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
CP020918	Flavobacterium faecale strain WV33 chromosome, complete genome	9 crisprs	DEDDh,RT,cas3,PD-DExK,csa3,WYL,cas9,cas1,cas2	0	21	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: CP020918_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP020918_1

469806-469947

Orphan

Consensus_repeat	Method
TATTCCCCCTAGCCCCCGAAGGGGGAACTCCTAGATTGTGGAAAATTTATGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP020918_1

>merge|CP020918|1|469806-469947|CRISPRCasFinder
TATTCCCCCTAGCCCCCGAAGGGGGAACTCCTAGATTGTGGAAAATTTATGGGGGAATATATTCGATTCAGTGTCGACTGGTACGGTGCTATTCCCCCTAGCCCCCGAAGGGGGAACTCCTTGATTGTGGAAAATTTATGGG

>CP020918|1|1|469806-469947|CRISPRCasFinder
TATTCCCCCTAGCCCCCGAAGGGGGAACTCCTAGATTGTGGAAAATTTATGGG	GGAATATATTCGATTCAGTGTCGACTGGTACGGTGC
TATTCCCCCTAGCCCCCGAAGGGGGAACTCCTTGATTGTGGAAAATTTATGGG

Protein	Signature genes	Signature genes Name	Protein_function
CP020918.1\|AWG20408.1\|465890_466490_+\|thiamine-phosphate-synthase	unknown	unknown	gnl\|CDD\|238317
CP020918.1\|AWG20421.1\|476946_479433_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379720
CP020918.1\|AWG20410.1\|467210_467852_+\|thiamine-phosphate-diphosphorylase	unknown	unknown	gnl\|CDD\|238317
CP020918.1\|AWG20407.1\|464028_465852_+\|phosphomethylpyrimidine-synthase-ThiC	unknown	unknown	gnl\|CDD\|236451
CP020918.1\|AWG20409.1\|466462_467218_+\|hydroxymethylpyrimidine/phosphomethylpyrimidine-kinase	unknown	unknown	gnl\|CDD\|238574
CP020918.1\|AWG20417.1\|473340_474072_+\|phosphatidic-acid-phosphatase	unknown	unknown	gnl\|CDD\|239488
CP020918.1\|AWG20413.1\|470103_470814_+\|thiamine-biosynthesis-protein-ThiF	unknown	unknown	gnl\|CDD\|238386
CP020918.1\|AWG23534.1\|461955_462087_+\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG20405.1\|462235_462805_+\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG20403.1\|460514_460814_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|315630
CP020918.1\|AWG20418.1\|474124_475084_-\|fasciclin	unknown	unknown	gnl\|CDD\|367095
CP020918.1\|AWG20406.1\|463677_463884_+\|thiamine-biosynthesis-protein-ThiS	unknown	unknown	gnl\|CDD\|340451
CP020918.1\|AWG20415.1\|471634_472276_-\|leucyl/phenylalanyl-tRNA--protein-transferase	unknown	unknown	gnl\|CDD\|234720
CP020918.1\|AWG20416.1\|472294_473212_-\|glutaminase	unknown	unknown	gnl\|CDD\|274797
CP020918.1\|AWG20414.1\|471263_471512_-\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG20419.1\|475103_475988_-\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG20404.1\|460843_461752_-\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG20411.1\|467832_468609_+\|thiazole-synthase	unknown	unknown	gnl\|CDD\|234687
CP020918.1\|AWG20422.1\|479575_480391_-\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|131350
CP020918.1\|AWG20420.1\|476326_476695_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378639

Protein	Function_ID	Function_description	E-value
CP020918.1\|AWG20408.1\|465890_466490_+\|thiamine-phosphate-synthase	gnl\|CDD\|238317	cd00564, TMP_TenI, Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.	2.41916e-25
CP020918.1\|AWG20421.1\|476946_479433_-\|TonB-dependent-receptor	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	2.74549e-70
CP020918.1\|AWG20410.1\|467210_467852_+\|thiamine-phosphate-diphosphorylase	gnl\|CDD\|238317	cd00564, TMP_TenI, Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.	4.15936e-58
CP020918.1\|AWG20407.1\|464028_465852_+\|phosphomethylpyrimidine-synthase-ThiC	gnl\|CDD\|236451	PRK09284, PRK09284, thiamine biosynthesis protein ThiC; Provisional.	0
CP020918.1\|AWG20409.1\|466462_467218_+\|hydroxymethylpyrimidine/phosphomethylpyrimidine-kinase	gnl\|CDD\|238574	cd01169, HMPP_kinase, 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.	3.095e-62
CP020918.1\|AWG20413.1\|470103_470814_+\|thiamine-biosynthesis-protein-ThiF	gnl\|CDD\|238386	cd00757, ThiF_MoeB_HesA_family, ThiF_MoeB_HesA. Family of E1-like enzymes involved in molybdopterin and thiamine biosynthesis family. The common reaction mechanism catalyzed by MoeB and ThiF, like other E1 enzymes, begins with a nucleophilic attack of the C-terminal carboxylate of MoaD and ThiS, respectively, on the alpha-phosphate of an ATP molecule bound at the active site of the activating enzymes, leading to the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD and ThiS. MoeB, as the MPT synthase (MoaE/MoaD complex) sulfurase, is involved in the biosynthesis of the molybdenum cofactor, a derivative of the tricyclic pterin, molybdopterin (MPT). ThiF catalyzes the adenylation of ThiS, as part of the biosynthesis pathway of thiamin pyrophosphate (vitamin B1). .	3.05016e-116
CP020918.1\|AWG20403.1\|460514_460814_+\|hypothetical-protein	gnl\|CDD\|315630	pfam12987, DUF3871, Domain of unknown function, B. Theta Gene description (DUF3871). Based on Bacteroides thetaiotaomicron gene BT_2984, a putative uncharacterized protein As seen in gene expression experiments (http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE2231). It appears to be upregulated in the presence of host or other bacterial species vs when in culture.	5.09126e-44
CP020918.1\|AWG20418.1\|474124_475084_-\|fasciclin	gnl\|CDD\|367095	pfam02469, Fasciclin, Fasciclin domain. This extracellular domain is found repeated four times in grasshopper fasciclin I as well as in proteins from mammals, sea urchins, plants, yeast and bacteria.	2.87946e-26
CP020918.1\|AWG20406.1\|463677_463884_+\|thiamine-biosynthesis-protein-ThiS	gnl\|CDD\|340451	cd00565, Ubl_ThiS, ubiquitin-like (Ubl) domain found in sulfur carrier protein ThiS. ThiS, also termed Thiamine biosynthesis protein (ThiaminS), is a sulfur carrier protein involved in thiamin biosynthesis in prokaryotes. It has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub), and is activated in an ATP-dependent manner by sulfurtransferases, similar to the activation mechanism of Ub-activating enzyme E1. ThiS has common evolutionary origin with Ub-related protein modifiers in eukaryotes, a beta-grasp fold as Ub, and is closely related to proteins MoaD and Urm1.	4.31447e-11
CP020918.1\|AWG20417.1\|473340_474072_+\|phosphatidic-acid-phosphatase	gnl\|CDD\|239488	cd03394, PAP2_like_5, PAP2_like_5 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.	8.56958e-25
CP020918.1\|AWG20416.1\|472294_473212_-\|glutaminase	gnl\|CDD\|274797	TIGR03814, Glutaminase_1, glutaminase A. This family describes the enzyme glutaminase, from a larger family that includes serine-dependent beta-lactamases and penicillin-binding proteins. Many bacteria have two isozymes. This model is based on selected known glutaminases and their homologs within prokaryotes, with the exclusion of highly-derived (long branch) and architecturally varied homologs, so as to achieve conservative assignments. A sharp drop in scores occurs below 250, and cutoffs are set accordingly. The enzyme converts glutamine to glutamate, with the release of ammonia. Members tend to be described as glutaminase A (glsA), where B (glsB) is unknown and may not be homologous (as in Rhizobium etli). Some species have two isozymes that may both be designated A (GlsA1 and GlsA2). [Energy metabolism, Amino acids and amines].	9.00763e-156
CP020918.1\|AWG20422.1\|479575_480391_-\|AraC-family-transcriptional-regulator	gnl\|CDD\|131350	TIGR02297, AraC-type_DNA-binding_domain-containing_protein, 4-hydroxyphenylacetate catabolism regulatory protein HpaA. This putative transcriptional regulator, which contains both the substrate-binding, dimerization domain (pfam02311) and the helix-turn-helix DNA-binding domain (pfam00165) of the AraC famil, is located proximal to genes of the 4-hydroxyphenylacetate catabolism pathway.	1.03e-23
CP020918.1\|AWG20415.1\|471634_472276_-\|leucyl/phenylalanyl-tRNA--protein-transferase	gnl\|CDD\|234720	PRK00301, aat, leucyl/phenylalanyl-tRNA--protein transferase; Reviewed.	4.67421e-125
CP020918.1\|AWG20411.1\|467832_468609_+\|thiazole-synthase	gnl\|CDD\|234687	PRK00208, thiG, thiazole synthase; Reviewed.	2.55428e-157
CP020918.1\|AWG20420.1\|476326_476695_-\|hypothetical-protein	gnl\|CDD\|378639	pfam11325, DUF3127, Domain of unknown function (DUF3127). This bacterial family of proteins has no known function. However, it does show distant similarity to pfam00436, with proteins such as Prevotella buccalis HMPREF0650_0099 being similar to both families. This suggests that this family may have a DNA-binding function.	1.36108e-41

>CP020918.1|AWG20411.1|467832_468609_+|thiazole-synthase
MDTSLFKIGNKELSSRLFLGTGKFGSNSQMAEAILASESELVTVALKRIDLETDTDAILSHLKHPRINLLPNTSGARTAKEAIFAAQLAREALETNWLKLEIHPDPKYLMPDAIETLRATEELAKLGFIVLPYIHADPVLCKRLEDAGTAAVMPLGSPIGTNKGLKTIDFLEIIIEQSKVPVIIDAGIGAPSDAAKAMELGADAVLVNTAIAVAGNPKLMAEAFKEAVIAGRKAFEAKLGQQYKHAVASSPLTAFLYE
>CP020918.1|AWG20410.1|467210_467852_+|thiamine-phosphate-diphosphorylase
MLNRLQYISQGATIEDQLFNIHQALDHGCDWVQMRFKTAESTTELLKLAEATKMLCDEYLATFIINDAVLLAHEVDADGVHLGLTDMGIPEARSILGTSKIIGGTANTLEDILLHVSNGCDYVGLGPFRYTKTKDKLSPILGIEGYKNSMEQLKLQQIKTPIYAIGGIQLEDVSEIIATGIHGIAVSGLITESISKTKLITQLNEKLYGYVLV
>CP020918.1|AWG20409.1|466462_467218_+|hydroxymethylpyrimidine/phosphomethylpyrimidine-kinase
MPTNRPFVLSIAGFDPSAGAGVLADIKTFEQHKVYGLSVLTANTIQTESHFSSIQWVAIEQVLESILVLFEKYKIETVKIGIVPSIEYLKAIVDLIKKQSPTTKIVWDTVLTSSTSFNFLAIQDRIALVEILRKIDLITPNYNEILVLGSNAAPINSIINQLTSHCAVLLKGGHNQNELGIDYLHTKDRFFRLSPKIDTIYEKHGSGCVLSAAITANLALGHDLLQSCKKAKDYIEQFLLSNPSLLGNHHA
>CP020918.1|AWG20408.1|465890_466490_+|thiamine-phosphate-synthase
MIIISNPVAVPNEIVTIHALFEAGMQLFHIRKPDFSEEEMNVFIAAIGLEYHSKLVLHSHHHIADSHSIKRIHFPEKLRSETTSTELRAYKSRGFTLSTSTHNIEDFNLLDSNFDYAFLSPVFESISKENYNPKGNLFEEIKNRSNFNTQLIGLGGIEFSNIEKTLEAGFNDVALLGTIWTSNQPIEKFKLCQQIVLSY
>CP020918.1|AWG20407.1|464028_465852_+|phosphomethylpyrimidine-synthase-ThiC
MTNEQEISRQPFPNSTKVYIDGEIHPIKVAMREIKLSDTKLSRGGVEENPPVTIYDTSGPYTDPNIEIDIRKGLPRLREQWIKDRNDVEELSEITSNYGKERLEDEKLNHLRFEYLHKPMRAKKGANVSQLHYAKKGIITPEMEYIAIRENQRIELIEQQTKAMQCQHAGHSFGANTPKTKITPEFVRSEIARGRAIIPNNINHPESEPMIVGRNFLVKINANIGNSAVTSSIEEEVEKAVWACRWGADTIMDLSTGKNIHETREWIIRNSPVPIGTVPIYQALEKVNGVAEDLTWEVFRDTLIEQAEQGVSYFTIHAGVLLRYIHLTANRVTGIVSRGGSIMAKWCLFHHKENFLYTHFEEICEIMKQYDVAFSLGDGLRPGSIADANDAAQFAELETLGELTKVAWKHDVQVFIEGPGHVPMHMIKENMDKQLEHCDEAPFYTLGPLTTDIAPGYDHITSAIGAAMIGWYGCAMLCYVTPKEHLGLPNKKDVKDGVITYKISAHAADLAKGHPGAQYRDNALSKARFEFRWEDQFNLSLDPDTAREFHDETLPADGAKVAHFCSMCGPKFCSMKISQEIRDVAEAEKGMQEKSEEFIEQGKEIYI
>CP020918.1|AWG20406.1|463677_463884_+|thiamine-biosynthesis-protein-ThiS
MELKINNQKKQFEANTLSIQAMLDIEIPQKQNGIAVAINSNVIPKSNWVDLLLSETDDILIISATQGG
>CP020918.1|AWG20405.1|462235_462805_+|hypothetical-protein
MSQYNNYIAELNDEGSILKIEIIKSWLLEHENYFKFLINETTCRKWSKWIKDKSIHLFPCACHTREGFCVFIQTYYELEKIMDLHRRQDEIAVVLKGFDRIKNNPDLEFEWVEKYSQIADFFEGKLQITGEEGKLINFMFDKDEFYTAILFEDIKMEIYCSEEYQIRSKSQENTLIFDEDELSYDDDNY
>CP020918.1|AWG23534.1|461955_462087_+|hypothetical-protein
MWESLWTCGVSNPLTVIEQFTYILFVRRLDKNQLLQEKNLSKN
>CP020918.1|AWG20404.1|460843_461752_-|hypothetical-protein
MNDYKEKIVGCWKNDKIEYKFESDGALSIYWVHANSQAQGNWSIWGDDEIIFNYGDVNTLPWNGKINYITNDELSITDEYNDVGSIDIMFRSNRISKIDFDAIILTLQQFDVEPKEVDVNTVSKLQKEDLPKKSLKEKVIDFTTSFFGIAFFVVIIVGFLYFFYTSFVRESHVIQSFTAGIIFLSISTFMIFHHLSDDIKVVKFTDNLFVVLVVAIITLPLLYVALQILFLVLTLWYFVICIVGIVCIVAIYNKKTLKKIYKFLIIMTLLLSLYFLYDAKGILTINFDVRFDNKKIENTNNS
>CP020918.1|AWG20403.1|460514_460814_+|hypothetical-protein
MGKARLYQHLPKSKKACIANVNFTDGHINTIARDYYEDASFSRDEQGYINLWDVYNLFTKANKSSYIDTFLDRNVNAFDFVKGIQKALMGDESYCWFLS
>CP020918.1|AWG20413.1|470103_470814_+|thiamine-biosynthesis-protein-ThiF
MSIIQDFLRYNRQTILPEIGDEGQEKLKKAKVLVIGAGGLGCPILQYLATAGVGTIGIVDFDTIEIHNLHRQILYTEEQLGLPKATTAKATVEKLNPLIAVLAFEEKLTFENASQIISQFDFVVDGSDNFSTRYLVNDTCVALGKTLVYGSILGFEGQIAVFNHQGSKNLRDLFPEPPNPKDVPNCSFNGVLGTLPGMIGTIMAHETLKLITGLPTLRNELILYKTLEWGFVKLNF
>CP020918.1|AWG20414.1|471263_471512_-|hypothetical-protein
MQVLLQKHFFYCHKRSIFATLSFGEGLGERTVALLCQEKIGFLSPGFPLPSGAVNPEFLFINNLYEYFNIFEKKIGNHTITT
>CP020918.1|AWG20415.1|471634_472276_-|leucyl/phenylalanyl-tRNA--protein-transferase
MVQLSDALVFPNVNTANRDGIVAIGGDLSAARLQLAYQSGIFPWFEQGDPIIWWSPNPRMVLFLDEVRVTKSMRNILNRQEFKVTFNQDFLGVISNCQRIKRDGQNGTWITNDMIDAYCNLHQLGIAQSVEVWQNDQLVGGLYGVDMGHVFCGESMFSKVSNASKVAFISLVHHLKSNQYQLLDCQVYNPHLESLGCREIERNDFMKILRNEV
>CP020918.1|AWG20416.1|472294_473212_-|glutaminase
MEDIHSVLDSIYNKFKDFEDIGEKATYIPELANVDERLFGISLTTVNQRQVNLGDAHQKFSVQSISKVLMLIMAYNLEGDALWQRVDVEPSGAGFNSMILLELEKGIPRNPLINAGAIVIADVLLSHYKDPESEFINFVRRLTNDPTVTFDDKVFESEKGVGYRNYALINMMKSFGNIQNPIDEVMDFYFKICSLSMSCAQLSKTFLFFANDGVDPITNEIILTPSRNKRINAIMLLCGFYDEAGEFAYRVGLPGKSGVGGGILAILPNMYSIVVFSPKLNPKGNSYRGMAFLECLTTELSDSVF
>CP020918.1|AWG20417.1|473340_474072_+|phosphatidic-acid-phosphatase
MRKLPVILFLCLLVNQMNGQINDTIVKTQKLTYKKFILPAALVATGSLLLNTDRNRKIQADANRFFGSDFHTRLDDITVFVPVGQLYAGGLFGFEAKNSLKHRTISVVTANALSFTLVSVLKNIVKAHRPDDSDQLSFPSGHSAIAFTNAALLFQEYKDDNIWYASSGFLFATTTGFLRVANNKHFASDVFAGAGIGLASGFLVTYWNPLQNIHLGKKQKGTAFVYPQLGNQIGIGAVILPNF
>CP020918.1|AWG20418.1|474124_475084_-|fasciclin
MKNFNIKSAVLALTLMGTLVSCDTDYKDETPSIAGIAVANPNFSTLEGAAVQGGVVGVLSNSNPNDPSGHYTVFAPTNDAFARLGLVDSGSLGGLQNSFLTNTLLYHVSNGDLMGSGIKAGGTAPSLLGVDRRFISRGADLYINGSKIILTDVSASNGTIHGIDKVMIATGVNIVESAILLKDAKVFKAPELTFLVQAVITSGLAGTLSSSSANFTIYAPTDAAFKAAGFATVQDVANTSPAVLQQVLLNHAIVGGKFTSEHSGTTAATAGGGMLTYSAFTNGIFTVKSNGITTPANMVIPDIQCSNGVVHVIDKVLLP
>CP020918.1|AWG20419.1|475103_475988_-|hypothetical-protein
MIKRQLLLILAVTAFGYVNTAHSQSPISGFMQGKGKGNVSVSFSSEKYDDVYFVPEKVEGVPVFNKTTITSTSIYATYGISDQVDVVMVLPYVTAKGHATDEVLTNLGLENKRQGFQDVSVFVKYSPFNFDFGSSSLRLIGAVGVKTPLSNYKVEEGFQSIIAIGNRSTTVSTTGMAMFKMNSGVFASGQVAGNYASNDVPNSVTTELKVGYAAKSFYGDVFIANQKSTGGVDIFGEGFAGYFPTTKVNYTKIGVDLYAPVYKDWGVSAGASTLVAGRNIGQATGFYGGLVYKF
>CP020918.1|AWG20420.1|476326_476695_-|hypothetical-protein
MEVIGRVKVINPEQQVSAAFKKRELVVTTEEQYPQHILVEFTQDKCDLLNNYGVGESVKVSINLRGREWVNPQGETRYFNSIQGWRIEKAGAEAPSAPSAPAAPVFPAATNLNEEEADDLPF
>CP020918.1|AWG20421.1|476946_479433_-|TonB-dependent-receptor
MKLNQFIAFVAFLVSAAVFGQVSGKVVDGDFPLEYATATLFSTETKAVVAGVVTTKEGTFKIGSLKNDSYYLEVSFIGFDKQVFKDIVISSKNKSVNLGLISLVSGGNQLNAVVVQSVKGTVISKIDRQVYDAKSFQNSQGGSAIDVLRNLPSISLDAQGDVSVRGTTGFRVLLNGKPTQGNISTILGQLPANAIDRIEVVTAPSAKYDPDGKAGLLNIITKKGATNGQYAQLNVKGGFPSIENYDNKKKAQRYGIDGTYTIKKDKWDISLGGSYGRNDIQGRREGNVFTNNITENYKTQFPSDGERSTNELNYSGRFTVDYTPSITDNFSVGFYGGKRKVDRQADIYYNNKRTDLTTGAVLKSFDYYNENLRVRDGDFALGSFDYTHKFEDKSKLTASFLYEYTLLGGPTTNLNLGYTDSSIVYQDEYNTNDNPLYGTRAQLDYEFKPFSFGKIEAGYQFRKLKNNGDFIYQRRNLSSGIYEIVPEFTSQVNLDRSIHSGYLQLNGSKTKWEYAAGLRLESMNRDFYLKGFNTAAENLTYDYVKLFPSASAQYTMDNNVKVKAGYSKRVDRAPTYQMNPFKEREHSETFEQGDKNLRPEFTDLIELGISKNFKGGNTLFATAYYRDVHNLINRVNTLSYTTAGVLNDTILDRIYTNVGRGKTLGLEIGSQFKPSTKWTNFIGANIYNFNIDGSFNGKAIKSNAIQYSINANSTYNFTPTTSMQFTLNYLSKKITAQGEDSRFYSPNLTFRKSFLDNQLIATLQWQNIDMGMLNTNEQRISTQSTGQYYTTTNYVYEVDMVLLNLSYTFNKTKSSAKFIESEFGKKEF
>CP020918.1|AWG20422.1|479575_480391_-|AraC-family-transcriptional-regulator
MKEAIAVYTKIPNVTDIKIEPFDVNKRYTKPHRHNKYIELVYFKAGSGFHYVDSVAYKIEPPIVFGISNNEVHHWEIDTVPEGFVIIVKDGFLEKTIDKHINQQLYRLNKEQVIKVQPDESIDKLFEVLCLEMKQHSIQKEVVEGSLKALLGKIIGYSNRVECMVEIDKAVHFEELLLQELRNDVAFYADLMSINVAQLNAICKKSFSKTASQVITTHIIQESKRQLLYTDRTISEIGYSLDFKDVSHFVKYFKRHTAITPLTFKQNGILV

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Crispr_ID: CP020918_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP020918_2

1328140-1328280

Orphan

Consensus_repeat	Method
TTAAAATTAGTGTTCATTTGTGTAATTTGTGTCTATATTTTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP020918_2

>merge|CP020918|2|1328140-1328280|CRISPRCasFinder
TTAAAATTAGTGTTCATTTGTGTAATTTGTGTCTATATTTTCTAGTCATTTTAATTAAAAGCATCAATCAAAATTCGTGTAATTCATATTTTTTAAGTTTTAAAATTCGTGTTCATTTGTGTAATTTGTGTCTATATTTTC

>CP020918|2|2|1328140-1328280|CRISPRCasFinder
TTAAAATTAGTGTTCATTTGTGTAATTTGTGTCTATATTTTC	TAGTCATTTTAATTAAAAGCATCAATCAAAATTCGTGTAATTCATATTTTTTAAGTT
TTAAAATTCGTGTTCATTTGTGTAATTTGTGTCTATATTTTC

Protein	Signature genes	Signature genes Name	Protein_function
CP020918.1\|AWG21091.1\|1334750_1335107_-\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21087.1\|1328858_1329614_+\|UDP-2,3-diacylglucosamine-hydrolase	unknown	unknown	gnl\|CDD\|277343
CP020918.1\|AWG21090.1\|1333862_1334678_+\|S1/P1-Nuclease	unknown	unknown	gnl\|CDD\|211382
CP020918.1\|AWG21094.1\|1337967_1339656_-\|single-stranded-DNA-specific-exonuclease-RecJ	unknown	unknown	gnl\|CDD\|273193
CP020918.1\|AWG21095.1\|1339734_1340079_-\|type-III-effector	unknown	unknown	gnl\|CDD\|378082
CP020918.1\|AWG21076.1\|1319887_1320370_-\|acetyl-CoA-carboxylase,-biotin-carboxyl-carrier-protein	unknown	unknown	gnl\|CDD\|235777
CP020918.1\|AWG21080.1\|1322427_1323471_-\|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA	unknown	unknown	gnl\|CDD\|377232
CP020918.1\|AWG21088.1\|1329711_1330875_-\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21086.1\|1328382_1328835_+\|6-carboxytetrahydropterin-synthase-QueD	unknown	unknown	gnl\|CDD\|376501
CP020918.1\|AWG21084.1\|1325509_1327186_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379073
CP020918.1\|AWG21092.1\|1335220_1336282_-\|ADP-heptose--LPS-heptosyltransferase	unknown	unknown	gnl\|CDD\|340821
CP020918.1\|AWG21089.1\|1330886_1333430_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
CP020918.1\|AWG21083.1\|1324943_1325345_-\|methylmalonyl-CoA-epimerase	unknown	unknown	gnl\|CDD\|319912
CP020918.1\|AWG21079.1\|1321777_1322326_-\|DNA-binding-protein	unknown	unknown	gnl\|CDD\|376863
CP020918.1\|AWG21081.1\|1323529_1324117_+\|riboflavin-synthase	unknown	unknown	gnl\|CDD\|236455
CP020918.1\|AWG21082.1\|1324153_1324360_-\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21078.1\|1321570_1321768_-\|50S-ribosomal-protein-L32	unknown	unknown	gnl\|CDD\|234901
CP020918.1\|AWG21093.1\|1336690_1337968_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863
CP020918.1\|AWG21077.1\|1320394_1321393_-\|3-oxoacyl-ACP-synthase	unknown	unknown	gnl\|CDD\|236475
CP020918.1\|AWG21085.1\|1327189_1327957_-\|amidohydrolase	unknown	unknown	gnl\|CDD\|143599

Protein	Function_ID	Function_description	E-value
CP020918.1\|AWG21090.1\|1333862_1334678_+\|S1/P1-Nuclease	gnl\|CDD\|211382	cd11010, S1-P1_nuclease, S1/P1 nucleases and related enzymes. This family summarizes both S1 and P1 nucleases (EC:3.1.30.1) which cleave RNA and single stranded DNA with no base specificity. S1 nuclease is more active on DNA than RNA. Its reaction products are oligonucleotides or single nucleotides with 5' phosphoryl groups. Although its primary substrate is single-stranded, it may also introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. It is used as a reagent in nuclease protection assays and in removing single stranded tails from DNA molecules to create blunt ended molecules and opening hairpin loops generated during synthesis of double stranded cDNA. P1 nuclease cleaves its substrate at every position yielding nucleoside 5' monophosphates, and it does not recognize or act on double-stranded DNA. It is useful at removing single stranded strands hanging off the end of double stranded DNA and at completely cleaving melted DNA for simple DNA composition analysis.	1.64445e-84
CP020918.1\|AWG21084.1\|1325509_1327186_+\|hypothetical-protein	gnl\|CDD\|379073	pfam13205, Big_5, Bacterial Ig-like domain.	2.05967e-18
CP020918.1\|AWG21094.1\|1337967_1339656_-\|single-stranded-DNA-specific-exonuclease-RecJ	gnl\|CDD\|273193	TIGR00644, recJ, single-stranded-DNA-specific exonuclease RecJ. All proteins in this family are 5'-3' single-strand DNA exonucleases. These proteins are used in some aspects of mismatch repair, recombination, and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair].	1.0459e-175
CP020918.1\|AWG21095.1\|1339734_1340079_-\|type-III-effector	gnl\|CDD\|378082	pfam08888, HopJ, HopJ type III effector protein. Pathovars of Pseudomonas syringae interact with their plant hosts via the action of Hrp outer protein (Hop) effector proteins, injected into plant cells by the type III secretion system. The proteins in this family are called HopJ after the original member HopPmaJ.	2.61384e-62
CP020918.1\|AWG21076.1\|1319887_1320370_-\|acetyl-CoA-carboxylase,-biotin-carboxyl-carrier-protein	gnl\|CDD\|235777	PRK06302, PRK06302, acetyl-CoA carboxylase biotin carboxyl carrier protein.	8.84713e-49
CP020918.1\|AWG21080.1\|1322427_1323471_-\|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA	gnl\|CDD\|377232	pfam04166, PdxA, Pyridoxal phosphate biosynthetic protein PdxA. In Escherichia coli the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that is thought to involve the condensation of 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose, catalyzed by the enzymes PdxA and PdxJ, to form either pyridoxine (vitamin B6) or pyridoxine 5'-phosphate.	1.46865e-126
CP020918.1\|AWG21086.1\|1328382_1328835_+\|6-carboxytetrahydropterin-synthase-QueD	gnl\|CDD\|376501	pfam01242, PTPS, 6-pyruvoyl tetrahydropterin synthase. 6-Pyruvoyl tetrahydrobiopterin synthase catalyzes the conversion of dihydroneopterin triphosphate to 6-pyruvoyl tetrahydropterin, the second of three enzymatic steps in the synthesis of tetrahydrobiopterin from GTP. The functional enzyme is a hexamer of identical subunits.	6.48389e-29
CP020918.1\|AWG21087.1\|1328858_1329614_+\|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.	1.01061e-55
CP020918.1\|AWG21092.1\|1335220_1336282_-\|ADP-heptose--LPS-heptosyltransferase	gnl\|CDD\|340821	cd03789, GT9_LPS_heptosyltransferase, lipopolysaccharide heptosyltransferase and similar proteins. Lipopolysaccharide heptosyltransferase (2.4.99.B6) is involved in the biosynthesis of lipooligosaccharide (LOS). Lipopolysaccharide (LPS) is a major component of the outer membrane of gram-negative bacteria. LPS heptosyltransferase transfers heptose molecules from ADP-heptose to 3-deoxy-D-manno-octulosonic acid (KDO), a part of the inner core component of LPS. This family also contains lipopolysaccharide 1,2-N-acetylglucosaminetransferase EC 2.4.1.56 and belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	2.14707e-30
CP020918.1\|AWG21089.1\|1330886_1333430_-\|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.	4.21346e-32
CP020918.1\|AWG21083.1\|1324943_1325345_-\|methylmalonyl-CoA-epimerase	gnl\|CDD\|319912	cd07249, MMCE, Methylmalonyl-CoA epimerase (MMCE). MMCE, also called methylmalonyl-CoA racemase (EC 5.1.99.1) interconverts (2R)-methylmalonyl-CoA and (2S)-methylmalonyl-CoA. MMCE has been found in bacteria, archaea, and in animals. In eukaryotes, MMCE is an essential enzyme in a pathway that converts propionyl-CoA to succinyl-CoA, and is important in the breakdown of odd-chain length fatty acids, branched-chain amino acids, and other metabolites. In bacteria, MMCE participates in the reverse pathway for propionate fermentation, glyoxylate regeneration, and the biosynthesis of polyketide antibiotics. MMCE is closely related to glyoxalase I and type I extradiol dioxygenases.	4.9981e-49
CP020918.1\|AWG21079.1\|1321777_1322326_-\|DNA-binding-protein	gnl\|CDD\|376863	pfam02620, DUF177, Uncharacterized ACR, COG1399. This family is nearly universally conserved in bacteria and plants except the Chlorophyceae algae. Thus far, mutantional analysis in bacteria have not established a function. In contrast, mutants have embryo lethal phenotypes in maize and Arabidopsis. In maize, the mutant embryos arrest at an early transition stage.It has been suggested that family members specifically affect 23S rRNA accumulation in plastids as well as bacteria.	1.09658e-20
CP020918.1\|AWG21081.1\|1323529_1324117_+\|riboflavin-synthase	gnl\|CDD\|236455	PRK09289, PRK09289, riboflavin synthase.	5.76051e-97
CP020918.1\|AWG21078.1\|1321570_1321768_-\|50S-ribosomal-protein-L32	gnl\|CDD\|234901	PRK01110, rpmF, 50S ribosomal protein L32; Validated.	4.18303e-17
CP020918.1\|AWG21093.1\|1336690_1337968_-\|MFS-transporter	gnl\|CDD\|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	3.27467e-59
CP020918.1\|AWG21077.1\|1320394_1321393_-\|3-oxoacyl-ACP-synthase	gnl\|CDD\|236475	PRK09352, PRK09352, beta-ketoacyl-ACP synthase 3.	1.09186e-175
CP020918.1\|AWG21085.1\|1327189_1327957_-\|amidohydrolase	gnl\|CDD\|143599	cd07575, Xc-1258_like, Xanthomonas campestris XC1258 and related proteins, members of the nitrilase superfamily (putative class 13 nitrilases). Uncharacterized subgroup belonging to a larger nitrilase superfamily comprised of nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes, which depend on a Glu-Lys-Cys catalytic triad. This superfamily has been classified in the literature based on global and structure based sequence analysis into thirteen different enzyme classes (referred to as 1-13), class 13 represents proteins that at the time were difficult to place in a distinct similarity group; this subgroup either represents a new class or one that was included previously in class 13. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. XC1258 is a homotetramer.	6.23026e-158

>CP020918.1|AWG21085.1|1327189_1327957_-|amidohydrolase
MKIALVQAALEWENPNANRMMFETKIKEIDLAVELIILPEMFSTGFTMNPATQAETMTGDTVKWMQDLAKSRNCAFTGSLVIQENNNFYNRMLFVFPTGEIETYDKRHLFTLAGEEKVYTAGSQKVIVDYLGWKICLQVCYDLRFPVFSRNTENYDLLLYVANWPEKRVLAWDSLLRARAIENLCYVAAVNRVGQDANDLHYNGHSQVVAPLGDYVVSPQTDEAVFVTDLDLQLVQSTRQQFNFLNDGDAFEIKF
>CP020918.1|AWG21084.1|1325509_1327186_+|hypothetical-protein
MFIKNSIAFCLVLVLSLLGCAKRGNITGGLKDSLAPILIASYPKNFTTNFTGNEISLTFDEYIKLKDANKQLVVSPPMKYEPVITPTNASKYLNIRIKDTLLPNTTYSFNFGQSITDNNEGNPLNQFKYVFSTGTYIDSLSLGGTIKDALEKESDSFVSVMLYDQNDKFKDSIVYTDMPRYITNTLDSLKTFRLENLKAGKYLLVALKDNNKNNKFNSKEEKIGFLKQAISIPNDTLFELELFKEVIPFKAFKPTQASSNKLYLGYDGTQDFKLSKPKVVLTKEGVVLPTIVTQMPKKDSLQIWYKPLKNDSLVIAISRDKYEQKYSFKVKDQKTKDTLTVSALQTGTIGYRERFTLETGTPLVTIDKSKFSFVNGAKETVEFQTEHDAFNQKLYIDFKKVPAEKYNLTLLPGALVDFFDTKSDTLSYKFATKELDQVGNLKIKLQNVKKYPIIVQLTNQAGEVKETEYSTGGDLVEFKLIDPSVYTLRIIYDDNKNQQYDSGNYLAKRYAEEVVYFSKDIDVRVNWDVEQTFDVSLPYVPEPKKKPAKKGEGGNGPR
>CP020918.1|AWG21083.1|1324943_1325345_-|methylmalonyl-CoA-epimerase
MKKIEHIGIAVKNLEDSNLLFEKLLGTAPYKLEEVVSEGVQTSFFISGPNKIELLAATHPNSAIAKFLEKKGEGIHHIAFEVSDIDQEIIRLKSEGFVFVDEIPKIGADNKRIVFLHPKNTNGVLIELCQEIK
>CP020918.1|AWG21082.1|1324153_1324360_-|hypothetical-protein
MKKNLHKYYYLFILLLAGTFGVIAQPPAPLPPPPGLPINDGVLFLGIAALSYGIFTIYNHTKKRKSLG
>CP020918.1|AWG21081.1|1323529_1324117_+|riboflavin-synthase
MFTGIIETLGTIREIVKEQDNIHVTVESEITNELKIDQSVAHNGVCLTVVKIEGTAYTVTAIAETIQKTNLGSWKVGSQVNLERAMKLGDRLDGHIVQGHVDQIGTCIAVSETNGSWAYTFEYDEALNNITIEKGSITVNGVSLTVVNSKKNQFSVAIIPYTHEHTNFHDFEVGTKINLEFDVIGKYVSRLYSNK
>CP020918.1|AWG21080.1|1322427_1323471_-|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA
MMKKAENIIVGISIGDLNGIGSEVVLKTFEDSRMLELCTPVIFANVKILSFIKKNLDSAVSLHGIDKIDQLIPGKINVLNVWKEGVDLNLGTNDEKVGDYAIKSFVAATQALKDNQIDVLVTAPINKYNIQSDTFKFPGHTDYLDQELEGDALMMMVQGNLRIGLLTDHLPLNQVSAALTETLIKKKIETVRKSLIQDFSITKPKIAVLGLNPHCGDGGVIGKEDDAVLKPTIQKIFSKGTLVFGPFAADGFFGSGQYEKYDAIIATYHDQGLIPFKTLSFGNGVNYTAGLNKIRTSPDHGTAYDIAGKGKADYNSFKEAVYLAIDVYRSRIEYSEISENPLKVREK
>CP020918.1|AWG21079.1|1321777_1322326_-|DNA-binding-protein
MSSTKEYLIPFVGLKTGKHHFEYQLNNAFFEIFDYDEYQNSDIKVNVVLEKQSNMLELNFKHDGTINAPCDLTGEDFDLPIKGNMKLIVRFGEEFNNDNEELLILPFGEFEIDIAQYMYEMIVLSVPQRRVHPGVKDGSLKSEALEKLNELTIKEINETKEVQKEENIDPRWDKLKQLLTDK
>CP020918.1|AWG21078.1|1321570_1321768_-|50S-ribosomal-protein-L32
MAHPKRKISKTRRDKRRTHYKATVAQIATCPITGEAHLYHRAYWHEGKMYYRGQVVIDKSEATFA
>CP020918.1|AWG21077.1|1320394_1321393_-|3-oxoacyl-ACP-synthase
MNKMTAAITAVGAYVPDFVLTNKVLETMVDTNDEWITSRTGIKERRILKDTDKGTSFLAIKAAQDLIAKGNIDPLEIDMIIMATATPDMPVAATGAYVATEIGAINAFAYDLQAACSSFLYGMSTASAYIESGRYKKVLLIGADKMSSIVDYTDRTTCIIFGDGAGAVLFEPNYEGLGFQDEYLRSDGVGRHFLKIPAGGSLVPTTMQTVKDNRHNIMQDGKTVFKYAVTNMADASEQILKRNNLTNDDVDWLVPHQANKRIIDATASRMNLDESKVLMNIERYGNTTSATLPLVISDFEHLFKKGDTIIFAAFGGGFTWGSVYLKWAYDKK
>CP020918.1|AWG21076.1|1319887_1320370_-|acetyl-CoA-carboxylase,-biotin-carboxyl-carrier-protein
MDLKEIQNLIKFVSNTGVAEVKLEMDDVKITIRTTLEGSTTETTYVQQAPQAPVQQVIAPVAAAPVAAAPVAAAPAVEESKYITVKSPIIGTFYRKPSPDKPMFVEVGTTIGTGDVLCVIEAMKLFNEIESEVSGKIVKILVDDMSPVEFDQPLFLVDPS
>CP020918.1|AWG21086.1|1328382_1328835_+|6-carboxytetrahydropterin-synthase-QueD
MSNIRITKQFNFETGHALYGYDGKCKNVHGHSYKLSVTVMGRPIKDRTNVKFGMVIDFSDLKKIVTEEVVDQFDHATVFNETTPHVELAKELQIRGHHVILVDYQPTSENMVIDFAERIKRRLPVGIELFSLKLQETESSFAEWYASDNL
>CP020918.1|AWG21087.1|1328858_1329614_+|UDP-2,3-diacylglucosamine-hydrolase
MLLANNKKIYFASDQHFGAPTAALSLPREKKFVAWLDEIKQDAEAIFLLGDLFDFWFEYKTVVPKGFVRVLGKLAELRDSGIPIYFFVGNHDLWMRDYFETELNIPVYHDNKEFTFGGKTFLIGHGDGKGPGDMGYKRMKKVFVHPFSKWLFGWLHPDIGVGLAQYLSVKNKMISGDEDVKFLGEDKEWLILYAKRKLETKHYNYLIFGHRHLPMIRSVGENADYVNLGDWITYFTYGVFDGENFELKEYK
>CP020918.1|AWG21088.1|1329711_1330875_-|hypothetical-protein
MKNLKYLFLSLALGLLSCESELEKTYDELGNIPSPVRTDLKYTLVDADYAAIDGTSKTDDYEKFKGIPSEEDAIAKLPAVILSRLVRVEGAIAVITYNLYKPNTLTSSTTYTVTTADYTSQGGNISRFGNFSNETEVGNFLKSKYPAATKGTGVKLTYKIFSGGVQTLTNTFVLNSNNVWEATYTLVAADYTALGESFTNFSDKTVAENRIAIYLKSTLMPYANAGDTKSVIFTYTYRDGSNARKYEDILVKYQYDGAKWAAIPALTTQTSNFKYKSGVWVSNNVIKYAFASADYTNAAVGLAGVADLADEVSNLTSFGNFNRTAADTAWNTDEMLQALNVVLKKNFPTTEVGQEYLVSVSVYNGSPSIETFAVVLTASGSYVYFVQ
>CP020918.1|AWG21089.1|1330886_1333430_-|TonB-dependent-receptor
MKKILLFLVFALVAFTKTYSQNKKIISGNVQDEKQLPLIGASVVIDGTNEGAITNGDGKFEFSTEKKQGILLISSVGFETQKMNFHTNNSKDLEIVLESSSLGLDEVVVFSSRAVDRKTPVAVSTIKKDAIELKLGNGEFVEILKSVPGVYASKEGGGFGDGEVTLRGFNSENVAVLINGIPVNDMESGRVFWSNWTGLGSVSSSIQVQRGLGASKVAVPSIGGTINTITDNTASKEGGQVSYTIGNNNYQKVGVKLNTGQMGNGYAATVYADKISGDGFVDGTPFEGVSYFASVSKKINHDHKLVFTATGATQTHGQRFERLSIQDYRTSDRGIKLNKGWGYKNGQLFALSQNTFNKPLISLNHYWTLNSKNKISTAVYYSSGKGGVSFEAGADSGKLTGPNAYRLGTFGPVDVDRVVDENIANGESTAIIQSSANNHIWMGAISTWTSNIDENFTFIGGLDYRYYKGSHYREVSDLLGGQFYKDNGDVNNPNRATVVGDKIGFFNENFVNWIGNFAQLEYDKDKVTAFVAVNASNTSYSRLDHFRKLNSDPTRQTDNVNFFGFGAKTGGNYRLDDYNNVFVNVGYFERAPYSSAVWATNNNDQTNKDAKNQKILSFEIGYGLRLPKFAANVNLYRTQWDDRSQTDTRTALNATTNAQEVIYTNILGVDALHQGVELDFEYRPSSDFTLTGMLSLGDWKWKNNVNAVITDSNQNVISNLNLFIKGLPVGRSAQTTAALGTQYHLTPKTSFNIDYNYTDRYYADFNPGTRTSAGAEPWKVPSFHLFDASILHKFHILSLNAKVIARMNNVFNTEYITRANDLDGTAAGATVFFGSGRTFSISSIINF
>CP020918.1|AWG21090.1|1333862_1334678_+|S1/P1-Nuclease
MKNLILALAISVSVANYAAPTWGKTGHRTVGEVAAKHLKNRTTKKINDLLQNESVASVAVYADDIKSDSQYNKYYSWHYVNFNGDKKYKEEPINPEGDVIQGIKTCIEKIRSKETTKEEKGFFLKMLIHFVGDLHMPLHAGNASDKGGNDVKVKWFGADSNLHRVWDSDMIDDYQMSYTELATNNDIMASKDEVKAMEQGTLLDWVVESRQLALKLYSETHQDDKLGYKYMYQNFPVAQDQLEKGGVRLALILNEVFKGKSKWLDTFLTDI
>CP020918.1|AWG21091.1|1334750_1335107_-|hypothetical-protein
MKEIQTIYQNEFGVSFYWKVENQTCHDTVQLVFKETGLQLNANELVEFKCLIEDSISKNKCCDDCSLKSNCTKYLLKTPFHELDLAMSIAEMDLMNNLISTTLFKINLNDYQSGMGRN
>CP020918.1|AWG21092.1|1335220_1336282_-|ADP-heptose--LPS-heptosyltransferase
MSFKIKINEFRRKITHGLTRYVGTSKGNKDFDSNSKVVFKNVLINRPNHRLGNLLLITPLVQEINEAFPDCKVDLFVRGGLAPIIFENYKSVDNYIILPRKPFNELVKYAKVWFKLKDKKYDLVLNIDNNSSSGRLSTQFANADFKFFGEEDETVKSQYPDYEHFAKFPVYEFRNYIQKLGHPAKKTAVPTLNMKLTEAELAAAKTILDTIAPNNKKTICVFTFATGSKCYPPSWWNPLYEKLQASFPDYNIIEVLPVENVSQIDFKAPTFYSKDVREIAAFIANTALFIGADSGIMHLASTAQIPVLGLFSVTNPVKYAPYGNASLAVDTNSNSAEQIIDIAKSQLAAHWKA
>CP020918.1|AWG21093.1|1336690_1337968_-|MFS-transporter
MSIEKIKKDPYEALRYKEFNTFLLVRFAMVFAWSMQFIVIEWQVYSITKDPLSLGLIGLMEVIPAVSMALFAGHIVDQKEKKSMLLKCILGFSVVSFGLFLLTWPPVVMGYNQQTILYAIYFMVFLGGIVRSFIGPTIFSFLSLIVPKKVYPNAATWSSSVWQIGSVVGPAVAGFSIHLIGVHWSMCSVFVCSVVALLALTQIAAKPILNPKIGEPIMQSLTEGLKFVFNNKTVLGAITLDMVAVLFGGAVALLPVFAQDILKVGPEGFGFLRAAPAVGAFLTMLITAYVPLNTNAGMKLLIAIFGFGICIIIFGLSSIFWISLVALFLSGVFDGISVVIRQTILFLKTPDHMRGRVSAVNSMFVGSSNELGAFESGLTARLMGTVTSVVFGGSMTLLIVLLTGTLSPTFRKLDLNKEIEKDELI
>CP020918.1|AWG21094.1|1337967_1339656_-|single-stranded-DNA-specific-exonuclease-RecJ
MRWTIKPKPSAEKIQHLAHALQVEDFVATLLVQRGIETFEDAKAFFRPSLSHLHDPYLMKDMDKAVIRIEKAIANNERILVFGDYDVDGTTAVSLVASYLKTYYSNVDTYIPDRYLEGYGVSFKGIDYAEDNEFSLIIALDCGIKSIDHVNYAKERNIDFIICDHHRPGDQLPAAVAVLDPKRSDCTYPYDELCGCGVGFKLIQALGTNRDQTIEDLIPYLDLVATAIAADIVPMTGENRVMAYFGLKVINDSPRPGIKALVHQVKKQTLDITDVVFIVAPRINAAGRIRHGNYAVQLLTEFDFEQAQAFASEIEKNNADRKELDQQITKEALNQIITNQEEDRFSTVVFQEDWHKGVIGIVASRLIETHYRPTLVFTKSGEKYAASARSVKGFDVYNALEACADHLEQFGGHMYAAGMTLQAENYPAFKNAFEKQVQATILPEQRVPEIEVDAEIDFNDISPKFIRILKQFEPFGPQNMTPVFMSKNVIETGYAKPMGKENEHLRLFVKQNQSEGLAAIGFGLGNKLEIVTNQKPFEAAYCIDENEWNGKTTTQLRLKDIR
>CP020918.1|AWG21095.1|1339734_1340079_-|type-III-effector
MKIEQFLAQLNENPTSIAFADTIATIEANYDFTPTAFQNGNTHNGAGTNSGSCKLFSFAKTQNLSQELTLACFGSYYFDEVLGDSEGTSHQNIRNFMVSGWNGIQFEGDALARK

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Crispr_ID: CP020918_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP020918_3

2123049-2123148

Orphan

Consensus_repeat	Method
CTGCGCTTGCAAAGAGCATCAAAACTATGTTCAACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP020918_3

>merge|CP020918|3|2123049-2123148|CRISPRCasFinder
CTGCGCTTGCAAAGAGCATCAAAACTATGTTCAACGTTTATAAACTGAAAACTGCCACTGAACACTGCGCTTGCAAAGAGCATCAAAACTACGTTCAACG

>CP020918|3|3|2123049-2123148|CRISPRCasFinder
CTGCGCTTGCAAAGAGCATCAAAACTATGTTCAACG	TTTATAAACTGAAAACTGCCACTGAACA
CTGCGCTTGCAAAGAGCATCAAAACTACGTTCAACG

Protein	Signature genes	Signature genes Name	Protein_function
CP020918.1\|AWG21707.1\|2108392_2111692_-\|oar-protein	unknown	unknown	gnl\|CDD\|379297
CP020918.1\|AWG21716.1\|2124042_2126166_+\|dipeptidyl-carboxypeptidase-II	unknown	unknown	gnl\|CDD\|341051
CP020918.1\|AWG21714.1\|2122450_2122813_-\|four-helix-bundle-protein	unknown	unknown	gnl\|CDD\|319869
CP020918.1\|AWG21712.1\|2118748_2120986_-\|isocitrate-dehydrogenase-(NADP(+))	unknown	unknown	gnl\|CDD\|377178
CP020918.1\|AWG23608.1\|2131733_2132291_+\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21721.1\|2130757_2131621_+\|hydroxymethylglutaryl-CoA-lyase	unknown	unknown	gnl\|CDD\|163676
CP020918.1\|AWG23607.1\|2113518_2114496_-\|23S-rRNA-(adenine(1618)-N(6))-methyltransferase	unknown	unknown	gnl\|CDD\|236964
CP020918.1\|AWG21722.1\|2132287_2133688_+\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21715.1\|2123190_2123868_-\|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD	unknown	unknown	gnl\|CDD\|234581
CP020918.1\|AWG21709.1\|2114597_2115260_-\|thiamine-diphosphokinase	unknown	unknown	gnl\|CDD\|153431
CP020918.1\|AWG21711.1\|2116207_2118616_-\|collagen-binding-protein	unknown	unknown	gnl\|CDD\|238657
CP020918.1\|AWG21723.1\|2133883_2134252_+\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21720.1\|2129678_2130611_+\|peptidylprolyl-isomerase	unknown	unknown	gnl\|CDD\|238194
CP020918.1\|AWG21710.1\|2115381_2116203_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379442
CP020918.1\|AWG21706.1\|2104691_2107745_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
CP020918.1\|AWG21717.1\|2126409_2127405_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223669
CP020918.1\|AWG21708.1\|2112083_2113415_-\|phosphodiesterase	unknown	unknown	gnl\|CDD\|277335
CP020918.1\|AWG21719.1\|2128322_2129504_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|340882
CP020918.1\|AWG21713.1\|2121585_2121936_-\|50S-ribosomal-protein-L19	unknown	unknown	gnl\|CDD\|235418
CP020918.1\|AWG21718.1\|2127517_2128186_+\|peroxiredoxin	unknown	unknown	gnl\|CDD\|239268

Protein	Function_ID	Function_description	E-value
CP020918.1\|AWG21707.1\|2108392_2111692_-\|oar-protein	gnl\|CDD\|379297	pfam13620, CarboxypepD_reg, Carboxypeptidase regulatory-like domain.	2.20197e-17
CP020918.1\|AWG21716.1\|2124042_2126166_+\|dipeptidyl-carboxypeptidase-II	gnl\|CDD\|341051	cd06456, M3A_DCP, Peptidase family M3, dipeptidyl carboxypeptidase (DCP). Peptidase family M3 dipeptidyl carboxypeptidase (DCP; Dcp II; peptidyl dipeptidase; EC 3.4.15.5). This metal-binding M3A family also includes oligopeptidase A (OpdA; EC 3.4.24.70). DCP cleaves dipeptides off the C-termini of various peptides and proteins, the smallest substrate being N-blocked tripeptides and unblocked tetrapeptides. DCP from Escherichia coli is inhibited by the anti-hypertensive drug captopril, an inhibitor of the mammalian angiotensin converting enzyme (ACE, also called peptidyl dipeptidase A). OpdA may play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. It can also cleave N-acetyl-L-Ala. This family also includes Arabidopsis thaliana organellar oligopeptidase OOP (At5g65620), which plays a role in targeting peptide degradation in mitochondria and chloroplasts; it degrades peptide substrates that are between 8 to 23 amino acid residues, and shows a weak preference for hydrophobic residues (F/L) at the P1 position.	0
CP020918.1\|AWG21714.1\|2122450_2122813_-\|four-helix-bundle-protein	gnl\|CDD\|319869	cd16377, 23S_rRNA_IVP_like, 23S rRNA-intervening sequence protein and similar proteins. A family of functionally uncharacterized bacterial proteins, some of which are encoded by an atypically large intervening sequence present within some 23S rRNA genes. The distantly related bAvd protein, which also forms a homopentamer of four-helix bundles, has been suggested to interact with nucleic acids and a reverse transcriptase.	1.70553e-40
CP020918.1\|AWG21712.1\|2118748_2120986_-\|isocitrate-dehydrogenase-(NADP(+))	gnl\|CDD\|377178	pfam03971, IDH, Monomeric isocitrate dehydrogenase. NADP(+)-dependent isocitrate dehydrogenase (ICD) is an important enzyme of the intermediary metabolism, as it controls the carbon flux within the citric acid cycle and supplies the cell with 2-oxoglutarate EC:1.1.1.42 and NADPH for biosynthetic purposes.	0
CP020918.1\|AWG21721.1\|2130757_2131621_+\|hydroxymethylglutaryl-CoA-lyase	gnl\|CDD\|163676	cd07938, DRE_TIM_HMGL, 3-hydroxy-3-methylglutaryl-CoA lyase, catalytic TIM barrel domain. 3-hydroxy-3-methylglutaryl-CoA lyase (HMGL) catalyzes the cleavage of HMG-CoA to acetyl-CoA and acetoacetate, one of the terminal steps in ketone body generation and leucine degradation, and is a key enzyme in the pathway that supplies metabolic fuel to extrahepatic tissues. Mutations in HMGL cause a human autosomal recessive disorder called primary metabolic aciduria that affects ketogenesis and leucine catabolism and can be fatal due to an inability to tolerate hypoglycemia. HMGL has a TIM barrel domain with a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. The cleavage of HMG-CoA requires the presence of a divalent cation like Mg2+ or Mn2+, and the reaction is thought to involve general acid/base catalysis. This family belongs to the DRE-TIM metallolyase superfamily. DRE-TIM metallolyases include 2-isopropylmalate synthase (IPMS), alpha-isopropylmalate synthase (LeuA), 3-hydroxy-3-methylglutaryl-CoA lyase, homocitrate synthase, citramalate synthase, 4-hydroxy-2-oxovalerate aldolase, re-citrate synthase, transcarboxylase 5S, pyruvate carboxylase, AksA, and FrbC. These members all share a conserved triose-phosphate isomerase (TIM) barrel domain consisting of a core beta(8)-alpha(8) motif with the eight parallel beta strands forming an enclosed barrel surrounded by eight alpha helices. The domain has a catalytic center containing a divalent cation-binding site formed by a cluster of invariant residues that cap the core of the barrel. In addition, the catalytic site includes three invariant residues - an aspartate (D), an arginine (R), and a glutamate (E) - which is the basis for the domain name "DRE-TIM".	1.19687e-106
CP020918.1\|AWG23607.1\|2113518_2114496_-\|23S-rRNA-(adenine(1618)-N(6))-methyltransferase	gnl\|CDD\|236964	PRK11727, PRK11727, 23S rRNA (adenine(1618)-N(6))-methyltransferase RlmF.	0
CP020918.1\|AWG21715.1\|2123190_2123868_-\|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD	gnl\|CDD\|234581	PRK00026, trmD, tRNA (guanine-N(1)-)-methyltransferase; Reviewed.	2.02774e-143
CP020918.1\|AWG21709.1\|2114597_2115260_-\|thiamine-diphosphokinase	gnl\|CDD\|153431	cd07995, TPK, Thiamine pyrophosphokinase. Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin pyrophosphokinase) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamine) to form the coenzyme thiamine pyrophosphate (TPP). TPP is required for central metabolic functions, and thiamine deficiency is associated with potentially fatal human diseases. The structure of thiamine pyrophosphokinase suggests that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.	2.33956e-48
CP020918.1\|AWG21711.1\|2116207_2118616_-\|collagen-binding-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.	8.82789e-21
CP020918.1\|AWG21720.1\|2129678_2130611_+\|peptidylprolyl-isomerase	gnl\|CDD\|238194	cd00317, cyclophilin, cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40, a co-chaperone of the hsp90 chaperone system; human cyclophilin A, a chaperone in the HIV-1 infectious process and; human cyclophilin H, a component of the U4/U6 snRNP, whose isomerization or chaperoning activities may play a role in RNA splicing. .	3.09847e-61
CP020918.1\|AWG21710.1\|2115381_2116203_-\|hypothetical-protein	gnl\|CDD\|379442	pfam14054, DUF4249, Domain of unknown function (DUF4249). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 279 and 365 amino acids in length. There are two completely conserved residues (C and G) that may be functionally important.	6.30656e-31
CP020918.1\|AWG21706.1\|2104691_2107745_-\|TonB-dependent-receptor	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	4.1529e-25
CP020918.1\|AWG21717.1\|2126409_2127405_+\|alpha/beta-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	3.3181e-34
CP020918.1\|AWG21708.1\|2112083_2113415_-\|phosphodiesterase	gnl\|CDD\|277335	cd07389, MPP_PhoD, Bacillus subtilis PhoD and related proteins, metallophosphatase domain. PhoD (also known as alkaline phosphatase D/APaseD in Bacillus subtilis) is a secreted phosphodiesterase encoded by phoD of the Pho regulon in Bacillus subtilis. PhoD homologs are found in prokaryotes, eukaryotes, and archaea. PhoD contains a twin arginine (RR) motif and is transported by the Tat (Twin-arginine translocation) translocation pathway machinery (TatAyCy). This family also includes the Fusarium oxysporum Fso1 protein. PhoD 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.	7.97593e-41
CP020918.1\|AWG21719.1\|2128322_2129504_+\|MFS-transporter	gnl\|CDD\|340882	cd17324, MFS_NepI_like, Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily. This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	8.39353e-70
CP020918.1\|AWG21713.1\|2121585_2121936_-\|50S-ribosomal-protein-L19	gnl\|CDD\|235418	PRK05338, rplS, 50S ribosomal protein L19; Provisional.	9.35007e-52
CP020918.1\|AWG21718.1\|2127517_2128186_+\|peroxiredoxin	gnl\|CDD\|239268	cd02970, PRX_like2, Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.	2.57486e-43

>CP020918.1|AWG21714.1|2122450_2122813_-|four-helix-bundle-protein
MDFKSLLAFQKSFELAMEIFKLTKSFPKEETYSLSDQIRRSSRSVSANIAEAYRKRRYPNHFISKLTDSDAENSETNVWLQFALQCDYINQETFDTLNNKSLEIGKLINYMINNPGKFGC
>CP020918.1|AWG21713.1|2121585_2121936_-|50S-ribosomal-protein-L19
MANLVDFVNSEFVTKKDFPVFGAGDTITVYYEIKEGEKTRTQFFKGVVIQRRGTGSTETFTIRKMSGAVGVERIFPVNLPALQKVEINKKGAVRRARIFYFRELTGKKARIKDKRR
>CP020918.1|AWG21712.1|2118748_2120986_-|isocitrate-dehydrogenase-(NADP(+))
MTQKSKIVYTLTDEAPLLATYSFLPIVQAFTSTAGIEIETEDISVAARILANFPEFLTEDQKVKDSLAALGKLANAPEANIIKLPNVSASIPQLKGAIAELQAHGYNVPNYPEDPQTDAEKEIKAKYAKISGSAVNPVLREGNSDRRAPKAVKNYAKANPHSMGAWTADSKTSVASMTEGDFYGSEKSVTVADATDVKIEFVAKDGATTVLKASTPLKVGEIIDSSVMHLNALKSFVAKTIAEAKVEGVLLSVHLKATMMKVSDPIIFGAIVEVYFADVFAKYATLFAELGVNTKNGLGDVYAKIAGRPEQAEVEAAINAAIENGPALAMVNSDKGITNLHVPSDVIVDASMPAMIRTSGQMWNKAGKLQDTIAIIPDRCYAGIYTATIDFCKKHGAFDPTTMGSVPNVGLMAQKAEEYGSHDKTFQISASGTVRVVEVNGNVVMEQAVEANDIFRMCQAKDAPIQDWVKLAVNRARLSATPAVFWLDENRAHDREIIKKVNLYLKDHDTTGLDIRILDPIAATQFTCERIIKGLDTISVTGNVLRDYLTDLFPILEVGTSAKMLSIVPLMNGGGLFETGAGGSAPKHVEQFTQEGYLRWDSLGEFLALGASLEHLGQSLNNEKAIILSETLDQANDAFLKNDKSPARKVGGIDNRGSQFYLAMYWAQALAAQTKDSELQAIFAPIAKELTDNEATINAELIGAQGKPQAIGGHYQPTPALLSKAMRPSATFNSIMDKITALKTA
>CP020918.1|AWG21711.1|2116207_2118616_-|collagen-binding-protein
MLNCKLFAFTLTFLFCLPIFAQTEDKATVSNQKFTLSGVISDSKNNETLIGVNLYVEETKSSINTNQYGFYSITLPQGSYTVQVSYIGFENVSKKITLDKNTRLNFNLSDSEEMLKEVIVTGTNTSTPIRKPEMSVNRLSISSIKKMPVVLGEVDVIKSLLLLPGVTNAGEGASGFNVRGGGADQNLILLDEATIFNSSHVFGFFSVFNPDAIKDLKLYKGGIPANFGGRASSVLDIYQKDGSSKSFHASGGIGLIASRILLEGPLVKNKGSFLIGGRSSYAHLFLKLSEDQKNNTAYFYDLNTKLSYKLNENNNLYLSGYFGRDVFAISKSFSNTYGNATLNLRWNHLFSDKLFTNLSLIYSDYYYGLDLDFVGFKWDSGIKNYNLKYDFKNYISDKFKLSYGLNAIYYSFNPGTIKPSNLDSGINFDQLDKKYAFEPALYVSAEQEISKRIAVTYGLRYSMFYRLGQSTVNIYENNNPVTFNADQQIYEKATPIGTEFYNKNKVIQSYNYLEPRLALSYQLNEDSSLKGSYNRMVQYLQLISNTSSPTPLDVWTPSDNFIKPQIADQVAVGYFKNFSDNMYSLDIETYYKKIQNRLDYIDGADLIANKAIEQIILNGRMRSYGLEIMFRKNEGKLNGWISYTLSKSQQQTPGRTADEIGINNGNWYNSIYDKTHNLAVTAAYKKSEKWTFGANFVLQTGQPVTYPNGQYSYSGIVVPSYGLRNENRLPAYHHLDVSATLTPTKNKDRDWKGEWVFSIYNLYNRKNAASINFRQNSDTGTNEAVRTSIFGMVPAVSYNFKF
>CP020918.1|AWG21710.1|2115381_2116203_-|hypothetical-protein
MKKISLLLLFIVTLVSSSCEEVVQVDLDTAAPKLVIEATIKWQKGTAGNNQKIKLTTTTSYFSNIIPTVSGAKITVKNSSNTVFTFNEIATSGEYGCSNFVPKINETYTLTVIANGQTYTASEILKSVAPIDEIEQKNDGGFTGKDIQLKTYFTDPAPETNYYLYQYSYTGQVTQTFYGDIDTFFQGNKFFSLSQNDDLKIGDEVSVTHYGISKTYYNYMSILISIAGGSSGGPFQAPPATVRGNIINTTNKDNYALGYFALTEIDSRVFTIK
>CP020918.1|AWG21709.1|2114597_2115260_-|thiamine-diphosphokinase
MSSHHIVRDDQEPALIIANGAACNPELLGQLLEWSPIVIVLDSAMERVMKLDIKVDVLLGDFDRGFDPNYYKEKQYPIEIIHTPDQNKTDLEKAFDYLIEKKIPAVNVVWATGRRADHTITNLTNIVRYRNLLKIVILDDHSKVFLLNRKFEKWYTEGTPISLIPIGTVTGIASENLFYPLTNESLTIGYKTGSSNHVTKDGIVKIEHLEGDLLLMECMD
>CP020918.1|AWG23607.1|2113518_2114496_-|23S-rRNA-(adenine(1618)-N(6))-methyltransferase
MMAKQLTEKTKLHPRNLHRSRYDFKLLIERYPALKNFVSTNKHDPESSDETIDFSDPDAVKALNKALLITYYGIQNWDIPKDYLCPPIPGRADYIHNVADLLATTNGGIIPEGESIHGLDIGVGANCIYPILGNSIYGWNFVGTDIDDKALKNCSKIIESNPKLVDAISLQQQIEARFIFKNIITPEDKFEFILCNPPFHTSQEEATQGSIRKINNLENTRTTKPILNFGGHNTELWCEGGEFRFISQMIYESAKYPMQILWFTTLVAKQSHLKSLYKVLNKVNAANIRTIDMAQGQKTSRILAWSFLSDQQQEEWQFQKSDQVI
>CP020918.1|AWG21708.1|2112083_2113415_-|phosphodiesterase
MRSKLSVLAFFISIVLFAQNGILKSGPMVGYCEMKEAMIWLQTTETAKVKIEYFDIENPTVHYFSDEFQSSKEVAYTYHILLDQLQEGKKYQYQLIINDKKVTVPYETTFRSKKFWQWRENAPEFKIAFGSCSYINENPLDRPGKGYGSEYEIFETIAKQNPDIMLWGGDNTYLREADYDSKTGIYHRNTHTRAIKEIQPLLAKAQNIAIWDDHDFGPDDSNRSFYNKYLTQKAFKDFWANKSYGMDPSQQEGVYTTFNWGDAEFFLLDNRFFRSPDERKTGKLTMLGDKQLEWLIDALATSRANFKIVVIGGQVLNSDPKTENYGHYPEEKEKLLSEIAANDIKGVLFLSGDRHFSELSRLERPNTYPLYDWTVSPLTAGVASGKYVAYDNKLRVKDSAFFTHNFGTITFSRDNDNRKMELLLLDKDGNTLWTRTITKNELQ
>CP020918.1|AWG21707.1|2108392_2111692_-|oar-protein
MRKLLFILLLAIQSIGFAQVTKSSISGTVKSTKGEALPGATVEVIHEPTGSKYYATTDGNGRYSVPAIRPGGPYTVKTSFVSYTTTEITEISAPLGNNITINVSLKEETNALKEVVIKSTSGSNLFSKNKTGASQQFSTREINSVPVTGSRSISSVTKYSANAGANGSFGGQDSRLNNFTIDGSVFNNGFGLGGDAQAGGRTGSTAISMDAIEQLQVNIAPFDVRQSGFLGTGINAVTRSGSNEVEGSVYHSFQNNSKTYLGTKAGDNTISSGKFNQKIYGARLGMPIIKNKLFFFGNFETVDNVSPATNWIANDGSGTQTGQVTRTTVTDLNLVSKTLFDNFGYVTGPYQGYDANSTSTKYLARIDWNINDNNKLNVRYVHHDSESDQLVSNSTSAGAGNRRTNVNSLSYQNSGYTVQDNTRSIVLELDSKLSNRTNNNFIAGYDKQIEDRGLQGGGIFPTIDILDGNATYISAGLDPFTKGNKLDYSTLHFTDNLTVTAGKHTIVFGANYERFISNNSFIIANNAAYTFNSLASFIATMAEASTLNGVPTTVNKPSRTQYNYSLLGGDDANQVFKSNKIDLYAQDNIKVSEKLNITFGLRASQLWFANTGIANKFLTGYTNTAGVAVAPLTFADGQTFDSGKGQKSQLLFEPRVGFNLDVYGDKTTQLRGGSGIFTGRPPYVLLSNAIGNSGAITNGFSSTTSGFTADPGQYLTPSSLAPSPKFQLNATADNYKFPQVWKSTIAIDQKLPFGFTGTVESIFGQNINAATYYDANLDAPVGTFGGTDNRTRFARTDAGVRVQDDISGAYVLTSKSKGYFYSTTFKLEYAYQRGLWGSLAYTHSGAYDLNSVGSTAASAYNGTATVNGNNNLTLSNSSNNTPHRIVGTLGYKIQYGGEFGGATSFSLGYIGEQTGANSYTVNGDLNGDQIRGNDLIYVPNSASELRFDPLVASGVTYTEAQQRTALDAYINQDSYLSERRGQYAQRNASTIPMLHRMDLSVTQDFFIKAGKHRNSLQVRADILNFTNMINKNWGVSQRFTNTSPLVYVRTDAATNTPIYKLGTQTVNGTSVLLKDTYQKNTSTSDVWQAQLTLRYTFGR
>CP020918.1|AWG21706.1|2104691_2107745_-|TonB-dependent-receptor
MKKLLLFLSLIFCGIVTAQDIKVSGVVTDDSKGTLPGTTVMVKGTSKGTTTDVNGKYTISAKMGESLQFSFIGLETKTIKVTGSTINVMLAGGGETLQDVVVLGSRSAARTVTESAVPIDVINMKDIASQGSQANLNQILNMVAPSFTSNTTTVADGTDHIDPAQLRGLGPDQVLVLVNGKRRHTSSLVNINGSPGRGSVGTDLNAIPAFAIEKIEVLRDGAAAQYGSDAIAGVINVNVKKATNKLDINILGGSYFSKGANDHRGGNDGNNAQLDVNYGTGLGKEKSFVNVTGSFQLRGQTSRANDATGNIFNAFNAIEQRATEKEQNINSLWGNINNTTNSAQILTSIKSNALGVNYFTAAQQASILGATSISQMQTALNFDATAGELNYRNLQRSAFNMNVGQSSLQSAQFFVNAAYPINDNVELYAFGGTSHRTGEAAGFYRRPNQSRTYTFLYPNGFLPEIHSTINDISAAVGIRGTMMKDWKFDLSNTFGRNGFDYNIENTLNASLRENSPTSFDAGGLAFSQNTTNFDISKKINKLNVAFGAEVRHENFQIKEGEPDSYNQYDINGDIVTATTATNIKATDFYGNVRPGGAQVFPGFKPANTVDKGRTSGAIYADLEYDVTDKWLLNGALRYENYSDFGGTTNYKLATRYKLTDNVNLRGAVSTGFRAPSLHQIYYNSTATQFVGGVPFEVGTFSNDSPAAKLLGIPQLKQEDSQSASFGFTAKIPEAKLTITADAYIVKIKNRVVLTDQFSRPGGTPATGTAAAQLNALFDNANATAATFFANAIDTQSKGIDVVISHKANVGNGLTLKTDLSGTISKTNKVGDIKGSQILKDNGQTNRYFSETSRIYLEEAVPRAKANLTNTLTVKKFDFFLRNVYFGQVTDPNIADVNGDGKINAIVVNGQAVENEHPHWGARIVTDLSVGYKISSSTKIVIGANNIFDIYPSKNLGPQTVAQRASGVDSSGNVVYSATTSSNNSIDLSNANQFTYSRNTSQFGQNGRFLFARLSLSF
>CP020918.1|AWG21715.1|2123190_2123868_-|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD
MRIDIITVLPELLRSPFEASIMKRAIDKGLVEVHFHNLRDYTTNKQKSVDDYAYGGGAGMVMNIQPIDDCISHLKSERTYDEIIYMSPDGETLNQKMANTMSMYENIIILCGHYKGVDQRVRDHFITKEISIGDYVLSGGELGALVLSDALIRLIPGVLSDETSALTDSFQDGLLSGPIYTRPAEYKGWKVPDVLLSGHSGKIDQWREDMAYEHTKNRRPDLLEE
>CP020918.1|AWG21716.1|2124042_2126166_+|dipeptidyl-carboxypeptidase-II
MRIVTNLLLASTAALAFAPLHSIQAQNKSIKMTNPLLQKSSLQYQAPAFNLIKDADYKPAFEFGLAAQDKQITAIANSPAKATFQNTVLALEISGEDLKRATTAFYSQTGANTNPTLQALQVAYAPIFSAHRDKTYLNSKLYNRFKSIDLKTLKGEDKKLTEHYIQEFELAGANLSDADKEKMKKINGELASLGTLFGNKLLTARKNGAVFFDNESELAGLPTGEIKAAKEKATEAGQSGKFLIGLTNTTQQPVLQNLTNRTSREKIFHASWTRAEKNDDGDTREVLEKMARLRLQKANLMGKKNFAEWKQQDQMAKTPDRAMHLLAEIAGPAVKKAKAEAQEIQDLIDAQKGGFKLEPWDWDFYAEQVRKAKYDLDENQVKPYFELTTVLEKGVFFAAKKMYGITFKQRSDLPVYHPDVFAYEVFDNDGKSMAIYYLDFYTRDNKNGGAWMNSLVKQSHYQNQKPVIVNVYNFTKPVDGAPSLISFDNVTTMFHEFGHTLHGLFANQNYATLSGTSVPRDFVEFPSQINEHAALDPEVLKNYAIHYQTKQEIPQDLIDKIKKSETFNSGYHVTELLAASTLDMNWHSVENEKDFKPTLIFEKEALEKYGLLVNEVPTRYHTPYFAHIWSGGYSAGYYAYTWSKTLDYNAFDWMKANGGMTRENCERFRKYILSVGNSVDLNQAFKDFIGHDMEIEPYLKNAGLKDN
>CP020918.1|AWG21717.1|2126409_2127405_+|alpha/beta-hydrolase
MKMKLTVGLFLFTLLSFAQQEKLQWLDSNLSNYEYPFPVHFITLNIQQQELKMEYMDVKPNNYNGKNILLLHGKNFNGAYWKTTIDALTQKGFRVIVPDQIGFGKSSKPDNFQYTFQQLAQNTKQILDSLGIQKTAVLGHSMGGMVAARFALMFPEVTEKLILENPIGLEDWKLKVPYQSVDWWYKGELNQSYDKIKKYQLDSYYDGKWKPEYDQWVNLLAGWTLNSDFKKLAWNSALMYDMIFTQPVVYEFQNIKAPTLLIIGTRDRTALGKPLVSEDVRKTMGLYENLGKETQKKIIGSKLVEIPNIGHMPHIESFDKFINPLLDFLEK
>CP020918.1|AWG21718.1|2127517_2128186_+|peroxiredoxin
MSTANSTIGLQNTLDNAKNTWEATAPEQIKEIYADGIADVIRQNVIANAKKNDDIAPDFTLTNAVGKEVSLSELLKKGPIVLTWYRGGWCPYCNMTLHYLQEQLPNIQLKGANLLALTPELPDKSMSTAEKHQLQFEVLSDVGNKVAKEYGIVFKLTDDVADSYQKGFDLHGYNGDESDELPLAATYVIGQDGKIVYTFLDAEYRNRAEAEPILKALDNLNN
>CP020918.1|AWG21719.1|2128322_2129504_+|MFS-transporter
MNLSKKNVLFMAIATGIIVANIYYCQPLIVLIAAEFNIPPADAGTIAYLTQAGYAIGLFLMVPLGDKLERKTQIMYTTFASIIALILAATAQNYLILEIASLLIGMTSIVPQLILPLAAALSAPENRGKVVGTIMSGLLVGILLSRTLSGFVGNVLGWRAMFWIAAGLCMVLFFIIKKQFPQNKPVFIGSYGQLIGSLFTLIKEQPLLREATLINVFSFAQFGAFWTTMVLLLSGAPFHYNSATIGLFGVVGASGALAAPLLGKLSDKGGSRVAVGYGCLFIALSFVIFYFSSANVYGVICGIVLIDIGLQSVHISNQTRVYSILPEARNRMNTVFMSFSFLGTAAGTAFGLFMWQLGGWQAVTLGGLFLSALAFTVYGITYKSKRKLHCANA
>CP020918.1|AWG21720.1|2129678_2130611_+|peptidylprolyl-isomerase
MENGIYAKFNTSKGAILVKLEHELTPGTVGNFVALAEGNMENKIKPQGQKFYDGLKFHRVIPDFMVQGGCPQGTGTGDPGYKFDDEFHKDLRHNAPGVLSMANSGPGSNGSQFFITHVATPWLDDKHTVFGNVIEGQDVVDAIAQGDNLDSVEIIRVGEEAQKWNAIEAFVGLKGARLKKQAALKAETEAKMETLAAGFEKTESGLRYQFIQRGDGKQAEAGKTVSVHYEGSLESGKVFDSSYPRKKPIEFRLGQGQVIEGWDEGIALLKVGDKARFVIPSDLGYGANGAGGVIPPNATLIFDVELMEVK
>CP020918.1|AWG21721.1|2130757_2131621_+|hydroxymethylglutaryl-CoA-lyase
MKEVKIIECPRDAMQGIKTFIPTEQKAAYIQSLLRVGFDTIDFGSFVSPRAIPQMQDTSALLDQLDLSATTSKLLAIIANTKGAEIAATHSQIDYLGFPFSISENFQMRNTHKTIAESLITLEEILNIADQSNKQVVAYLSMGFGNPYGDPWNMEIVAQWTERMSNMGVKILSLSDTVGSSTPDVIHYLYSHLVPKYPQIEFGAHFHTTYDKWFEKIDAATKGGCTRFDGAIQGFGGCPMAKDELTGNMPTEKLLSYFTSNKINTNLNPLSFESAYNEASKLFNNYK
>CP020918.1|AWG23608.1|2131733_2132291_+|hypothetical-protein
MKNFELLMQKIVSLLFLSLILVSCSSKLDFDQVNDLKLEPVIVANLSYFDIAAPDFVTNGQETIVSGSLQNFDVFRDSFFRDNLVQSDFFFEITNTINRQYRLNLLLLNSQNRILYSINFNVSASAGTPQVVTQKEIFKDVKLDLLKQSQRIAYHIIMLPGKSLTAASTGHLIFKSSATVYMDIQ
>CP020918.1|AWG21722.1|2132287_2133688_+|hypothetical-protein
MRKQLLTFSLLLCSLVSLAQNKQILYNFTAVPQSMMTNPGADVSYKFYFGVPFLSGFSANVGSTGFSAYDLFAANGVDFNTKLRTVVNETTNKDKLVLNEQLEVFNGGFRLGERDNYTYFSFGMYQELDAIVYVPKDPLVLALDGNQNYIGRSFNLGDLNAKAEAVSVLHFGFHKNITEKLILGARAKIYTSGFNVTTTKNAGYVYTIPSNNTVYEQQIYSDLQLQTSGLSNYIDNNAGFEGGKKTAKKAFLGPDLGLGFDLGFTYNPKKNIQWTGSILDIGFINHSSDAKTYTYKGIYNYQGVNPNFSNINNSGDTYQEFQDAIPLDTTRATYKTWRPIKVNASYQYSWNDHRTDAPCDCLGKSNQAYQNGVGAQLFMMSTPKAPMIALTGFYQRRIFTGLNMKATYTVDSFSYSNIGLGLSANIGAFNLYLMGDNLLAYRDLSKAKSLSFQMGLNFVFKGKEEE
>CP020918.1|AWG21723.1|2133883_2134252_+|hypothetical-protein
MKKYLLIIAFLCIGQLVAQDISGNDPDKTLKEKIYTANKKRVMNFSKKQFDALFFEFFEKKNNVNTILSKEEFYQYTIQIAIFSDRLATLYPEEIQIANESKAKWLAEQYDDYLSVIKAKTK

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Crispr_ID: CP020918_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP020918_4

2449757-2449869

Orphan

Consensus_repeat	Method
TACTACGCAAAGTTTGCAAAGCTTTGCGTTCCTAGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP020918_4

>merge|CP020918|4|2449757-2449869|CRISPRCasFinder
TACTACGCAAAGTTTGCAAAGCTTTGCGTTCCTAGCGATTTTATTGAAAGGGTAAATAACCGCAAAGGACGCAAAGTACTACGCAAAGTTCGCAAAGCTTTGCGTTCCTAGCG

>CP020918|4|4|2449757-2449869|CRISPRCasFinder
TACTACGCAAAGTTTGCAAAGCTTTGCGTTCCTAGCG	ATTTTATTGAAAGGGTAAATAACCGCAAAGGACGCAAAG
TACTACGCAAAGTTCGCAAAGCTTTGCGTTCCTAGCG

Protein	Signature genes	Signature genes Name	Protein_function
CP020918.1\|AWG21940.1\|2451780_2452020_-\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21938.1\|2451161_2451359_+\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21929.1\|2439564_2441043_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|293753
CP020918.1\|AWG21933.1\|2445531_2446047_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|273380
CP020918.1\|AWG21934.1\|2446350_2446512_+\|50S-ribosomal-protein-L34	unknown	unknown	gnl\|CDD\|366117
CP020918.1\|AWG21942.1\|2455794_2456475_-\|Crp/Fnr-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223736
CP020918.1\|AWG21930.1\|2441599_2442562_+\|IS30-family-transposase	unknown	unknown	gnl\|CDD\|225382
CP020918.1\|AWG21937.1\|2450766_2451000_-\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG23626.1\|2453796_2455602_+\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21928.1\|2438601_2438910_-\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG21941.1\|2452253_2453420_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377511
CP020918.1\|AWG23625.1\|2450017_2450464_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|225064
CP020918.1\|AWG21926.1\|2436594_2437227_+\|NAD-dependent-dehydratase	unknown	unknown	gnl\|CDD\|187554
CP020918.1\|AWG21936.1\|2450477_2450777_-\|plasmid-stabilization-protein	unknown	unknown	gnl\|CDD\|226194
CP020918.1\|AWG21932.1\|2443870_2445100_-\|IS4-family-transposase	unknown	unknown	gnl\|CDD\|372999
CP020918.1\|AWG21935.1\|2446654_2449507_+\|carbamoyl-phosphate-synthase-large-subunit	unknown	unknown	gnl\|CDD\|235393
CP020918.1\|AWG21943.1\|2456582_2458970_+\|heavy-metal-translocating-P-type-ATPase	unknown	unknown	gnl\|CDD\|319851
CP020918.1\|AWG21939.1\|2451488_2451791_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|368240
CP020918.1\|AWG21931.1\|2442749_2443736_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|275056
CP020918.1\|AWG21927.1\|2437672_2438263_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378690

Protein	Function_ID	Function_description	E-value
CP020918.1\|AWG21941.1\|2452253_2453420_+\|hypothetical-protein	gnl\|CDD\|377511	pfam05426, Alginate_lyase, Alginate lyase. This family contains several bacterial alginate lyase proteins. Alginate is a family of 1-4-linked copolymers of beta -D-mannuronic acid (M) and alpha -L-guluronic acid (G). It is produced by brown algae and by some bacteria belonging to the genera Azotobacter and Pseudomonas. Alginate lyases catalyze the depolymerization of alginates by beta -elimination, generating a molecule containing 4-deoxy-L-erythro-hex-4-enepyranosyluronate at the nonreducing end. This family adopts an all alpha fold.	2.05886e-92
CP020918.1\|AWG21929.1\|2439564_2441043_-\|hypothetical-protein	gnl\|CDD\|293753	cd16029, 4-S, N-acetylgalactosamine 4-sulfatase, also called arylsulftase B. Sulfatases catalyze the hydrolysis of sulfuric acid esters from a wide variety of substrates. N-acetylgalactosamine 4-sulfatase catalyzes the removal of the sulfate ester group from position 4 of an N-acetylgalactosamine sugar at the non-reducing terminus of the polysaccharide in the degradative pathways of the glycosaminoglycans dermatan sulfate and chondroitin-4-sulfate. N-acetylgalactosamine 4-sulfatase is a lysosomal enzyme.	4.99952e-147
CP020918.1\|AWG21933.1\|2445531_2446047_-\|hypothetical-protein	gnl\|CDD\|273380	TIGR00990, Mitochondrial_import_receptor_subunit_TOM70, mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70). [Transport and binding proteins, Amino acids, peptides and amines].	0.00501415
CP020918.1\|AWG21934.1\|2446350_2446512_+\|50S-ribosomal-protein-L34	gnl\|CDD\|366117	pfam00468, Ribosomal_L34, Ribosomal protein L34.	2.32354e-11
CP020918.1\|AWG21942.1\|2455794_2456475_-\|Crp/Fnr-family-transcriptional-regulator	gnl\|CDD\|223736	COG0664, Crp, cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms].	4.50692e-39
CP020918.1\|AWG21930.1\|2441599_2442562_+\|IS30-family-transposase	gnl\|CDD\|225382	COG2826, Tra8, Transposase and inactivated derivatives, IS30 family [DNA replication, recombination, and repair].	2.12179e-84
CP020918.1\|AWG21943.1\|2456582_2458970_+\|heavy-metal-translocating-P-type-ATPase	gnl\|CDD\|319851	cd07553, P-type_ATPase_HM, P-type heavy metal-transporting ATPase; uncharacterized subfamily. Uncharacterized subfamily of the heavy metal-transporting ATPases (Type IB ATPases) which transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.	0
CP020918.1\|AWG23625.1\|2450017_2450464_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|225064	COG2153, ElaA, Predicted acyltransferase [General function prediction only].	7.79814e-62
CP020918.1\|AWG21926.1\|2436594_2437227_+\|NAD-dependent-dehydratase	gnl\|CDD\|187554	cd05243, SDR_a5, atypical (a) SDRs, subgroup 5. This subgroup contains atypical SDRs, some of which are identified as putative NAD(P)-dependent epimerases, one as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is very similar to the extended SDRs, GXXGXXG, and binds NADP. Generally, this subgroup has poor conservation of the active site tetrad; however, individual sequences do contain matches to the YXXXK active site motif, the upstream Ser, and there is a highly conserved Asp in place of the usual active site Asn throughout the subgroup. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	3.28912e-56
CP020918.1\|AWG21936.1\|2450477_2450777_-\|plasmid-stabilization-protein	gnl\|CDD\|226194	COG3668, ParE, Plasmid stabilization system protein [General function prediction only].	5.068e-05
CP020918.1\|AWG21932.1\|2443870_2445100_-\|IS4-family-transposase	gnl\|CDD\|372999	pfam14294, DUF4372, Domain of unknown function (DUF4372). This domain family is found in bacteria, and is approximately 80 amino acids in length. The family is found in association with pfam01609. There is a single completely conserved residue G that may be functionally important.	4.4897e-19
CP020918.1\|AWG21935.1\|2446654_2449507_+\|carbamoyl-phosphate-synthase-large-subunit	gnl\|CDD\|235393	PRK05294, carB, carbamoyl-phosphate synthase large subunit.	0
CP020918.1\|AWG21939.1\|2451488_2451791_-\|hypothetical-protein	gnl\|CDD\|368240	pfam05016, ParE_toxin, ParE toxin of type II toxin-antitoxin system, parDE. ParE is the toxin family of a type II toxin-antitoxin family. It is toxic towards DNA gyrase, but is neutralized by the antitoxin ParD. The family also encompasses RelE/ParE described in.	0.00145385
CP020918.1\|AWG21931.1\|2442749_2443736_-\|hypothetical-protein	gnl\|CDD\|275056	TIGR04211, hypothetical_protein, SH3 domain protein. Members of this protein family have a signal peptide, a strongly conserved SH3 domain, a variable region, and then a C-terminal hydrophobic transmembrane alpha helix region.	0.000142098
CP020918.1\|AWG21927.1\|2437672_2438263_-\|hypothetical-protein	gnl\|CDD\|378690	pfam11667, DUF3267, Putative zincin peptidase. This family of proteins has a conserved HEXXH motif, suggesting the members are putative peptidases of zincin fold.	3.06799e-17

>CP020918.1|AWG21935.1|2446654_2449507_+|carbamoyl-phosphate-synthase-large-subunit
MPKDTSIKSVLIIGSGPIVIGQACEFDYAGSQSARSIREEGIEVILINSNPATIMTDPSMADHIYLKPLTTKSIIEILKEHPQIDSVLPTMGGQTALNLCLEADEKGIWKDFGVKMIGVDVNAINITEDREQFKQLLQKIGVPTAPAEICTSYLRGKEIAQEYGFPLVIRPSFTLGGTGGAVVYKPEDFDKLLTQGLEASPIHEVLIDKALMGWKEYELELLRDKNDNVVIICSIENMDPMGIHTGDSITVAPAMTLSDTTFQKLRDYAILMMRSIGNFAGGCNVQFAVSPDEKEDIVAIEINPRVSRSSALASKATGYPIAKIATKLALGYNLDELQNQITKSTSALFEPTLDYVIVKIPRWNFDKFEGSDRTLGIQMKSVGEVMGIGRSFQEALHKATQSLEIKRNGLGADGKGYTNYEQVIEKLTNASWDRVFVIYDAIAMGIPLSRIHEITKIDMWFLKQYEELYTLEKEISKYTVANLPKELLLEAKQKGFADRQIAHMMKCLESEVHTLRMDKNINRVFKLVDTCAAEFEAKTPYYYSTFEAEIEKADGTRYVDNESIVTDKKKIVVLGSGPNRIGQGIEFDYSCVHGVLAAKECGYETIMINCNPETVSTDFDTADKLYFEPVYWEHIYDIIQHEKPEGVIVQLGGQTALKLAEKLSKYGVKIIGTSFDALDLAEDRGRFSDLLTELDIPFPQFGIAETADEASALADTLDFPLLIRPSYVLGGQGMKIVINKQELEEHVVNLLKTIPGNKLLLDHYLDGAIEAEADAICDGENVYIIGIMEHIEPCGVHSGDSNATLPPFNLGEFVMQQIKDHTKKIALGLKTVGLINIQFAIKDETVYIIEANPRASRTVPFIAKAYGEPYVNYATKVMLGHNKVTDFTFNPQLKGFAIKQPVFSFSKFPNVNKALGPEMKSTGESILFIDDLKDDQFYELYSRRKMYLSK
>CP020918.1|AWG21934.1|2446350_2446512_+|50S-ribosomal-protein-L34
MSKRTFQPSKRKRRNKHGFMDRMASANGRKVLARRRAKGRHKLTVSCDPRHKK
>CP020918.1|AWG21933.1|2445531_2446047_-|hypothetical-protein
MFHKNIKLIIAGLLVIASIWQFTEHNIGNGIFLILLTVFPIFFYFKNEFILLAFLKLRKQDFPGATKMLAFIRNPEAALVQKQQGYFNYLHGIMLSQTNLTQAEKYFKKAIELGLSMDMDLAVAKLNLAGVAMTRRRKLEATNLLNEAKKLDKQGMLTDQIKMMKDQMKKM
>CP020918.1|AWG21932.1|2443870_2445100_-|IS4-family-transposase
MGLFKRNKNNNKPLLRQILDLVPRWILESCVKKHQSDKGCSKYKTYDQFVALTFGQLNKCYTLSDISTGIGVCESFITDLGLNQSPARSTMSDGNKKRTWKVYEALYVKLLSHYDKVLKNDNHRTIIQEIKDHSIKLIDSTTISLCLSMFDWAKFRTAKGGIKIHTCFDDALQIPDLINITEAKTHDSKGLGQNIFPKNTIIVEDRAYFDFVLMLNRIFAQNIFVTRIKTNTDYIIVNELELPLDKDQDILKDEIITLSGKKAVETTINEHNLRLVTVYREEDNKVIHIITNNLDWTARTIADLYKKRWDIELFFKAMKQNLQIKTFLGTSENAVKSQIYVALISYLLLELINRTIAKKVKTFSNFVEKIRVCLAFYLSLEYVCNQVNEGAKKVINQNKIVFKPDLFSQ
>CP020918.1|AWG21931.1|2442749_2443736_-|hypothetical-protein
MSERELENLFIEFLLNRGYSRDNLLSQFAIRIDQEKTLFRPDLLIIDTVNKEYIGLIEFKNRIDERIEEITLGQFYKLFSYLGTKNIPAYLVIPIDEQDFQIFGLTKDNSFEPISKDDFPNFKTLSAKRITEEKIKQRELYKKKCAELEDKKRRNKQSSYLALLSLIVGISASLIAVFFQQKGFDKQSKQPDLCCDSLENQFKNLQDKVLVLERQLNNIAKSNNKTDTIFRNSNLSFLEKRVKIIETGISDNPEKTLSLLQVRQEIELLKKADDYSKELTQSKLDVIQKEMEVQNTWMLGVLIAIFGTILSLVIPNLLARRNGNHTNT
>CP020918.1|AWG21930.1|2441599_2442562_+|IS30-family-transposase
MSHLTIEQRYEIATLRSQGFSMSKIGGFIGRDKSVISRELSRNSDQRNNVYKAKLAQSKASIRQHEKAKKIRFTEQIKARVIHLLEEDFSPEQIVGYCSDKNFECVSIETIYQFIWSDKKKGGQHYKHLRTKGKRYAKRGALKGSRGIIKDRVGIENRPLVVEEKQRIGDLEIDLVIGKNHKGALLTINDRASGVLKMAKINSKESQEIQEKLIELLMDWKPILHTITSDNGKEFANHKKVSEILEISYFFANPYCSWERGANENLNGLVRQYFPKKYNFDLITEEEVLRVTNKLNNRPRKRFGFKSPNEIFEQKLKQCA
>CP020918.1|AWG21929.1|2439564_2441043_-|hypothetical-protein
MNKLIMKKRNLLLIIAMTIFSVSCSLLAKKDTDRSTTNTVAQKDSKSQPNVIFILVDDMGFGDVGYNGSEIATPNLDKMARKGMTLNRNYVYPICSPTRASLLTGQNPLYYGIDGPISDDNGLPIDLKIMPEYFKDLGYQTFMVGKWHLGIGNTDYWPISRGFDSHYGFLGGSIDYYTHVYSGGLDWQREGVSLREEGHATDLFTAEAKKIINDRDPNNPFFLYLAYNAPHTPLQTTPKNSGLNKDVTPGNRYVYAEMVTQVDDGIGQIIEALENQGILENTIVVFSSDNGGLLSLGSNNGELRGGKGSPWEGGMRVPGLIMWSNHITAGQVLDQQIAIQDWLPTLLDAVGGESSPLEIQSGQTMWSAINSGIKIERNPLIIGSASGKAVFDWPWKLVREGDDGEHQLYNVLEDPYEKENLAQVKPEILTRLETVLAALPNVPTRRTVDEKASSANGSIKKTHKSQGRNIDYEAREKETREPWAEAALKGNN
>CP020918.1|AWG21928.1|2438601_2438910_-|hypothetical-protein
MGTQPTNQTMLDKDFVTSQIKKNIKLFNPLDFCNNGGWPNFDELEIVILSDVENTNGNQIKVSILYSCDYPASCSCFEGNSKPDSLHKELFIGNDGSFEVLS
>CP020918.1|AWG21927.1|2437672_2438263_-|hypothetical-protein
MQNLDHYKKDKLTINIVKANIYGIFGAIPIVIVYLFPFLLLWKDKLNPHAFRTSIKEAALSYTRFEVLAIIMLVITLGIVVHELIHGITWAKYTKKRFKSIKFGFLWKMLTPYCHCTEPLRVKEYITGAIMPAIILGFLPAIYAILFGNIFVLLFAILFTVVAIGDFMIINLLRKEDMNSLVLDHPSEAGCFIYRK
>CP020918.1|AWG21926.1|2436594_2437227_+|NAD-dependent-dehydratase
MENILVAGANGTTGKKIIALLHTSDNFNPIAMVRKEEQQTYFKDQNIETVLGDLTDNVDSVFNTKIDRVIFAAGSGGKNVVGVDQEGAKKMIDASKKANVKKFVMLSSMGADKPEEATQLVDYLKAKHNADEYLKSSGLEYSIVRPGTLTNDDQLATIELALKLNKRGEISRADVAQTLVQSLADKTATNATFEIIKGEKNITEALAQMN
>CP020918.1|AWG23625.1|2450017_2450464_+|GNAT-family-N-acetyltransferase
MNIVWLIKPFEALTVNELYDMLQLRSEVFVVEQNCVYLDLDGKDKKGLHLIGTYDGKIVACTRLFKPGISYEYASIGRVVVAQAYRDKKWGHDLMRESIAGIKEHYGETNITIGAQLYLKKFYESHGFVQSTEMYLEDGIPHIEMKRE
>CP020918.1|AWG21936.1|2450477_2450777_-|plasmid-stabilization-protein
MNYKIVVSPIAKQNIEDAVDYYVKQVSTKVALEFLKDYRKTYKALQKNPFYQFHDTNYRFIPFKKFKYIAFFIVDEKNKTVFINAIFNTYQDPEKQPRI
>CP020918.1|AWG21937.1|2450766_2451000_-|hypothetical-protein
MNTQQLQKDKLNIINWISQLEDVSVVEKVKALMGSSVKKYTLTTEQQKILDKQLGLDPTLYTDADKIYSDLKAKHEL
>CP020918.1|AWG21938.1|2451161_2451359_+|hypothetical-protein
MLRVENYVNYFFAAKANKEPELTMLIRDADKKLTQQLTTVVDKEMIASNDAKLKYNFDGIRTDKI
>CP020918.1|AWG21939.1|2451488_2451791_-|hypothetical-protein
MRAKVKFALHVKQDIKQATTWYNQAQKGLGTRFFKNIKEEINFIANQPECFQIRYETIHVAVIKIFPYTIHYQFLKSENTIIILGVFHTSIHPEKWTKRL
>CP020918.1|AWG21940.1|2451780_2452020_-|hypothetical-protein
MDAIRQFIDVKGKSFQVNLPEGFTATRVEVIILPSELSNENEIPNWQMDLVSERIEAIKQNPDLVLEEDQFWNDLENEG
>CP020918.1|AWG21941.1|2452253_2453420_+|hypothetical-protein
MKKIVIMLTFVACTGMQAQVAVWNMKSLDTAKANKEPEIAMLIRDADKKLTQQLTTVVDKEMTPSSGDKHDYMSMGRYWWPDPIKADGLPYIRKDGVSNPEIEKLDRYPLGAFAKSIETLSLAYYVTGNEKYAQKAVDNLKIWFVNPDTRMNPNMNYGQTIPGIRNGLGRGEGVLDTYSFLEMLDGVELLKKSKSFLINDQEAVKQWFTAYVNWLLTAPVAKEEQEAKNNHGTAFDVQLARYALFIGNEDLTRKIVSDFPQNRLFSQIQPDGSQPLELERTTALGYSTFNLTHFLDMTKIGKVMGIDLLQAKSQDGRSIQKAIDFLIPFLNMSVSSFPYKQIKDWDEVREKLLWQMYRLDKMVEKPLYKEVYQKKLKKSKKDIGILLF
>CP020918.1|AWG23626.1|2453796_2455602_+|hypothetical-protein
MIKTNSPHSFHIPVMGLGYTIDSPIRVAHYGISSVVSIVDDDLIEKMNRYYSQKFNFKYQEITQKMHDYRAERVTAYLNLMDTVVKQKFNDFKEELAASKTVLTNYLAMLPQTSDLKKGLQNRMEEGKEAILNYLDSHLSPGAIDVNIMTKVDKDNFDKDQQLPIEFNDAHASLRGFANSNLRSSVVLSAGMNPRLYSYFENFDCFFPNTEDQLEKKIILKVSDFRSAMIQGNFLAKKGLWVSEYRIESGLNCGGHAFATEGLLLGPILEEFKEKKDQLIQSAHDLMVKALTIKGKHIPEQPLELIITAQGGVGTAQEHDFLLEHYQLDSIGWGSPFLLVPEATSVDPETRKLLAKAKEEDFYLSAISPLGIPFNAVKGTTNEAFKQKRIDDEVPGSSCPKKFLALSKEYGAKGMCSASKKYQDLKLEELATQKDSFSPEAYSKRKNVITDKSCLCVGLANASYLENDIAIKGQKQGVVVCPGPNLAYFDHEVSLLDMVEHIYGTTSILTVPNRPNLFVNELKMYVDYLRNEIANFSETIAAGQIKKWKTFRDNLLSGIQYYNDMFANAAVLPENNENTKGQLAFYKQEIEAIMIPELAVA
>CP020918.1|AWG21942.1|2455794_2456475_-|Crp/Fnr-family-transcriptional-regulator
MGKCDQCIVRQYTSMKALNKDEVIKLANCKTSYTVKKGDIIFSEGDPMNGVFCIKDGVCKLSKLTSSGKDQIVKISKRGELLGQRSMISDESANLSAIALEDMEICFIPKTEILGFFDDNNQFSMNMMKSVCGDLKTSDDHIISMAQKNVKSRLAETLLYLETNFGNNPDGSLHIQLTREELSGMIGTATESCIRLLSEFKKLGYIELDGKKTTIKDHSSLKKMAE
>CP020918.1|AWG21943.1|2456582_2458970_+|heavy-metal-translocating-P-type-ATPase
MDASKCFHCGLDIVEAEEIVFDEKSFCCNGCKTVYEIFSVNDMTCYYDFENSPGATPLDIQGKYDFLDNDQIVAKLLEFEEEKTAIVSLSIPHIHCSSCIWILENLQKLESGISTSQVNFSQKKVRIVYDQTAVSLKSIVLLLSRIGYEPYITLENYETGSKNVDRSLTYKLGVAFFCFGNIMLLSFPEYFEVGEYWLDTYKPFFRGLILILSLPAFLYSASGYYVSAFKSIKSGLLNIDVPIALGIIVMFVRSLVDITFNYGSGFFDSLTGLIFFMLLGKSFQMKTYNFLNFERDFKSYFPIAITRLMDGNKEESIPVYEIEKGDRLLIRNQELIPVDGILMSETASIDYSFVTGEADPVTKKSGDKIFAGGKQMGKVIEMQVLHSVSQSYLTQLWSNDIFQKTVDQKHKSITDTVSRYFTPILLVIAFVSFAFWLFIDTKTAFNVFTAILIVACPCALALTAPFTLGNILRIVGKQKFYLKNALVIEQLAAVDTIVFDKTGTITTNKKAAIEYKGKTLVHHQLAFVKNSLRASNHPLSRMLYDFLPETQSVKLDDFVEITGKGIQATIDGIVVQLGSASFCGLESQDSTEIKNTSVHIKIDGHYLGAYEFKNQYRDGLEHLFQDLSKKYELKVLSGDNEGERATLETILPRGTELVFNQKPDEKLEFIKRLQESGKNVMMVGDGLNDAGALAQSNIGISISENVNVFSPACDGILEANEFEKLNYFLQLAKKSMLVIKMSFGLSLLYNIVGLSFAITGNLLPLVAAILMPLSTITIVSFVTIMSNYYGRKVVK

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Crispr_ID: CP020918_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP020918_5

3379173-3379307

Orphan

Consensus_repeat	Method
ATTAAGGATTTTTGAATTAAGGTATTAGGATTTTTAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP020918_5

>merge|CP020918|5|3379173-3379307|CRISPRCasFinder
ATTAAGGATTTTTGAATTAAGGTATTAGGATTTTTAAAGTGATTAACGATTGGTAATTAACGATTTTTGATTGCTGATTTGTTAGAACGGAATAAAAATTAAGGATTTTTGAATTAAGGAATTAGGATTTTTAAA

>CP020918|5|5|3379173-3379307|CRISPRCasFinder
ATTAAGGATTTTTGAATTAAGGTATTAGGATTTTTAAA	GTGATTAACGATTGGTAATTAACGATTTTTGATTGCTGATTTGTTAGAACGGAATAAAA
ATTAAGGATTTTTGAATTAAGGAATTAGGATTTTTAAA

Protein	Signature genes	Signature genes Name	Protein_function
CP020918.1\|AWG22649.1\|3391555_3394042_+\|glycoside-hydrolase-family-2	unknown	unknown	gnl\|CDD\|225789
CP020918.1\|AWG22636.1\|3374277_3375429_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270453
CP020918.1\|AWG22639.1\|3377838_3379074_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|270303
CP020918.1\|AWG22638.1\|3376697_3377837_+\|CoA-transferase	unknown	unknown	gnl\|CDD\|367110
CP020918.1\|AWG22634.1\|3372300_3373143_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224332
CP020918.1\|AWG22633.1\|3371399_3372245_+\|integrase	unknown	unknown	gnl\|CDD\|222853
CP020918.1\|AWG22647.1\|3389116_3390079_-\|IS30-family-transposase	unknown	unknown	gnl\|CDD\|225382
CP020918.1\|AWG22630.1\|3367734_3368505_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235852
CP020918.1\|AWG22648.1\|3390509_3391379_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|185687
CP020918.1\|AWG22635.1\|3373184_3374237_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|237401
CP020918.1\|AWG22646.1\|3388126_3388966_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|271154
CP020918.1\|AWG22637.1\|3375537_3376680_+\|carnitine-dehydratase	unknown	unknown	gnl\|CDD\|367110
CP020918.1\|AWG22641.1\|3380691_3381135_+\|dehydratase	unknown	unknown	gnl\|CDD\|239530
CP020918.1\|AWG22640.1\|3379609_3380680_+\|oxidoreductase	unknown	unknown	gnl\|CDD\|223745
CP020918.1\|AWG22642.1\|3381221_3382787_+\|alpha-L-fucosidase	unknown	unknown	gnl\|CDD\|214829
CP020918.1\|AWG22645.1\|3386237_3387413_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|185687
CP020918.1\|AWG22644.1\|3384737_3385895_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|185687
CP020918.1\|AWG22631.1\|3370051_3370861_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|197271
CP020918.1\|AWG22632.1\|3371037_3371349_+\|transposase	unknown	unknown	gnl\|CDD\|366690
CP020918.1\|AWG22643.1\|3382873_3384460_+\|acetylglucosamine-6-sulfatase	unknown	unknown	gnl\|CDD\|293755

Protein	Function_ID	Function_description	E-value
CP020918.1\|AWG22649.1\|3391555_3394042_+\|glycoside-hydrolase-family-2	gnl\|CDD\|225789	COG3250, LacZ, Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].	2.44463e-71
CP020918.1\|AWG22636.1\|3374277_3375429_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|270453	cd14750, PBP2_TMBP, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose; possesses type 2 periplasmic binding fold. This group represents the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	1.47894e-20
CP020918.1\|AWG22639.1\|3377838_3379074_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|270303	cd13585, PBP2_TMBP_like, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold. This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	5.12616e-50
CP020918.1\|AWG22638.1\|3376697_3377837_+\|CoA-transferase	gnl\|CDD\|367110	pfam02515, CoA_transf_3, CoA-transferase family III. CoA-transferases are found in organisms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.	6.65697e-120
CP020918.1\|AWG22634.1\|3372300_3373143_-\|hypothetical-protein	gnl\|CDD\|224332	COG1414, IclR, Transcriptional regulator [Transcription].	3.09928e-43
CP020918.1\|AWG22633.1\|3371399_3372245_+\|integrase	gnl\|CDD\|222853	PHA02517, PHA02517, putative transposase OrfB; Reviewed.	9.35107e-26
CP020918.1\|AWG22647.1\|3389116_3390079_-\|IS30-family-transposase	gnl\|CDD\|225382	COG2826, Tra8, Transposase and inactivated derivatives, IS30 family [DNA replication, recombination, and repair].	2.12179e-84
CP020918.1\|AWG22630.1\|3367734_3368505_-\|hypothetical-protein	gnl\|CDD\|235852	PRK06688, PRK06688, enoyl-CoA hydratase; Provisional.	1.013e-59
CP020918.1\|AWG22648.1\|3390509_3391379_-\|hypothetical-protein	gnl\|CDD\|185687	cd02178, GH16_beta_agarase, Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.	1.89255e-73
CP020918.1\|AWG22635.1\|3373184_3374237_+\|hypothetical-protein	gnl\|CDD\|237401	PRK13499, PRK13499, L-rhamnose/proton symporter RhaT.	1.73964e-85
CP020918.1\|AWG22646.1\|3388126_3388966_-\|hypothetical-protein	gnl\|CDD\|271154	cd14488, CBM6-CBM35-CBM36_like_2, uncharacterized members of the carbohydrate binding module 6 (CBM6) and CBM35_like superfamily. Carbohydrate binding module family 6 (CBM6, family 6 CBM), also known as cellulose binding domain family VI (CBD VI), and related CBMs (CBM35 and CBM36). These are non-catalytic carbohydrate binding domains found in a range of enzymes that display activities against a diverse range of carbohydrate targets, including mannan, xylan, beta-glucans, cellulose, agarose, and arabinans. These domains facilitate the strong binding of the appended catalytic modules to their dedicated, insoluble substrates. Many of these CBMs are associated with glycoside hydrolase (GH) domains. CBM6 is an unusual CBM as it represents a chimera of two distinct binding sites with different modes of binding: binding site I within the loop regions and binding site II on the concave face of the beta-sandwich fold. CBM36s are calcium-dependent xylan binding domains. CBM35s display conserved specificity through extensive sequence similarity, but divergent function through their appended catalytic modules.	0.00189729
CP020918.1\|AWG22637.1\|3375537_3376680_+\|carnitine-dehydratase	gnl\|CDD\|367110	pfam02515, CoA_transf_3, CoA-transferase family III. CoA-transferases are found in organisms from all lines of descent. Most of these enzymes belong to two well-known enzyme families, but recent work on unusual biochemical pathways of anaerobic bacteria has revealed the existence of a third family of CoA-transferases. The members of this enzyme family differ in sequence and reaction mechanism from CoA-transferases of the other families. Currently known enzymes of the new family are a formyl-CoA: oxalate CoA-transferase, a succinyl-CoA: (R)-benzylsuccinate CoA-transferase, an (E)-cinnamoyl-CoA: (R)-phenyllactate CoA-transferase, and a butyrobetainyl-CoA: (R)-carnitine CoA-transferase. In addition, a large number of proteins of unknown or differently annotated function from Bacteria, Archaea and Eukarya apparently belong to this enzyme family. Properties and reaction mechanisms of the CoA-transferases of family III are described and compared to those of the previously known CoA-transferases.	1.84045e-121
CP020918.1\|AWG22641.1\|3380691_3381135_+\|dehydratase	gnl\|CDD\|239530	cd03446, MaoC_like, MoaC_like Similar to the MaoC (monoamine oxidase C) dehydratase regulatory protein but without the N-terminal PutA domain. This protein family has a hot-dog fold similar to that of (R)-specific enoyl-CoA hydratase, the peroxisomal Hydratase-Dehydrogenase-Epimerase (HDE) protein, and the fatty acid synthase beta subunit.	1.11034e-44
CP020918.1\|AWG22640.1\|3379609_3380680_+\|oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	7.47268e-41
CP020918.1\|AWG22642.1\|3381221_3382787_+\|alpha-L-fucosidase	gnl\|CDD\|214829	smart00812, Alpha_L_fucos, Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.	1.77765e-124
CP020918.1\|AWG22645.1\|3386237_3387413_+\|hypothetical-protein	gnl\|CDD\|185687	cd02178, GH16_beta_agarase, Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.	8.66127e-69
CP020918.1\|AWG22644.1\|3384737_3385895_-\|hypothetical-protein	gnl\|CDD\|185687	cd02178, GH16_beta_agarase, Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.	1.10337e-32
CP020918.1\|AWG22631.1\|3370051_3370861_-\|hypothetical-protein	gnl\|CDD\|197271	cd09174, PLDc_Nuc_like_unchar2, Putative catalytic domain of uncharacterized hypothetical proteins closely related to Nuc, , an endonuclease from Salmonella typhimurium. Putative catalytic domain of uncharacterized hypothetical proteins, which show high sequence homology to the endonuclease from Salmonella typhimurium and vertebrate phospholipase D6. Nuc and PLD6 belong to the phospholipase D (PLD) superfamily. They contain a short conserved sequence motif, the HKD motif (H-x-K-x(4)-D, where x represents any amino acid residue), which characterizes the PLD superfamily and is essential for catalysis. Nuc and PLD6 utilize a two-step mechanism to cleave phosphodiester bonds: Upon substrate binding, the bond is first attacked by a histidine residue from one HKD motif to form a covalent phosphohistidine intermediate, which is then hydrolyzed by water with the aid of a second histidine residue from the other HKD motif in the opposite subunit. However, proteins in this subfamily have two HKD motifs in a single polypeptide chain.	1.93138e-31
CP020918.1\|AWG22632.1\|3371037_3371349_+\|transposase	gnl\|CDD\|366690	pfam01527, HTH_Tnp_1, Transposase. Transposase proteins are necessary for efficient DNA transposition. This family consists of various E. coli insertion elements and other bacterial transposases some of which are members of the IS3 family.	2.56739e-07
CP020918.1\|AWG22643.1\|3382873_3384460_+\|acetylglucosamine-6-sulfatase	gnl\|CDD\|293755	cd16031, G6S_like, unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS). N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.	0

>CP020918.1|AWG22639.1|3377838_3379074_+|ABC-transporter-substrate-binding-protein
MSKPKFKIAVRKFDAFETSIAKIWDAFCAETGCDFELEATAFDLHPLYDTILKNKGLANGDWDVSLINTDWITEAFATNAVEDLTPYIAANSPADFPEGWSESLLYKQRFEGKTVGLPFHDGPECLIYRKDLFDSMEEQITFYGLHGKQLEVPKTWDDLMEVAEFFNRPDQGLYGTTFAAYPDGHNTVFDFCLQLWTRGGDLFDLNKKIKINTQIAIEGMEFYRSALKNTKAIHPDSREFDSVKSGMAFANGNLAMMVNWFGFASFGEVYPDSKVKGKIDVTNVPAGPNGEGVSLNAYWMYVIGKGSTNKDLAYDFIQFAVNAKNDKLLTLEGGIGCRKSTWHDKEVNELVPYYYKLEELHKNTRSLPRKSNWSEIADVIDQIVVEVINSDKSIALILEEAQGKIDLIEEV
>CP020918.1|AWG22638.1|3376697_3377837_+|CoA-transferase
MKPLQDILIVDLSQFLSAPSATLRLADLGARVIKVERPETGDICRQLYVSNVILNGESTVFRAINRNKESFQADLKVEKDKAQVLKLIEKADVLVHNFRPGVIERLGFDYETIKKINPSIVYGDISGYGDEGPWKSKPGQDLLVQSLSGVTWLNGKISDGPVPVGLAIVDILAGAHLAQGILAGLIKKAKTGEGSKVSISMLESILDFQFESITTFYHDGGAPTIRPESNSAHAYLGAPYGVYQTASGYMSLAMGAIPFVGELIGCGALSAYPERESWFTERNEIKKILANHLLTNTTEHWLSLLEPADIWCAKIMNWDELFAHDGFKILEMIQKVKMGDGFEYETTRCPIKIDGQYMKSSLGSPALGEHTEAIIKEML
>CP020918.1|AWG22637.1|3375537_3376680_+|carnitine-dehydratase
MKPLEGIVVLEFAQFMAGPSAGLRLADLGARVIKIERPVHGEAGRQIALKNLFLDGSSLVFHTVNRNKESYAADLKNPEDLECVRQLIAKADVMTHNFRPGVMEKIGLDYEKVKAINPKMIYATVTGYGTEGAWVKKPGQDLLVQSMSGFVNLTGNKNDDPVPVGAAVSDIITGSHLAQGILASIYKRTKTNQGAWVEVSLLESTLDLQFEVLTTYLNDGNQKPIRAEKGNANPYLGAPYGVYKTKDSYLSLAMGNILNMGKVLGCAPIASYIDSDSWFTKKDEIMAILSDFLIHKETQEWLDILEPAGIWASAVFNYDDLLNHEGYKVLQMDQKLKLLSGEEVHTLRCPIRMDDERIFAPKPAPRVGQHTADIRKEFNL
>CP020918.1|AWG22636.1|3374277_3375429_+|ABC-transporter-substrate-binding-protein
MESQPIKLKGITWNHSRGFTSMVATAQRFSELNPNVEITWEKRSLQAFADEPIDELAKRYDLLVIDHPWAGFAGKTKVILPLDEYLPKAFIADLAENTVGHSHVSYSSNGHQYALAIDAATPVASSRPDILEAKGLKLPTNYDELLALAKKGLVVMPGIPQDTLMNFYMMCCNLGEEVCVSKEHVVSQEIGIKALQMLRALAVEMDPAMYDWNPIKVYEAMTLTDNYAYCPWAYGYSNYSRNGYARKLLHFHDMIEINGVGAISTLGGTGLAVSAQSKEIETAMKYLEYVGSEAIQKTVFFDGGGQPGHRKAWTDEYTNSITADYFKNTLPGLDRAFLRPRYNGHMYFQDRAGAPIRNYLMNGGDELALLQQLNELYLKSLEI
>CP020918.1|AWG22635.1|3373184_3374237_+|hypothetical-protein
MANPLLGTFIHGVGGVSASTCYVPYQKVKKWSWDTYWLFQASFAWFIFPFVIGFLTVPDLLGVFENSDTTILINATLLGAVYGFGGMCFGFAIKHIGYSLTYTISIGISAILGTIVPLIMHGEFVEKYNAAGGSTIFIGMFLALIGIALCGVAGYRKEADLKRNAVEGANLPSFDMKKGLTLTIIAGVLSAVFGISLEVGAPVAELAGKYGAGNYEGNANLILSTFGAFVTNLIWFLIAGIKNKTLKEFVDVKSIGAKNYGINAGMSILSGALWYGQFFFYGIAHVQMGAYKFASWVIHMSMLIFFSYIIGIVMKEWVAVSKRTYTTLLYALIILVVSFFVMTYGSMQGE
>CP020918.1|AWG22634.1|3372300_3373143_-|hypothetical-protein
MYILYMKQTRSGLNLLNLSRKTQKMAEENNTKYNAPALDKGLDILEYLSSEGIPLSQAEIAQGISKTPSEIYRMLVCLEERGYLIRGSNAGKYRLSLKMYSLSHRHTPFDELKRVSHYPMQNLSEKIRQSCHLSIINNDQLLIIAQMRSPNAVSLSIEEGTHFPLTLTTSGRVFLSIYLEDKRNDFLSRDEHYSKWTKKKQEEFKESILQVQKDGYRSAESNITSGITDFAVPIGLNDSDLNAVLAVSVFSSSIDNEISREKIIEALKEAQGEINKLIGG
>CP020918.1|AWG22633.1|3371399_3372245_+|integrase
MLGMNQSSYYRRPSLGKKGNKPSVFTYNKFKGMVSQETVIASVKEILSHEFIDCGYRLMTSYLHRDGYKINHKKLYRIMKEEGLLKLENRINRSGSGRKFVKYRKVITVRPFQCIEMDIKMVWIPSVGKNAYLLSIIDVHTRRILKDYFSFSIKQNKVITFLSDLFLEYQYPENVVIRSDNGSQFIAKSVREYLGIIGVQQEFTHVATPEENAHIEAYHGILKKEVFQRVDYRTFGEIEQILKRYVIFYNNNRLHGLLGRITPMEKWNQDKDLILLEKLTA
>CP020918.1|AWG22632.1|3371037_3371349_+|transposase
MKYKKWSLEEKLEILSSCEDLGVVETCRKYSVSTGSLYSWKKKHEKQGEAGLKVTYDDRSKELKQAEEENRILRKLLANKEIELEIGRELLKKKFGTSDPRKI
>CP020918.1|AWG22631.1|3370051_3370861_-|hypothetical-protein
MESTRASFQNIGKTIEELILKSKTSIYISVAWFTNKELLGLLTEKARNGVNIQIIISDDIVNKRQNPKDFISVGGNFNILQTNSGKFLHEKFAFFDNETILTGSYNWTYFAEYKNHESVIISNNELLVKQFSIRFKKLLEIVVNFNNELLVNRVNIGADIAEEEFEKLEQDLEQDLIRALEESKKLNTKIKFELVYPLIKSYGAIGASKRLMLTGTDKIQSGFIKMWELNRMDLTFESIITKKKYQLLFDIKTLNNAHERLQKFEKSSH
>CP020918.1|AWG22630.1|3367734_3368505_-|hypothetical-protein
MDSIICSQNGALITITLNKPPANSYELNFLTALGNTIENTNQDPTTKVVLINSASEKFFCAGADIKVFGSNTVEQNKEMVVAARRVCHLISTSTKIFIAAFRGHILGGGLELAMACDIRLASQGNYLIGLPEIKLGLIPGNGGTVRLITLIGASRAMELLVTGNTINAVTAHQFGLINHLYPADTFGKDVLDYCKNLASGAGEAMASIKKFTLESQGMNLQQALQLETALVNPLYETPDGIEGFKAFIEKRTPNFK
>CP020918.1|AWG22640.1|3379609_3380680_+|oxidoreductase
MDINYKPTLPIENRPIYIIGAGGIVRDAHLPAYKSVGFTIAGITNRTRERAEEVAKQFAIPTVYDTVADMVKDAPSYAIYDLTLMPNQFVQTLEQLPDEAAVLIQKPMGDDFEQTLAILQVCRRKKLKAAVNCQMRFAPYIMAAKDIIDRGLIGELYDFEVRLTTYTPWEYFPNVVNHPRLEIQQHSIHYIDLIRSFLGNPKKVYSKTLKNPGKTMSSTRTTTIMDYNDAMRAIINTNHDHNFGEKNQESFVKWEGTKGAIKARIGLLLDYPNGKPDLFEYCIVTEGQEPKWIEVPLKGSWFPDAFVGTMASLMRFVEGSTTELPTSVEDVVHSMAIVEAAYESNDNGGILPNYSI
>CP020918.1|AWG22641.1|3380691_3381135_+|dehydratase
MHILSRFYEDYELGSKRETFGRTITETDFVVHAGHTGDFFPHHMDAEWCKTQPFKQRIAHGTLTFSVGIGMTATEINPEAFSKGYDRLRFVKPVYIGDTINVVITISEKKDSNKPEFGQVNEHVEIFNQNGDLVLVCDHILLAKKKI
>CP020918.1|AWG22642.1|3381221_3382787_+|alpha-L-fucosidase
MKNTVLGLVTIALVSCNAQQKTTQNKVTNKKIEYKADWKSLEQHKTPEWFLDAKFGIYCHWGPYSVPEYKNEWYSHWMYINKDNPEAKNGKESEYYTHHVNTYGPLDKFGYKDFISMFKAEKFDAAAWADLFEKSGAKFSGPVSEHADGFAMWDSDLTKWDAKEMGPKRDIMGELSKEIRKRGMKFIATFHRQWLYAWYPTWDETTDASDPRYAGLYGPKVKKGDFLFPDNPNRKKLGAASYYPLADEQFNKEWLARLKEITNKYNPDMVWFDNKMDIIGEDYRKEFLEYYYNHAEKKNQEVVSTYKFHDFAEGTAVLDLERARMSEKKDFPWLTDDSIDWKSWSHISDPNYKSTNRLLDFLIDVVSKNGAVLLNITPKANGEIPEPVKERLLQMGDWLKTNGEAIYGTRTFDIYGEGDAEVKEGHLSEDKNADNTAKDIRFTRKGEVVYATVLDWPAENQLVIHSFKKGSPYLTKGIESIEFLANKKKMKFTVENDGLHIQLPKEKVGDYAFAFKITPKK
>CP020918.1|AWG22643.1|3382873_3384460_+|acetylglucosamine-6-sulfatase
MKKTGLSITLAVLLFCQLGISQRSSKNQPNIIYIMSDDHTAQAIGAYGSRLAKLNPTPTIDKLAAEGMLFENAFVTNSICTPSRACIITGQYSQTNGVLDLDGELDPAKEYLPMEMKKLGYTTAMIGKWHLKNEPSAFDYYKVLHSQGKYFNPTFFEKGKGEWMKNEVKSVGHSTDVITDITLDYLKKRDKSKPFFIMHHYKAPHDMFEFAPRYADYLKDVEIPEPASLYFQPNFGSEATVGKNGKLGAVIGSSISDRHLYRNYVNMLLKDTVSGTIATHLAYQEYLKRYLRCVKGVDDNLARLFDYLKKEGLWENTVIVYTGDQGMMLGEHDLIDKRWMYDESMRMPFIVHYPKMVKAGSKTDLLINNTDFAPTLIELAKGKKPSYMQGFSFINTLEGKAEKNWRTATYYRYWMHNIHHWVPAHFGVRSKQYKLIFFYAKHYLPEAEWNKFYWNKEMRIYGYNTPVAWEFYDLKNDPEEMNNHYKDPKYKDIIASLKEEILKQRKELNETDANYPEIQKVIDKHWND
>CP020918.1|AWG22644.1|3384737_3385895_-|hypothetical-protein
MTMFQLTLKNQIMKLKKLQKISLGLLTVFFTVSTIVAQPAAPSGKKWVKATYLSDDFNGSFDTSKWEQSIWNYAGTPTLMNNNNSGVSGGNLWIKATDNGQSNSGAWFQSSRVQSKAKVGFPMYTECRIKAANISAYSTYWLNNGDANNRDEIDICENNPKPSITSQTYRPYTMYSQYFIVKNGVTERNAGNFDNRNLPAGNPAKGVKWNTYQVLGCYWKDSKHVQFYINGAPAGSLTTTGVFTLAQNIIWDLWTGPFDYLGGLAVRSDLANEAQSTMYVDWINTYTLANITGKEVESKLKSETYNYKTSVSPNPVSNLLQVTLKSENDYNSYSIIDPLGRSVAQGKIAVGSAEYNVNVSSLKSGIYFLILNGEDDSEKIKIMKN
>CP020918.1|AWG22645.1|3386237_3387413_+|hypothetical-protein
MIKKHYLLGFFYLILSACSTNGTDNEPKKEEKQVDTTPPEISCVADINVGIDYFASNAIVTYTAPIGTDNVAGASTTQTAGLASGATFPVGVTTNTFQVKDVAGNSVSCSFKVTVTKNDPSADLPYLTEVNPAPTSKKWVKVDALSDEFNLNALDEVKWKNTDPSQWIGRAPGLFKKSTVSQNDGNLQLTADILPAPEVVNGNTFTHAGSYITSNTTAQVGYFIECRMKANKTFMSSTFWLINKRNEATGCDARTTELDIQECVGQVTGTASWTLTTDQQMGSNLHSRSTSCPETPVGSVGGNTLLSGKASEEYHVYAAWWKSPTEIEFYLDGKKVRTATPVANFNLGMYMKMVVETYDWNPVPAGGGMNGSAQDRTTYYDWVRTWKLIDN
>CP020918.1|AWG22646.1|3388126_3388966_-|hypothetical-protein
MKLTISILSLVAISLISCSKSKDDIDLIEITDPETEVITPKEEEVIVEGTDPIKIPICDGVTQPVPELINENVIPVDKKCGIFLEKNGLLIFEAENTSSDFDKWIYETAIPGYRGTGYLRYNGPFTGSSPLVYKFKIENSGIYRFMIRSSKPAGVEQDANNDCFIKMEGNFVAGEMNSCIANADRNSTQTNPLKTDTKFFGTGGDGEFKNAAGQLDLHSVKPWATYNFKAGETYTLTITGRSSKFSIDRILIADLNKYDYAKYNAYAKNAVQNDCVVEN
>CP020918.1|AWG22647.1|3389116_3390079_-|IS30-family-transposase
MSHLTIEQRYEIATLRSQGFSMSKIGGFIGRDKSVISRELSRNSDQRNNVYKAKLAQSKASIRQHEKAKKIRFTEQIKARVIHLLEEDFSPEQIVGYCSDKNFECVSIETIYQFIWSDKKKGGQHYKHLRTKGKRYAKRGALKGSRGIIKDRVGIENRPLVVEEKQRIGDLEIDLVIGKNHKGALLTINDRASGVLKMAKINSKESQEIQEKLIELLMDWKPILHTITSDNGKEFANHKKVSEILEISYFFANPYCSWERGANENLNGLVRQYFPKKYNFDLITEEEVLRVTNKLNNRPRKRFGFKSPNEIFEQKLKQCA
>CP020918.1|AWG22648.1|3390509_3391379_-|hypothetical-protein
MNKINYAILVLLASYSGLKAQDSTRPASYYTDTISFSAAPKRMTDKLPLSHQKDKKWVLQKYLSDEFAGLKLDSDKWYDTNPKWLGRAPSMANSENVSLEKGNLVLRINQVKEPKYKNDYTHNVGWVVSKKSITYGYFEMRAKLMDAPWVSCFWLYNWWYKDNWKTEIDICENNPGAAKNRHTLTSNLHVFSAPVDKGNVTKLKSHPQNYYIPFELQKDYHVWGLEWDKDFIRWYIDGVLFRESPNVYWHQDLHINFNSESNKWLLALPDDNRLNEDFNVDYVRVWQKK
>CP020918.1|AWG22649.1|3391555_3394042_+|glycoside-hydrolase-family-2
MKARKLILSTVAFLALFVAKNSSAQSVVDKKGVQNFNQNWLFKKDTLQGAEKIAYQDSNWKKINLPHDWAIEGPFSNKNNARTGGLPVHGIAWYRKHFVVDNKNKGSQIAVAFDGVMNNAKVWINGNYVGERPYGYIGFELDLTPYIKYGQENVIAVQVAPEDLSARWYPGAGIYRNVYLKVKNDIHIPQWGTYITTPIVSDAKATVAIQTTIKNAGNLSSNAVLVTTIKNNKGVVVASQSKAISLVKSSEQKVSQNLEVLKPARWDIQSPTLYTSISQVKVNNQVVEEYQTNFGIRTIKFDANNGFLLNGKRVQLNGVCMHHDLGPLGAAVNYRANERQMQIMKSMGTNALRTSHNPPSPEILEVCDKLGIVVIVEAFDEWQLPKVPNGYSKFFDQWHEKDLRDMIKRDRNHPSVIMWSIGNEILEQSKKDGWILTKHLNDICHDEDNTRPTTAGFNYYPQPFMNKLAYQIDVVGMNYWPADYKEIKEKNPNIILYGSETSSQTSSRGVYHLPIEFNEKHETNQVSSYDTTVGPPWAYAPDVEFEAQEKNPFSLGEFIWTGFDYLGEPTPYGGRDNSTNGYWNKDWPSHASYFAPVDLCGFPKDRYYLYQSQWTTKPMVHVLPHWNWEGKEGDIIPVYSYTNCDEVELFVNGKSMGKKVKGKDFTEIPSEYHGFEKGMYKTKYRLSWNVPYQPGSIKVVGYKNGKQAAVKEIKTAGAPALIKLSADRNVITADGKDLSFITVRIEDANGNLCPNADNLVNFKVEGAGIQAAVGNGDAASLASFQANNSKAFSGMCLLIVKATDKKGTIKITATSSNLKTAETIVTTK

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Crispr_ID: CP020918_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP020918_6

3538268-3538348

Orphan

Consensus_repeat	Method
TTGAATCATACCGCTTTGCGAATG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP020918_6

>merge|CP020918|6|3538268-3538348|CRISPRCasFinder
TTGAATCATACCGCTTTGCGAATGCCCAGCTGTCCGAAGTATTCATTTAAACTAAACTTGAATCATACCGCTGTGCGAATG

>CP020918|6|6|3538268-3538348|CRISPRCasFinder
TTGAATCATACCGCTTTGCGAATG	CCCAGCTGTCCGAAGTATTCATTTAAACTAAAC
TTGAATCATACCGCTGTGCGAATG

Protein	Signature genes	Signature genes Name	Protein_function
CP020918.1\|AWG22718.1\|3520814_3522692_+\|sulfatase	unknown	unknown	gnl\|CDD\|293772
CP020918.1\|AWG22717.1\|3519239_3520649_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|350132
CP020918.1\|AWG22731.1\|3544631_3545477_-\|transglutaminase	unknown	unknown	gnl\|CDD\|224224
CP020918.1\|AWG22721.1\|3530190_3531309_+\|histidine-kinase	unknown	unknown	gnl\|CDD\|176240
CP020918.1\|AWG22730.1\|3543304_3544444_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379751
CP020918.1\|AWG22719.1\|3522895_3524134_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|275036
CP020918.1\|AWG22727.1\|3538672_3538972_+\|nucleotidyltransferase	unknown	unknown	gnl\|CDD\|143393
CP020918.1\|AWG22736.1\|3551701_3552550_+\|transglutaminase	unknown	unknown	gnl\|CDD\|224224
CP020918.1\|AWG22732.1\|3545615_3546581_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377234
CP020918.1\|AWG22729.1\|3541831_3543151_+\|sulfatase	unknown	unknown	gnl\|CDD\|293773
CP020918.1\|AWG22722.1\|3531403_3532273_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|185687
CP020918.1\|AWG22720.1\|3524489_3526391_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|275036
CP020918.1\|AWG22723.1\|3532345_3534841_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225789
CP020918.1\|AWG22728.1\|3539378_3541544_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|375510
CP020918.1\|AWG22733.1\|3546593_3548036_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225190
CP020918.1\|AWG22724.1\|3534845_3535652_+\|acetyl-esterase	unknown	unknown	gnl\|CDD\|223700
CP020918.1\|AWG22726.1\|3537210_3538224_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379095
CP020918.1\|AWG22725.1\|3536012_3536840_+\|serine-protease	unknown	unknown	gnl\|CDD\|379142
CP020918.1\|AWG22735.1\|3550925_3551669_+\|peptidase	unknown	unknown	gnl\|CDD\|239734
CP020918.1\|AWG22734.1\|3549107_3550391_-\|ATP-dependent-RNA-helicase-RhlE	unknown	unknown	gnl\|CDD\|236722

Protein	Function_ID	Function_description	E-value
CP020918.1\|AWG22718.1\|3520814_3522692_+\|sulfatase	gnl\|CDD\|293772	cd16153, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	2.49972e-76
CP020918.1\|AWG22717.1\|3519239_3520649_-\|hypothetical-protein	gnl\|CDD\|350132	cd18620, GH43_XylA-like, Glycosyl hydrolase family 43-like protein such as Clostridium stercorarium alpha-L-arabinofuranosidase XylA. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. The GH43_XylA-like subgroup includes Clostridium stercorarium alpha-L-arabinofuranosidase XylA, and enzymes that have been annotated as having beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), endo-alpha-L-arabinanase (EC 3.2.1.-) as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan.	1.98952e-133
CP020918.1\|AWG22731.1\|3544631_3545477_-\|transglutaminase	gnl\|CDD\|224224	COG1305, COG1305, Transglutaminase-like enzymes, putative cysteine proteases [Amino acid transport and metabolism].	1.42284e-29
CP020918.1\|AWG22721.1\|3530190_3531309_+\|histidine-kinase	gnl\|CDD\|176240	cd08279, Zn_ADH_class_III, Class III alcohol dehydrogenase. Glutathione-dependent formaldehyde dehydrogenases (FDHs, Class III ADH) are members of the zinc-dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. 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. Class III ADH are also known as glutathione-dependent formaldehyde dehydrogenase (FDH), which convert aldehydes to corresponding carboxylic acid and alcohol. 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 an 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.	1.20278e-151
CP020918.1\|AWG22730.1\|3543304_3544444_-\|hypothetical-protein	gnl\|CDD\|379751	pfam15887, Peptidase_Mx, Putative zinc-binding metallo-peptidase. This family has a highly conserved HHExxH motif with a highly conserved ED pairing downstream. HExxH is indicative of a zinc-binding metallo-peptidase.	4.2382e-140
CP020918.1\|AWG22719.1\|3522895_3524134_+\|hypothetical-protein	gnl\|CDD\|275036	TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.	9.09524e-09
CP020918.1\|AWG22727.1\|3538672_3538972_+\|nucleotidyltransferase	gnl\|CDD\|143393	cd05403, NT_KNTase_like, Nucleotidyltransferase (NT) domain of Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. S. aureus KNTase is a plasmid encoded enzyme which confers resistance to a wide range of aminoglycoside antibiotics which have a 4'- or 4''-hydroxyl group in the equatorial position, such as kanamycin A. This enzyme transfers a nucleoside monophosphate group from a nucleotide (ATP,GTP, or UTP) to the 4'-hydroxyl group of kanamycin A. This enzyme is a homodimer, having two NT active sites. The nucleotide and antibiotic binding sites of each active site include residues from each monomer. Included in this subgroup is Escherichia coli AadA5 which confers resistance to the antibiotic spectinomycin and is a putative aminoglycoside-3'-adenylyltransferase. It is part of the aadA5 cassette of a class 1 integron. This subgroup also includes Haemophilus influenzae HI0073 which forms a 2:2 heterotetramer with an unrelated protein HI0074. Structurally HI0074 is related to the substrate-binding domain of S. aureus KNTase. The genes encoding HI0073 and HI0074 form an operon. Little is known about the substrate specificity or function of two-component NTs. The characterized members of this subgroup may not be representive of the function of this subgroup. This subgroup belongs to the Pol beta-like NT superfamily. In the majority of enzymes in this superfamily, two carboxylates, Dx[D/E], together with a third more distal carboxylate, co-ordinate two divalent metal cations involved in a two-metal ion mechanism of nucleotide addition. These carboxylate residues are conserved in this subgroup.	1.55571e-10
CP020918.1\|AWG22736.1\|3551701_3552550_+\|transglutaminase	gnl\|CDD\|224224	COG1305, COG1305, Transglutaminase-like enzymes, putative cysteine proteases [Amino acid transport and metabolism].	1.51374e-25
CP020918.1\|AWG22732.1\|3545615_3546581_-\|hypothetical-protein	gnl\|CDD\|377234	pfam04168, Alpha-E, A predicted alpha-helical domain with a conserved ER motif. An uncharacterized alpha helical domain containing a highly conserved ER motif and typically found as a tandem duplication. Contextual analysis suggests that it functions in a distinct peptide synthesis/modification system comprising of a transglutaminase, a peptidase of the NTN-hydrolase superfamily, an active and inactive circularly permuted ATP-grasp domains and a transglutaminase fused N-terminal to a circularly permuted COOH-NH2 ligase domain.	1.49648e-116
CP020918.1\|AWG22729.1\|3541831_3543151_+\|sulfatase	gnl\|CDD\|293773	cd16154, sulfatase_like, uncharacterized sulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	1.42943e-172
CP020918.1\|AWG22722.1\|3531403_3532273_+\|hypothetical-protein	gnl\|CDD\|185687	cd02178, GH16_beta_agarase, Beta-agarase, member of glycosyl hydrolase family 16. Beta-agarase is a glycosyl hydrolase family 16 (GH16) member that hydrolyzes the internal beta-1,4-linkage of agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea, marine red algae. Agarose is a linear chain of galactose units linked by alternating L-alpha-1,3- and D-beta-1,4-linkages that are additionally modified by a 3,6-anhydro-bridge. Agarose forms thermo-reversible gels that are widely used in the food industry or as a laboratory medium. While beta-agarases are also found in two other families derived from the sequence-based classification of glycosyl hydrolases (GH50, and GH86) the GH16 members are most abundant. This domain adopts a curved beta-sandwich conformation, with a tunnel-shaped active site cavity, referred to as a jellyroll fold.	3.341e-54
CP020918.1\|AWG22720.1\|3524489_3526391_+\|hypothetical-protein	gnl\|CDD\|275036	TIGR04183, hypothetical_protein, Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.	1.12504e-10
CP020918.1\|AWG22723.1\|3532345_3534841_+\|hypothetical-protein	gnl\|CDD\|225789	COG3250, LacZ, Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].	1.43538e-68
CP020918.1\|AWG22728.1\|3539378_3541544_-\|hypothetical-protein	gnl\|CDD\|375510	pfam18040, BPA_C, beta porphyranase A C-terminal. This is the C-terminal domain found in Bacteroides plebeius of proteins such as beta-porphyranase A (BPA), a beta-galactanase that cleaves the beta-1,4 glycosidic bond. Porphyranase degrade red seaweed glycans. This domain adopts a beta sandwich shape.	1.38621e-34
CP020918.1\|AWG22733.1\|3546593_3548036_-\|hypothetical-protein	gnl\|CDD\|225190	COG2308, COG2308, Uncharacterized conserved protein [Function unknown].	0
CP020918.1\|AWG22724.1\|3534845_3535652_+\|acetyl-esterase	gnl\|CDD\|223700	COG0627, COG0627, Predicted esterase [General function prediction only].	9.77404e-18
CP020918.1\|AWG22726.1\|3537210_3538224_+\|hypothetical-protein	gnl\|CDD\|379095	pfam13271, DUF4062, Domain of unknown function (DUF4062). This presumed domain is functionally uncharacterized. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 80 amino acids in length. There is a conserved SST sequence motif.	6.98384e-34
CP020918.1\|AWG22725.1\|3536012_3536840_+\|serine-protease	gnl\|CDD\|379142	pfam13365, Trypsin_2, Trypsin-like peptidase domain. This family includes trypsin-like peptidase domains.	4.21364e-09
CP020918.1\|AWG22735.1\|3550925_3551669_+\|peptidase	gnl\|CDD\|239734	cd03765, proteasome_beta_bacterial, Bacterial proteasome, beta subunit. The 20S proteasome, multisubunit proteolytic complex, is the central enzyme of nonlysosomal protein degradation in both the cytosol and nucleus. It is composed of 28 subunits arranged as four homoheptameric rings that stack on top of one another forming an elongated alpha-beta-beta-alpha cylinder with a central cavity. The proteasome alpha and beta subunits are members of the N-terminal nucleophile (Ntn)-hydrolase superfamily. Their N-terminal threonine residues are exposed as a nucleophile in peptide bond hydrolysis. Mammals have 7 alpha and 7 beta proteasome subunits while archaea have one of each.	5.86627e-47
CP020918.1\|AWG22734.1\|3549107_3550391_-\|ATP-dependent-RNA-helicase-RhlE	gnl\|CDD\|236722	PRK10590, PRK10590, ATP-dependent RNA helicase RhlE; Provisional.	0

>CP020918.1|AWG22726.1|3537210_3538224_+|hypothetical-protein
MSDIKKYSVFVSSTYQDLIEERKEVIQALLELDCIPIGMELFPATDDDQWTLIKELINECDYYILIIGGRYGSLNKEGISFTQMEYEYAIEIGVPVISFLHKTPGEIKSSKTDRDSEKEQKLENFRKISSEKLIKYWNSPEELGSIVSRSLIKLIKTKPRIGWVKSDRVSSDEANLEILELKQKIQELENEIKKSEENINKDLLQDDDIFIVKYGYKIKKYDSWDQKTIEVEWNTLFAKTCAILIDEAKEEDFRLRIDSYIKYLTKIEGFEYELVNLFSDNFLSILIQLKALNLVEKSDKKRSLKDNSTYWKLTKKGDNLITKLRAIKRENEFIDAE
>CP020918.1|AWG22725.1|3536012_3536840_+|serine-protease
MDLSISEQLTYSTVRIECELKTGGTSTGTGFFFNFLEDKTSNTHVPVVVTNKHVIKNASKGKLIITKANEKGEPIDTEHFTLAFDNFESFWRLHPEADVDLCAMPIAPFVNEAQKRGDKLFYIPFTKDLLPTEKHKEELTAIEDVLMIGYPNGIWDSVNNMPIFRKGTTATNPLIDYNGKKEIMIDIAAFPGSSGSPVLIFNEGGYRDKKGNTYMGANRIILLGVLFAGPQATATGEIVMTPNLQRPISVSQIPNNLGLIIKSERIIEMEKLFNQ
>CP020918.1|AWG22724.1|3534845_3535652_+|acetyl-esterase
MESKFRTTEISNPEFESNNLRFITVKTPNLQGRGDICVFVPPMKDLKNVPIVTLLHGVYGSAWIWAHKAGVHLTALKMMQEGKIKPMVLAMPSDGLWGDGSAYLPHNDKNFESWIVDDVVNAVIENIDCTSSTSDLFISGLSMGGFGALHLGAKYPLRYKAISAHSSITNKNQMPLFVEEDENQYNQVNSSDEDVLETILKNKTELPYLRFDCGKDDLLIEHNRLLHQQLNEANINHTYEEFEGAHEWAYWQEHVQDSLLFFSQFVTL
>CP020918.1|AWG22723.1|3532345_3534841_+|hypothetical-protein
MKNIWTTIGLFLLTFHANAQQTDLLKNWKFTNYDYGAAFQENFDDSTWEKVTVPHDWAVKGDFDFANDVQLTMVVQDGDSKPFYRTGRSGALPYVGIGWYRTQYSVSAADLKGKVQIMFDGAMSNSKVFVNGQYVGERPFGYISFYFDVTKFLKAGDNTIAVRLENFNSQSRWYPGAGLYRKVSVIKTHATHVKTWGTFVTTPSISKKKAIANLNLELAGNGKYTIKNEVLNPAGKVVSSKTSSVQINDNQLVNEQFEISKPELWSLENPNLYQLKTTILAGNEVVDTYSTTFGIRTVRYEVDGFYLNDKKVRFNGVNMHHDLGPVGAAFHRELFVRQMKKMKAMGVNAIRFSHNPPAPEALDVCDELGLLAIDEAFDEWQIGKVTNGYSIHFDKWSKTDLTDMILRDRNHPSIIMWSIGNEIMEQYKHDPNKITSYLNKIVKSLDTTRATTAGFNSAKNAIVSGMATTVDVAAFNYKAGIYGAIRKQYPNLKFFASETGGSVSVRNSYKFPVVFDTIHGKRGDSSHTVVYPDGHPGNFETTNVPWGYPAYKEFASQEKNPSVYGEFVWTGYDYLGEPSPYHNAEARSSYFAPVDFVGLEKDKFYQYQAQWNKDAKVLHFFPHWTWPDLKVKSFPVVCYTNYEKAELFVNGKSYGIKTKKPISKLDFESNNLAKEASGGGNWDLFKAYAIVWDDVVYEPGEAKIVAYDKNNKKVAETKRVTAGAPHSIKIEPEIATIQNGEVGVYVISMVDKDGNLCPHFNDDMDIEVSGAASFLAAGNGDPVNMQNLSKPKRKFFNGQAVIFVQSNSKGKITLATKTKNIQATSTELAVK
>CP020918.1|AWG22722.1|3531403_3532273_+|hypothetical-protein
MKKNILFIAGTFLTFSSLLSAQIKAPEGKSWQLVSELSDEFNGKKLDTKKWIADPEGHPEFGWIGRSPALFIENAVTVENGYLNIEVGKLDERFVSNKYNTATNYDYYGGIIRAVKPVTYGYYFESTFKMSKTEMGGGFWIMSKNTCGKKHEIDITESVGSISPLAQEWGKKWDKIMHSNTILRNTTCNEEKRDQGMILPETKNSEKFYTYGCWWKSPNELLFYLDGKYVYTLTPPADFDQQMFIHFSIEVYDWNPIPEKDSKLMTASKKDRTALIDYIRTYKLVTVKP
>CP020918.1|AWG22721.1|3530190_3531309_+|histidine-kinase
MSITCKAAIAKGDGTFSIETITVENPQADEVLVQVKAAGLCHTDHDSLNWGKPIVMGHEGAGIVTAIGSNVSSVKVGDAVILNWATPCGKCFQCEHENEHICENNSPVVAGGNGYTPGHAHLEGTSWNGTPIIRSFNIGTLSEYTLVKESAVVKNPIQDMSYPAASIVSCGVMTGFGSAVNTAKVEANSSAVVLGTGGVGLNVIQGIKVSKAAMIIAIDINQQRLDMAVEFGATHTILADKNDKGLLNAAKIVKEMTNGRGADYAFECTAIPALGAAPLAMVRNAGTAVQVSGIEEEVLIDMSLFEWDKKYINPLYGKCNPQKDFPIIVEHYRKGEIMLDEMITNTYPLEDLQQALDDMLSGKNAKGVIVFE
>CP020918.1|AWG22720.1|3524489_3526391_+|hypothetical-protein
MKKNYFLSPSRNNFLGLMIMGCGLFSSSIVAQTYTWKPAVASGNWADAANWTNALASKTVTASSGVTDIVVNNTNQIKIGDKVTGTTAGQIATGTVVTAVNETTNTVTLSLATTAALSGSNNVKFARATVSYPGDNGNPDSAIIAAGSVTLDADISISQLSLHTTTTPAQGVLTIPSGRTLNIANNSSALYIRGGKLTNNGTLNLTPQSNNAAINCQVPANNVAGLDTGYGGTGTLTTTVDGTGGFITFTNAGALTLPVINLNAATTTITILGTGNVFNTAGGATTAGNGKIGGTGVTVTLSQSAGRLFNINTGAGGTSSIEVLSGTVLTLNPAIGGNSPIYVNANGSDASLINNGSIIFNGDYGTSAGIVGSGLNSSEVYNNGTLRLPVTAVGTNSNAIGSNLSKFVNTGIVETNSGSSILTDLSAVNNTFTSGTLSPGGVGNSKMNISGASLPLNTTTLKIDVSGNGAVAGTDMDQINANTASAAVTISGAKLALNITATPPTGITTYAILSTNGGTVTGTFASVTGLLAGWALDYSDTSKVVLKYDSSTLGVKKLNAFEFAVYPNPVRETLNIQTQESLTKAQIVDASGKVVLSQNNPSDAINVASLSKGIYMLRLTSANGVSTSKIVKK
>CP020918.1|AWG22719.1|3522895_3524134_+|hypothetical-protein
MKKLLLLFVTGLGAITISQAQTQTLSLSTDATSLNAIVISDNGYILEETGPGVYTQRTITVTSTNDPGNASATNGAGDPSPIAPGNSNVFFVVKNGTGTASQTNVATAGTLSNSNAATVVIDGTDPTINTRTWVLSVLTLQSGNIAPLGAGYDFRPTGGTSSNPPQAVSIVGTYTVPVVEKHSYEFNNGTNTEGFSAINSAITVSGGKMVITTDAVAGNAPHTVGIIRKTDPTNYINAETYKYAHVYYRNKSFNNQLRISTGSAPSGTNGSNYTTLTLNMTDASPYEVAVINLSNAVTWIGIVDTFDVQHRTTGTSSLAGTLEIDRIEFSTGPTLGLSTKQVTELVNVYPNPTTGAITISDLKDSKTINIYNMLGAVVKTLPATNTIDISDLATGTYFLKTDTGLSSKIIKQ
>CP020918.1|AWG22718.1|3520814_3522692_+|sulfatase
MKVKLFALCVLSFAASNSQLLAQKTVKKPNILWILTDDQRKDSNGYYNQITTGKNDSPLGYIESPNLDALAKEGVVFPNMYCNSPACAPSRNGILAGKYPHHSGVYGFEYFNGEAEFFTKTMPQIMVENGYETSLFGKAGYRNKSVDKKSATKKTEDLYKGFYQKYVLDTELERGGVTDWNKETTYGKVNGKSGKIDTRMQFFYPNNVKKSWTTEDNISDAEKAIKASVEKELDILYHNANDGEESTLIIGGVNSMPADKTLDGNILTEYRNYLQNQNKPYQSLLGDKMAGANTSKPIFTSLSFHFPHTPVMPPKEFRDRFKDKVYKIPAFDKKEELSKLPKQLVDLYNKLRIDGYSYEDKQQAIRDYYAFCAFGDYIIGKAIAEFKAYSKKNNQEYIILYTCGDHGWQLGEQGIESKFSPWELSTHTTGILVSSDKKAVPAGKVYDGFAEYVDIMPTILAAGGVDLKAKEYQFLDGFDLAEMYSNPQLNKDYIIGEINSVAGPRSYMRTKDFAFSMRPRPLNGGPGGRYKPNENVRWGLDAPRQEVQLAFYDLRKDPMERNNLANDKNYIALTDWFRTKLGNIILGDGRIECDWKQKNVYNTSTFALGADDKKIDIPKNIVPKI
>CP020918.1|AWG22717.1|3519239_3520649_-|hypothetical-protein
MDFWTYKMLHCCSFEVKDCIFQSLNYFSNKMKKNTIITLFLTLFVLVVKAQNPIVPAGMYIADPEAHVWKDGKLYLYGSRDESDDYWCSYSHHVLNTSDLKKWTVTENAFASKGANDQVSYHDNLLFAPDCAYKDGTYYLYYCSPGKKLTEGVATSSSPFGPFENGKQIKGAYQIDPAVLIDDDGQGYYYWGQGKPKVAKLKPNLIEIDSTSIVEPLDAKGNVAFHEGSSIRKIGKLYYFVFADDSRNNKPTCLGYAIGKSPMGPFEYKGVLIDNVACDPASWNNHGSIEKFKDQWYVFYHRSTHNSQKFRKACVEPIFIKKDGTIDEVEMSSQGASAPLDATAIIEAEWACHLSGNVRVTGIAATDIKSEGLAAFKDGDFVGYKYLDFPKNCSEFELKAVVHSKITIEIRQGSEHGNLIGTCVLEPSKDYQIVKTSIRNVKKGKQALFLTFKNETNSSDNSLDWFRFN
>CP020918.1|AWG22727.1|3538672_3538972_+|nucleotidyltransferase
MILIEQNIDRLKTICSTYNVDKMYLFGSALNSNFNDKSDIDFLVKFKPFDLSQYFDNYINLKENLKILFGREVDLLEEQTLKNPILINSINKSKELIYG
>CP020918.1|AWG22728.1|3539378_3541544_-|hypothetical-protein
MKKQYLILLLVPAAFFAQVKVAVNLNVKHTVGGVSTFERSKFITMHSNTTDTEWDGDNQIGDLRNNFLNGLDVYLGRETGLITYTLNQVAQDPARAGYASPTDIASRGLSSRNSFAAKTNLAQYESRKGGMIFGGQLYPFWTGVGQKPTAKGWNIANGTATGEYMGRFMKEFFGGNGPSLPAFLEIVNEPDYELLGGVKEYTKTIAEIANFHIAAADAIRAQMPNTKICGYTNSFPYYEVGEFQRWFNRDKMFMDMAGSKMDYYSIHLYDFPTIGGKRQMRSGSNLEATFDMMDHYGMLSVGSVKPYVLSEYGAQTHDSNNQQWSSYRDWLNVKSFNSMLMSFLERPNTIASAIPFVIVKAEWGYNSTTGVPYTSRLMRKANEPASYTGQWVYTDFVKFYQQWKNVKGTRVDIKSDDPDILVKAYVDGNKGYVIINNLEQAVKTIDLNLFDHDANNLTQIVKRYLTLTANQTDLQETTTTSPITSLTIGSESHVVLEYTFANPIAIDRTLDETKYYADDYLKPIVAANTPVVYNVNGITKATYGEAILRIGVGRATGKSLVPVIKVNNTLVTTPTDFRGDNQPQRDSFFGVLEIPVPYNLLDVNNVISVQFPDAGGNVSSVCMQVNNFSHNIRVLATNTFKYDSQISLAPNPASDMVTLKIVEELIGSSASIYNMQSALVQTEKLSQLDNNFTIAKLPKGVYFVVLKKNNTTMAKVKLIVN
>CP020918.1|AWG22729.1|3541831_3543151_+|sulfatase
MKNNTTHVTERPHLFLILIVFVFLGCSKNDNNSETLTTNTTAPNILFIIADDLGKDAISGFSEGSIKPSTPNIDAIRTNGLSFTNFWAYPTCSPTRASILTGKYGYRTGVKWAGDVLSTTELSLQDYIKKQTNSKYATALVGKWHLSGSSDTFNPEVFGIDYYAGFLRGEVENYYSWTMSENGSSKVVTDYATTKFTDLAIDWIGTQSKPWFMWLAYNAPHTPFHVPPSNMHKQGNLPEYKDGMDAAPYYMAAIEAMDFQIGQLLATMSEAQKANTIIIFIGDNGTPNEVAQSPYSSKTAKGTVYQGGINVPMFISGKGVSRNGTENNLVSSTDLFATIAQIAGSTTTQINDSTSFLSLLSQSSATRSYQYAEKNNGTIDTWTISNGSYKLIQYTTGVNELYYLVSDPYELNNLIKGTLTSAQTSAKTALEAELSIIRK
>CP020918.1|AWG22730.1|3543304_3544444_-|hypothetical-protein
MKIFQCGYCAHSLYFECYTCENCGHLAGFRDEDRTMLTFDPQGDTLISDREQKEYKYCKNKEYNVCNWVVEKDSPEEFCQACQLNRTIPNLSDAENFEKWQNLEVAKHRLIYQLQKIGLDLKSKLDNKEGFCFDFVVQKHDPKLMTGHANGVITILLKEADSVLREQMRRQLMEPYRTLIGHLRHEVGHYFWDRLIYNNKRLLKQYRLLFGNERVNYGDSLKKYYKDGAPENWQESFISKYATSHSWEDWAETWAHYLHIMDMLETAYFFGLNVRPVDMHEAMKENMKVNVTFDPYTVEDFDIIVETCIPLSFAVNSINRAMGVPDVYPFVITPDMVKKMKFIHKLLLPQRVKKVRTESSSRKKKSTIKDLGKDTTTSN
>CP020918.1|AWG22731.1|3544631_3545477_-|transglutaminase
MKFKITHTTIYTFDSDVFLEPHYLRFRPKQTPYVSVDCHALTIVFEPIGHKQVLDEENNMVDFCWFEGMTNQLTITATTVLETKEYNPFDFLIYPLQFNQLPLQYDALQKKLLFGTLEGQMISQELLDYGNAILKASDFNTIAFLTQLTKQLHDDFIVEYREVGSPLQPDETFVIKRGSCRDLSWMQINLLRQFGIAARFVSGYYYFDMISPSYELHAWVEVFLPGIGWLGLDPSHGIFTGNTHFAIASSATFENTMPVSGGIRGSATSQLRTQLSIEKFI
>CP020918.1|AWG22732.1|3545615_3546581_-|hypothetical-protein
MLGRVANTLHWMNRYLERAENYARFLDVNFNLSLELPPNEIQQWQPLVVITGDWDLYQKLNTVVEKNKVIYFLAFEEKNPNSIFSCIFRARENARAVRTEITKEVWEQINALYFLVKEGQEKENYDDENIRDFFNDIKKGCQLVYGMYNSTISRNEGYNFGRLGQVLERADKTSRVLDAKYHFLLSSPKSVGSSIDLIQWAALLKSVSAYDMYRKKYGKLSPSSIAEFLILDREFPRSILACLLSAEHSLIKLAVSTDKAENKAQTKLAALRSQLEESDINEIITKGMHEYLHEIQHNLNDISSAIFTVFFAVESNFPEVN
>CP020918.1|AWG22733.1|3546593_3548036_-|hypothetical-protein
MPKLNLSEYDTKGYYDEMFDENNKVRPNYKLFSEQLEKLSHKKLQSLQHATDRAQLSLGMTFNVYNDNQGVERILHLDIIPRIIDNTEWTYLEKGLQQRIRALNLFIQDIYNDQKVFKDKIIPKELILSSVSYLKQLQGFTPPKDIWCHITGSDLIKGGDGQYYVLEDNLRCPSGVSYMLENREILKRTFPELFKKLEVKPVYNYTHILRDTLESLTDVEKPTVVVLTPGIYNSAYFEHSYLAQQMGAELVEGKDLVVKNDIVYMNTTRGLQRVDVIYRRVDDEFIDPRAFNKDSVLGTPGLFGAYLKKNVVLVNAPGTGVVDDKAVYAYIPRIIKYYLGEEMILPNVQTYICDEEADCKYVIENIHNLVVKQTDASGGYGMLIGPKSTKKEQEEFIAKIKHNPRNYIAQPMINLSRVPTLTEDTIEGRHVDLRPYALYGAGDSIKIIPGALTRVALKKGSIVVNSSQGGGSKDTWILNN
>CP020918.1|AWG22734.1|3549107_3550391_-|ATP-dependent-RNA-helicase-RhlE
MSFQSLGLSEALLKAISKKGYTTPSPIQQKAIPPVLEGKDVLASAQTGTGKTAGFTLPVLHILSENPKTKFRPIRALILTPTRELAAQIYENVKEYSEFLDIRSTVIFGGVNQNPQAATIRQGIDVLVATPGRLLDLEKQGLVSLKRVEIFVLDEADRMLDMGFLRDIERVMKLMPAKRQNLMFSATFSKDIKKLAHGILQHPVQVEATPENTTVDAIDQLVYRVAKDLKADLMIKLITEGKWKQVLVFTRTKHGANNLCEKLAKAGISGAAIHGNKSQGARTKALSGFKDGSLRVLVATDIAARGLDIPLLPHVINYEIPNIPEDYVHRIGRTGRAGASGEALSLVSSDELTFLKDIEKLIEMKLPVEIIKGFEPDPNESTEPVKMGRGGQNRTPRNSAKPAGNGNRNSGNDNRSRAPKRTNDRRN
>CP020918.1|AWG22735.1|3550925_3551669_+|peptidase
MTYCLAIKLKQGLVALADTRITAGSSASTKKKISIEQHDRQSYFMMTSGLRSVRDKTMNYFEDLENQTHSYTKLYQVVTTYGEQLKRVAAEDKAALWQSGLTFNLHTIIGGQLTEDTEPKLFLIYPEGNWVELEEDSPHVIIGNSSQGKAILNSIITADTTIKEALKAGLLSFESTRASANNVDYPIDVALYKKDSYFMLEKRYEQQELAYVSQIWEDKLKQLVLDLPDDWIDPRFESQNLMQTVYL
>CP020918.1|AWG22736.1|3551701_3552550_+|transglutaminase
MKFNIQSTISYAVSAPTTFIFNIHAIRSNSQKILTESLVLDPPLAVEEFSYNGGAGRFVRLKSEGNANFTINYSATVETNYAIIDQRQEFQTVPVAELDGDIIPFLFPSRYCQSDKLQKLAYTEFGSIENVYSKVLAITDWIYNNVEYRSGSTDSQTAALDTITDRVGVCRDFAHLGISLCRALSIPARYLTCYAYTLQPPDFHACFEAYIGGNWIVFDATRLVPLNSLVKIANGRDAADAAVASIFGNAMSQNIQVSCEVAQDDFTPFWYNDNLMNGLSLQ

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Crispr_ID: CP020918_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP020918_7

4042704-4045096

orTypeII

Consensus_repeat	Method
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	CRISPRCasFinder
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	PILER-CR

31 spacers

cas2,cas1,cas9

The CRISPR arrays of CP020918_7

>merge|CP020918|7|4042704-4045096|CRISPRCasFinder,PILER-CR
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACGTATTCTGATATATGTATAAATCCATGATTGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACATATCTTTCAATTGTCTAAAAGTAACTAAGGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACATGTTCGTCCAGATAATTGGATTAGTATTAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACAGTAAATGAATCCTTAACAGTATCAATTGGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACATTAGGGGGTTATTCTTATTGGCTATTCGAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACCTAAAGTTAATCGTATATTCCGATAATTTTGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACACTACACCTACTTCTATCCTTGTTATGTCAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTGTTCAGCAAATATACAAATAACAATTGGAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTGTTCAGCAAATATACAAATAACAATTGGAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACACTGCATGAGTATCGCATCCTTGCGGTAACGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTTCCCTCTATACCTTTCATCAGCATATTCTGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACATTATACCTACTTCTATCCTTGTTATGTCAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTTCTATAAAGAAGAAGAAAGTACAAAAACAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACCCATATTGGGATGCAAACGGAGAAGGATTAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTCAGCAGTTATTTTATTTAATGCTTCATTGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTAAAAACAATAGAACCCGTAGTTAAGGGCGGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTATCAATTAGCTCTGGTGTTAAAATATCCGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTTTTTCGTCTCCCCTTCTTACCCAATATTGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTGATAATGAAATACTATTAATATCTGTTACGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACCTATTTTCACAAAGAAAACTTTCTATTTTAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTATCAATTAGCTCTGGTGTTAAAATATCCGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTTTTTCGTCTCCCCTTCTTACCCAATATTGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTGATAATGAAATACTATTAATATCTGTTACGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACCTACATTTACAATCTCATAATTTTATTTTGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACATAGAAAAGAATTATGTCAAGAGAAATAAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACAATCCATTACAAACATGGTCTGAAGTATTCGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACTATTTTCGCCTACCACAACACCTGCAACCGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACAGAAGCTCCTGAACTAAAAGCAGAACCTAAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACAGTACGCTTAAAGCAATAATAAGTATAAATGTTGGGAATTATAAGCTAAAATACAATTTTGAAGGCAATTCACAACTTGTTACGTCTAAAATTTATGCTCCGGATAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAACATATTGCACTAAATTCAATGGCTAAAATTAGTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC

>CP020918|7|7|4042704-4045096|CRISPRCasFinder
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	GTATTCTGATATATGTATAAATCCATGATT
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ATATCTTTCAATTGTCTAAAAGTAACTAAG
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ATGTTCGTCCAGATAATTGGATTAGTATTA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	AGTAAATGAATCCTTAACAGTATCAATTG
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ATTAGGGGGTTATTCTTATTGGCTATTCGA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	CTAAAGTTAATCGTATATTCCGATAATTTT
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ACTACACCTACTTCTATCCTTGTTATGTCA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TGTTCAGCAAATATACAAATAACAATTGGA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TGTTCAGCAAATATACAAATAACAATTGGA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ACTGCATGAGTATCGCATCCTTGCGGTAAC
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TTCCCTCTATACCTTTCATCAGCATATTCT
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ATTATACCTACTTCTATCCTTGTTATGTCA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TTCTATAAAGAAGAAGAAAGTACAAAAACA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	CCATATTGGGATGCAAACGGAGAAGGATTA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TCAGCAGTTATTTTATTTAATGCTTCATT
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TAAAAACAATAGAACCCGTAGTTAAGGGCG
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TATCAATTAGCTCTGGTGTTAAAATATCC
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TTTTTCGTCTCCCCTTCTTACCCAATATT
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TGATAATGAAATACTATTAATATCTGTTAC
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	CTATTTTCACAAAGAAAACTTTCTATTTTA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TATCAATTAGCTCTGGTGTTAAAATATCC
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TTTTTCGTCTCCCCTTCTTACCCAATATT
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TGATAATGAAATACTATTAATATCTGTTAC
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	CTACATTTACAATCTCATAATTTTATTTT
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ATAGAAAAGAATTATGTCAAGAGAAATAA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	AATCCATTACAAACATGGTCTGAAGTATTC
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TATTTTCGCCTACCACAACACCTGCAACC
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	AGAAGCTCCTGAACTAAAAGCAGAACCTAA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	AGTACGCTTAAAGCAATAATAAGTATAAAT
GTTGGGAATTATAAGCTAAAATACAATTTTGAAGGCAATTCACAAC	TTGTTACGTCTAAAATTTATGCTCCGGATA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ATATTGCACTAAATTCAATGGCTAAAATTA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC

>CP020918|7|1|4044521-4045096|PILER-CR
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ATAGAAAAGAATTATGTCAAGAGAAATAA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	AATCCATTACAAACATGGTCTGAAGTATTC
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	TATTTTCGCCTACCACAACACCTGCAACC
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	AGAAGCTCCTGAACTAAAAGCAGAACCTAA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	AGTACGCTTAAAGCAATAATAAGTATAAAT
GTTGGGAATTATAAGCTAAAATACAATTTTGAAGGCAATTCACAAC	TTGTTACGTCTAAAATTTATGCTCCGGATA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC	ATATTGCACTAAATTCAATGGCTAAAATTA
GTTGGGAATTATAAGCTAAAATACAATTTTGAAAGCAATTCACAAC

Protein	Signature genes	Signature genes Name	Protein_function
CP020918.1\|AWG23088.1\|4036520_4040582_+\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|187774
CP020918.1\|AWG23092.1\|4045381_4046416_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378416
CP020918.1\|AWG23098.1\|4052213_4052915_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274590
CP020918.1\|AWG23090.1\|4041316_4042210_+\|subtype-II-CRISPR-associated-endonuclease-Cas1	cas1	cd09720_cas1_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|274694
CP020918.1\|AWG23100.1\|4053435_4054275_-\|phytoene-synthase	unknown	unknown	gnl\|CDD\|173831
CP020918.1\|AWG23096.1\|4050217_4051513_-\|deoxyribodipyrimidine-photolyase	unknown	unknown	gnl\|CDD\|223492
CP020918.1\|AWG23084.1\|4030367_4031228_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|212168
CP020918.1\|AWG23101.1\|4054289_4055747_-\|phytoene-dehydrogenase	unknown	unknown	gnl\|CDD\|274273
CP020918.1\|AWG23085.1\|4031532_4031985_-\|tRNA-(uridine(34)/cytosine(34)/5--carboxymethylaminomethyluridine(34)-2'-O)--methyltransferase-TrmL	unknown	unknown	gnl\|CDD\|349967
CP020918.1\|AWG23099.1\|4052960_4053401_-\|carotene-hydroxylase	unknown	unknown	gnl\|CDD\|178211
CP020918.1\|AWG23095.1\|4049238_4050147_-\|TIGR01777-family-protein	unknown	unknown	gnl\|CDD\|187553
CP020918.1\|AWG23097.1\|4051512_4051974_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|176862
CP020918.1\|AWG23082.1\|4028381_4028795_+\|GxxExxY-protein	unknown	unknown	gnl\|CDD\|372581
CP020918.1\|AWG23086.1\|4032010_4032601_-\|pseudouridine-synthase	unknown	unknown	gnl\|CDD\|211334
CP020918.1\|AWG23091.1\|4042240_4042588_+\|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|226043
CP020918.1\|AWG23094.1\|4048256_4048847_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377274
CP020918.1\|AWG23087.1\|4032813_4036215_+\|endonuclease	unknown	unknown	gnl\|CDD\|197338
CP020918.1\|AWG23083.1\|4029465_4030251_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224045
CP020918.1\|AWG23089.1\|4040761_4041193_+\|transposase	unknown	unknown	gnl\|CDD\|376616
CP020918.1\|AWG23093.1\|4046792_4048193_+\|DNA-recombination-protein-RmuC	unknown	unknown	gnl\|CDD\|376878

Protein	Function_ID	Function_description	E-value
CP020918.1\|AWG23088.1\|4036520_4040582_+\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	gnl\|CDD\|187774	cd09643, Csn1, CRISPR/Cas system-associated protein Cas9. CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Very large protein containing McrA/HNH-nuclease related domain and a RuvC-like nuclease domain; signature gene for type II.	3.85664e-54
CP020918.1\|AWG23092.1\|4045381_4046416_-\|hypothetical-protein	gnl\|CDD\|378416	pfam10282, Lactonase, Lactonase, 7-bladed beta-propeller. This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyze 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.	8.51154e-91
CP020918.1\|AWG23098.1\|4052213_4052915_-\|hypothetical-protein	gnl\|CDD\|274590	TIGR03462, Bifunctional_lycopene_cyclase/phytoene_synthase, lycopene cyclase domain. This domain is often repeated twice within the same polypeptide, as is observed in Archaea, Thermus, Sphingobacteria and Fungi. In the fungal sequences, this tandem domain pair is observed as the N-terminal half of a bifunctional protein, where it has been characterized as a lycopene beta-cyclase and the C-terminal half is a phytoene synthetase. In Myxococcus and Actinobacterial genomes this domain appears as a single polypeptide, tandemly repeated and usually in a genomic context consistent with a role in carotenoid biosynthesis. It is unclear whether any of the sequences in this family truly encode lycopene epsilon cyclases. However a number are annotated as such. The domain is generally hydrophobic with a number of predicted membrane spanning segments and contains a distinctive motif (hPhEEhhhhhh). In certain sequences one of either the proline or glutamates may vary, but always one of the tandem pair appear to match this canonical sequence exactly.	2.11969e-13
CP020918.1\|AWG23090.1\|4041316_4042210_+\|subtype-II-CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|274694	TIGR03639, cas1_NMENI, CRISPR-associated endonuclease Cas1, subtype II/NMENI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is a prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 variant of the NMENI subtype of CRISPR/Cas system.	1.47448e-103
CP020918.1\|AWG23100.1\|4053435_4054275_-\|phytoene-synthase	gnl\|CDD\|173831	cd00683, Trans_IPPS_HH, Trans-Isoprenyl Diphosphate Synthases, head-to-head. These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze a head-to-head (HH) (1'-1) condensation reaction. This CD includes squalene and phytoene synthases which catalyze the 1'-1 condensation of two 15-carbon (farnesyl) and 20-carbon (geranylgeranyl) isoprenyl diphosphates, respectively. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions (DXXXD) located on opposite walls. These residues mediate binding of prenyl phosphates. A two-step reaction has been proposed for squalene synthase (farnesyl-diphosphate farnesyltransferase) in which, two molecules of FPP react to form a stable cyclopropylcarbinyl diphosphate intermediate, and then the intermediate undergoes heterolysis, isomerization, and reduction with NADPH to form squalene, a precursor of cholestrol. The carotenoid biosynthesis enzyme, phytoene synthase (CrtB), catalyzes the condensation reaction of two molecules of geranylgeranyl diphosphate to produce phytoene, a precursor of beta-carotene. These enzymes produce the triterpene and tetraterpene precursors for many diverse sterol and carotenoid end products and are widely distributed among eukareya, bacteria, and archaea.	3.5524e-60
CP020918.1\|AWG23096.1\|4050217_4051513_-\|deoxyribodipyrimidine-photolyase	gnl\|CDD\|223492	COG0415, PhrB, Deoxyribodipyrimidine photolyase [DNA replication, recombination, and repair].	2.5555e-149
CP020918.1\|AWG23084.1\|4030367_4031228_+\|hypothetical-protein	gnl\|CDD\|212168	cd11669, TTHB210-like, Hypothetical protein TTHB210, a sigma(E)-regulated gene product found in Thermus thermophilus, and similar proteins. TTHB210 is an uncharacterized protein found in Thermus thermophilus, and is controlled by the sigma(E) /anti-sigma(E) regulatory system. It is one of the five proteins of the extracytoplasmic function (ECF) sigma factor sigma(E)-regulated gene products whose physiological function have not been determined. Its crystallographic structure reveals a novel homodecamer although it is a dimer in solution.	3.66454e-23
CP020918.1\|AWG23101.1\|4054289_4055747_-\|phytoene-dehydrogenase	gnl\|CDD\|274273	TIGR02734, Phytoene_desaturase_lycopene-forming, phytoene desaturase. Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	2.01523e-123
CP020918.1\|AWG23085.1\|4031532_4031985_-\|tRNA-(uridine(34)/cytosine(34)/5--carboxymethylaminomethyluridine(34)-2'-O)--methyltransferase-TrmL	gnl\|CDD\|349967	cd18094, SpoU-like_TrmL, SAM-dependent tRNA methylase related to TrmL. tRNA (Um34/Cm34) methyltransferase TrmL catalyzes the methyl transfer from S-adenosyl-L-methionine (AdoMet) to the 2'-OH at position 34 in both tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). It is part of the SpoU family of MTases, a subfamily of the SPOUT methyltransferase superfamily. The SPOUT methyltransferase superfamily is a large class of S-adenosyl-L-methionine (AdoMet or SAM)-dependent RNA MTases which are structurally characterized by a deep trefoil knot.	6.94777e-78
CP020918.1\|AWG23099.1\|4052960_4053401_-\|carotene-hydroxylase	gnl\|CDD\|178211	PLN02601, PLN02601, beta-carotene hydroxylase.	4.63763e-18
CP020918.1\|AWG23095.1\|4049238_4050147_-\|TIGR01777-family-protein	gnl\|CDD\|187553	cd05242, SDR_a8, atypical (a) SDRs, subgroup 8. This subgroup contains atypical SDRs of unknown function. Proteins in this subgroup have a glycine-rich NAD(P)-binding motif consensus that resembles that of the extended SDRs, (GXXGXXG or GGXGXXG), but lacks the characteristic active site residues of the SDRs. A Cys often replaces the usual Lys of the YXXXK active site motif, while the upstream Ser is generally present and Arg replaces the usual Asn. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	1.67263e-108
CP020918.1\|AWG23097.1\|4051512_4051974_-\|hypothetical-protein	gnl\|CDD\|176862	cd07820, SRPBCC_3, Ligand-binding SRPBCC domain of an uncharacterized subfamily of proteins. Uncharacterized group of the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain superfamily. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands. SRPBCC domains include the steroidogenic acute regulatory protein (StAR)-related lipid transfer (START) domains of mammalian STARD1-STARD15, the C-terminal catalytic domains of the alpha oxygenase subunit of Rieske-type non-heme iron aromatic ring-hydroxylating oxygenases (RHOs_alpha_C), Class I and II phosphatidylinositol transfer proteins (PITPs), Bet v 1 (the major pollen allergen of white birch, Betula verrucosa), CoxG, CalC, and related proteins. Other members of the superfamily include PYR/PYL/RCAR plant proteins, the aromatase/cyclase (ARO/CYC) domains of proteins such as Streptomyces glaucescens tetracenomycin, and the SRPBCC domains of Streptococcus mutans Smu.440 and related proteins.	5.24161e-60
CP020918.1\|AWG23082.1\|4028381_4028795_+\|GxxExxY-protein	gnl\|CDD\|372581	pfam13366, PDDEXK_3, PD-(D/E)XK nuclease superfamily. Members of this family belong to the PD-(D/E)XK nuclease superfamily.	7.04527e-48
CP020918.1\|AWG23086.1\|4032010_4032601_-\|pseudouridine-synthase	gnl\|CDD\|211334	cd02566, PseudoU_synth_RluE, Pseudouridine synthase, Escherichia coli RluE. This group is comprised of bacterial proteins similar to E. coli RluE. Pseudouridine synthases catalyze the isomerization of specific uridines in an RNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. Escherichia coli RluE makes psi2457 in 23S RNA. psi2457 is not universally conserved.	7.57393e-66
CP020918.1\|AWG23091.1\|4042240_4042588_+\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	2.55216e-27
CP020918.1\|AWG23094.1\|4048256_4048847_+\|hypothetical-protein	gnl\|CDD\|377274	pfam04264, YceI, YceI-like domain. E. coli YceI is a base-induced periplasmic protein. The recent structure of a member of this family shows that it binds to poly-isoprenoid. The structure consists of an extended, eight-stranded, antiparallel beta-barrel that resembles the lipocalin fold.	1.93449e-09
CP020918.1\|AWG23087.1\|4032813_4036215_+\|endonuclease	gnl\|CDD\|197338	cd10283, MnuA_DNase1-like, Mycoplasma pulmonis MnuA nuclease-like. This subfamily includes Mycoplasma pulmonis MnuA, a membrane-associated nuclease related to Deoxyribonuclease 1 (DNase1 or DNase I, EC 3.1.21.1). The in vivo role of MnuA is as yet undetermined. This subfamily belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.	1.10706e-17
CP020918.1\|AWG23083.1\|4029465_4030251_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224045	COG1120, FepC, ABC-type cobalamin/Fe3+-siderophores transport systems, ATPase components [Inorganic ion transport and metabolism / Coenzyme metabolism].	2.27138e-77
CP020918.1\|AWG23089.1\|4040761_4041193_+\|transposase	gnl\|CDD\|376616	pfam01797, Y1_Tnp, Transposase IS200 like. Transposases are needed for efficient transposition of the insertion sequence or transposon DNA. This family includes transposases for IS200 from E. coli.	8.27863e-31
CP020918.1\|AWG23093.1\|4046792_4048193_+\|DNA-recombination-protein-RmuC	gnl\|CDD\|376878	pfam02646, RmuC, RmuC family. This family contains several bacterial RmuC DNA recombination proteins. The function of the RMUC protein is unknown but it is suspected that it is either a structural protein that protects DNA against nuclease action, or is itself involved in DNA cleavage at the regions of DNA secondary structures.	6.06018e-125

>CP020918.1|AWG23091.1|4042240_4042588_+|CRISPR-associated-endonuclease-Cas2
MYDEHYTRLNQYRSLWILVFFDLPTETRKERKIASGFRKKLLDDGFSMFQFSIYMRFCASRENAEVHTKRIKSNLPEHGKIGVMQITDKQFGMMELFYGKKPVDPEKPSQQLELF
>CP020918.1|AWG23090.1|4041316_4042210_+|subtype-II-CRISPR-associated-endonuclease-Cas1
MIKRTLFFGNPAYLSTKNEQLVISYPDKSLETKTVAIEDIGVIVLENQQITITNGLLEKLTNNNVALINCDQYHLPIGLLMPLSGHTEQTERFKNQINASVPLKKNLWQQTISSKISNQAGLLKEKGIPCRKMEIWAKEVSSGDALNHESRAAVFYWANLFTIENFTRGQKEIAPNNLLNYGYAILRGITARALVSSGMLPTLGIFHRNKYNAYCLADDIMEPYRPYVDLIVSNIIENEDTIEELTIDMKKQLLSIASIDVCIDGKNSPLMVAMSRTTNSLNECFEGSSRKLLYPVF
>CP020918.1|AWG23089.1|4040761_4041193_+|transposase
MPYIKTYIHFVWSTKNRVPFLDNKELRQKVWRHIKENGDKKGIYIDFVNGYSDHCHCLVSLGADQTIQKTMQLIKGESSFWINQSKLCLNKFEWQDEYFAVSVSESILDKVRNYIKNQEEHHSQHTFAEEYNEFITKYKFQKE
>CP020918.1|AWG23088.1|4036520_4040582_+|type-II-CRISPR-RNA-guided-endonuclease-Cas9
MKKILGLDLGTTSIGWAYINEAENESEISSIINSGVRIVPLTTDEEADFKKGNTISINADRTLKRGARRGLQRFKQRRNALLQTFRGNNFITSNYVYAETGKQTTFSSYKLRAKSATEQVSKEELVQVLLMLNKKRGYKSSRKAKTAEEGDAIDGMKIAKELNDKNQTPGEWIYNSLLNGGKFVPEFYRSDLQTELERIIRFQNQFYPEIFNSKLLEEIQGKTRTATSQHFTKILKIELSENKGTREQTKLQHYKWRNDSLSCALDLKVIAFILTEINNQINQSSGYLGAISDRSKELYFNQETVGQFQFKQLEQNSHAKLKNQVFYRQDYVDEFEQIWETQSKFYPELDEKLKIEVRDITIFYQRKLKSQKHLVSFCEFEKGHKAIPKSSPLFQDFRIWQNLNNIVVKNETTKEPFLLGEELKNNIAQELLFKESMTDIQMLTFCELKKGTHTVNFKKIEGNRTNTALFKAFEKILTIEGYDLDFTKMSHSEIRNAISPLFETIGIDTSLLYFDNSIEGNDFDKQPYYQLWHLLYSAEEDEVLKQTLMKKFGFKENHIPFLLNINLQADYGSLSARAIKKVLPHLMDGHIYDKACLLTGYNHSSSLTTEQNESRILKNQLELLKKNSLRNPVVEKILNQMINVINAIIEDPNMGKPDEIRVELARELKANNEQRNEMTKAINNATKTHDDIRKLLAVEYGIARVTRNDIIRYKLWKETGGISLYTGKPIEPSRLFTKDYDIEHIIPKSRLFDDSFSNKTLCERTLNIEKSNKTAYSFLQEKLTEEEFDQFEKRIKGMFGKISRTKQNKLLIADNQIPEGFIDRQLRETQYIAKKAKEILLEVSRNVTATIGSVTDKLREDWELIDVMQELNWNKYDTLGLTYEEKGKNGERLYKIKDWTKRNDHRHHAMDAITVAFTKPAYIQYLNNLNARTNTDKKGNSIIGIENKYLKRDKNNKLRFIEPMPNFRSEAKKQLESILISYKAKNKVVTNNKNITKKIGGTNQKLQLTPRGQLHKETVYGKMQQYATKEEKVNANFTQDYIAKVAKKEYREALLKRLSENDNDPKKAFTGKNSLAKTPIYISLEDNIVVPEKVKIVWLEDNYTIRKDITPDLKLEKVIDVGLRQILQNRLNEFKGDAKKAFVNLDENPIWQNKAKGIAMKRVTISGVSNALALHTKKDNFGNEILDKDENPIPVDFVSTGNNHHVAIYRDEKGNLQDEVVSFYDAVVRKNLGLSIINKTHKYGWEFLFTMKQNEYFIFPSDSFDPQEVDLFNPANYHLISPNMFRVQKFSKVEYGNSSVRDYVFRQHLETTLNDKKELKDIAFKSIKSLPYFSNIIKIRINHLGQIVQIGEY
>CP020918.1|AWG23087.1|4032813_4036215_+|endonuclease
MKLHYTCKTAWTIFAFFATIVATVQAQATMPTAQTIPFSQNFDGLATNATVYPAGFQGWNTDSSPGSTYNTSAIPAGDKPLALGSASSSAGALYNYNGKIGFLNTTPLDNTIAFAFTTAGKSAIQVQYDAMTIRNPYSGSNTRINEMVLQYRVGNSTAFISLPDTAYSNNTTLENTSGGTTPQNLQTIKVTLPSECDNKSLVQIRWISRQVSGAGSRPSFAIDNISVINDITPPVTAASFPKASSILSDGFDFSNQINEIGKTYYVVVPSGSAEPSKLQLMNGQDANGNAALSAGVLTVANANQPYTATITGLTIGTAYIVYSVSEDAYQNLQLTTNSLNVSTSSTLVPSIKITTAAVAFGFQEQGFDSSAMTFTFKGSHITSNVIVTAPANFNVSKDNITFDSTVLFSAAEFLSNATPTVYVRFKPTNTLAYAGQILIESDGATSKNIAVSGKGINPYLQDFNDPEVLTNSGWTSYNEQGTNNSWSTTTTARNLNSAPGAVVMNGYSDNGASSDWFISPKLHLDSFSQFALLSFYSRKYYSGPSLKLKVSTDYDGVSSPSTATWTEIQGNFPTTTDIYTKSEFINLNAFKTSHTYVAWVYETTAGGPNNAAEWSVDDIAITNNAAFLAANPELDFEDVTVNTISTSKSFTVVAGGYGPITVAAPADYQVSLDNSTFTSSVLISESDALAGKLVYARFTPTSKSIAITGPITVTGTGLNQAKGFLKGSSLPKSETFDIVTYNLEFFGSEVIGSTGTEFGPVDDPLQIDNVAAVMNKLDADIYCVQEVSDDAAMETLLTKISINGKTFAKSISTSWSYSFNAPTADFPPQKLVVLYNTQTASVKSTKVLFKDFYDQVRAGTATLPNYPDSPSSFFSSGRLPYMVTIETNLGGVKKDISLIDLHARANSGSDINKYNMRKYDAEYLKDALDAEYPNDNLVLLGDFNDDVKTSVIAGNDSSYKKFVDDTTNYNALTLGISQQGAFSYLSSNGFLDHIIISNELTADYIPNSTAVYDPRNDISNYVNTTSDHGPVIARFNLQNTLSTKAFGTEVNYAKLYPNPTKDVVNFTLTTPTSATVTFKLYDSLGREIGTDKAINANASKQASVSLSTVPAGTYFYTLTSANKIVQKGKLIKE
>CP020918.1|AWG23086.1|4032010_4032601_-|pseudouridine-synthase
MSDHHHFIIHKPYGYLSQFIYELKRKKKLLGELHDFPVGTMAIGRLDEDSEGLLLLTTDGKVSEEIRSKKVEKEYYVQVDGIITQEAIDLLKEGVEIGFDGGKYTTKKCEARLITEIPDFGPRGKKIRDERHGPTTWAAITVNEGKFRQVRKMTAAVGFPTLRLVRVRIGNVHLQSLKAGDVIEVANFSADDQKSL
>CP020918.1|AWG23085.1|4031532_4031985_-|tRNA-(uridine(34)/cytosine(34)/5--carboxymethylaminomethyluridine(34)-2'-O)--methyltransferase-TrmL
MLNIVLVEPEIPNNTGNIGRLCVGTESRLHLVHPFGFVINDKNLKRSGLDYWVHLDVTEYNTVADWKAQIPDLSRVFLMSSHAEKSYLDIEFQDGDWLVFGKESKGLSADVLAQFENHLTIPMSKNIRSFNIANSVAFVIGEAKRQIGVR
>CP020918.1|AWG23084.1|4030367_4031228_+|hypothetical-protein
MKRNFTLFTKTVVLFGVLLIQSCTDDVVVPNNITYLLKGKITETKMRIYAGPEVAVGDGLARTWVTLDSKGYPMEIAIEISEDAIKNPGEDSEMDMADGAMEMEHGQMIMLPLHSQAQKSTPFNHVGINWNPHGHPPAQVFDSPHFDFHFYTIPLEEQLAIPGWSTATDALFNTYPDAAFLPANYFTPPGADTAEAQMGKHWIPTNIGDYLPFSKILVYGSYNGKVNFIEPMVTQAYLLQKINTSESYSQPLKVQTKGNYPTKYNIYHDTKTGKTQITLSDFVTRN
>CP020918.1|AWG23083.1|4029465_4030251_+|ABC-transporter-ATP-binding-protein
MTNKTILKAANLGIGYIHKKETKTIATNINLDLKQGSLIALVGGNGIGKSTLLRTLTGIQKPIDGKVLLNDQAISSYSPLELAQNLSVVLTEKLPPSNLSVYELVALGRQPYTNWIGKLTATDVQKVQHAMELTQIDHLATKKHFEISDGQLQKVLVARALAQDTPLIVLDEPTTHLDLLHKVALFKLLKNLSKETQKCILFSTHDIDMAIQLSDEMIIMTPDNCVQDQPCNFIANGTFDTIFKDDHIAFDSEKGKFIIRN
>CP020918.1|AWG23082.1|4028381_4028795_+|GxxExxY-protein
MITQKYLDELTYEVIGASIEVHRIIGRGLLETVYHQCLKEELSIRNINFKSEIKIPLIYKGKELVTDFRCDFFIENCLVVELKSVTQMIPIYEAQLQTYMNLLKAPKGILLNFNCFNLFKEGQKTFVNEHFKKLPLK
>CP020918.1|AWG23092.1|4045381_4046416_-|hypothetical-protein
MHFFIGSYTHMLTPTFGGRGDGIYVVHIDEQGTVELVHTVPTENPAYLAISDDNRFLYTITEKEQDAVVKAFTIHADFSLSFLNQELIPGSLPCHLVYCNGHIVVACYGSGNVLHYQTQADGKIMPHASHHIHTGKGVNASRQEAPHAHQAVLHPDQKTLFVPDLGIDTVKVYELGSSYLQPKPDLDITTVAGGGVRHLVFNKAGTLGYLSHELTGQVSVLEQQNLNWEVVELHESLPASYAGTPIASAIRLHPNERFLYAANRGYDGITVFEVQANSLQLKHHFKTHGEELREFNITPDGRFLIACHQISDQIMTFKIQEDGSCELISQTDSLISPVCVCFLK
>CP020918.1|AWG23093.1|4046792_4048193_+|DNA-recombination-protein-RmuC
MSALVINSLIFFIAIFLGFIIGKLLSSANFRSAKSSLDERILGLQAQVQQTKEQLASDRLSFEKKQEKVQYEKEQLRHEKESLVIQLSKKEADFDNLWERNKEQKQEVEQLQEKFTKEFENLANKILDEKSTKFTEQNKENMKNILSPLQEKIQLFEKKVDDTHKESIDYHAALRQQILGLREMNLQMSKETLNLTKALKGDSKMQGNWGELVLERVLEKSGLEKDREYHVQQSFTTAEGNRVFPDVVINLPDGKKMIVDSKVSLTSYERFVNEEDDALKASYLREHVLSIRRHVEQLGEKNYHDLYQIESPDFVLLFIPIEPAFALALNEDNSLYNKAFEKNIVIVTPATLLATLRTIDSMWTNQKQQENAFEIARQAGALYDKFEGFVTDLIKIGKKLEETKTEYSGAMNKLVEGKGNLITSVEKLKKMGAKAKKSLPENIINRAVASNDIQPEIEASNSSNSN
>CP020918.1|AWG23094.1|4048256_4048847_+|hypothetical-protein
MKTNLLLLTLLLSQICFSQKTLTVSNATAQFEASVPIFEPVAAKNEQVAVALNTKRGYISFSIPMTKFRFASSLMEQHFNDHYLETDRYPNANFKGIIENFDLNAITDYPTNYLIKGKLKIHGQSKNITATIRLQRTMIGFVLTSNFSVLTDDYRVEIPFLIRNKISKTVNISIEVPFQTEATNLGAITVQTKPTN
>CP020918.1|AWG23095.1|4049238_4050147_-|TIGR01777-family-protein
MKKKVLITGGTGFVGQHLTQLLVDNGFEISILSRSKRKNTPAVSYYKWDLETQYIDNKAVLEADYIIHLAGENIAGGRWTESRKKTIIASRVEPVELIKSVLAANGKMVEAFISASGVGYYGAITDAKICKESTDPENDFLGTTCQLWEAAADAMHLNANRIVKIRTGLVLGKNDGFLKKMLPPFKWGIGSPLGSGKQYMPWIHIDDLCAMYLLALQKPEMEGAYNAAIQDSTTNKIFSKTLAAIIGYKMWFPAVPAFVLRLLLGKIAVIVLEGRRVSASKVEKLGFRFKYINLDSAIRSCL
>CP020918.1|AWG23096.1|4050217_4051513_-|deoxyribodipyrimidine-photolyase
MSKAKVSFFWFRRDLRLEDNVGLFNALTSDVPVIPIFIFDKAILENLPKNDARVTFIHESLQKINEALKTSGTSLLVKHGNTVAVWQELMLEYDIQGVYWNKDYEPFAIARDLSISSELKNNGIESFSFKDQVIFEESDITKADGLPYTVYTPFKNKWLAKFKTDGPLAIYDTEKHFSNFFNSNFEFPTLSTIGFEESSIKVKTHNLTKIKNYQDLRDFPAVDGTSYLSPHLRFGTVSVRKLAVWAEKTNAVFLSELIWREFFMQILFHFPKVVTNNFKSAYDGIEWRNNEEDFKRWCSGTTGYPMVDAGMRELNETGYMHNRVRMVVASFLCKHLMISWQWGEAYFAQKLLDYDLSANVGNWQWAAGTGCDAAPYFRVFNPEIQMKKFDEKGVYIRKWIPEFDLGYVGPMVEHAFARDRAIATYKAGIVK
>CP020918.1|AWG23097.1|4051512_4051974_-|hypothetical-protein
MKLYKKESVQYVDATLDECWAFFSSPKNLQKITPQDMGFQITDYDGKSMYPGQIIQYLVSPLLGLKLSWVTEITAVKDKSYFIDEQRFGPYVIWHHKHFFEATATGVKMTDVVHYGLPLGFLGRIMNTLVVKAKLNEIFAYREMAVNKLFNSK
>CP020918.1|AWG23098.1|4052213_4052915_-|hypothetical-protein
MSLYLILNIASFIIPFLYSFEKRMRFSNRWKAFIPSLAITAIFFIGWDIFFTKVGVWHFNPRYHTGLEIFGLPIEEWLFFFCIPYASLFIHFAFHYFLPKVALSPKAVFRIYAVIIAIVLPILVLNFGKWYTTVNYSLLIILLTYTVIKAPHVLQTFFITFLLILVPFALVNGILTGSFIDEPVVYYNDLENLGIRLGTIPVEDVAYAFSMLLMSLVIMDKIERKPNNLGVPR
>CP020918.1|AWG23099.1|4052960_4053401_-|carotene-hydroxylase
MISFLITLAVFLVMECVTWLTHKYVMHGFMWYFHADHHQPKYAGIFERNDIFFVIFAIPSIVLFYLGAQAGFNHLFFIGLGITIYGFCYFMIHDVLIHQRFKWFKNSKNKYLIGLRKGHKVHHKHLGKEEGECFGMLFVPFKYWKI
>CP020918.1|AWG23100.1|4053435_4054275_-|phytoene-synthase
MKNLFDTVSFKCSKLVTKNYSTSFSLAVYMLSPSIRNDIYSIYGFVRFADEIVDSFHGFDKEDLINDFEKEYYKAFKAGISLNPILNSFQQTVKENNISDDLIQAFLKSMKLDLVKGNYDTVEDYNEYIYGSADVVGLMCLKVFVKGNNAKYEALKGEAMRLGSAFQKVNFLRDLKDDNLILNRNYFPGVDLKSFDEKSKQAIIAEIEEDFRIAHQGIKKLPIEAKFGVYTAYVYYKKLLHKLEKTPSHQIGNTRIRVSNYSKMGLLAKSFVSYKLKLV
>CP020918.1|AWG23101.1|4054289_4055747_-|phytoene-dehydrogenase
MKKSISIIGSGFSALSAASYLAKAGHKVTVFEKNDSIGGRARQFKAAGFTFDMGPSWYWMPDVFERFFADFGKKTTDYYELIKLSPAYNVYYGEQDFIAIADNLEDIVTTFESIEKGSGAELRDFIGKAKSNYDIAIKDLVYRPGVSPLELVTIETTKKLGQFFSTIKKDVRKKFKNQKLVQILEFPVLFLGAKPSDTPSFYSFMNYADFGLGTWHPKTGMYDVVKAMSSLATELGVVFKTNSNIDKIIVEAGVAKGIVVNGEKILSDVVLSGADYHHTETLLDAPYRAYSEKYWETRVFAPSSLLFYVGFNKKIKNVAHHDLFFDVDFDAHAKDIYDKPKWPADPLFYANFPSITDPTAAPDGMEAGFFLIPLAPGISDTNELREFYFDKIITRFEKITQQKVKDAIVYKKSFCKNDFVSEYNSFKGNAYGMANTLLQTAFLRPKLKSSKVDNLFFTGQLTVPGPGVPPALISGKLVSELIINQ

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Crispr_ID: CP020918_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP020918_8

4605583-4605689

Orphan

Consensus_repeat	Method
CTTTGGCGATAGCCAATCCGTTTTA	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP020918_8

>merge|CP020918|8|4605583-4605689|CRISPRCasFinder
CTTTGGCGATAGCCAATCCGTTTTACCAGCGTTCCATCTTCCGAGTTAGCTTCTCCCTATATACAAATCCGTTTTATCATCGCTTTGGCGATAGCCAATCCGTTTTA

>CP020918|8|8|4605583-4605689|CRISPRCasFinder
CTTTGGCGATAGCCAATCCGTTTTA	CCAGCGTTCCATCTTCCGAGTTAGCTTCTCCCTATATACAAATCCGTTTTATCATCG
CTTTGGCGATAGCCAATCCGTTTTA

Protein	Signature genes	Signature genes Name	Protein_function
CP020918.1\|AWG23509.1\|4613689_4614652_-\|IS30-family-transposase	unknown	unknown	gnl\|CDD\|225382
CP020918.1\|AWG23494.1\|4596472_4596679_+\|hypothetical-protein	unknown	unknown	unknown
CP020918.1\|AWG23508.1\|4613277_4613493_+\|YqaE/Pmp3-family-membrane-protein	unknown	unknown	gnl\|CDD\|376592
CP020918.1\|AWG23511.1\|4617030_4617906_-\|protein-(glutamine-N5)-methyltransferase,-release-factor-specific	unknown	unknown	gnl\|CDD\|236467
CP020918.1\|AWG23505.1\|4608670_4609522_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379325
CP020918.1\|AWG23507.1\|4611569_4612961_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379583
CP020918.1\|AWG23495.1\|4596667_4596886_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378182
CP020918.1\|AWG23506.1\|4609497_4611567_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|270622
CP020918.1\|AWG23510.1\|4615054_4616296_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|182528
CP020918.1\|AWG23496.1\|4596910_4597726_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|378820
CP020918.1\|AWG23497.1\|4597803_4598481_-\|RNA-helicase	unknown	unknown	gnl\|CDD\|350669
CP020918.1\|AWG23502.1\|4604105_4604681_-\|nucleotide-exchange-factor-GrpE	unknown	unknown	gnl\|CDD\|271355
CP020918.1\|AWG23512.1\|4618020_4619067_+\|riboflavin-biosynthesis-protein-RibD	unknown	unknown	gnl\|CDD\|273015
CP020918.1\|AWG23501.1\|4602936_4604058_-\|molecular-chaperone-DnaJ	unknown	unknown	gnl\|CDD\|237660
CP020918.1\|AWG23498.1\|4598813_4599977_-\|response-regulator	unknown	unknown	gnl\|CDD\|225114
CP020918.1\|AWG23500.1\|4601750_4602668_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213236
CP020918.1\|AWG23499.1\|4600353_4601676_-\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|378925
CP020918.1\|AWG23504.1\|4607983_4608661_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238119
CP020918.1\|AWG23503.1\|4605700_4607071_-\|histidine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234586
CP020918.1\|AWG23493.1\|4595703_4596501_-\|haloacid-dehalogenase	unknown	unknown	gnl\|CDD\|319818

Protein	Function_ID	Function_description	E-value
CP020918.1\|AWG23509.1\|4613689_4614652_-\|IS30-family-transposase	gnl\|CDD\|225382	COG2826, Tra8, Transposase and inactivated derivatives, IS30 family [DNA replication, recombination, and repair].	2.12179e-84
CP020918.1\|AWG23508.1\|4613277_4613493_+\|YqaE/Pmp3-family-membrane-protein	gnl\|CDD\|376592	pfam01679, Pmp3, Proteolipid membrane potential modulator. Pmp3 is an evolutionarily conserved proteolipid in the plasma membrane which, in S. pombe, is transcriptionally regulated by the Spc1 stress MAPK (mitogen-activated protein kinases) pathway. It functions to modulate the membrane potential, particularly to resist high cellular cation concentration. In eukaryotic organisms, stress-activated mitogen-activated protein kinases play crucial roles in transmitting environmental signals that will regulate gene expression for allowing the cell to adapt to cellular stress. Pmp3-like proteins are highly conserved in bacteria, yeast, nematode and plants.	0.00200181
CP020918.1\|AWG23511.1\|4617030_4617906_-\|protein-(glutamine-N5)-methyltransferase,-release-factor-specific	gnl\|CDD\|236467	PRK09328, PRK09328, N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional.	1.91639e-95
CP020918.1\|AWG23505.1\|4608670_4609522_+\|hypothetical-protein	gnl\|CDD\|379325	pfam13672, PP2C_2, Protein phosphatase 2C. Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.	4.80643e-06
CP020918.1\|AWG23507.1\|4611569_4612961_+\|hypothetical-protein	gnl\|CDD\|379583	pfam14362, DUF4407, Domain of unknown function (DUF4407). This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.	1.14805e-47
CP020918.1\|AWG23495.1\|4596667_4596886_-\|hypothetical-protein	gnl\|CDD\|378182	pfam09413, DUF2007, Putative prokaryotic signal transducing protein. This is a family of putative prokaryotic signal transducing proteins of Pii-type.	0.00359877
CP020918.1\|AWG23506.1\|4609497_4611567_+\|hypothetical-protein	gnl\|CDD\|270622	cd00180, PKc, Catalytic domain of Protein Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.	4.9343e-08
CP020918.1\|AWG23510.1\|4615054_4616296_+\|ABC-transporter-permease	gnl\|CDD\|182528	PRK10535, PRK10535, macrolide ABC transporter ATP-binding protein/permease MacB.	1.63808e-39
CP020918.1\|AWG23496.1\|4596910_4597726_-\|alpha/beta-hydrolase	gnl\|CDD\|378820	pfam12146, Hydrolase_4, Serine aminopeptidase, S33. This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.	1.94211e-15
CP020918.1\|AWG23497.1\|4597803_4598481_-\|RNA-helicase	gnl\|CDD\|350669	cd00268, DEADc, DEAD-box helicase domain of DEAD box helicases. DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.	5.81519e-25
CP020918.1\|AWG23502.1\|4604105_4604681_-\|nucleotide-exchange-factor-GrpE	gnl\|CDD\|271355	cd00446, GrpE, nucleotide exchange factor GrpE. GrpE is the adenine nucleotide exchange factor of DnaK (Hsp70)-type ATPases. In bacteria, the DnaK-DnaJ-GrpE (KJE) chaperone system functions at the fulcrum of protein homeostasis. GrpE participates actively in response to heat shock by preventing aggregation of stress-denatured proteins; unfolded proteins initially bind to DnaJ, the J-domain ATPase-activating protein (Hsp40 family), whereupon DnaK hydrolyzes its bound ATP, resulting in a stable complex. The GrpE dimer binds to the ATPase domain of Hsp70 catalyzing the dissociation of ADP, which enables rebinding of ATP, one step in the Hsp70 reaction cycle in protein folding. In eukaryotes, only the mitochondrial Hsp70, not the cytosolic form, is GrpE dependent. Over-expression of Hsp70 molecular chaperones is important in suppressing toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, as well as several polyQ-diseases such as Huntington's disease and ataxias.	2.1081e-35
CP020918.1\|AWG23512.1\|4618020_4619067_+\|riboflavin-biosynthesis-protein-RibD	gnl\|CDD\|273015	TIGR00326, eubact_ribD, riboflavin biosynthesis protein RibD. This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD].	1.21348e-96
CP020918.1\|AWG23501.1\|4602936_4604058_-\|molecular-chaperone-DnaJ	gnl\|CDD\|237660	PRK14289, PRK14289, molecular chaperone DnaJ.	7.83925e-148
CP020918.1\|AWG23498.1\|4598813_4599977_-\|response-regulator	gnl\|CDD\|225114	COG2204, AtoC, Response regulator containing CheY-like receiver, AAA-type ATPase, and DNA-binding domains [Signal transduction mechanisms].	3.14752e-175
CP020918.1\|AWG23500.1\|4601750_4602668_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213236	cd03269, ABC_putative_ATPase, ATP-binding cassette domain of an uncharacterized transporter. This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.	4.88948e-114
CP020918.1\|AWG23499.1\|4600353_4601676_-\|ABC-transporter-permease	gnl\|CDD\|378925	pfam12698, ABC2_membrane_3, ABC-2 family transporter protein. This family is related to the ABC-2 membrane transporter family pfam01061.	5.01807e-31
CP020918.1\|AWG23504.1\|4607983_4608661_+\|hypothetical-protein	gnl\|CDD\|238119	cd00198, vWFA, 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.	6.52312e-10
CP020918.1\|AWG23503.1\|4605700_4607071_-\|histidine--tRNA-ligase	gnl\|CDD\|234586	PRK00037, hisS, histidyl-tRNA synthetase; Reviewed.	4.34269e-142
CP020918.1\|AWG23493.1\|4595703_4596501_-\|haloacid-dehalogenase	gnl\|CDD\|319818	cd07516, HAD_Pase, phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily. Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	2.81575e-70

>CP020918.1|AWG23502.1|4604105_4604681_-|nucleotide-exchange-factor-GrpE
MFKNVFKNKGNMTTENTEIDQKIEDVTLDNNATEEQVLAEELSVEEQLTKDLANEKDKFLRLFAEFENYKRRTTKERIELFKTANADVVGALLPVLDDFDRAIIEIAKSENEAVTKGVQLIHEKLKNTLNSKGLEVVDVNAGDAFNADFAEAITQIPAPSDDMKGKIVDVLEKGYKLGDKIIRFPKVVIGQ
>CP020918.1|AWG23501.1|4602936_4604058_-|molecular-chaperone-DnaJ
MKKDFYEILGIAKGADAAAIKKGYRKKAIEFHPDKNPGDKTAEEKFKEAAEAYEVLSDPAKKQKYDQYGHQAFDGSGGFGGGGGHGGMNMDDIFSQFGDIFGGGGFGGFGGGGSRGPQRVKGSNLRIKVKLTLEEIANGVEKKVKVKRKVQAPGVSYKTCSTCNGQGQVMRVTNTILGRMQSASTCPTCGGAGQQLDKKPAEADAQGMIQEDETVSIKIPAGVVDGMQLKVSSKGNDAPGNSVPGDLIVAIEELEHEFLKREGENLHYDLYISFPEAILGVSKDIEAVNGKVRIKLEDGIQSGKILRLKGKGIPNINGYGNGDLLVHVNVWTPKELNKEQRQFFEKNMDSDNFIPNPEKSDKSFFEKVKDMFS
>CP020918.1|AWG23500.1|4601750_4602668_-|ABC-transporter-ATP-binding-protein
MSNLLEVKNVVKQYGDYTALNAVSLSIPKGSIYGLLGPNGAGKTSLIRIINQITLPDSGEIILDGEKLQSKHIQHIGYLPEERGLYQSMKVGEQCLYLAQMKGLSKAEAKKQLDYWFDRLEIQGWWNKKIQELSKGMAQKIQFVVCVLHQPKLLILDEPFSGFDPVNANVIKDEILALKEKGTTILFSTHRMESVEELCDEIALIHKSNKLIEGKLNDVKRQFRTNSYEVGILSSDVEGLMFAITQKFSVNPANFKTLNNELKLEIHIGDATPNELLNILVQKGQVTHFVEKIPSVNDIFIQTVS
>CP020918.1|AWG23499.1|4600353_4601676_-|ABC-transporter-permease
MSIISLIIKREFISKVRNKSFIVMTFLSPLLFVGITVFISYLSSMKSDTKQIAIHDPSGVFVKELVAQNQEEAEYKYVDLTPIPVEYLRDSIANQSYEGLLLIPNTTDATSLETKIQLIANTSPSIALIEKVQNVIGKKITQLNLEKAHLDTLAIKKAQSTVVLSLAKSSGEETIKGLNEIKIFIGGAFGYLVMMFIIMYGNMVMRSVIEEKTNRIIEIIISSVKPFQLMIGKIIGTSLAGILQFMIWAVIGLSIMTFASYFFGVNVGPTARLTPEMMTAEQSQMMTTVQMYIKELWNLPIASILLGFIVYFIGGYFLYSSFYAAIGAAVDNQTDSQQFLLPIIIPLMLSVYIGFFSVVHDPQGTIAVVFSMIPLTSPIVMLMRIPFGVPLWQIVVSVSILFGTFFGVVWFAAKIYRVGILMYGKKPSWKELYRWLKYAG
>CP020918.1|AWG23498.1|4598813_4599977_-|response-regulator
MPKILIIEDEAAIRRVLTKILSEENDTYEVEEAEDGSIGFEKIKINDYDLVLCDIKMPKMDGVELLEAVKKIKPEIPMVMISGHGDMETAINTMRLGAFDYISKPPDLNRLLNTVRNALDRKQLVVENKILKKKVSKNYEMIGESEAIDHIKIMIDKVAPTDARVLVTGANGTGKELVAHQLHEKSDRASFPLIEVNCAAIPSELIESELFGHVKGAFTSAVKDRAGKFEAADKGTIFLDEIGDMSLSAQAKVLRALQENIITRVGADKDIKVDVRVVAATNKDLKTEIAEGRFREDLYHRLAVILIKVPSLNDRREDIPLLITHFANKIASENGTAVKKFSVKAVNLLQAYDWTGNIRELRNVIERLIILGGTEISEDDVKLFASK
>CP020918.1|AWG23497.1|4597803_4598481_-|RNA-helicase
MKLKKLNEGLQQSLIDCGLTEANQMQKETFSTIKSGADCLILAPAGSGKTTTIVLNVIQQLVKEGEQSPRALIVVQDKEKVVEMLAMFEKLGAHTDLTVYGTHDKGDTDYDKNYISGGIDVLVGTPHKLSEMLSTAGYNVNRLKMFIVDDADPMLKLRHETKIARISSSIAKTQRIIFATDLTERIEALADKMLVEPFEFEFYDEEEEQEGEDEEDTEDEIVEEK
>CP020918.1|AWG23496.1|4596910_4597726_-|alpha/beta-hydrolase
MEVVKVVKFLVCTVVPFVGVLYALLLVYVYYNQTSMIFHTEKLPANYKFDYPQKFEEINTKSFDNVNLNGLLFRAENPKGLVFYLHGNAGTLGTWGSISKIYTDLGYDIFIMDYRGFGKSDGEIVDETQINKDVALVYSKLCKRYAEKDIYIAGYSIGSGLATILASNNQPKALLLQSPYYSFTELSSKIAPYFPNFIKRFKLESYSYFTKIKAPIYIFHGEDDELIPVDNGLKLSKLKSAGIHYFGLKNQGHGDMNENEVFQKELQTILN
>CP020918.1|AWG23495.1|4596667_4596886_-|hypothetical-protein
MGLMKVFSGSEVLALALKEKIEAINIDVVMKDNIQSARLAGFGSYGQAVELFVQETEYGKVFPIIEEFRLSI
>CP020918.1|AWG23494.1|4596472_4596679_+|hypothetical-protein
MSKTSILYFIFYSKGLIFFYFYHLGQSDNYFYKYARNICQVEHCQDNFSRIKSKKDRNNARFETVLNT
>CP020918.1|AWG23493.1|4595703_4596501_-|haloacid-dehalogenase
MKYKMLVLDMDDTLLNDDHIISKENKEMITKAQALGVYVILASGRPTPAMLDYAKELNMENSYMISFNGAVITDLKTNEIVFEQSLTQEQIHTLYDYSQKSKTHIITYLDGEVVSETNSEYIDVELNITGLKHNVVPDFKKAVYKSAIKCILLEEPSYLKEVEKDLKATMPHFSICMSKPFFLEVAQTGIDKAYSIKILAEKLNILQSEIIAVGNAGNDLTMVEYAGLGVWVDNVEPELRDRANVIVASNNNHGVAEVIEKYILG
>CP020918.1|AWG23503.1|4605700_4607071_-|histidine--tRNA-ligase
MASKPSIPKGTRDFSPAEVAKRQYIIQTIKTNFEKFGFQPIETPSFENSETLMGKYGEEGDRLIFKILNSGDYLAKANAGHLEAKDSTKLTASISEKALRYDLTVPFARYVVQHQNEIEFPFKRYQIQPVWRADRPQKGRFREFFQCDADVVGSKSLWQEVELVQLYDAVFTDLGLAGATVKINNRKILSGIAEVIGASDKLIDFTVALDKLDKIGEDGVKKEMIEKGISEDAITKVQPLFNFTGTTTEKLAQLAQLLADSQEGMKGVEELRFICENVINLGLSTAELDLDVTLARGLNYYTGAIFEVSAPKGVAMGSIGGGGRYDDLTGIFGLKNMSGVGISFGLDRIYLVVEELNLFPQTVTVSTKALFINYGEKESFYAMNAIKQLRAAGIKVELYPDNAKVGKQFQHADKRFIPFAVIAAEDEMSQGKYALKNLATGEQNLLDLEELKAALK
>CP020918.1|AWG23504.1|4607983_4608661_+|hypothetical-protein
MEQTGLIIDKPEVPRTFHQLGILVLDGSGSMNATGRGQLTKAQEVEMGVKELFTRFDGSSKKSNFSFSCIKFDTSSTTTLQPTPFQEIDYFSENFNPLDGKGRGTHIFEALNEAKKMAEEFLNNAPQDGLRHSVVILLMSDGLCFQPETTIAVADNIKLNPSVVIASAYFAELGNSDNEATEIKNLLQNVSTNPVKYYATVYDGEALRKFFESSISQSAGIGKIN
>CP020918.1|AWG23505.1|4608670_4609522_+|hypothetical-protein
MNSYIITKSITPKIKNEDYIESFKNEKLGIKGFIVGDGIGSHFKPSEGSEFCVKTLKSYIENCSAIEELNLTHFYTKVYNDLKNEFTDNEKDNLEIDKTQSYGTTLICVIELEEKFIISYLGNGSIWHIRGNFYDFSPQRYLPWNAINVLNPHTVEENGKEALYKFIALECTENQLKPSILEISKDNELYGDIILASTDGLFSNDHNPIAKDREGNLWISGDKKIELLLSTLKKSLQDNSIEEVNINANIDEYLNQITENKLIDDDTSFGIIIPSKSTTITQE
>CP020918.1|AWG23506.1|4609497_4611567_+|hypothetical-protein
MNNHNTRIVLKTIQISTSLSTNLLSEFQNVQTIEIENKPFAEGAFGEVYVCLKVNGQKPSVPQVIKLFKEDSQNKQDHNYNTIRKLQQKIDVKNQQLKQNSGKIITDSYPALKGLPQFSFEGNINGKLYRGFASTNLKKIGFEEFIDILDKSYKEYQKISIDKKMLIAFHLASGFKLLQEIFFIHADLKPEAIFINTKSNECAIIDFDSGTITENKDDTPNTWGAPNDWVAPEIWEQLKQIGSGGLQQVKVNLLSDLWSVAVGIHYILTTTHPLFYLNELSPRVTKEYFKKYKWPEIAENEPFFNERNKTQYIPVKNWLQNTLPNSIYKQLYNTVNYGYLNPIQRTTYNEWEKVLSSVQVPPIITQFKSNSKQILLGNELTLEWEIQNSTSVKIDNGIGIVKSSDVISIKPSKNTIYKLMAKNAFDKIEQTLEIEVLPPPKIVEFKSKHQKIGYGNTTQLVWNIENAQNVELNIGGKTEILTNKDERNINPTEHTKYVLIITALDGITKTEKEVTVKVFKKIEIKSFTSDFIFVVQSIPITLTWEVENASKIIIEDDFGKQRDVSNSSNLIEHIKKDCTYRIRCSNDLFNAVSEKISINLVQNKYELDLNGLVPRFDQILPDIGKAINLDRDFIPSLDYEKVLNIQTIDCNLSIDLSNGEIETKIAKKITKPKIIKIIVEKLKSYIQTS
>CP020918.1|AWG23507.1|4611569_4612961_+|hypothetical-protein
MRDFFIWCSGASVEIVKKCDDKEISKYANIGIVVFCVAFLSIFSATYFLSFAFNTEGTNFVWLYLPIGIIWAFIILSLDRAIVSTISKNDSFNIQILKSIPRVALALMIGIVVATPLEFKIFEKEVNNVIISKVEKIVKKDFEKDFQGKLKLWETKVNDEEKSYSEDKRTYEDEITGKKSGIPGKGKRADEYMRNELNSLSKLNIAKDSLTQIRQTIVEADQNISWPDEIDKYKSKNIGVIERVNVLYSLGGTHLAITILFILIELLPLLTKLLSNRGGYDELIISEERNKLHQADVNQLKESELKEEILSLENKKHTQKAKLRVQIEQNLQKEILTELSKAQNEIALKRVEEFRQKNLNNLNLPTIQQPVNKEKLEDKFWLQIGTTDKIEYFFRNGKLRDNELLYSKDGTVSKGLWNFNQTKTELSIELENNKTDFEIVEILTNKLKLKDKDRNDFLEFEKA
>CP020918.1|AWG23508.1|4613277_4613493_+|YqaE/Pmp3-family-membrane-protein
MLLAILIPWLSFFINGKIIRGIVCLILQITIIGWIPAAIWALSSRNSSKMDKKLKQMEKKIIASNISNSKG
>CP020918.1|AWG23509.1|4613689_4614652_-|IS30-family-transposase
MSHLTIEQRYEIATLRSQGFSMSKIGGFIGRDKSVISRELSRNSDQRNNVYKAKLAQSKASIRQHEKAKKIRFTEQIKARVIHLLEEDFSPEQIVGYCSDKNFECVSIETIYQFIWSDKKKGGQHYKHLRTKGKRYAKRGALKGSRGIIKDRVGIENRPLVVEEKQRIGDLEIDLVIGKNHKGALLTINDRASGVLKMAKINSKESQEIQEKLIELLMDWKPILHTITSDNGKEFANHKKVSEILEISYFFANPYCSWERGANENLNGLVRQYFPKKYNFDLITEEEVLRVTNKLNNRPRKRFGFKSPNEIFEQKLKQCA
>CP020918.1|AWG23510.1|4615054_4616296_+|ABC-transporter-permease
MFNLFKENIQIALGSIRTQILRTVLTVIIIAIGITALVGILTVVSALENTISTDFSSMGANTFSIKQYENELRNRRGETRKIINPVISYPDAVAFKNKFHFSLTETSLSFKATSTAEVKFETEKTDPEIAIMGVDEYFLINSGLETSLGRNFTNFDISNNTYSCIVGSDFEKGLLKDVNPIGKTISIRGARFKVVGVLKEKGATFGNNQDLRVLIPIQLARSLFTAPNINYTVSILTQKNEFLNQAIDHAISTMRNIRGLSPVKENNFGIVRSDDLINKILGITKYLGLASWGIGVITILGSSIALMNIMIVSVTERTREIGVRKALGAKKSTVAIQFFIETLLIGQFGGIIGIILGILIGFGIATAMKFDFVIPWLAIFAAFMTSFIVAIISGLYPAIKAATLDPIEALRYE
>CP020918.1|AWG23511.1|4617030_4617906_-|protein-(glutamine-N5)-methyltransferase,-release-factor-specific
MNIRQYRSQFISKLAPLYGEDEAESFFYLILENKRQLQRVDLAMQPDLTFSEEELAVWSQIEGELEEQKPIQYLLGCTSFFGLEFMVNENVLIPRPETEELVDWIVQSQKLPIKKDTEQTEPAKIKILDIGTGSGCIAIALAKNIPNAEVFAIDVSIKALATARKNAENNAVSVTFLEKNILETLDLEQQFDIIVSNPPYVRNLEKAEIKNNVLENEPHLALFVADNDALIFYSKIAQLATKNLNPNGKLFFEINQYLGKEMTELLQKYNFKNIALKKDIYGNDRMMYGEI
>CP020918.1|AWG23512.1|4618020_4619067_+|riboflavin-biosynthesis-protein-RibD
MNTNEKYIQRCIDLAKNGLGTTYPNPMVGCVIVHKNRIIGEGWHKKAGEGHAEVNAVNAVIDKALLTEATIYVSLEPCSHFGKTPPCCDLIIAHKIPNVVVGTVDPNSQVAGSGIKRLIEAGINVTVGVLEDECNELNKRFFTFHQKKRPYIMLKWAETQDGFIAPATRKEQKPVWITGTAARQLVHKWRSDEQAIMVGTQTAIDDNPKLDVRDWTGHAPTRVVLDRHNRIPSSQNLFDGSVKTIVICESTTQKSTENCIFESIDFEKEIPNQIIAVLYKHQIQSLLIEGGRQLLQTFIDSGLWDEALVFTGTPYFTSGIPAPILTHHSVVDQKMIGPDELKKYKYHD

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Crispr_ID: CP020918_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP020918_9

4616891-4616969

Orphan

Consensus_repeat	Method
TAGAATAAAATCTGTGAAAATCTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of CP020918_9

>merge|CP020918|9|4616891-4616969|CRISPRCasFinder
TAGAATAAAATCTGTGAAAATCTGGGGAATCTGTGTTTAACTTACAGAAGGAACTTAGAATAAAATCTGTGGAAATCTG

>CP020918|9|9|4616891-4616969|CRISPRCasFinder
TAGAATAAAATCTGTGAAAATCTG	GGGAATCTGTGTTTAACTTACAGAAGGAACT
TAGAATAAAATCTGTGGAAATCTG

Protein	Signature genes	Signature genes Name	Protein_function
CP020918.1\|AWG23514.1\|4620513_4620921_-\|thioesterase	unknown	unknown	gnl\|CDD\|223894
CP020918.1\|AWG23513.1\|4619059_4619662_+\|haloacid-dehalogenase	unknown	unknown	gnl\|CDD\|319790
CP020918.1\|AWG23508.1\|4613277_4613493_+\|YqaE/Pmp3-family-membrane-protein	unknown	unknown	gnl\|CDD\|376592
CP020918.1\|AWG23505.1\|4608670_4609522_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379325
CP020918.1\|AWG23507.1\|4611569_4612961_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379583
CP020918.1\|AWG23506.1\|4609497_4611567_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|270622
CP020918.1\|AWG23511.1\|4617030_4617906_-\|protein-(glutamine-N5)-methyltransferase,-release-factor-specific	unknown	unknown	gnl\|CDD\|236467
CP020918.1\|AWG23502.1\|4604105_4604681_-\|nucleotide-exchange-factor-GrpE	unknown	unknown	gnl\|CDD\|271355
CP020918.1\|AWG23512.1\|4618020_4619067_+\|riboflavin-biosynthesis-protein-RibD	unknown	unknown	gnl\|CDD\|273015
CP020918.1\|AWG23723.1\|4619863_4620496_+\|YigZ-family-protein	unknown	unknown	gnl\|CDD\|376491
CP020918.1\|AWG23501.1\|4602936_4604058_-\|molecular-chaperone-DnaJ	unknown	unknown	gnl\|CDD\|237660
CP020918.1\|AWG23510.1\|4615054_4616296_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|182528
CP020918.1\|AWG23509.1\|4613689_4614652_-\|IS30-family-transposase	unknown	unknown	gnl\|CDD\|225382
CP020918.1\|AWG23504.1\|4607983_4608661_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238119
CP020918.1\|AWG23503.1\|4605700_4607071_-\|histidine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234586

Protein	Function_ID	Function_description	E-value
CP020918.1\|AWG23514.1\|4620513_4620921_-\|thioesterase	gnl\|CDD\|223894	COG0824, FcbC, Predicted thioesterase [General function prediction only].	3.57598e-43
CP020918.1\|AWG23513.1\|4619059_4619662_+\|haloacid-dehalogenase	gnl\|CDD\|319790	cd02603, HAD_sEH-N_like, N-terminal lipase phosphatase domain of human soluble epoxide hydrolase, Escherichia coli YihX/HAD4 alpha-D-glucose 1-phosphate phosphatase, and related domains, may be inactive. This family includes the N-terminal phosphatase domain of human soluble epoxide hydrolase (sEH). sEH is a bifunctional enzyme with two distinct enzyme activities, the C-terminal domain has epoxide hydrolysis activity and the N-terminal domain (Ntermphos), which belongs to this family, has lipid phosphatase activity. The latter prefers mono-phosphate esters, and lysophosphatidic acids (LPAs) are the best natural substrates found to date. In addition this family includes Gallus gallus sEH and Xenopus sEH which appears to lack phosphatase activity, and Escherichia coli YihX/HAD4 which selectively hydrolyzes alpha-Glucose-1-P, phosphatase, has significant phosphatase activity against pyridoxal phosphate, and has low beta phosphoglucomutase activity. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	5.27957e-36
CP020918.1\|AWG23508.1\|4613277_4613493_+\|YqaE/Pmp3-family-membrane-protein	gnl\|CDD\|376592	pfam01679, Pmp3, Proteolipid membrane potential modulator. Pmp3 is an evolutionarily conserved proteolipid in the plasma membrane which, in S. pombe, is transcriptionally regulated by the Spc1 stress MAPK (mitogen-activated protein kinases) pathway. It functions to modulate the membrane potential, particularly to resist high cellular cation concentration. In eukaryotic organisms, stress-activated mitogen-activated protein kinases play crucial roles in transmitting environmental signals that will regulate gene expression for allowing the cell to adapt to cellular stress. Pmp3-like proteins are highly conserved in bacteria, yeast, nematode and plants.	0.00200181
CP020918.1\|AWG23505.1\|4608670_4609522_+\|hypothetical-protein	gnl\|CDD\|379325	pfam13672, PP2C_2, Protein phosphatase 2C. Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.	4.80643e-06
CP020918.1\|AWG23507.1\|4611569_4612961_+\|hypothetical-protein	gnl\|CDD\|379583	pfam14362, DUF4407, Domain of unknown function (DUF4407). This family of proteins is found in bacteria. Proteins in this family are typically between 366 and 597 amino acids in length. There is a single completely conserved residue R that may be functionally important.	1.14805e-47
CP020918.1\|AWG23506.1\|4609497_4611567_+\|hypothetical-protein	gnl\|CDD\|270622	cd00180, PKc, Catalytic domain of Protein Kinases. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.	4.9343e-08
CP020918.1\|AWG23511.1\|4617030_4617906_-\|protein-(glutamine-N5)-methyltransferase,-release-factor-specific	gnl\|CDD\|236467	PRK09328, PRK09328, N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional.	1.91639e-95
CP020918.1\|AWG23502.1\|4604105_4604681_-\|nucleotide-exchange-factor-GrpE	gnl\|CDD\|271355	cd00446, GrpE, nucleotide exchange factor GrpE. GrpE is the adenine nucleotide exchange factor of DnaK (Hsp70)-type ATPases. In bacteria, the DnaK-DnaJ-GrpE (KJE) chaperone system functions at the fulcrum of protein homeostasis. GrpE participates actively in response to heat shock by preventing aggregation of stress-denatured proteins; unfolded proteins initially bind to DnaJ, the J-domain ATPase-activating protein (Hsp40 family), whereupon DnaK hydrolyzes its bound ATP, resulting in a stable complex. The GrpE dimer binds to the ATPase domain of Hsp70 catalyzing the dissociation of ADP, which enables rebinding of ATP, one step in the Hsp70 reaction cycle in protein folding. In eukaryotes, only the mitochondrial Hsp70, not the cytosolic form, is GrpE dependent. Over-expression of Hsp70 molecular chaperones is important in suppressing toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, as well as several polyQ-diseases such as Huntington's disease and ataxias.	2.1081e-35
CP020918.1\|AWG23512.1\|4618020_4619067_+\|riboflavin-biosynthesis-protein-RibD	gnl\|CDD\|273015	TIGR00326, eubact_ribD, riboflavin biosynthesis protein RibD. This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD].	1.21348e-96
CP020918.1\|AWG23723.1\|4619863_4620496_+\|YigZ-family-protein	gnl\|CDD\|376491	pfam01205, UPF0029, Uncharacterized protein family UPF0029.	1.18768e-50
CP020918.1\|AWG23501.1\|4602936_4604058_-\|molecular-chaperone-DnaJ	gnl\|CDD\|237660	PRK14289, PRK14289, molecular chaperone DnaJ.	7.83925e-148
CP020918.1\|AWG23510.1\|4615054_4616296_+\|ABC-transporter-permease	gnl\|CDD\|182528	PRK10535, PRK10535, macrolide ABC transporter ATP-binding protein/permease MacB.	1.63808e-39
CP020918.1\|AWG23509.1\|4613689_4614652_-\|IS30-family-transposase	gnl\|CDD\|225382	COG2826, Tra8, Transposase and inactivated derivatives, IS30 family [DNA replication, recombination, and repair].	2.12179e-84
CP020918.1\|AWG23504.1\|4607983_4608661_+\|hypothetical-protein	gnl\|CDD\|238119	cd00198, vWFA, 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.	6.52312e-10
CP020918.1\|AWG23503.1\|4605700_4607071_-\|histidine--tRNA-ligase	gnl\|CDD\|234586	PRK00037, hisS, histidyl-tRNA synthetase; Reviewed.	4.34269e-142

>CP020918.1|AWG23510.1|4615054_4616296_+|ABC-transporter-permease
MFNLFKENIQIALGSIRTQILRTVLTVIIIAIGITALVGILTVVSALENTISTDFSSMGANTFSIKQYENELRNRRGETRKIINPVISYPDAVAFKNKFHFSLTETSLSFKATSTAEVKFETEKTDPEIAIMGVDEYFLINSGLETSLGRNFTNFDISNNTYSCIVGSDFEKGLLKDVNPIGKTISIRGARFKVVGVLKEKGATFGNNQDLRVLIPIQLARSLFTAPNINYTVSILTQKNEFLNQAIDHAISTMRNIRGLSPVKENNFGIVRSDDLINKILGITKYLGLASWGIGVITILGSSIALMNIMIVSVTERTREIGVRKALGAKKSTVAIQFFIETLLIGQFGGIIGIILGILIGFGIATAMKFDFVIPWLAIFAAFMTSFIVAIISGLYPAIKAATLDPIEALRYE
>CP020918.1|AWG23509.1|4613689_4614652_-|IS30-family-transposase
MSHLTIEQRYEIATLRSQGFSMSKIGGFIGRDKSVISRELSRNSDQRNNVYKAKLAQSKASIRQHEKAKKIRFTEQIKARVIHLLEEDFSPEQIVGYCSDKNFECVSIETIYQFIWSDKKKGGQHYKHLRTKGKRYAKRGALKGSRGIIKDRVGIENRPLVVEEKQRIGDLEIDLVIGKNHKGALLTINDRASGVLKMAKINSKESQEIQEKLIELLMDWKPILHTITSDNGKEFANHKKVSEILEISYFFANPYCSWERGANENLNGLVRQYFPKKYNFDLITEEEVLRVTNKLNNRPRKRFGFKSPNEIFEQKLKQCA
>CP020918.1|AWG23508.1|4613277_4613493_+|YqaE/Pmp3-family-membrane-protein
MLLAILIPWLSFFINGKIIRGIVCLILQITIIGWIPAAIWALSSRNSSKMDKKLKQMEKKIIASNISNSKG
>CP020918.1|AWG23507.1|4611569_4612961_+|hypothetical-protein
MRDFFIWCSGASVEIVKKCDDKEISKYANIGIVVFCVAFLSIFSATYFLSFAFNTEGTNFVWLYLPIGIIWAFIILSLDRAIVSTISKNDSFNIQILKSIPRVALALMIGIVVATPLEFKIFEKEVNNVIISKVEKIVKKDFEKDFQGKLKLWETKVNDEEKSYSEDKRTYEDEITGKKSGIPGKGKRADEYMRNELNSLSKLNIAKDSLTQIRQTIVEADQNISWPDEIDKYKSKNIGVIERVNVLYSLGGTHLAITILFILIELLPLLTKLLSNRGGYDELIISEERNKLHQADVNQLKESELKEEILSLENKKHTQKAKLRVQIEQNLQKEILTELSKAQNEIALKRVEEFRQKNLNNLNLPTIQQPVNKEKLEDKFWLQIGTTDKIEYFFRNGKLRDNELLYSKDGTVSKGLWNFNQTKTELSIELENNKTDFEIVEILTNKLKLKDKDRNDFLEFEKA
>CP020918.1|AWG23506.1|4609497_4611567_+|hypothetical-protein
MNNHNTRIVLKTIQISTSLSTNLLSEFQNVQTIEIENKPFAEGAFGEVYVCLKVNGQKPSVPQVIKLFKEDSQNKQDHNYNTIRKLQQKIDVKNQQLKQNSGKIITDSYPALKGLPQFSFEGNINGKLYRGFASTNLKKIGFEEFIDILDKSYKEYQKISIDKKMLIAFHLASGFKLLQEIFFIHADLKPEAIFINTKSNECAIIDFDSGTITENKDDTPNTWGAPNDWVAPEIWEQLKQIGSGGLQQVKVNLLSDLWSVAVGIHYILTTTHPLFYLNELSPRVTKEYFKKYKWPEIAENEPFFNERNKTQYIPVKNWLQNTLPNSIYKQLYNTVNYGYLNPIQRTTYNEWEKVLSSVQVPPIITQFKSNSKQILLGNELTLEWEIQNSTSVKIDNGIGIVKSSDVISIKPSKNTIYKLMAKNAFDKIEQTLEIEVLPPPKIVEFKSKHQKIGYGNTTQLVWNIENAQNVELNIGGKTEILTNKDERNINPTEHTKYVLIITALDGITKTEKEVTVKVFKKIEIKSFTSDFIFVVQSIPITLTWEVENASKIIIEDDFGKQRDVSNSSNLIEHIKKDCTYRIRCSNDLFNAVSEKISINLVQNKYELDLNGLVPRFDQILPDIGKAINLDRDFIPSLDYEKVLNIQTIDCNLSIDLSNGEIETKIAKKITKPKIIKIIVEKLKSYIQTS
>CP020918.1|AWG23505.1|4608670_4609522_+|hypothetical-protein
MNSYIITKSITPKIKNEDYIESFKNEKLGIKGFIVGDGIGSHFKPSEGSEFCVKTLKSYIENCSAIEELNLTHFYTKVYNDLKNEFTDNEKDNLEIDKTQSYGTTLICVIELEEKFIISYLGNGSIWHIRGNFYDFSPQRYLPWNAINVLNPHTVEENGKEALYKFIALECTENQLKPSILEISKDNELYGDIILASTDGLFSNDHNPIAKDREGNLWISGDKKIELLLSTLKKSLQDNSIEEVNINANIDEYLNQITENKLIDDDTSFGIIIPSKSTTITQE
>CP020918.1|AWG23504.1|4607983_4608661_+|hypothetical-protein
MEQTGLIIDKPEVPRTFHQLGILVLDGSGSMNATGRGQLTKAQEVEMGVKELFTRFDGSSKKSNFSFSCIKFDTSSTTTLQPTPFQEIDYFSENFNPLDGKGRGTHIFEALNEAKKMAEEFLNNAPQDGLRHSVVILLMSDGLCFQPETTIAVADNIKLNPSVVIASAYFAELGNSDNEATEIKNLLQNVSTNPVKYYATVYDGEALRKFFESSISQSAGIGKIN
>CP020918.1|AWG23503.1|4605700_4607071_-|histidine--tRNA-ligase
MASKPSIPKGTRDFSPAEVAKRQYIIQTIKTNFEKFGFQPIETPSFENSETLMGKYGEEGDRLIFKILNSGDYLAKANAGHLEAKDSTKLTASISEKALRYDLTVPFARYVVQHQNEIEFPFKRYQIQPVWRADRPQKGRFREFFQCDADVVGSKSLWQEVELVQLYDAVFTDLGLAGATVKINNRKILSGIAEVIGASDKLIDFTVALDKLDKIGEDGVKKEMIEKGISEDAITKVQPLFNFTGTTTEKLAQLAQLLADSQEGMKGVEELRFICENVINLGLSTAELDLDVTLARGLNYYTGAIFEVSAPKGVAMGSIGGGGRYDDLTGIFGLKNMSGVGISFGLDRIYLVVEELNLFPQTVTVSTKALFINYGEKESFYAMNAIKQLRAAGIKVELYPDNAKVGKQFQHADKRFIPFAVIAAEDEMSQGKYALKNLATGEQNLLDLEELKAALK
>CP020918.1|AWG23502.1|4604105_4604681_-|nucleotide-exchange-factor-GrpE
MFKNVFKNKGNMTTENTEIDQKIEDVTLDNNATEEQVLAEELSVEEQLTKDLANEKDKFLRLFAEFENYKRRTTKERIELFKTANADVVGALLPVLDDFDRAIIEIAKSENEAVTKGVQLIHEKLKNTLNSKGLEVVDVNAGDAFNADFAEAITQIPAPSDDMKGKIVDVLEKGYKLGDKIIRFPKVVIGQ
>CP020918.1|AWG23501.1|4602936_4604058_-|molecular-chaperone-DnaJ
MKKDFYEILGIAKGADAAAIKKGYRKKAIEFHPDKNPGDKTAEEKFKEAAEAYEVLSDPAKKQKYDQYGHQAFDGSGGFGGGGGHGGMNMDDIFSQFGDIFGGGGFGGFGGGGSRGPQRVKGSNLRIKVKLTLEEIANGVEKKVKVKRKVQAPGVSYKTCSTCNGQGQVMRVTNTILGRMQSASTCPTCGGAGQQLDKKPAEADAQGMIQEDETVSIKIPAGVVDGMQLKVSSKGNDAPGNSVPGDLIVAIEELEHEFLKREGENLHYDLYISFPEAILGVSKDIEAVNGKVRIKLEDGIQSGKILRLKGKGIPNINGYGNGDLLVHVNVWTPKELNKEQRQFFEKNMDSDNFIPNPEKSDKSFFEKVKDMFS
>CP020918.1|AWG23511.1|4617030_4617906_-|protein-(glutamine-N5)-methyltransferase,-release-factor-specific
MNIRQYRSQFISKLAPLYGEDEAESFFYLILENKRQLQRVDLAMQPDLTFSEEELAVWSQIEGELEEQKPIQYLLGCTSFFGLEFMVNENVLIPRPETEELVDWIVQSQKLPIKKDTEQTEPAKIKILDIGTGSGCIAIALAKNIPNAEVFAIDVSIKALATARKNAENNAVSVTFLEKNILETLDLEQQFDIIVSNPPYVRNLEKAEIKNNVLENEPHLALFVADNDALIFYSKIAQLATKNLNPNGKLFFEINQYLGKEMTELLQKYNFKNIALKKDIYGNDRMMYGEI
>CP020918.1|AWG23512.1|4618020_4619067_+|riboflavin-biosynthesis-protein-RibD
MNTNEKYIQRCIDLAKNGLGTTYPNPMVGCVIVHKNRIIGEGWHKKAGEGHAEVNAVNAVIDKALLTEATIYVSLEPCSHFGKTPPCCDLIIAHKIPNVVVGTVDPNSQVAGSGIKRLIEAGINVTVGVLEDECNELNKRFFTFHQKKRPYIMLKWAETQDGFIAPATRKEQKPVWITGTAARQLVHKWRSDEQAIMVGTQTAIDDNPKLDVRDWTGHAPTRVVLDRHNRIPSSQNLFDGSVKTIVICESTTQKSTENCIFESIDFEKEIPNQIIAVLYKHQIQSLLIEGGRQLLQTFIDSGLWDEALVFTGTPYFTSGIPAPILTHHSVVDQKMIGPDELKKYKYHD
>CP020918.1|AWG23513.1|4619059_4619662_+|haloacid-dehalogenase
MIEAIVFDFGDVFINLDKPATFDGLKKLGATEWNHDLDQLNQQFEMGKISEDDFLSGIQKHCNNATIPEIKKTWNAILADFPLYRLEFLQMLSQKYRLFLLSNTDAIHIARFQKKVGETFYNDFYHCFEHVYFSFEVGMRKPNIEIYEHVLNNHSLEANKTLFVDDKLENTEAAKSIGMHVWNLQVGKEDVVDLFEKNIL
>CP020918.1|AWG23723.1|4619863_4620496_+|YigZ-family-protein
MNINDTYKTIAAPTEETLFKEKSSKFFGYAFPMENEEEVKPIIEGIRKIHSAARHICYAYQIGTETVQYRANDDGEPSNTAGAPIYGQIQSFGLTNVIVIVVRYFGGVKLGVGGLISAYKTSAQLTLESADVIEKTIDVHYILSFDYQNMNKAMRVIKEKKLEIVTQEMEMDPDTTLPIGKIEIKTRKKNAEIIFDTFLNLYEIDIKIKE
>CP020918.1|AWG23514.1|4620513_4620921_-|thioesterase
MKEFEFEVRVRYSETDQMGVVYHGNYAQYFEMGRVEWLRKMGVSYKKMEEEGVMLPVVSLTTNFKKPARYDDLLTIKTVFKSQTSVKIEFEYEIHNEAKELLTIGSSVLVFVNMKTGRPTVPPDYIKECLASISK

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	KX961631	Bacillus phage QCM11, complete genome	22256-22284	4	0.862
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NC_031015	Bacillus phage Claudi, complete genome	23366-23394	4	0.862
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	MT777452	Bacillus phage Baseball_field, complete genome	23878-23906	4	0.862
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NC_049963	Bacillus phage Juan, complete genome	21894-21922	4	0.862
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NC_031121	Bacillus phage Aurora, complete genome	22575-22603	4	0.862
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NC_049962	Bacillus phage SerPounce, complete genome	23206-23234	4	0.862
CP020918_7	7.31\|4045021\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4045021-4045050	30	NZ_CP016481	Synechococcus sp. PCC 7117 plasmid unnamed4, complete sequence	27121-27150	4	0.867
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	NC_029026	Enterococcus phage EFLK1, complete genome	25171-25200	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	MK268686	Enterococcus phage vB_EfaH_EF1TV, complete genome	295-324	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	MK268686	Enterococcus phage vB_EfaH_EF1TV, complete genome	141891-141920	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	AP018715	Enterococcus phage phiM1EF22 DNA, complete sequence	104780-104809	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	MK721192	Enterococcus phage vB_EfaM_Ef2.3, complete genome	285-314	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	MK721192	Enterococcus phage vB_EfaM_Ef2.3, complete genome	143356-143385	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	CAJDJZ010000002	Enterococcus phage vB_EfaH_149 genome assembly, contig: phage149-genome, whole genome shotgun sequence	105860-105889	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	AP018714	Enterococcus phage phiEF17H DNA, complete sequence	108053-108082	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	NC_009904	Enterococcus phage phiEF24C, complete genome	102310-102339	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	AP009390	Enterococcus phage phiEF24C DNA, complete genome	102310-102339	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	CAJDJY010000002	Enterococcus phage 156 genome assembly, contig: phage156-genome, whole genome shotgun sequence	105730-105759	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	MN854830	Enterococcus phage PBEF129, complete genome	295-324	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	MN854830	Enterococcus phage PBEF129, complete genome	141815-141844	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	AB609718	Enterococcus phage phiEF24C-P2 DNA, complete genome	102310-102339	5	0.833
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	LR031359	Enterococcus phage 156, complete genome	105730-105759	5	0.833
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	MN693136	Marine virus AFVG_25M110, complete genome	20716-20744	5	0.828
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	MN698246	Pelagibacter phage HTVC112P, complete genome	12868-12896	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP039193	Piscirickettsia salmonis strain Psal-160 plasmid unnamed3, complete sequence	1827-1855	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP039211	Piscirickettsia salmonis strain Psal-103 plasmid unnamed2, complete sequence	31252-31280	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP048068	Piscirickettsia salmonis strain Ps-8079A plasmid Ps8079A-p2, complete sequence	12869-12897	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP048068	Piscirickettsia salmonis strain Ps-8079A plasmid Ps8079A-p2, complete sequence	71368-71396	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038895	Piscirickettsia salmonis strain Psal-006a plasmid unnamed2, complete sequence	26936-26964	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038925	Piscirickettsia salmonis strain Psal-011 plasmid unnamed2, complete sequence	1827-1855	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038954	Piscirickettsia salmonis strain Psal-040 plasmid unnamed2, complete sequence	1707-1735	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038959	Piscirickettsia salmonis strain Psal-041 plasmid unnamed2, complete sequence	1707-1735	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP039198	Piscirickettsia salmonis strain Psal-161 plasmid unnamed3, complete sequence	1827-1855	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038813	Piscirickettsia salmonis strain Psal-001 plasmid unnamed2, complete sequence	1827-1855	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP013770	Piscirickettsia salmonis strain PM23019A plasmid p2PS3, complete sequence	13799-13827	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP033943	Piscirickettsia salmonis strain EM-90 plasmid pPSEM90-6, complete sequence	78936-78964	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP013765	Piscirickettsia salmonis strain PM21567A plasmid p3PS2, complete sequence	20271-20299	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP013759	Piscirickettsia salmonis strain AY6492A plasmid p2PS1, complete sequence	31490-31518	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP013776	Piscirickettsia salmonis strain PM37984A plasmid p3PS4, complete sequence	8448-8476	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP013780	Piscirickettsia salmonis strain PM51819A plasmid p2PS5, complete sequence	92652-92680	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP050941	Piscirickettsia salmonis strain Ps-2192A plasmid Ps2192A-p3, complete sequence	33465-33493	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038915	Piscirickettsia salmonis strain Psal-010a plasmid unnamed2, complete sequence	1827-1855	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP039207	Piscirickettsia salmonis strain Psal-182 plasmid unnamed3, complete sequence	1827-1855	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP039043	Piscirickettsia salmonis strain Psal-072 plasmid unnamed3, complete sequence	1707-1735	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038949	Piscirickettsia salmonis strain Psal-028 plasmid unnamed2, complete sequence	1707-1735	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038934	Piscirickettsia salmonis strain Psal-025 plasmid unnamed2, complete sequence	1827-1855	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038974	Piscirickettsia salmonis strain Psal-069 plasmid unnamed2, complete sequence	15253-15281	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP012414	Piscirickettsia salmonis strain PM15972A1 plasmid pPSA1-1, complete sequence	31298-31326	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP039037	Piscirickettsia salmonis strain Psal-071 plasmid unnamed2, complete sequence	1707-1735	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP039068	Piscirickettsia salmonis strain Psal-107 plasmid unnamed3, complete sequence	1827-1855	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038888	Piscirickettsia salmonis strain Psal-004 plasmid unnamed2, complete sequence	1827-1855	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP039216	Piscirickettsia salmonis strain Psal-104a plasmid unnamed2, complete sequence	16464-16492	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038910	Piscirickettsia salmonis strain Psal-009 plasmid unnamed2, complete sequence	1707-1735	5	0.828
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NZ_CP038878	Piscirickettsia salmonis strain Psal-002 plasmid unnamed2, complete sequence	1827-1855	5	0.828
CP020918_7	7.4\|4042978\|29\|CP020918\|CRISPRCasFinder	4042978-4043006	29	NZ_CP007544	Synechocystis sp. PCC 6714 plasmid pSYLB, complete sequence	63573-63601	6	0.793
CP020918_7	7.4\|4042978\|29\|CP020918\|CRISPRCasFinder	4042978-4043006	29	NZ_AP022840	Legionella sp. TUM19329 plasmid pTUM19329-1	100131-100159	6	0.793
CP020918_7	7.6\|4043129\|30\|CP020918\|CRISPRCasFinder	4043129-4043158	30	MT630433	Bacteroides phage vB_BfrS_23, complete genome	27367-27396	6	0.8
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	NZ_CP013238	Clostridium butyricum strain CDC_51208 plasmid pNPD4_2, complete sequence	401493-401522	6	0.8
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NZ_CP015507	Bacillus oceanisediminis 2691 plasmid pBO1, complete sequence	203777-203805	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NZ_CP031836	Lactobacillus amylolyticus strain L5 plasmid p1, complete sequence	12872-12900	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NZ_CP020458	Lactobacillus amylolyticus strain L6 plasmid pL6-1, complete sequence	12872-12900	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NC_022877	Bacillus thuringiensis YBT-1518 plasmid pBMB0232, complete sequence	163620-163648	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NC_022882	Bacillus thuringiensis YBT-1518 plasmid pBMB0233, complete sequence	68493-68521	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	MN693565	Marine virus AFVG_25M347, complete genome	12572-12600	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	MN698242	Pelagibacter phage HTVC103P, complete genome	11779-11807	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	MN698243	Pelagibacter phage HTVC104P, complete genome	12280-12308	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	AP013489	Uncultured Mediterranean phage uvMED DNA, complete genome, group G19, isolate: uvMED-CGR-C30A-MedDCM-OCT-S45-C81	9329-9357	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	AP013762	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C30-MedDCM-OCT-S40-C264, * SEQUENCING IN PROGRESS *	3815-3843	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	MN698245	Pelagibacter phage HTVC111P, complete genome	11278-11306	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	AP013487	Uncultured Mediterranean phage uvMED DNA, complete genome, group G19, isolate: uvMED-CGR-C30A-MedDCM-OCT-S33-C83	25685-25713	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	AP014258	Uncultured Mediterranean phage uvMED isolate uvMED-GF-U-MedDCM-OCT-S27-C55, * SEQUENCING IN PROGRESS *	18615-18643	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	AP013488	Uncultured Mediterranean phage uvMED DNA, complete genome, group G19, isolate: uvMED-CGR-C30A-MedDCM-OCT-S38-C82	23983-24011	6	0.793
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	AP013486	Uncultured Mediterranean phage uvMED DNA, complete genome, group G19, isolate: uvMED-CGR-C30A-MedDCM-OCT-S29-C73	2716-2744	6	0.793
CP020918_7	7.19\|4044114\|30\|CP020918\|CRISPRCasFinder	4044114-4044143	30	AJ630128	Bacteriophage S-PM2 complete genome	192369-192398	6	0.8
CP020918_7	7.19\|4044114\|30\|CP020918\|CRISPRCasFinder	4044114-4044143	30	NC_006820	Synechococcus phage S-PM2, complete genome	192369-192398	6	0.8
CP020918_7	7.19\|4044114\|30\|CP020918\|CRISPRCasFinder	4044114-4044143	30	LN828717	Synechococcus phage S-PM2 spontaneous deletion mutant, complete genome	182825-182854	6	0.8
CP020918_7	7.23\|4044416\|30\|CP020918\|CRISPRCasFinder	4044416-4044445	30	AJ630128	Bacteriophage S-PM2 complete genome	192369-192398	6	0.8
CP020918_7	7.23\|4044416\|30\|CP020918\|CRISPRCasFinder	4044416-4044445	30	NC_006820	Synechococcus phage S-PM2, complete genome	192369-192398	6	0.8
CP020918_7	7.23\|4044416\|30\|CP020918\|CRISPRCasFinder	4044416-4044445	30	LN828717	Synechococcus phage S-PM2 spontaneous deletion mutant, complete genome	182825-182854	6	0.8
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	MN693924	Marine virus AFVG_250M1079, complete genome	2710-2738	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	MN693947	Marine virus AFVG_250M1078, complete genome	2701-2729	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	MN694660	Marine virus AFVG_250M1077, complete genome	37667-37695	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NC_002118	Coxiella burnetii plasmid QpH1, complete sequence	34777-34805	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NC_002131	Coxiella burnetii strain R1140 plasmid QpDV, complete sequence	30054-30082	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NC_009726	Coxiella burnetii Dugway 5J108-111 plasmid pQpDG, complete sequence	1507-1535	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NC_005915	Caedibacter taeniospiralis plasmid pKAP298, complete sequence	25713-25741	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NZ_CP013668	Coxiella burnetii strain 3262 plasmid QpH1, complete sequence	1505-1533	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NZ_CP020617	Coxiella burnetii strain RSA 439 plasmid, complete sequence	1507-1535	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NZ_CP035111	Coxiella burnetii strain nine mile phase II plasmid unnamed, complete sequence	9687-9715	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NZ_CP040060	Coxiella burnetii strain RSA439 plasmid pQpH1, complete sequence	24384-24412	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NC_010115	Coxiella burnetii RSA 331 plasmid QpH1, complete sequence	27859-27887	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	LN833191	Coxiella burnetii Cb175_Guyana plasmid QpH1, complete sequence	1507-1535	6	0.793
CP020918_7	7.24\|4044492\|29\|CP020918\|CRISPRCasFinder	4044492-4044520	29	NC_004704	Coxiella burnetii RSA 493 plasmid pQpH1, complete sequence	1507-1535	6	0.793
CP020918_7	7.31\|4045021\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4045021-4045050	30	NZ_CP016869	Legionella pneumophila subsp. pneumophila strain FFI102 plasmid, complete sequence	66537-66566	6	0.8
CP020918_7	7.31\|4045021\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4045021-4045050	30	NC_011256	Borrelia duttonii Ly plasmid pl70, complete sequence	49031-49060	6	0.8
CP020918_7	7.31\|4045021\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4045021-4045050	30	NZ_CP016871	Legionella pneumophila subsp. pneumophila strain FFI103 plasmid, complete sequence	24343-24372	6	0.8
CP020918_7	7.31\|4045021\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4045021-4045050	30	NZ_CP016875	Legionella pneumophila subsp. pneumophila strain FFI329 plasmid, complete sequence	10617-10646	6	0.8
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	KJ801817	Enterococcus phage ECP3, complete genome	135191-135220	7	0.767
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	MK693030	Enterococcus phage vB_EfaM_Ef2.1, complete genome	277-306	7	0.767
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	MK693030	Enterococcus phage vB_EfaM_Ef2.1, complete genome	138880-138909	7	0.767
CP020918_7	7.3\|4042902\|30\|CP020918\|CRISPRCasFinder	4042902-4042931	30	MN693698	Marine virus AFVG_250M751, complete genome	27728-27757	7	0.767
CP020918_7	7.8\|4043281\|30\|CP020918\|CRISPRCasFinder	4043281-4043310	30	MN693961	Marine virus AFVG_250M531, complete genome	1315-1344	7	0.767
CP020918_7	7.9\|4043357\|30\|CP020918\|CRISPRCasFinder	4043357-4043386	30	MN693961	Marine virus AFVG_250M531, complete genome	1315-1344	7	0.767
CP020918_7	7.10\|4043433\|30\|CP020918\|CRISPRCasFinder	4043433-4043462	30	MH791397	UNVERIFIED: Enterococcus phage EfsSzw-1, complete genome	124766-124795	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	NZ_CP021878	Enterococcus wangshanyuanii strain MN05 plasmid unnamed5	33161-33190	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	KR709302	Staphylococcus phage 55-2, complete genome	1591-1620	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	MN694566	Marine virus AFVG_250M779, complete genome	28579-28608	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	KY963369	Bacillus phage Tavor_SA, complete genome	31268-31297	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	KR709303	Staphylococcus phage 55-3, complete genome	1591-1620	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	AY954955	Bacteriophage 42e, complete genome	29788-29817	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	MK211557	Staphylococcus phage Henu2, complete genome	14877-14906	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	NC_007052	Staphylococcus phage 42e, complete genome	29788-29817	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	NZ_LR135180	Enterococcus faecium isolate E0595 plasmid 2	8940-8969	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	NZ_LR132068	Enterococcus faecium isolate E0139 plasmid 2	8940-8969	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	NZ_CP037956	Enterococcus hirae strain CQP3-9 plasmid pCQP3-9_1, complete sequence	43652-43681	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	NC_017543	Paenibacillus polymyxa M1 plasmid pPPM1a, complete sequence	303983-304012	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	GU080336	Sulfolobus turreted icosahedral virus 2, complete genome	11667-11696	7	0.767
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	MN694296	Marine virus AFVG_250M539, complete genome	41321-41350	7	0.767
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	MT740314	Escherichia phage JEP1, complete genome	85866-85894	7	0.759
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NC_003042	Clostridium perfringens str. 13 plasmid pCP13, complete sequence	12914-12942	7	0.759
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	MN693558	Marine virus AFVG_25M213, complete genome	12167-12195	7	0.759
CP020918_7	7.19\|4044114\|30\|CP020918\|CRISPRCasFinder	4044114-4044143	30	MK250029	Prevotella phage Lak-C1, complete genome	79702-79731	7	0.767
CP020918_7	7.19\|4044114\|30\|CP020918\|CRISPRCasFinder	4044114-4044143	30	MK250016	Prevotella phage Lak-A1, complete genome	101966-101995	7	0.767
CP020918_7	7.23\|4044416\|30\|CP020918\|CRISPRCasFinder	4044416-4044445	30	MK250029	Prevotella phage Lak-C1, complete genome	79702-79731	7	0.767
CP020918_7	7.23\|4044416\|30\|CP020918\|CRISPRCasFinder	4044416-4044445	30	MK250016	Prevotella phage Lak-A1, complete genome	101966-101995	7	0.767
CP020918_7	7.29\|4044869\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4044869-4044898	30	MK250016	Prevotella phage Lak-A1, complete genome	365329-365358	7	0.767
CP020918_7	7.29\|4044869\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4044869-4044898	30	MN693440	Marine virus AFVG_25M540, complete genome	13097-13126	7	0.767
CP020918_7	7.1\|4042750\|30\|CP020918\|CRISPRCasFinder	4042750-4042779	30	NC_019521	Sphingomonas phage PAU, complete genome	6089-6118	8	0.733
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	NZ_LR214986	Mycoplasma cynos strain NCTC10142 plasmid 13	461753-461782	8	0.733
CP020918_7	7.13\|4043661\|30\|CP020918\|CRISPRCasFinder	4043661-4043690	30	MN693989	Marine virus AFVG_250M851, complete genome	19881-19910	8	0.733
CP020918_7	7.15\|4043813\|29\|CP020918\|CRISPRCasFinder	4043813-4043841	29	NC_029119	Staphylococcus phage SPbeta-like, complete genome	13037-13065	8	0.724
CP020918_7	7.18\|4044039\|29\|CP020918\|CRISPRCasFinder	4044039-4044067	29	NZ_CP054029	Rhizobium sp. JKLM19E plasmid pPR19E02, complete sequence	145367-145395	8	0.724
CP020918_7	7.19\|4044114\|30\|CP020918\|CRISPRCasFinder	4044114-4044143	30	MH319759	Marine virus AG-345-O18 Ga0172273_13 genomic sequence	20549-20578	8	0.733
CP020918_7	7.19\|4044114\|30\|CP020918\|CRISPRCasFinder	4044114-4044143	30	AP013385	Uncultured Mediterranean phage uvMED DNA, complete genome, group G15, isolate: uvMED-CGR-C16-MedDCM-OCT-S39-C44	17319-17348	8	0.733
CP020918_7	7.19\|4044114\|30\|CP020918\|CRISPRCasFinder	4044114-4044143	30	KC821624	Cellulophaga phage phi14:2, complete genome	15433-15462	8	0.733
CP020918_7	7.20\|4044190\|30\|CP020918\|CRISPRCasFinder	4044190-4044219	30	NZ_CP012953	Acinetobacter baumannii strain D36 plasmid pD36-1 clone GC1, complete sequence	83-112	8	0.733
CP020918_7	7.20\|4044190\|30\|CP020918\|CRISPRCasFinder	4044190-4044219	30	NZ_CP021374	Rhizobium sp. ACO-34A plasmid pRACO34Ab, complete sequence	260898-260927	8	0.733
CP020918_7	7.22\|4044341\|29\|CP020918\|CRISPRCasFinder	4044341-4044369	29	NZ_CP054029	Rhizobium sp. JKLM19E plasmid pPR19E02, complete sequence	145367-145395	8	0.724
CP020918_7	7.23\|4044416\|30\|CP020918\|CRISPRCasFinder	4044416-4044445	30	MH319759	Marine virus AG-345-O18 Ga0172273_13 genomic sequence	20549-20578	8	0.733
CP020918_7	7.23\|4044416\|30\|CP020918\|CRISPRCasFinder	4044416-4044445	30	AP013385	Uncultured Mediterranean phage uvMED DNA, complete genome, group G15, isolate: uvMED-CGR-C16-MedDCM-OCT-S39-C44	17319-17348	8	0.733
CP020918_7	7.23\|4044416\|30\|CP020918\|CRISPRCasFinder	4044416-4044445	30	KC821624	Cellulophaga phage phi14:2, complete genome	15433-15462	8	0.733
CP020918_7	7.25\|4044567\|29\|CP020918\|CRISPRCasFinder,PILER-CR	4044567-4044595	29	NC_018878	Bacillus thuringiensis Bt407 plasmid BTB_502p, complete sequence	170988-171016	8	0.724
CP020918_7	7.26\|4044642\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4044642-4044671	30	KC821618	Cellulophaga phage phi10:1, complete genome	26384-26413	8	0.733
CP020918_7	7.29\|4044869\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4044869-4044898	30	NZ_CP018748	Borreliella garinii strain CIP 103362 isolate 20047 plasmid unnamed3	18942-18971	8	0.733
CP020918_7	7.29\|4044869\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4044869-4044898	30	NZ_CP028868	Borreliella garinii strain 20047 plasmid cp32-6, complete sequence	18993-19022	8	0.733
CP020918_7	7.5\|4043053\|30\|CP020918\|CRISPRCasFinder	4043053-4043082	30	NZ_CP026117	Lactobacillus curvatus JCM 1096 = DSM 20019 plasmid pLDW-27, complete sequence	5181-5210	9	0.7
CP020918_7	7.16\|4043888\|30\|CP020918\|CRISPRCasFinder	4043888-4043917	30	NZ_CP009059	Borreliella afzelii K78 plasmid lp54, complete sequence	49776-49805	9	0.7
CP020918_7	7.16\|4043888\|30\|CP020918\|CRISPRCasFinder	4043888-4043917	30	NC_017241	Borreliella afzelii PKo plasmid lp54, complete sequence	49634-49663	9	0.7
CP020918_7	7.16\|4043888\|30\|CP020918\|CRISPRCasFinder	4043888-4043917	30	NZ_CP009214	Borreliella afzelii Tom3107 plasmid lp54, complete sequence	8487-8516	9	0.7
CP020918_7	7.26\|4044642\|30\|CP020918\|CRISPRCasFinder,PILER-CR	4044642-4044671	30	MN694255	Marine virus AFVG_250M362, complete genome	46917-46946	9	0.7

1. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to KX961631 (Bacillus phage QCM11, complete genome) position: , mismatch: 4, identity: 0.862

tcagc-agttattttatttaatgcttcatt	CRISPR spacer
-caccaagttattttatctaattcttcatt	Protospacer
 ** * ***********.**** *******

2. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NC_031015 (Bacillus phage Claudi, complete genome) position: , mismatch: 4, identity: 0.862

tcagc-agttattttatttaatgcttcatt	CRISPR spacer
-caccaagttattttatctaattcttcatt	Protospacer
 ** * ***********.**** *******

3. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to MT777452 (Bacillus phage Baseball_field, complete genome) position: , mismatch: 4, identity: 0.862

tcagc-agttattttatttaatgcttcatt	CRISPR spacer
-caccaagttattttatctaattcttcatt	Protospacer
 ** * ***********.**** *******

4. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NC_049963 (Bacillus phage Juan, complete genome) position: , mismatch: 4, identity: 0.862

tcagc-agttattttatttaatgcttcatt	CRISPR spacer
-caccaagttattttatctaattcttcatt	Protospacer
 ** * ***********.**** *******

5. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NC_031121 (Bacillus phage Aurora, complete genome) position: , mismatch: 4, identity: 0.862

tcagc-agttattttatttaatgcttcatt	CRISPR spacer
-caccaagttattttatctaattcttcatt	Protospacer
 ** * ***********.**** *******

6. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NC_049962 (Bacillus phage SerPounce, complete genome) position: , mismatch: 4, identity: 0.862

tcagc-agttattttatttaatgcttcatt	CRISPR spacer
-caccaagttattttatctaattcttcatt	Protospacer
 ** * ***********.**** *******

7. spacer 7.31|4045021|30|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP016481 (Synechococcus sp. PCC 7117 plasmid unnamed4, complete sequence) position: , mismatch: 4, identity: 0.867

-atattgcactaaattcaatggctaaaatta	CRISPR spacer
tatcttgc-ttaaattcaaaggctaaaatta	Protospacer
 ** **** .********* ***********

8. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to NC_029026 (Enterococcus phage EFLK1, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

9. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to MK268686 (Enterococcus phage vB_EfaH_EF1TV, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

10. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to MK268686 (Enterococcus phage vB_EfaH_EF1TV, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

11. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to AP018715 (Enterococcus phage phiM1EF22 DNA, complete sequence) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

12. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to MK721192 (Enterococcus phage vB_EfaM_Ef2.3, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

13. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to MK721192 (Enterococcus phage vB_EfaM_Ef2.3, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

14. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to CAJDJZ010000002 (Enterococcus phage vB_EfaH_149 genome assembly, contig: phage149-genome, whole genome shotgun sequence) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

15. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to AP018714 (Enterococcus phage phiEF17H DNA, complete sequence) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

16. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to NC_009904 (Enterococcus phage phiEF24C, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

17. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to AP009390 (Enterococcus phage phiEF24C DNA, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

18. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to CAJDJY010000002 (Enterococcus phage 156 genome assembly, contig: phage156-genome, whole genome shotgun sequence) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

19. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to MN854830 (Enterococcus phage PBEF129, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

20. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to MN854830 (Enterococcus phage PBEF129, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

21. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to AB609718 (Enterococcus phage phiEF24C-P2 DNA, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

22. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to LR031359 (Enterococcus phage 156, complete genome) position: , mismatch: 5, identity: 0.833

gtattctgatatatgtataaat---ccatgatt	CRISPR spacer
gtattctaatatatgtataaatagcctatg---	Protospacer
*******.**************   *.***

23. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to MN693136 (Marine virus AFVG_25M110, complete genome) position: , mismatch: 5, identity: 0.828

tcagcagttattttatttaatgcttcatt	CRISPR spacer
gcagcaggtaatttatttaatgcttctct	Protospacer
 ****** ** *************** .*

24. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to MN698246 (Pelagibacter phage HTVC112P, complete genome) position: , mismatch: 5, identity: 0.828

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccagcagttattttatataatgctaaatc	Protospacer
.*************** *******  **.

25. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP039193 (Piscirickettsia salmonis strain Psal-160 plasmid unnamed3, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

26. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP039211 (Piscirickettsia salmonis strain Psal-103 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

27. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP048068 (Piscirickettsia salmonis strain Ps-8079A plasmid Ps8079A-p2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

28. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP048068 (Piscirickettsia salmonis strain Ps-8079A plasmid Ps8079A-p2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

29. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038895 (Piscirickettsia salmonis strain Psal-006a plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

30. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038925 (Piscirickettsia salmonis strain Psal-011 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

31. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038954 (Piscirickettsia salmonis strain Psal-040 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

32. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038959 (Piscirickettsia salmonis strain Psal-041 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

33. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP039198 (Piscirickettsia salmonis strain Psal-161 plasmid unnamed3, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

34. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038813 (Piscirickettsia salmonis strain Psal-001 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

35. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP013770 (Piscirickettsia salmonis strain PM23019A plasmid p2PS3, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

36. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP033943 (Piscirickettsia salmonis strain EM-90 plasmid pPSEM90-6, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

37. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP013765 (Piscirickettsia salmonis strain PM21567A plasmid p3PS2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

38. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP013759 (Piscirickettsia salmonis strain AY6492A plasmid p2PS1, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

39. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP013776 (Piscirickettsia salmonis strain PM37984A plasmid p3PS4, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

40. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP013780 (Piscirickettsia salmonis strain PM51819A plasmid p2PS5, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

41. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP050941 (Piscirickettsia salmonis strain Ps-2192A plasmid Ps2192A-p3, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

42. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038915 (Piscirickettsia salmonis strain Psal-010a plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

43. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP039207 (Piscirickettsia salmonis strain Psal-182 plasmid unnamed3, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

44. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP039043 (Piscirickettsia salmonis strain Psal-072 plasmid unnamed3, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

45. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038949 (Piscirickettsia salmonis strain Psal-028 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

46. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038934 (Piscirickettsia salmonis strain Psal-025 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

47. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038974 (Piscirickettsia salmonis strain Psal-069 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

48. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP012414 (Piscirickettsia salmonis strain PM15972A1 plasmid pPSA1-1, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

49. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP039037 (Piscirickettsia salmonis strain Psal-071 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

50. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP039068 (Piscirickettsia salmonis strain Psal-107 plasmid unnamed3, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

51. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038888 (Piscirickettsia salmonis strain Psal-004 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

52. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP039216 (Piscirickettsia salmonis strain Psal-104a plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

53. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038910 (Piscirickettsia salmonis strain Psal-009 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

54. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP038878 (Piscirickettsia salmonis strain Psal-002 plasmid unnamed2, complete sequence) position: , mismatch: 5, identity: 0.828

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
aaagaaaagaattatgtcatgaggtatga	Protospacer
* ***************** ***. **.*

55. spacer 7.4|4042978|29|CP020918|CRISPRCasFinder matches to NZ_CP007544 (Synechocystis sp. PCC 6714 plasmid pSYLB, complete sequence) position: , mismatch: 6, identity: 0.793

agtaaatgaatccttaacagtatcaattg	CRISPR spacer
agaaaatgaatccttaacagaatggtttt	Protospacer
** ***************** ** . **

56. spacer 7.4|4042978|29|CP020918|CRISPRCasFinder matches to NZ_AP022840 (Legionella sp. TUM19329 plasmid pTUM19329-1) position: , mismatch: 6, identity: 0.793

agtaaatgaatccttaacagtatcaattg	CRISPR spacer
atcatatgaatctttaactgtatcaattc	Protospacer
* .* *******.***** *********

57. spacer 7.6|4043129|30|CP020918|CRISPRCasFinder matches to MT630433 (Bacteroides phage vB_BfrS_23, complete genome) position: , mismatch: 6, identity: 0.8

ctaaagttaatcgtatattccgataatttt	CRISPR spacer
ttaaagttattcgtttattccgatcgcttt	Protospacer
.******** **** ********* ..***

58. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to NZ_CP013238 (Clostridium butyricum strain CDC_51208 plasmid pNPD4_2, complete sequence) position: , mismatch: 6, identity: 0.8

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
tttaataaagaagaagaacgtataaaatct	Protospacer
**. ************** ***.**** *

59. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NZ_CP015507 (Bacillus oceanisediminis 2691 plasmid pBO1, complete sequence) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
tcagcagttattttatttatttctctttc	Protospacer
******************* * **.. *.

60. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NZ_CP031836 (Lactobacillus amylolyticus strain L5 plasmid p1, complete sequence) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
tcagcagtttttttatttaaagctagcta	Protospacer
********* ********** ***   *

61. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NZ_CP020458 (Lactobacillus amylolyticus strain L6 plasmid pL6-1, complete sequence) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
tcagcagtttttttatttaaagctagcta	Protospacer
********* ********** ***   *

62. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NC_022877 (Bacillus thuringiensis YBT-1518 plasmid pBMB0232, complete sequence) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
aaaacagttattttatttgatgcttctat	Protospacer
  *.**************.*******  *

63. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NC_022882 (Bacillus thuringiensis YBT-1518 plasmid pBMB0233, complete sequence) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
aaaacagttattttatttgatgcttctat	Protospacer
  *.**************.*******  *

64. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to MN693565 (Marine virus AFVG_25M347, complete genome) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccataagttattttatttaattcttcaaa	Protospacer
.**  **************** *****

65. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to MN698242 (Pelagibacter phage HTVC103P, complete genome) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccataagttattttatttaattcttcaaa	Protospacer
.**  **************** *****

66. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to MN698243 (Pelagibacter phage HTVC104P, complete genome) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccataagttattttatttaattcttcaaa	Protospacer
.**  **************** *****

67. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to AP013489 (Uncultured Mediterranean phage uvMED DNA, complete genome, group G19, isolate: uvMED-CGR-C30A-MedDCM-OCT-S45-C81) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccagcagttattttatacaatgctaaatc	Protospacer
.*************** .******  **.

68. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to AP013762 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C30-MedDCM-OCT-S40-C264, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccagcagttattttatacaatgctaaatc	Protospacer
.*************** .******  **.

69. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to MN698245 (Pelagibacter phage HTVC111P, complete genome) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccagcagttattttatacaatgctaaatc	Protospacer
.*************** .******  **.

70. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to AP013487 (Uncultured Mediterranean phage uvMED DNA, complete genome, group G19, isolate: uvMED-CGR-C30A-MedDCM-OCT-S33-C83) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccagcagttattttatacaatgctaaatc	Protospacer
.*************** .******  **.

71. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to AP014258 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-U-MedDCM-OCT-S27-C55, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccagcagttattttatacaatgctaaatc	Protospacer
.*************** .******  **.

72. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to AP013488 (Uncultured Mediterranean phage uvMED DNA, complete genome, group G19, isolate: uvMED-CGR-C30A-MedDCM-OCT-S38-C82) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccagcagttattttatacaatgctaaatc	Protospacer
.*************** .******  **.

73. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to AP013486 (Uncultured Mediterranean phage uvMED DNA, complete genome, group G19, isolate: uvMED-CGR-C30A-MedDCM-OCT-S29-C73) position: , mismatch: 6, identity: 0.793

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccagcagttattttatacaatgctaaatc	Protospacer
.*************** .******  **.

74. spacer 7.19|4044114|30|CP020918|CRISPRCasFinder matches to AJ630128 (Bacteriophage S-PM2 complete genome) position: , mismatch: 6, identity: 0.8

tgataatgaaatactattaatatctgttac	CRISPR spacer
tgataatgaaattctatcaatatctgaatt	Protospacer
************ ****.********   .

75. spacer 7.19|4044114|30|CP020918|CRISPRCasFinder matches to NC_006820 (Synechococcus phage S-PM2, complete genome) position: , mismatch: 6, identity: 0.8

tgataatgaaatactattaatatctgttac	CRISPR spacer
tgataatgaaattctatcaatatctgaatt	Protospacer
************ ****.********   .

76. spacer 7.19|4044114|30|CP020918|CRISPRCasFinder matches to LN828717 (Synechococcus phage S-PM2 spontaneous deletion mutant, complete genome) position: , mismatch: 6, identity: 0.8

tgataatgaaatactattaatatctgttac	CRISPR spacer
tgataatgaaattctatcaatatctgaatt	Protospacer
************ ****.********   .

77. spacer 7.23|4044416|30|CP020918|CRISPRCasFinder matches to AJ630128 (Bacteriophage S-PM2 complete genome) position: , mismatch: 6, identity: 0.8

tgataatgaaatactattaatatctgttac	CRISPR spacer
tgataatgaaattctatcaatatctgaatt	Protospacer
************ ****.********   .

78. spacer 7.23|4044416|30|CP020918|CRISPRCasFinder matches to NC_006820 (Synechococcus phage S-PM2, complete genome) position: , mismatch: 6, identity: 0.8

tgataatgaaatactattaatatctgttac	CRISPR spacer
tgataatgaaattctatcaatatctgaatt	Protospacer
************ ****.********   .

79. spacer 7.23|4044416|30|CP020918|CRISPRCasFinder matches to LN828717 (Synechococcus phage S-PM2 spontaneous deletion mutant, complete genome) position: , mismatch: 6, identity: 0.8

tgataatgaaatactattaatatctgttac	CRISPR spacer
tgataatgaaattctatcaatatctgaatt	Protospacer
************ ****.********   .

80. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to MN693924 (Marine virus AFVG_250M1079, complete genome) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
ttttgttaacaatttcataattttatttt	Protospacer
.* ..** *****.***************

81. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to MN693947 (Marine virus AFVG_250M1078, complete genome) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
ttttgttaacaatttcataattttatttt	Protospacer
.* ..** *****.***************

82. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to MN694660 (Marine virus AFVG_250M1077, complete genome) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
ttttgttaacaatttcataattttatttt	Protospacer
.* ..** *****.***************

83. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NC_002118 (Coxiella burnetii plasmid QpH1, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

84. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NC_002131 (Coxiella burnetii strain R1140 plasmid QpDV, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

85. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NC_009726 (Coxiella burnetii Dugway 5J108-111 plasmid pQpDG, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

86. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NC_005915 (Caedibacter taeniospiralis plasmid pKAP298, complete sequence) position: , mismatch: 6, identity: 0.793

ctaca-tttacaatctcataattttatttt	CRISPR spacer
-ggcattttacaatctcataaccttattta	Protospacer
  .** ***************..******

87. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NZ_CP013668 (Coxiella burnetii strain 3262 plasmid QpH1, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

88. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NZ_CP020617 (Coxiella burnetii strain RSA 439 plasmid, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

89. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NZ_CP035111 (Coxiella burnetii strain nine mile phase II plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

90. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NZ_CP040060 (Coxiella burnetii strain RSA439 plasmid pQpH1, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

91. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NC_010115 (Coxiella burnetii RSA 331 plasmid QpH1, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

92. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to LN833191 (Coxiella burnetii Cb175_Guyana plasmid QpH1, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

93. spacer 7.24|4044492|29|CP020918|CRISPRCasFinder matches to NC_004704 (Coxiella burnetii RSA 493 plasmid pQpH1, complete sequence) position: , mismatch: 6, identity: 0.793

ctacatttacaatctcataattttatttt	CRISPR spacer
gtccatttacaatctcctatttttatctc	Protospacer
 * ************* ** ******.*.

94. spacer 7.31|4045021|30|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP016869 (Legionella pneumophila subsp. pneumophila strain FFI102 plasmid, complete sequence) position: , mismatch: 6, identity: 0.8

----atattgcactaaattcaatggctaaaatta	CRISPR spacer
tagaat----cactaaattaaatggcttaaatta	Protospacer
    **    ********* ******* ******

95. spacer 7.31|4045021|30|CP020918|CRISPRCasFinder,PILER-CR matches to NC_011256 (Borrelia duttonii Ly plasmid pl70, complete sequence) position: , mismatch: 6, identity: 0.8

atattgcactaaattcaatggctaaaatta	CRISPR spacer
ctgttgcactaaaggcaatggctaaaaatg	Protospacer
 *.**********  ************ *.

96. spacer 7.31|4045021|30|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP016871 (Legionella pneumophila subsp. pneumophila strain FFI103 plasmid, complete sequence) position: , mismatch: 6, identity: 0.8

----atattgcactaaattcaatggctaaaatta	CRISPR spacer
tagaat----cactaaattaaatggcttaaatta	Protospacer
    **    ********* ******* ******

97. spacer 7.31|4045021|30|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP016875 (Legionella pneumophila subsp. pneumophila strain FFI329 plasmid, complete sequence) position: , mismatch: 6, identity: 0.8

----atattgcactaaattcaatggctaaaatta	CRISPR spacer
tagaat----cactaaattaaatggcttaaatta	Protospacer
    **    ********* ******* ******

98. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to KJ801817 (Enterococcus phage ECP3, complete genome) position: , mismatch: 7, identity: 0.767

gtattctgatatatgtataaatccatgatt	CRISPR spacer
gtattctaatatatgtataaataggctatg	Protospacer
*******.**************  .. **

99. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to MK693030 (Enterococcus phage vB_EfaM_Ef2.1, complete genome) position: , mismatch: 7, identity: 0.767

gtattctgatatatgtataaatccatgatt	CRISPR spacer
gtattctaatatatgtataaataggctatg	Protospacer
*******.**************  .. **

100. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to MK693030 (Enterococcus phage vB_EfaM_Ef2.1, complete genome) position: , mismatch: 7, identity: 0.767

gtattctgatatatgtataaatccatgatt	CRISPR spacer
gtattctaatatatgtataaataggctatg	Protospacer
*******.**************  .. **

101. spacer 7.3|4042902|30|CP020918|CRISPRCasFinder matches to MN693698 (Marine virus AFVG_250M751, complete genome) position: , mismatch: 7, identity: 0.767

atgttcgtccagataattggattagtatta	CRISPR spacer
ataatcatccagataattggattaggacgt	Protospacer
**. **.****************** *.

102. spacer 7.8|4043281|30|CP020918|CRISPRCasFinder matches to MN693961 (Marine virus AFVG_250M531, complete genome) position: , mismatch: 7, identity: 0.767

tgttcagcaaatatacaaataacaattgga	CRISPR spacer
tgttcagcaaaaatacaaatcacagcataa	Protospacer
*********** ******** ***..  .*

103. spacer 7.9|4043357|30|CP020918|CRISPRCasFinder matches to MN693961 (Marine virus AFVG_250M531, complete genome) position: , mismatch: 7, identity: 0.767

tgttcagcaaatatacaaataacaattgga	CRISPR spacer
tgttcagcaaaaatacaaatcacagcataa	Protospacer
*********** ******** ***..  .*

104. spacer 7.10|4043433|30|CP020918|CRISPRCasFinder matches to MH791397 (UNVERIFIED: Enterococcus phage EfsSzw-1, complete genome) position: , mismatch: 7, identity: 0.767

actgcatgagtatcgcatccttgcggtaac	CRISPR spacer
tctaattgagtttcccatccttgcggtaaa	Protospacer
 **.  ***** ** **************

105. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to NZ_CP021878 (Enterococcus wangshanyuanii strain MN05 plasmid unnamed5) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
gagaaaaaagaagaagaaagtaccaaaact	Protospacer
    * ***************** *****

106. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to KR709302 (Staphylococcus phage 55-2, complete genome) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
acagacaaaaaagaagaaagtaaaaaaaca	Protospacer
 .  *.***.************ *******

107. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to MN694566 (Marine virus AFVG_250M779, complete genome) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
acttttaaagaagaagaaattacagaaact	Protospacer
 ..* ************** ****.****

108. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to KY963369 (Bacillus phage Tavor_SA, complete genome) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
aaagaaaaagaagaagaaaaaacaaaaaca	Protospacer
    * *************. *********

109. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to KR709303 (Staphylococcus phage 55-3, complete genome) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
acagacaaaaaagaagaaagtaaaaaaaca	Protospacer
 .  *.***.************ *******

110. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to AY954955 (Bacteriophage 42e, complete genome) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
acagacaaaaaagaagaaagtaaaaaaaca	Protospacer
 .  *.***.************ *******

111. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to MK211557 (Staphylococcus phage Henu2, complete genome) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
acagacaaaaaagaagaaagtaaaaaaaca	Protospacer
 .  *.***.************ *******

112. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to NC_007052 (Staphylococcus phage 42e, complete genome) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
acagacaaaaaagaagaaagtaaaaaaaca	Protospacer
 .  *.***.************ *******

113. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to NZ_LR135180 (Enterococcus faecium isolate E0595 plasmid 2) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
cccttgcaaaaagaagaaagaacaaaaaca	Protospacer
..**   **.********** *********

114. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to NZ_LR132068 (Enterococcus faecium isolate E0139 plasmid 2) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
cccttgcaaaaagaagaaagaacaaaaaca	Protospacer
..**   **.********** *********

115. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to NZ_CP037956 (Enterococcus hirae strain CQP3-9 plasmid pCQP3-9_1, complete sequence) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
cccttgcaaaaagaagaaagaacaaaaaca	Protospacer
..**   **.********** *********

116. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to NC_017543 (Paenibacillus polymyxa M1 plasmid pPPM1a, complete sequence) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
ttatataaagaagaagaaggtacgctcaaa	Protospacer
** ***************.****.   * *

117. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to GU080336 (Sulfolobus turreted icosahedral virus 2, complete genome) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
taaggtagagaagaagaaagaacaaaaaaa	Protospacer
*   .**.************ ******* *

118. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to MN694296 (Marine virus AFVG_250M539, complete genome) position: , mismatch: 7, identity: 0.767

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
tattttaaagaagaaaaaagaacaaaaaat	Protospacer
* .* **********.**** *******

119. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to MT740314 (Escherichia phage JEP1, complete genome) position: , mismatch: 7, identity: 0.759

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ttgacagttattttatttaaagcttgaca	Protospacer
*...**************** **** *.

120. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NC_003042 (Clostridium perfringens str. 13 plasmid pCP13, complete sequence) position: , mismatch: 7, identity: 0.759

tcagcagttattttatttaatgcttcatt	CRISPR spacer
attgcagttattttttctaatgcttcttc	Protospacer
 . *********** *.********* *.

121. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to MN693558 (Marine virus AFVG_25M213, complete genome) position: , mismatch: 7, identity: 0.759

tcagcagttattttatttaatgcttcatt	CRISPR spacer
ccatatgttattttatttaatccttcaaa	Protospacer
.**   *************** *****

122. spacer 7.19|4044114|30|CP020918|CRISPRCasFinder matches to MK250029 (Prevotella phage Lak-C1, complete genome) position: , mismatch: 7, identity: 0.767

tgataatgaaatactattaatatctgttac	CRISPR spacer
agataaagaaatacaattaatatcattttg	Protospacer
 ***** ******* *********  **

123. spacer 7.19|4044114|30|CP020918|CRISPRCasFinder matches to MK250016 (Prevotella phage Lak-A1, complete genome) position: , mismatch: 7, identity: 0.767

tgataatgaaatactattaatatctgttac	CRISPR spacer
agataaagaaatacaattaatatcattttg	Protospacer
 ***** ******* *********  **

124. spacer 7.23|4044416|30|CP020918|CRISPRCasFinder matches to MK250029 (Prevotella phage Lak-C1, complete genome) position: , mismatch: 7, identity: 0.767

tgataatgaaatactattaatatctgttac	CRISPR spacer
agataaagaaatacaattaatatcattttg	Protospacer
 ***** ******* *********  **

125. spacer 7.23|4044416|30|CP020918|CRISPRCasFinder matches to MK250016 (Prevotella phage Lak-A1, complete genome) position: , mismatch: 7, identity: 0.767

tgataatgaaatactattaatatctgttac	CRISPR spacer
agataaagaaatacaattaatatcattttg	Protospacer
 ***** ******* *********  **

126. spacer 7.29|4044869|30|CP020918|CRISPRCasFinder,PILER-CR matches to MK250016 (Prevotella phage Lak-A1, complete genome) position: , mismatch: 7, identity: 0.767

agtacgcttaaagcaataataagtataaat	CRISPR spacer
aataataataaagctataataagtataaaa	Protospacer
*.**    ****** **************

127. spacer 7.29|4044869|30|CP020918|CRISPRCasFinder,PILER-CR matches to MN693440 (Marine virus AFVG_25M540, complete genome) position: , mismatch: 7, identity: 0.767

agtacgcttaaagcaataataagtataaat	CRISPR spacer
atgattattgaagcaatattaagtataaat	Protospacer
*  *.  **.******** ***********

128. spacer 7.1|4042750|30|CP020918|CRISPRCasFinder matches to NC_019521 (Sphingomonas phage PAU, complete genome) position: , mismatch: 8, identity: 0.733

gtattctgatatatgtataaatccatgatt	CRISPR spacer
gtattatgatatatgtataaaaggactgta	Protospacer
***** ***************   *. .*

129. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to NZ_LR214986 (Mycoplasma cynos strain NCTC10142 plasmid 13) position: , mismatch: 8, identity: 0.733

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
aaaaataaagaagaagaaagaagaaaatta	Protospacer
    **************** * **** .*

130. spacer 7.13|4043661|30|CP020918|CRISPRCasFinder matches to MN693989 (Marine virus AFVG_250M851, complete genome) position: , mismatch: 8, identity: 0.733

ttctataaagaagaagaaagtacaaaaaca	CRISPR spacer
gatattaaagaagaagaaattacagaaata	Protospacer
  .  ************** ****.***.*

131. spacer 7.15|4043813|29|CP020918|CRISPRCasFinder matches to NC_029119 (Staphylococcus phage SPbeta-like, complete genome) position: , mismatch: 8, identity: 0.724

tcagcagttattttatttaatgcttcatt	CRISPR spacer
gctttagttaatttatttaatgcttctgc	Protospacer
 *  .***** ***************  .

132. spacer 7.18|4044039|29|CP020918|CRISPRCasFinder matches to NZ_CP054029 (Rhizobium sp. JKLM19E plasmid pPR19E02, complete sequence) position: , mismatch: 8, identity: 0.724

tttttcgtctccccttcttacccaatatt	CRISPR spacer
cgcgtcatctccccttcttatccaataac	Protospacer
. . **.*************.****** .

133. spacer 7.19|4044114|30|CP020918|CRISPRCasFinder matches to MH319759 (Marine virus AG-345-O18 Ga0172273_13 genomic sequence) position: , mismatch: 8, identity: 0.733

tgataatgaaatactattaatatctgttac	CRISPR spacer
cctaaatgacataatattaatatctgtatc	Protospacer
.   ***** *** *************  *

134. spacer 7.19|4044114|30|CP020918|CRISPRCasFinder matches to AP013385 (Uncultured Mediterranean phage uvMED DNA, complete genome, group G15, isolate: uvMED-CGR-C16-MedDCM-OCT-S39-C44) position: , mismatch: 8, identity: 0.733

tgataatgaaatactattaatatctgttac	CRISPR spacer
acattgtgaaatactatcaatatctgtaca	Protospacer
  ** .***********.*********

135. spacer 7.19|4044114|30|CP020918|CRISPRCasFinder matches to KC821624 (Cellulophaga phage phi14:2, complete genome) position: , mismatch: 8, identity: 0.733

tgataatgaaatactattaatatctgttac	CRISPR spacer
tctagctgaaatattattaatacctgttaa	Protospacer
*   . *******.********.******

136. spacer 7.20|4044190|30|CP020918|CRISPRCasFinder matches to NZ_CP012953 (Acinetobacter baumannii strain D36 plasmid pD36-1 clone GC1, complete sequence) position: , mismatch: 8, identity: 0.733

ctattttcacaaagaaaactttctatttta	CRISPR spacer
atatattcacaaagaaaactttcagtgaag	Protospacer
 *** ****************** .*   .

137. spacer 7.20|4044190|30|CP020918|CRISPRCasFinder matches to NZ_CP021374 (Rhizobium sp. ACO-34A plasmid pRACO34Ab, complete sequence) position: , mismatch: 8, identity: 0.733

ctattttcacaaagaaaactttctatttta	CRISPR spacer
cgctgaaaacaaagaaatctttctattttt	Protospacer
*  *    ********* ***********

138. spacer 7.22|4044341|29|CP020918|CRISPRCasFinder matches to NZ_CP054029 (Rhizobium sp. JKLM19E plasmid pPR19E02, complete sequence) position: , mismatch: 8, identity: 0.724

tttttcgtctccccttcttacccaatatt	CRISPR spacer
cgcgtcatctccccttcttatccaataac	Protospacer
. . **.*************.****** .

139. spacer 7.23|4044416|30|CP020918|CRISPRCasFinder matches to MH319759 (Marine virus AG-345-O18 Ga0172273_13 genomic sequence) position: , mismatch: 8, identity: 0.733

tgataatgaaatactattaatatctgttac	CRISPR spacer
cctaaatgacataatattaatatctgtatc	Protospacer
.   ***** *** *************  *

140. spacer 7.23|4044416|30|CP020918|CRISPRCasFinder matches to AP013385 (Uncultured Mediterranean phage uvMED DNA, complete genome, group G15, isolate: uvMED-CGR-C16-MedDCM-OCT-S39-C44) position: , mismatch: 8, identity: 0.733

tgataatgaaatactattaatatctgttac	CRISPR spacer
acattgtgaaatactatcaatatctgtaca	Protospacer
  ** .***********.*********

141. spacer 7.23|4044416|30|CP020918|CRISPRCasFinder matches to KC821624 (Cellulophaga phage phi14:2, complete genome) position: , mismatch: 8, identity: 0.733

tgataatgaaatactattaatatctgttac	CRISPR spacer
tctagctgaaatattattaatacctgttaa	Protospacer
*   . *******.********.******

142. spacer 7.25|4044567|29|CP020918|CRISPRCasFinder,PILER-CR matches to NC_018878 (Bacillus thuringiensis Bt407 plasmid BTB_502p, complete sequence) position: , mismatch: 8, identity: 0.724

atagaaaagaattatgtcaagagaaataa	CRISPR spacer
cgggaaaagaattatttcaagagagaatg	Protospacer
  .************ ********.*  .

143. spacer 7.26|4044642|30|CP020918|CRISPRCasFinder,PILER-CR matches to KC821618 (Cellulophaga phage phi10:1, complete genome) position: , mismatch: 8, identity: 0.733

aatccattacaaacatggtctgaagtattc	CRISPR spacer
aatccattacaaacatgggcggagtttaaa	Protospacer
****************** * **. *

144. spacer 7.29|4044869|30|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP018748 (Borreliella garinii strain CIP 103362 isolate 20047 plasmid unnamed3) position: , mismatch: 8, identity: 0.733

agtacgcttaaagcaataataagtataaat	CRISPR spacer
tttgaaattaaagcaataaaaagtaaaaat	Protospacer
  *. . ************ ***** ****

145. spacer 7.29|4044869|30|CP020918|CRISPRCasFinder,PILER-CR matches to NZ_CP028868 (Borreliella garinii strain 20047 plasmid cp32-6, complete sequence) position: , mismatch: 8, identity: 0.733

agtacgcttaaagcaataataagtataaat	CRISPR spacer
tttgaaattaaagcaataaaaagtaaaaat	Protospacer
  *. . ************ ***** ****

146. spacer 7.5|4043053|30|CP020918|CRISPRCasFinder matches to NZ_CP026117 (Lactobacillus curvatus JCM 1096 = DSM 20019 plasmid pLDW-27, complete sequence) position: , mismatch: 9, identity: 0.7

attagggggttattcttattggctattcga	CRISPR spacer
tcgacagggttatttttattggctattttg	Protospacer
 . * .********.************. .

147. spacer 7.16|4043888|30|CP020918|CRISPRCasFinder matches to NZ_CP009059 (Borreliella afzelii K78 plasmid lp54, complete sequence) position: , mismatch: 9, identity: 0.7

taaaaacaatagaacccgtagttaagggcg	CRISPR spacer
aaaaaataatagaacccgtagtagaaaaaa	Protospacer
 *****.*************** .*... .

148. spacer 7.16|4043888|30|CP020918|CRISPRCasFinder matches to NC_017241 (Borreliella afzelii PKo plasmid lp54, complete sequence) position: , mismatch: 9, identity: 0.7

taaaaacaatagaacccgtagttaagggcg	CRISPR spacer
aaaaaataatagaacccgtagtagaaaaaa	Protospacer
 *****.*************** .*... .

149. spacer 7.16|4043888|30|CP020918|CRISPRCasFinder matches to NZ_CP009214 (Borreliella afzelii Tom3107 plasmid lp54, complete sequence) position: , mismatch: 9, identity: 0.7

taaaaacaatagaacccgtagttaagggcg	CRISPR spacer
aaaaaataatagaacccgtagtagaaaaaa	Protospacer
 *****.*************** .*... .

150. spacer 7.26|4044642|30|CP020918|CRISPRCasFinder,PILER-CR matches to MN694255 (Marine virus AFVG_250M362, complete genome) position: , mismatch: 9, identity: 0.7

aatccattacaaacatggtctgaagtattc	CRISPR spacer
gcgttattacgtacatggtctgaagtatat	Protospacer
.  ..*****. **************** .

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

3313025 : 3323355

Bacillus_phage(75.0%)

integrase,tRNA,transposase

attL 3319808:3319867|attR 3322994:3323415

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
AWG22585.1\|3313025_3314429_+\|tRNA	tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE	NA	NA	NA	NA
AWG23666.1\|3314615_3315965_+	sulfurtransferase	NA	NA	NA	NA
AWG23667.1\|3316014_3316935_+	HNH endonuclease	NA	NA	NA	NA
AWG22586.1\|3316953_3317235_-	hypothetical protein	NA	NA	NA	NA
AWG22587.1\|3317304_3318150_-\|integrase	integrase	A0A1P8CWQ3	Bacillus_phage	5.7e-15	27.1
AWG22588.1\|3318200_3318512_-\|transposase	transposase	NA	NA	NA	NA
AWG22589.1\|3318598_3318805_-	transcriptional regulator	B5LPU7	Bacillus_virus	8.5e-05	49.2
AWG22590.1\|3318961_3319807_-\|integrase	integrase	A0A1P8CWQ3	Bacillus_phage	5.7e-15	27.1
3319808:3319867	attL	NA	NA	NA	NA
AWG22591.1\|3319857_3320169_-\|transposase	transposase	NA	NA	NA	NA
AWG22592.1\|3320356_3321883_-	hypothetical protein	NA	NA	NA	NA
AWG22593.1\|3322147_3322993_-\|integrase	integrase	A0A1P8CWQ3	Bacillus_phage	5.7e-15	27.1
AWG22594.1\|3323043_3323355_-\|transposase	transposase	NA	NA	NA	NA
3322994:3323415	attR	NA	NA	NA	NA

DBSCAN-SWA_2

3756144 : 3784456

Bacillus_phage(28.57%)

integrase,tRNA,transposase

attL 3774979:3775028|attR 3784457:3784506

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
AWG22869.1\|3756144_3758079_-\|tRNA	threonine--tRNA ligase	A0A2K9L6B6	Tupanvirus	6.5e-123	37.2
AWG22870.1\|3758357_3759134_-	hypothetical protein	NA	NA	NA	NA
AWG22871.1\|3759397_3759889_-	glyoxalase	NA	NA	NA	NA
AWG22872.1\|3760009_3760888_-	NAD(P)-dependent oxidoreductase	NA	NA	NA	NA
AWG22873.1\|3760937_3761297_-	hypothetical protein	NA	NA	NA	NA
AWG22874.1\|3761413_3761776_+	transcriptional regulator	NA	NA	NA	NA
AWG23684.1\|3761892_3762138_+	hypothetical protein	NA	NA	NA	NA
AWG22875.1\|3764252_3764492_+	hypothetical protein	NA	NA	NA	NA
AWG22876.1\|3764998_3765610_+	hypothetical protein	NA	NA	NA	NA
AWG22877.1\|3765606_3766008_+	hypothetical protein	NA	NA	NA	NA
AWG22878.1\|3766075_3766438_+	ketosteroid isomerase	NA	NA	NA	NA
AWG22879.1\|3766971_3767892_-	hypothetical protein	NA	NA	NA	NA
AWG22880.1\|3768191_3768539_-	hypothetical protein	NA	NA	NA	NA
AWG22881.1\|3768535_3769825_-	hypothetical protein	NA	NA	NA	NA
AWG22882.1\|3770069_3771350_+	2-amino-3-ketobutyrate CoA ligase	NA	NA	NA	NA
AWG22883.1\|3771463_3772093_+	TetR family transcriptional regulator	NA	NA	NA	NA
AWG22884.1\|3772397_3772658_-	hypothetical protein	NA	NA	NA	NA
AWG23685.1\|3772807_3773647_+\|integrase	integrase	A0A1P8DJJ6	Virus_Rctr41k	1.2e-25	32.1
AWG22885.1\|3773631_3774768_+\|transposase	IS91 family transposase	NA	NA	NA	NA
AWG22886.1\|3774797_3774986_+	hypothetical protein	NA	NA	NA	NA
3774979:3775028	attL	NA	NA	NA	NA
AWG22887.1\|3775028_3775874_-\|integrase	integrase	A0A1P8CWQ3	Bacillus_phage	5.7e-15	27.1
AWG22888.1\|3775924_3776236_-\|transposase	transposase	NA	NA	NA	NA
AWG22889.1\|3776311_3776716_-	hypothetical protein	A0A1J0MFJ5	Staphylococcus_phage	9.4e-08	31.4
AWG22890.1\|3776719_3777937_-	hypothetical protein	A0A2I6PCS6	Staphylococcus_phage	6.6e-12	37.0
AWG22891.1\|3778191_3778677_-	hypothetical protein	NA	NA	NA	NA
AWG22892.1\|3779383_3780679_+	group II intron reverse transcriptase/maturase	Q775D8	Bordetella_phage	6.5e-10	26.4
AWG22893.1\|3780755_3781316_-	hypothetical protein	NA	NA	NA	NA
AWG22894.1\|3781339_3781609_-	hypothetical protein	NA	NA	NA	NA
AWG22895.1\|3781724_3782117_+	hypothetical protein	NA	NA	NA	NA
AWG22896.1\|3782106_3782715_+	hypothetical protein	NA	NA	NA	NA
AWG22897.1\|3783248_3783560_+\|transposase	transposase	NA	NA	NA	NA
AWG22898.1\|3783610_3784456_+\|integrase	integrase	A0A1P8CWQ3	Bacillus_phage	5.7e-15	27.1
3784457:3784506	attR	NA	NA	NA	NA

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. CP020918

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection