027366_-	Uncharacterised protein	NA	NA	NA	NA
SQG09487.1\|1027362_1027848_-	endolysin/phage lysozyme	D5LH07	Escherichia_phage	3.2e-42	55.6
SQG09488.1\|1027844_1028195_-	Uncharacterised protein	NA	NA	NA	NA
SQG09489.1\|1028191_1028641_-	Mor transcription activator family	NA	NA	NA	NA
SQG09490.1\|1028975_1029359_-	Uncharacterised protein	NA	NA	NA	NA
SQG09491.1\|1029511_1030150_-	phage-like protein	A0A2H4J8A1	uncultured_Caudovirales_phage	5.8e-20	37.6
SQG09492.1\|1030191_1030419_-	Uncharacterised protein	NA	NA	NA	NA
SQG09493.1\|1030493_1030769_-	regulatory protein	NA	NA	NA	NA
SQG09494.1\|1030769_1033106_-\|integrase	phage integrase	D5LH15	Escherichia_phage	9.6e-137	43.3
1040256:1040274	attR	NA	NA	NA	NA

DBSCAN-SWA_4

1925854 : 1941223

Pseudomonas_phage(33.33%)

portal,tail,lysis,capsid,terminase,head

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SQG10319.1\|1925854_1926553_-	Peptidase S24-like	A0A1B5FPF4	Escherichia_phage	1.0e-09	33.0
SQG10320.1\|1926860_1927115_+	CI repressor	NA	NA	NA	NA
SQG10321.1\|1927224_1927755_+	Uncharacterised protein	B7SYH6	Stenotrophomonas_phage	6.1e-39	46.2
SQG10322.1\|1927751_1928063_+	Uncharacterised protein	NA	NA	NA	NA
SQG10323.1\|1928483_1928954_+	Uncharacterised protein	A0A248SL49	Klebsiella_phage	1.0e-13	41.7
SQG10324.1\|1928943_1929606_+	Uncharacterised protein	A0A1B0VMD9	Pseudomonas_phage	8.2e-25	37.8
SQG10325.1\|1929602_1929797_+	Uncharacterised protein	NA	NA	NA	NA
SQG10326.1\|1929796_1930165_+	Uncharacterised protein	NA	NA	NA	NA
SQG10327.1\|1930161_1930365_+	Uncharacterised protein	NA	NA	NA	NA
SQG10328.1\|1930435_1931152_+	Uncharacterised protein	C8CLH7	Xylella_phage	4.7e-50	49.1
SQG10329.1\|1931246_1931465_-	Uncharacterised protein	NA	NA	NA	NA
SQG10330.1\|1931594_1932083_+	lysozyme	D5LH07	Escherichia_phage	4.6e-65	76.4
SQG10331.1\|1932079_1932394_+	Uncharacterised protein	NA	NA	NA	NA
SQG10332.1\|1932390_1932867_+\|lysis	bacteriophage lysis protein	NA	NA	NA	NA
SQG10333.1\|1932863_1933208_+	Uncharacterised protein	A0A2H4J7A6	uncultured_Caudovirales_phage	2.1e-40	66.7
SQG10334.1\|1933370_1933634_+	Uncharacterised protein	NA	NA	NA	NA
SQG10335.1\|1933633_1934032_+	HNH endonuclease	A0A2H4PHY5	Pseudomonas_phage	2.4e-11	49.3
SQG10336.1\|1934114_1934495_+\|terminase	Phage terminase, small subunit	Q9XJT7	Pseudomonas_phage	8.0e-33	57.1
SQG10337.1\|1934498_1936169_+\|terminase	terminase	A0A0U4B0C7	Pseudomonas_phage	3.9e-225	69.2
SQG10338.1\|1936168_1937473_+\|portal	phage portal protein, HK97 family	C7BGG8	Burkholderia_phage	1.2e-59	37.1
SQG10339.1\|1937435_1938197_+	peptidase S14 ClpP	C7BGG9	Burkholderia_phage	3.5e-48	50.3
SQG10340.1\|1938265_1939510_+\|capsid	phage major capsid protein, HK97 family	C7BGH0	Burkholderia_phage	4.8e-95	47.1
SQG10341.1\|1939567_1939972_+	Uncharacterised protein	NA	NA	NA	NA
SQG10342.1\|1939975_1940398_+\|head,tail	Phage gp6-like head-tail connector protein	NA	NA	NA	NA
SQG10343.1\|1940394_1940727_+\|head,tail	Bacteriophage head-tail adaptor	B5WZS5	Pseudomonas_phage	1.5e-11	35.5
SQG10344.1\|1940719_1941223_+	phage protein, HK97 gp10 family	A4JX05	Burkholderia_virus	1.3e-09	32.5

DBSCAN-SWA_5

2231749 : 2237337

Stenotrophomonas_phage(83.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SQG10601.1\|2231749_2232109_+	phage-like protein	Q38057	Xanthomonas_phage	9.9e-25	49.1
SQG10602.1\|2232655_2233876_-	Zonula occludens toxin	B1NI81	Stenotrophomonas_phage	4.4e-40	30.1
SQG10603.1\|2233872_2234157_-	Protein of uncharacterised function (DUF2523)	NA	NA	NA	NA
SQG10604.1\|2234156_2235056_-	Uncharacterised protein	Q4LAU2	Stenotrophomonas_phage	4.0e-14	68.0
SQG10605.1\|2235175_2235313_-	Uncharacterised protein	NA	NA	NA	NA
SQG10606.1\|2235336_2235528_-	Uncharacterised protein	NA	NA	NA	NA
SQG10607.1\|2235531_2235834_-	Uncharacterised protein	B1NI78	Stenotrophomonas_phage	8.0e-36	73.5
SQG10608.1\|2235840_2236947_-	phage replication protein NMA0782	S0F3I3	Stenotrophomonas_phage	1.0e-192	87.0
SQG10609.1\|2237109_2237337_-	Uncharacterised protein	S0F3S0	Stenotrophomonas_phage	6.9e-08	43.9

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. LS483377

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection