CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP007588	Weissella ceti strain WS08 chromosome, complete genome	3 crisprs	cas3,DEDDh,DinG,csa3	0	1	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP007588_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP007588_1

20104-20209

Orphan

Consensus_repeat	Method
CCGAATTAGCTCAGTTGGTAGAGCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP007588_1

>merge|NZ_CP007588|1|20104-20209|CRISPRCasFinder
CCGAATTAGCTCAGTTGGTAGAGCACACGACTGTTAATCGTGTTGTCGTCGGTTCGAGCCCGACATTCGGAGTCTGATTTGCCGACTTAGCTCAGTTGGTAGAGCA

>NZ_CP007588|1|1|20104-20209|CRISPRCasFinder
CCGAATTAGCTCAGTTGGTAGAGCA	CACGACTGTTAATCGTGTTGTCGTCGGTTCGAGCCCGACATTCGGAGTCTGATTTG
CCGACTTAGCTCAGTTGGTAGAGCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP007588.1\|WP_009765221.1\|13559_14510_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP007588.1\|WP_009495724.1\|29775_31203_+\|NADP-dependent-phosphogluconate-dehydrogenase	unknown	unknown	gnl\|CDD\|236453
NZ_CP007588.1\|WP_009495729.1\|24154_24799_+\|gluconate-kinase	unknown	unknown	gnl\|CDD\|212659
NZ_CP007588.1\|WP_009495727.1\|26110_27370_+\|tyrosine--tRNA-ligase	unknown	unknown	gnl\|CDD\|237360
NZ_CP007588.1\|WP_009765220.1\|12249_13503_+\|hydroxymethylglutaryl-CoA-reductase,-degradative	unknown	unknown	gnl\|CDD\|153082
NZ_CP007588.1\|WP_009765215.1\|3901_4129_+\|S4-domain-containing-protein-YaaA	unknown	unknown	gnl\|CDD\|274378
NZ_CP007588.1\|WP_038527960.1\|9969_12144_+\|LTA-synthase-family-protein	unknown	unknown	gnl\|CDD\|224287
NZ_CP007588.1\|WP_009765216.1\|4131_5256_+\|DNA-replication/repair-protein-RecF	unknown	unknown	gnl\|CDD\|234608
NZ_CP007588.1\|WP_009495731.1\|22638_23547_+\|decarboxylating-6-phosphogluconate-dehydrogenase	unknown	unknown	gnl\|CDD\|236582
NZ_CP007588.1\|WP_009495733.1\|20917_21556_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP007588.1\|WP_009765218.1\|7267_9808_+\|DNA-gyrase-subunit-A	unknown	unknown	gnl\|CDD\|235502
NZ_CP007588.1\|WP_009495726.1\|27639_28926_+\|purine-permease	unknown	unknown	gnl\|CDD\|274468
NZ_CP007588.1\|WP_009765214.1\|2563_3694_+\|DNA-polymerase-III-subunit-beta	unknown	unknown	gnl\|CDD\|235541
NZ_CP007588.1\|WP_009765217.1\|5282_7226_+\|DNA-topoisomerase-(ATP-hydrolyzing)-subunit-B	unknown	unknown	gnl\|CDD\|235542
NZ_CP007588.1\|WP_009495728.1\|25197_25833_+\|NAD(P)H-binding-protein	unknown	unknown	gnl\|CDD\|187555
NZ_CP007588.1\|WP_009495725.1\|28925_29498_+\|xanthine-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|181705
NZ_CP007588.1\|WP_009495732.1\|21652_22495_-\|MurR/RpiR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224651
NZ_CP007588.1\|WP_009495730.1\|23667_24123_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|236715
NZ_CP007588.1\|WP_002828338.1\|104_239_-\|50S-ribosomal-protein-L34	unknown	unknown	gnl\|CDD\|366117
NZ_CP007588.1\|WP_009765213.1\|976_2368_+\|chromosomal-replication-initiator-protein-DnaA	unknown	unknown	gnl\|CDD\|234667

Protein	Function_ID	Function_description	E-value
NZ_CP007588.1\|WP_009495724.1\|29775_31203_+\|NADP-dependent-phosphogluconate-dehydrogenase	gnl\|CDD\|236453	PRK09287, PRK09287, NADP-dependent phosphogluconate dehydrogenase.	0
NZ_CP007588.1\|WP_009495729.1\|24154_24799_+\|gluconate-kinase	gnl\|CDD\|212659	cd07770, FGGY_GntK, Gluconate kinases; a subfamily of the FGGY family of carbohydrate kinases. This subfamily is composed of a group of gluconate kinases (GntK, also known as gluconokinase; EC 2.7.1.12) encoded by the gntK gene, which catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, members in this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Some uncharacterized homologous sequences are also included in this subfamily. The Lactobacillus gnt operon contains a single gntK gene. The gnt operons of some bacteria, such as Corynebacterium glutamicum, have two gntK genes. For example, the C. glutamicum gnt operon has both a gluconate kinase gntV gene (also known as gntK) and a second hypothetical gntK gene (also known as gntK2). Both gluconate kinases encoded by these genes belong to this family, however the protein encoded by C. glutamicum gntV is not included in this model as it is truncated in the C-terminal domain.	5.9165e-15
NZ_CP007588.1\|WP_009495727.1\|26110_27370_+\|tyrosine--tRNA-ligase	gnl\|CDD\|237360	PRK13354, PRK13354, tyrosyl-tRNA synthetase; Provisional.	0
NZ_CP007588.1\|WP_009765220.1\|12249_13503_+\|hydroxymethylglutaryl-CoA-reductase,-degradative	gnl\|CDD\|153082	cd00644, HMG-CoA_reductase_classII, Class II hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). Hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR), class II, prokaryotic enzyme is a homodimer. Class II enzymes are found primarily in prokaryotes and Archaeoglobus fulgidus and are soluble as they lack the membrane region. Enzymes catalyze the synthesis of coenzyme A and mevalonate in isoprenoid synthesis. Bacteria, such as Pseudomonas mevalonii, which rely solely on mevalonate for their carbon source, catalyze the reverse reaction, using an NAD-dependent HMGR to deacetylate mevalonate into 3-hydroxy-3-methylglutaryl-CoA. Human and bacterial HMGR differ in their active site architecture.	0
NZ_CP007588.1\|WP_009765215.1\|3901_4129_+\|S4-domain-containing-protein-YaaA	gnl\|CDD\|274378	TIGR02988, YaaA_near_RecF, S4 domain protein YaaA. This small protein has a single S4 domain (pfam01479), as do bacterial ribosomal protein S4, some pseudouridine synthases, tyrosyl-tRNA synthetases. The S4 domain may bind RNA. Members of this protein family are found almost exclusively in the Firmicutes, and almost invariably just a few nucleotides upstream of the gene for the DNA replication and repair protein RecF. The few members of this family that are not near recF are found instead near dnaA and/or dnaN, the usual neighbors of recF, near the origin of replication. The conserved location suggests a possible role in replication in the Firmicutes lineage. [DNA metabolism, DNA replication, recombination, and repair].	1.37047e-30
NZ_CP007588.1\|WP_038527960.1\|9969_12144_+\|LTA-synthase-family-protein	gnl\|CDD\|224287	COG1368, MdoB, Phosphoglycerol transferase and related proteins, alkaline phosphatase superfamily [Cell envelope biogenesis, outer membrane].	2.61394e-143
NZ_CP007588.1\|WP_009765216.1\|4131_5256_+\|DNA-replication/repair-protein-RecF	gnl\|CDD\|234608	PRK00064, recF, recombination protein F; Reviewed.	9.28798e-153
NZ_CP007588.1\|WP_009495731.1\|22638_23547_+\|decarboxylating-6-phosphogluconate-dehydrogenase	gnl\|CDD\|236582	PRK09599, PRK09599, NADP-dependent phosphogluconate dehydrogenase.	0
NZ_CP007588.1\|WP_002828338.1\|104_239_-\|50S-ribosomal-protein-L34	gnl\|CDD\|366117	pfam00468, Ribosomal_L34, Ribosomal protein L34.	1.48868e-09
NZ_CP007588.1\|WP_009765218.1\|7267_9808_+\|DNA-gyrase-subunit-A	gnl\|CDD\|235502	PRK05560, PRK05560, DNA gyrase subunit A; Validated.	0
NZ_CP007588.1\|WP_009495726.1\|27639_28926_+\|purine-permease	gnl\|CDD\|274468	TIGR03173, pbuX, xanthine permease. All the seed members of this model are observed adjacent to genes for either xanthine phosphoribosyltransferase (for the conversion of xanthine to guanine, GenProp0696) or genes for the conversion of xanthine to urate and its concomitant catabolism (GenProp0640, GenProp0688, GenProp0686 and GenProp0687). A number of sequences scoring higher than trusted to this model are found in different genomic contexts, and the possibility exist that these transport related compounds in addition to or instead of xanthine itself. The outgroup to this family are sequences which are characterized as uracil permeases or are adjacent to established uracil phosphoribosyltransferases.	5.07475e-151
NZ_CP007588.1\|WP_009765214.1\|2563_3694_+\|DNA-polymerase-III-subunit-beta	gnl\|CDD\|235541	PRK05643, PRK05643, DNA polymerase III subunit beta; Validated.	3.09287e-129
NZ_CP007588.1\|WP_009765217.1\|5282_7226_+\|DNA-topoisomerase-(ATP-hydrolyzing)-subunit-B	gnl\|CDD\|235542	PRK05644, gyrB, DNA gyrase subunit B; Validated.	0
NZ_CP007588.1\|WP_009495728.1\|25197_25833_+\|NAD(P)H-binding-protein	gnl\|CDD\|187555	cd05244, BVR-B_like_SDR_a, biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs. Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. 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.	4.7755e-40
NZ_CP007588.1\|WP_009495725.1\|28925_29498_+\|xanthine-phosphoribosyltransferase	gnl\|CDD\|181705	PRK09219, PRK09219, xanthine phosphoribosyltransferase; Validated.	1.15233e-117
NZ_CP007588.1\|WP_009495730.1\|23667_24123_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|236715	PRK10562, PRK10562, putative acetyltransferase; Provisional.	6.83348e-28
NZ_CP007588.1\|WP_009495732.1\|21652_22495_-\|MurR/RpiR-family-transcriptional-regulator	gnl\|CDD\|224651	COG1737, RpiR, Transcriptional regulators [Transcription].	6.24541e-71
NZ_CP007588.1\|WP_009765213.1\|976_2368_+\|chromosomal-replication-initiator-protein-DnaA	gnl\|CDD\|234667	PRK00149, dnaA, chromosomal replication initiator protein DnaA.	4.29506e-180

>NZ_CP007588.1|WP_009765221.1|13559_14510_+|hypothetical-protein
MIFSEDTQRLLAQANAIYPGSIILRASGDNTGIINNEQVQTEMLGSRMVLEVTDMTAPDYIATHELLHMVLSLNGFPQVFFQLETEDEALTEQMIVMGTYLYQPAANIIVYREQAKHGLLTEEVVAAYAKGVLAQLTKEDGTRAESALRFLTLLDAKIFMASVDMETTKYTDSFNDMYPEAWEAAEALFMEMNVAQVQDPATMHHAIMDVFAGFDRQMNAWGLPELNAKEFCTVTPVLSERQMRLKVSQVFEIKHVPYVNRTTKSAAFVGLGKKDKQNSFVLAVPVDATPEFFKGMYDLTVQELFDQLQQPFTLRA
>NZ_CP007588.1|WP_009765220.1|12249_13503_+|hydroxymethylglutaryl-CoA-reductase,-degradative
MNQWQGFYKLPWAERLALTAKNRDLNAEQVALIEQHYDAVGAQLIENYLYNFGVPTGLLLDLPVDGELAVVPMSTEEPSVIAAANNGAKMMRAGEGVTTTMETRLVRGQIIITDVTDMDELRAWIVAHESELMTQINATRPSMVRRGGGLKKLALQELADDIAEVTLFVDPKAAMGANVVNSLAEYTSSIFRAQGYNVLMGILSNYATESVVHGAVKIPVSALVAKDGTPGATIAAKIEQASRIEQLTPYRAVTSNKGIMNGVEAVALASGNDTRAINAALHAYASRDGQYRGLINWTVEQDMLVGKTDLPILIGVVGGSIGIVPAVQLNHVLMGNPTVERLSSLLAGVALAQNLAALRALVSTGIQAGHMALQGKSLALQVGATPEEVPAVALALEQQGHFDELTAREILETLRQS
>NZ_CP007588.1|WP_038527960.1|9969_12144_+|LTA-synthase-family-protein
MKHYSRFDWLKTRIGFVLLLVMLTWAKTQMANVLDFKLYADATFVQYLTLLLNPIPIAMLLIGASLYFKSAKIFYPVALIAYISNLVLLQVNMIYYREFSDFMSFNVMMGYDKVNQGLGASGFALSDPHDIFLWLDLVIIVGLILFRKMRLNAPAVSKLASFSITTFAIFIGMITLMLGEMERPQLITRQFDSKLMVKYLGVDGYTIFDIGRVRNVSELKKTAKKSDIDKIRDYMSSEYAPANAKYAGVAEGKNVFVIHLESFQQFSLNLDVNGQPVTPFLNSIYNSKDTIAFDNFFNQVGQGKTSDAENLLETSTFGLPQGSLFANQGSEQTFQAMPAILRQEGGYSSAVFHGNTAGFWNRNNVYKNMGYQYFFDASYFDTSGNKAAGYGLKDKLLFYDAVPYLERMQQPFYSKFITVTNHFPYTSDDVDKDPTFQTTDSGSKIVDGYFETNRYLDKSIEEFYAYLKKSGLYDNSIVVMYGDHYGISNSESKYLASLLGKNPEDWDAYDMMQLQRVPFIINMPGYGQGHIDHTFGGEVDVAPTLLHLLGVKDTEKYMQVGHDLLSKKKSNIVAMRDGSFITPKYTYVNERVYVTATGEELVDPAPAIEAEIEEAKQKAAKQLKVSDEINQKDLLRFYTPEGFEPVKAKDYNYSNALAKLKRLEDERGKHSTSLFSENNKQFTQKLYETNAPQKDEPRSDTTRLKQTNPDAGEASEPGFDQPNP
>NZ_CP007588.1|WP_009765218.1|7267_9808_+|DNA-gyrase-subunit-A
MTENEQNISRTVNANIGEQMKSSFLDYAMSVIVARALPDVRDGMKPVHRRIMYGMNELGVMPDKPYKKSARIVGDVMGKYHPHGDSAIYESMVRMAQDFSYRYMLVDGHGNFGSIDGDSAAAMRYTEARLSKIATEMLRDINKNTVNFVDNYDGTDREPAVLPARFPNLLVNGANGIAVGMATNIPPHNLGEIISAIHLLMENPDVTTAELMEAVPGPDFPTGGIALGKSGIRKAYETGKGTVTVRSKVEIETEKSGKERIIVTELPYMVNKARLIERIAELARDKRIEGITSINDESDREGYRIAIDIRRDVSASVVLNNLYKNTLMQTNFSFNMLAVQDGRPKLLSLKDMLKAYLKHQQEVIRRRTEFELKKAEARAHILEGLRIALDHIDAIIKIIRSSTTAEIAKTQLISDYALSDKQAQAILDMRLVRLTGLERDKIEKEYQELMAEIAEFKDILSKPERIDQIIYTELLEIQEKHGDDRRTELQIGDVTSIEDEDLIEEEDVIVSLTRGGYIKRMAQSEFRAQNRGGRGVQGMGVNDDDFIDQIAGTSTHDTLLFFTNAGKVYKLKGYEIPEYGRTAKGIPVINLLGIESGETIQTMISVNDDPENSDDYLFFTTRDGVVKRTAISEFGNIRAHGLRAINLRENDELIKVMKTVDSDNILIATQGGYAVSFKMDTIRAMGRTAAGVRGINLRENDMVIGAEVLVDDAHVLVITQNGYGKKTAVSEYPIKGRGGKGIKTAQITEKNGPLAGVAVVQGGEDVVLTTNMGVMIRFNVATVSETGRATQGVRLIRLDEEATVATFTTVEPEPEEDTTVTDDSMTEQVEALVDRAMSEEADTTEA
>NZ_CP007588.1|WP_009765217.1|5282_7226_+|DNA-topoisomerase-(ATP-hydrolyzing)-subunit-B
MAEEDTQMHTNAAEYDANQIQVLEGLEAVRKRPGMYIGTTTSQGLHHLVWEIVDNGIDEALAGFADHITVTVEADNSITVTDNGRGIPTDVQQQTGKPALETVFTVLHAGGKFGGGGYKVSGGLHGVGASVVNALSTTLDVTVIRDQKAHSMVFEQGRVTQDMVVTDAPNNDFERGTIVHFSPDPDIFQETTVYDIKTLTSRVRELAFLNKGLRISITDNRPEESVTESFYYEGGIKEYVVYLDDNKDVLFEDPIYVEGMEKGISVEVSLQYTDDYHTNMLSFTNNIHTYEGGTHETGFRSALTRVINDYARRTGQLKENEEALSGEDVREGLTAIVSVKHPDPQFEGQTKTKLGNSDARTAVDRMFSETFNRFMMENPTVAKQIVEKGIVASRARKAAKRAREATRKKSGLEISNLPGKLADNTSKNPEISELFIVEGDSAGGSAKQGRERLTQAILPIRGKILNVEKASLEKILGNEEIRSLFTAMGTGFGAEFDVEKAKYHKLIIMTDADVDGAHIRTLLMTLVYRYMRPLIDKGYFYIAQPPLYQVRQGKFVKYLDSDEELNELLPTLPATPKPVIQRYKGLGEMDAEQLWETTMDPEARHLLRVQMDDAVEADRIFTMLMGDKVEPRREFIEDNAEYAELDI
>NZ_CP007588.1|WP_009765216.1|4131_5256_+|DNA-replication/repair-protein-RecF
MELLALALHNFRNYQDLSTTFSPGVNVFLGPNAQGKTNLLEAIYALALTRSHRTNTDKELIGWSGDDARISGTIERRTGKVPLELSFSTKGKKAKVNHLDQPKLANYIGHLNVILFAPEDLELVKGAPAVRRQFIDREFSQMSPKYLYVANQYRAMLRQRNQYLKQLQTNKQTDLLFLDVLTEQLVNLASELIVRRLQLLKALNAAAMPIQSDITQGNETLQIKYVSQLNPDEMTDEKTIKNAMMTRFEKLRKRELFEGVTKLGPHRDDLQFMVNDHDVAVYGSQGQQRTTALAVKLAEIDLMFQETGEYPILLLDDVLSELDTDRQTHLLTAIQDKVQTFITTPSLSDVAKQLIKTPKIFNVRTGTLTEQSDV
>NZ_CP007588.1|WP_009765215.1|3901_4129_+|S4-domain-containing-protein-YaaA
MAQEIHIQTPYITLGQLLKQSSVIQTGGQAKWYLQENTVLVNQEPDARRGRKLYPGDIVAIPDGERFVINGMGAE
>NZ_CP007588.1|WP_009765214.1|2563_3694_+|DNA-polymerase-III-subunit-beta
MQFTINRAEFIKAMNNVSRAISSRTSMPILTGVKLEVEESGLILTGSDTDISIEIKIPVTDDKAKLVNLEAGSLVLPATFFANIVKRLPGETFTLTNTDGLQAKITSESAEFDINGQDANAYPRLPEVEVTNQLILPAETLTEVIGQTVIAVSKQLSQPILTGVHFIIAGGNLTAVATDRHRLAQRTVSFGNEDVNADIIIPGPSLIQLQAMLDTVESVEVRVSENQVVFQLGDDTLFYSRLLEGNYPDASRLIPTEKRTTLTINSRDLLQTIERAALLSHEGRSNVIQFTVSDDRSSISSNSPEVGRVEEEIFAAETAGDELTISFNPDYMREALKSFGDEEIQIGFKTPLDPFTLVPTNNATNFIQLITPVRTY
>NZ_CP007588.1|WP_009765213.1|976_2368_+|chromosomal-replication-initiator-protein-DnaA
MDPAELWTAIKEQLRESMSGDFGYQTYVERLQVIDLVSNEFSAQTLHLSTDQEKVAEEWRNPEGHYYRTFIQAAMTATAQLYAQPIFISPSVMYVPAEAVKPLAETPVDTQMVGTEVTANFISTTLDPDFRFDTFVSSVENKEAYSVAQAVAENPGTQWNPLLIYGGVGLGKTHLMQSIGNEVLRKNPNAKVKFITTEDFINDFTDALRRGTMDEFKHEYRTTNLLMVDDVQFLADKTKIQEEFFNTFNAITRENNQIVLTSDKLPKEIPGLEMRLVTRFGQGYSANITKPDLPTRVAILRNKSEQDGLNIPNDIIDEIAAAVDTNVRDLESVFNQVAAKIKFSPQPVTVDATRNILEQMSFKRQKVVTVPIIQTIVSNYFDLTVDDLTGTRRNKQIVTPRQIAMYLARELTQDSLPQIGRAFGGRDHTTVMHSTEKIEGAIGEDHILEQQVQEIRERLSDNG
>NZ_CP007588.1|WP_002828338.1|104_239_-|50S-ribosomal-protein-L34
MKRTYQPKKRHRERVHGFRKRMSTSNGRKVLARRRQKGRKVLSA
>NZ_CP007588.1|WP_009495733.1|20917_21556_+|hypothetical-protein
MVKQGKFASTTKQMQGQTNRYKAMSGQGKINAEEVSEYLMVRYHLTRGKKQSTLIENTLLRVLDVLVPTIQANSGALDESLAEHLKSVSMTVPWQYYKVMNDEWAPLQRWLKKELPAVPLTETLRVTTEVEPVDELIAQQLAINWWLNQSQGNTQRLAAVTEEKITSLMETFIPNGKLDWQIVQTIYSTIVFNANATLDVETQNWLKELSEL
>NZ_CP007588.1|WP_009495732.1|21652_22495_-|MurR/RpiR-family-transcriptional-regulator
MPQSAYARIKSMQQQLSGSDQKIANYILDDATDKQALTIQGLANAVNVSTATVSRFVKRIGFSSYREFSLSLAVPSQRSNTFFGEIEPQDNTEQIAQKVFNGAKNAIDATYEMIAAKDWQCAAEWLINARRVGLFGIGGSSIVALNGYHKLLRTPLDVEQHPDYDVQLMQSVRMRHDDVAIVISHSGRNKDTLKITRQLKANNVKVIAITAFPNSGLAQLADLVLASSAEEVNMRSESMSSLVAQITIMDSLFTLVGVKLAEDTQGIVDQMRTAIDSTRE
>NZ_CP007588.1|WP_009495731.1|22638_23547_+|decarboxylating-6-phosphogluconate-dehydrogenase
MKFAMIGLGKMGLNLVKNAVDNGNEVVVFDLNKDFVAEAAAYSDAVTPADSIDDMLAKLPTPKIAWVMVPAGVPTNSTIDTLIEKMDEGDFIIDGGNSNYKDNLEQNKRTTAAGIKFFDAGTSGGMSGARNGGNFMIGGDDEAAWKVLEPLFKGIALEDGYLYTGRLGSGHYLKMVHNGIEYGMMQAIAEGFEILEASQFDYDYEAVAKLWNHGSVVRSWLMELAEEQFAKDPKLSAISGRMHSSGEGKWTVEESLDLDVPAPVIALSLMMRYRSLQEDTFTGKVVSALRNGFGGHAMDSAK
>NZ_CP007588.1|WP_009495730.1|23667_24123_+|GNAT-family-N-acetyltransferase
MQNEPGEMMITLVDWSDEQQRERVLALWLQTNTVTHDFIPSEYWQKMYPMVSDLMADATIYVYWQDNQIIGFIGLMETYIAGIFVDSKHQNQGVGYQLIQYVQNKTAVLDLSVYALNEPAWRFYERQGFKIVSENLDDAVGEIEYQMHWAR
>NZ_CP007588.1|WP_009495729.1|24154_24799_+|gluconate-kinase
MTNTLTVHVTMNQITATWQGAHVAMELPLQVTAETLVKTLTDTMVSVLAGDTPDNIDINNAIEGLVALNENSESVAPILIADKNDQHFIEALTMNGIGGQLARKNAHDLTTTMPVVQILRLKNNAAEVYATATMYRPLTAYLRTVLTGHNILTEQEASMTGMFDQASHQWDTQALALTGLTAIQLPEVGDVVDYAVIAQALTAEMAAVPSVKVH
>NZ_CP007588.1|WP_009495728.1|25197_25833_+|NAD(P)H-binding-protein
MKLAIIGATGMTGKAVYAQAKEQGFDVTGIVRNESKGRDVLGADAQLLVSDVFDLTTEDLTQFDVVVDAFANHEKSYLNLDALTHLIHALREQTTRLMVVLGAGPLLDESGTYHYEFLKTLPGAEAWVDEPKYGVTALQVLQSTTNVNWTAISAQDGYVDGPATEYKMGKDHVMLAEDGESHVTSGNLAKALVAEVVTPQFKQDRFTVSDI
>NZ_CP007588.1|WP_009495727.1|26110_27370_+|tyrosine--tRNA-ligase
MTENILQELAWRGAINQQTDEQGLLAEMEKGQIGVYVGIDPTGSSMHIGHLIPFMMLKRFQKAGQRPVIVVGGATGSIGDPSGKKSERAMISEEDVTYNVAKIREQMTKLFGKDGFAIVNNRDWLGELTLIDFLRDYGKMFSINTMLAKDIVASRLETGISFTEFTYQIMQAIDFHELWTRENVRLQLGGSDQWGNITGGIDLIHKLEGSDAPAFGLTVPLLLKSDGTKFGKSEGGAIWLDPEKTTPYEFFQFWLNTADADVEKMLKFFTFLSEEEIAELMVATTEDAAARKAQRRLAEEVTKFVHGEDAVKTAELMTNVLFGKADVANLSRDEVAALAGNVPSFEIAAEPINVVDLVVAAGMEASKTRAREAVTNGAIRVNGEQITDIETVIDPAANYEGDFVIVKRGKKKWAVARVK
>NZ_CP007588.1|WP_009495726.1|27639_28926_+|purine-permease
METTQPNPFKSAILGLQHVLAMYSGGILVPLLIGTALQFNAQQMTVLISADIFMTGIGTLLQLKRTAFTGIGLPVVLGSAIQSVTPMINIGSTLGIGAMYGAAMGAGIFIILISSLFAKLRNYFPPVVTGSLITVIGFSLIPIAIMNLGGGDPEAANFGDLSHLLVGLVTMLIIVGLTLFAKNFTKAIAVLLGIIGGTIFASFLGEVSLAPIGSAAWFQVPTPFVFGTPSFHLSAIITMSVVALTSLIESTGVYFALSDLTGDKLTEKDLARGYRAEGLAVTVSAIFGAFPYSTFSQNVGVVRLSGLKSKRPIYYAAGILLLIGLLPKIGALATIIPNSVLGGAMFILFGTIGIQGITILSKVDFSTDRNLMIAAISISAGIGVAMYPQIFQQLPDMVRLIIQNAVVVTSMLAVFLNIVLPNREKELV
>NZ_CP007588.1|WP_009495725.1|28925_29498_+|xanthine-phosphoribosyltransferase
MQLLEEKIRREGRVLGTEVLKVDNFLNHQVDPELMAAMGREFAQLFADKGITKVMTVESSGIAPAVFTALELQVPMVFARKKKSLTLTDDNYTADVYSFTKQETNHIIVDKRFISSNDKVLLIDDFLANGQAVQGMMEILDAADADLVGVGIVIEKTFQKGRELLDEKGIHVESLARISAFEDGQVVFAD
>NZ_CP007588.1|WP_009495724.1|29775_31203_+|NADP-dependent-phosphogluconate-dehydrogenase
MKEADFGVVGLAVMGRNLALNVESRGYTVAVYNRSSERTEDLVETHADKHFVPTYSVKEFVASIKTPRRILMMVKAGAPTDATIDELLPYLDEGDILLDGGNTFFEDTIARSERLAHSGVNFIGMGVSGGELGALQGPSMMPGGQRAAYDLVEPILKQIAAKAPEDGKPTVAYVGPDGAGHYVKMVHNGIEYGDMQLIAEAYDLLKRVVGLNKDELAKTFATWNDGELNSYLTEITADILTRDDDLGSGKPMVEMILDRAGNKGTGKWSSQSALEIGAPQSLITESVYARYLSAMKDDRMIAADVLAGPEFVFSGDKQATIEDIREALYFGKIMSYAQGFDQLRLASNHYGWQLQYGELAQLWRAGAIIRARFLQRITDAYDVNPDLHNLLLDPYFQEIAEKYQASARRVIALAVAAGIPVPSLSSAIAYYDSYRSAVLPANLIQAQRDYFGAHTYERVDKPAGEMYHYSWYDEA

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Crispr_ID: NZ_CP007588_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP007588_2

84100-84191

Orphan

Consensus_repeat	Method
GGTGGTCGTGGTGGATACCGTGGCGGAAACCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP007588_2

>merge|NZ_CP007588|2|84100-84191|CRISPRCasFinder
GGTGGACAAGGTGGTGGTCGTGGTGGATACCGTGGCGGAAACCGTAATGGTGGACGCGGTGGTGACCGTGGTGGAAACCGTCGTGAAGGTGG

>NZ_CP007588|2|2|84100-84191|CRISPRCasFinder
GGTGGACAAGGTGGTGGTCGTGGTGGATACCG	TGGCGGAAACCGTAATGGTGGACGCGGT
GGTGACCGTGGTGGAAACCGTCGTGAAGGTGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP007588.1\|WP_009495675.1\|94583_96287_+\|LPXTG-cell-wall-anchor-domain-containing-protein	unknown	unknown	gnl\|CDD\|273478
NZ_CP007588.1\|WP_009495691.1\|74314_75490_+\|PDZ-domain-containing-protein	unknown	unknown	gnl\|CDD\|273938
NZ_CP007588.1\|WP_038527995.1\|73283_74060_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293819
NZ_CP007588.1\|WP_009495694.1\|71085_72402_+\|yycH-family-protein	unknown	unknown	gnl\|CDD\|276948
NZ_CP007588.1\|WP_009495671.1\|99681_100062_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP007588.1\|WP_009495674.1\|96472_97897_+\|dipeptidase-PepV	unknown	unknown	gnl\|CDD\|235988
NZ_CP007588.1\|WP_038528011.1\|99075_99663_+\|guanylate-kinase	unknown	unknown	gnl\|CDD\|223272
NZ_CP007588.1\|WP_009495689.1\|76348_77713_+\|HD-domain-containing-protein	unknown	unknown	gnl\|CDD\|224004
NZ_CP007588.1\|WP_038528001.1\|81285_82548_+\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	unknown	unknown	gnl\|CDD\|183779
NZ_CP007588.1\|WP_009495687.1\|78652_79234_+\|DNA-directed-RNA-polymerase-subunit-delta	unknown	unknown	gnl\|CDD\|275360
NZ_CP007588.1\|WP_009495673.1\|98036_99008_+\|DUF1002-domain-containing-protein	unknown	unknown	gnl\|CDD\|377628
NZ_CP007588.1\|WP_009495680.1\|86418_88713_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|226482
NZ_CP007588.1\|WP_038566597.1\|91211_93971_+\|LPXTG-cell-wall-anchor-domain-containing-protein	unknown	unknown	gnl\|CDD\|227596
NZ_CP007588.1\|WP_009495679.1\|88792_89809_+\|tryptophan--tRNA-ligase	unknown	unknown	gnl\|CDD\|183400
NZ_CP007588.1\|WP_009495688.1\|77742_78555_+\|Cof-type-HAD-IIB-family-hydrolase	unknown	unknown	gnl\|CDD\|182509
NZ_CP007588.1\|WP_009495678.1\|89825_90758_+\|exopolyphosphatase	unknown	unknown	gnl\|CDD\|274735
NZ_CP007588.1\|WP_009495693.1\|72430_73237_+\|regulator-of-two-component-system,-YycI-family-protein	unknown	unknown	gnl\|CDD\|378229
NZ_CP007588.1\|WP_009495686.1\|79398_81012_+\|CTP-synthase	unknown	unknown	gnl\|CDD\|235437
NZ_CP007588.1\|WP_009495681.1\|85998_86358_+\|type-II-toxin-antitoxin-system-PemK/MazF-family-toxin	unknown	unknown	gnl\|CDD\|367091
NZ_CP007588.1\|WP_009495690.1\|75744_76173_-\|DUF1934-domain-containing-protein	unknown	unknown	gnl\|CDD\|378129

Protein	Function_ID	Function_description	E-value
NZ_CP007588.1\|WP_009495675.1\|94583_96287_+\|LPXTG-cell-wall-anchor-domain-containing-protein	gnl\|CDD\|273478	TIGR01167, Zinc_metalloprotease_ZmpB, LPXTG-motif cell wall anchor domain. This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region. [Cell envelope, Other].	3.18622e-08
NZ_CP007588.1\|WP_009495691.1\|74314_75490_+\|PDZ-domain-containing-protein	gnl\|CDD\|273938	TIGR02037, Probable_periplasmic_serine_protease_do/HhoA-like, periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides].	7.1316e-87
NZ_CP007588.1\|WP_038527995.1\|73283_74060_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293819	cd07733, YycJ-like_MBL-fold, uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain. Includes the uncharacterized Bacillus subtilis YycJ protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	1.11364e-63
NZ_CP007588.1\|WP_009495694.1\|71085_72402_+\|yycH-family-protein	gnl\|CDD\|276948	cd15787, YycH_N, N-terminal domain of YycH and similar proteins. This protein appears to be a member of a somewhat larger structural family conserved in Firmicutes. YycH plays a role in signal transduction and is found immediately downstream of the essential histidine kinase YycG. YycG forms a two-component system together with its cognate response regulator YycF. YycH functions as a modulator of YycG activity, possibly by interacting with YchI. All three molecules (YchG, YchH, and YchI) have been characterized as membrane proteins, and they may be able to form homodimers. This model describes the N-terminal domain of YycH.	3.35976e-15
NZ_CP007588.1\|WP_009495674.1\|96472_97897_+\|dipeptidase-PepV	gnl\|CDD\|235988	PRK07318, PRK07318, dipeptidase PepV; Reviewed.	0
NZ_CP007588.1\|WP_038528011.1\|99075_99663_+\|guanylate-kinase	gnl\|CDD\|223272	COG0194, Gmk, Guanylate kinase [Nucleotide transport and metabolism].	8.40605e-34
NZ_CP007588.1\|WP_009495689.1\|76348_77713_+\|HD-domain-containing-protein	gnl\|CDD\|224004	COG1078, COG1078, HD superfamily phosphohydrolases [General function prediction only].	1.67403e-119
NZ_CP007588.1\|WP_038528001.1\|81285_82548_+\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	gnl\|CDD\|183779	PRK12830, PRK12830, UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Reviewed.	0
NZ_CP007588.1\|WP_009495687.1\|78652_79234_+\|DNA-directed-RNA-polymerase-subunit-delta	gnl\|CDD\|275360	TIGR04567, DNA-directed_RNA_polymerase_subunit_delta, DNA-directed RNA polymerase delta subunit. Members of this family are the RNA polymerase delta subunit, as found in the Firmicutes and the Mollicutes. All members of the seed alignment have an extended C-terminal low-complexity region, consisting largely of Asp and Glu, that is not included in the model. Proteins giving borderline scores should be checked to confirm a similar acidic C-terminal domain. [Transcription, DNA-dependent RNA polymerase].	4.06991e-38
NZ_CP007588.1\|WP_009495673.1\|98036_99008_+\|DUF1002-domain-containing-protein	gnl\|CDD\|377628	pfam06207, DUF1002, Protein of unknown function (DUF1002). This protein family has no known function. Its members are about 300 amino acids in length. It has so far been detected in Firmicute bacteria and some archaebacteria.	3.05412e-35
NZ_CP007588.1\|WP_009495680.1\|86418_88713_+\|AAA-family-ATPase	gnl\|CDD\|226482	COG3973, COG3973, Superfamily I DNA and RNA helicases [General function prediction only].	9.70788e-121
NZ_CP007588.1\|WP_038566597.1\|91211_93971_+\|LPXTG-cell-wall-anchor-domain-containing-protein	gnl\|CDD\|227596	COG5271, MDN1, AAA ATPase containing von Willebrand factor type A (vWA) domain [General function prediction only].	1.18258e-15
NZ_CP007588.1\|WP_009495679.1\|88792_89809_+\|tryptophan--tRNA-ligase	gnl\|CDD\|183400	PRK12282, PRK12282, tryptophanyl-tRNA synthetase II; Reviewed.	0
NZ_CP007588.1\|WP_009495688.1\|77742_78555_+\|Cof-type-HAD-IIB-family-hydrolase	gnl\|CDD\|182509	PRK10513, PRK10513, sugar phosphate phosphatase; Provisional.	1.91423e-81
NZ_CP007588.1\|WP_009495678.1\|89825_90758_+\|exopolyphosphatase	gnl\|CDD\|274735	TIGR03706, exo_poly_only, exopolyphosphatase. It appears that a single enzyme may act as both exopolyphosphatase (Ppx) and guanosine pentaphosphate phosphohydrolase (GppA) in a number of species. Members of the seed alignment use to define this exception-level model are encoded adjacent to a polyphosphate kinase 1 gene, and the trusted cutoff is set high enough (425) that no genome has a second hit. Therefore all members may be presumed to at least share exopolyphospatase activity, and may lack GppA activity. GppA acts in the stringent response. [Central intermediary metabolism, Phosphorus compounds].	5.26159e-77
NZ_CP007588.1\|WP_009495693.1\|72430_73237_+\|regulator-of-two-component-system,-YycI-family-protein	gnl\|CDD\|378229	pfam09648, YycI, YycH protein. This domain is exclusively found in YycI proteins in the low GC content Gram positive species. These two domains share the same structural fold with domains two and three of YycH pfam07435. Both, YycH and YycI are always found in pair on the chromosome, downstream of the essential histidine kinase YycG. Additionally, both proteins share a function in regulating the YycG kinase with which they appear to form a ternary complex. Lastly, the two proteins always contain an N-terminal transmembrane helix and are localized to the periplasmic space as shown by PhoA fusion studies.	2.52151e-27
NZ_CP007588.1\|WP_009495686.1\|79398_81012_+\|CTP-synthase	gnl\|CDD\|235437	PRK05380, pyrG, CTP synthetase; Validated.	0
NZ_CP007588.1\|WP_009495681.1\|85998_86358_+\|type-II-toxin-antitoxin-system-PemK/MazF-family-toxin	gnl\|CDD\|367091	pfam02452, PemK_toxin, PemK-like, MazF-like toxin of type II toxin-antitoxin system. PemK is a growth inhibitor in E. coli known to bind to the promoter region of the Pem operon, auto-regulating synthesis. This family represents the toxin molecule of a typical bacterial toxin-antitoxin system pairing. The family includes a number of different toxins, such as MazF, Kid, PemK, ChpA, ChpB and ChpAK.	7.17015e-38
NZ_CP007588.1\|WP_009495690.1\|75744_76173_-\|DUF1934-domain-containing-protein	gnl\|CDD\|378129	pfam09148, DUF1934, Domain of unknown function (DUF1934). Members of this family are found in a set of hypothetical bacterial proteins. Their precise function has not, as yet, been defined.	2.47895e-24

>NZ_CP007588.1|WP_038528001.1|81285_82548_+|UDP-N-acetylglucosamine-1-carboxyvinyltransferase
MKKLVIRGGRPLSGEVTIGGAKNSTVALIPAAILSEDPVRFDNVPDILDVYNLQVILESMNVKSDFTDGVLTIDPTQIVEAELPSTAIKSLRASYYFMGSLLGRFGRATVTFPGGDNIGPRPIDQHIKGFEALGATVTEENDTVHIVAENGLKGARIFLDMVSVGATMNIILAAVHAEGTTILENAAKEPEIIDLAMFLNNMGADVRGAGTDVIRIAGVEHLGSQATHTIIPDRIEAGTYLSIAAAQGEGVLVKNVIPEHMEAFISKMIEMGVELDVRDDSIYVPASKDLKPITVKTAPYPSFATDLQQPITPLLSRAQGESKIVETIYPARTRHVPELNSLGMVIESNESGLITIGHTDKMEGAVVKAAEIRAGAALVIAGLMSDGETIVEDAEHVLRGYDHIITKLTNLNADIEIVED
>NZ_CP007588.1|WP_009495686.1|79398_81012_+|CTP-synthase
MATKYIFVTGGVVSSLGKGIVAASLGRLLKNRGFKIAVQKFDPYINIDPGTMSPYQHGETFVTYDGLETDLDLGHYERFIDIAVNRYSNFTAGRIYSEVLEKERHGDYEGATVQVIPHITNMLKEKMMMAGKTTDADIVITEVGGTVGDIESLPFVEALRQMKREVGEENVFYIHTSLIPFLRAAGEAKTKPTQHSVSELRSLGIQPDMLVVRTENPISQDMRDKLALFTDVAPEAVIESLDVDILYQVVLNMQEQGMDDVVLKGLHLDAPTADMTDWTNMVDGIRNLSNKVKVALVGKYADLQDAYISVNEALRAGGYAIDTAVEINAINSELITDENVEEYLGDADAVMVPGGFGTRGTEGKLAAIKYARVNNVPFLGVCLGMQLATVEYARNVLGYEGANSIELDPETSHPIIALMNDQKAVTNIGGTLRLGLYSEMIKEGTKAFELYGQQEVQHRHRHRYEFNINFKDVFEEAGMVFSATSPDGTLMEMIELPENDFFMAAQAHPEFQSRPNHAEPLYAGLIKAALDQKMAKN
>NZ_CP007588.1|WP_009495687.1|78652_79234_+|DNA-directed-RNA-polymerase-subunit-delta
MAITQFEGQNKSELSMIEVARAILSDRHETMAFSDLLNEVQSFTGKTDDEIRARLAQFYTDLNIDGSFISLGDNVWGLRSWYPIDSIDEAVHLDLEEEEATAKPKKKRKKINAFLADVADDDDVIDYNDDDPEDDDFGAVETSKNEDEDAEAADDDSDDDSDDDFDEVAGGIGEEIGGIAPVDDDYGSGDIEK
>NZ_CP007588.1|WP_009495688.1|77742_78555_+|Cof-type-HAD-IIB-family-hydrolase
MIKLVTIDIDDTLVNSAKEITPRVKAAVQAATAAGVKIVLTTGRPITGVQAYLDELGLNNLEDQYVVTYNGAMIQTTAGTTIGGNPLNHAAYVKLADWAVEHDYYIQVESSAEAFTPSRKVNPAASGENYMINMPLNIVDVADMDPELAYVKFMFIEPAARLQEVRADLDKTDFAQEFTFVQSSTQFLEVLNQAASKGNALRTLAGHLNVDISETMAIGDQANDLTMIEAAGLGVAMGNAVPAIKAAAQEETTTQNEDGVGVALEKFVLA
>NZ_CP007588.1|WP_009495689.1|76348_77713_+|HD-domain-containing-protein
MAEVNKETIFRDPVLNSVVVKDQLILDLIGTTEFQRLRRIKQLGSANSVFHGAEHSRFSHSLGVYEIARRFSEQLAEFHATKVPGDGLWDPNERIVLLSAALLHDLGHGPYSHTFEHIFGTNHEDYTRAIITEPGTQINTVLKAYDPELPQKVADVINKTYANRQVVQLISSQIDADRMDYLLRDAYYTGATYGEFDLSRIIQMVRPYEGGIAFEEKGLYAIEDYVVSRYQMYVQVYFHPVSRSLEILLTHLLERAQYLFEEDAKSTRIDKNFISPALQVAFKHQDAIPVSEYLRLDDNVLLADISQWRFHSDAVLADLATRFIDRHPLKSIEVTDETRHLLPTLRALINDAGFEPRYYTAENDSFDQPYSDHQLQGKSPKTQIELIAQDGTLTDLSNGSAVVSTLMGRAFGDARFFFPKEMLQTDATGDLMADVYTDFQRYVRNGRLVVPTDK
>NZ_CP007588.1|WP_009495690.1|75744_76173_-|DUF1934-domain-containing-protein
MPQETAIALTAISKITQENQSETIETVTSGTATEMANATYIRYIEETSVDDTTLQTNVTIKLADDNTLQIRRSGAANARLTFDLTQPTTTHYRTAVGNFVFDIHTSALSINTTDGTCHVAYALKSGDDLIGHYDFALNYTTV
>NZ_CP007588.1|WP_009495691.1|74314_75490_+|PDZ-domain-containing-protein
MNSYETKGSGSDMKKTMKTVVIALLAGLIGGGLSVGLGAYYGVFEPKTEKVVNSSDTKVADTAVKDDSKATQAFKSVSGAIVSVINLQGSQNSDELLETASEGSGVIYKSSGRDAYVVTNNHVVDGSKKIQILMQDGTKEPAELVGTDVETDLAVLKISNKAVKDVAKFANSDQLQPGETALAIGSPLGSEYATSVTEGIISAPKREIETQAPNGQRLGKTTVIQTDAAINPGNSGGALVNLAGQVVGINSMKLSTSQSGTAVEGMGFAIPANTVVKIIEALEKDGKVTRPSLGVSLYDLSNISSVDQADVLKLPTKVKTGVVVIKTTRDGSAEKAGLKKFDVITKLNDISVSDANDLRNALYKFDVNEKITVTYYRDGKEQTVQLQLQSN
>NZ_CP007588.1|WP_038527995.1|73283_74060_+|MBL-fold-metallo-hydrolase
MLASSSTGNVTYVETPGRKVLLDAGLSGKKIEGLMQEVDRSLADVDSIFVSHEHSDHIAGVGILSRKYDMDIYANEETWAAMAPKIGKIAPEHIKICRPGEVIDLGDLEVESYSVSHDAANPQFYSFHHANKTFAALTDTGYVNDRMLSSLRNADALLFESNHDYEMLRMGSYAWSLKQRILGDKGHLSNEDGALALAEVIGSRTKNVFLGHLSQENNQQELAYLTVKGILEAKDFAVNHDFLMHNTEPLSASRLIDI
>NZ_CP007588.1|WP_009495693.1|72430_73237_+|regulator-of-two-component-system,-YycI-family-protein
MNIRKMLWTFLYLFLIVDGILLYQWVSVNDTVVDPASAKNIQQEIRMDGISFDSLDAHVPSGAYYSGEDGGSYLNKQKNQISDDWRVNVSGEKLRATPKEPVDLGDSMNSAKETLEKLVSDERNVISGEDYVYDPELSSNDNQDGLRVIVFSQKIGQETFVSSRGQIQFSFDEYFNLKSYTQTYVTGIQLLSEVPAILSERSAFFNAYQFNEIPNNSTLDWRKPGYATLMDVRGETIYIPVWTFSLTNAAGEKTMVRINALNGSLIKN
>NZ_CP007588.1|WP_009495694.1|71085_72402_+|yycH-family-protein
MNRRKWRALLKQYLLIVVLMILVAVSLMLSFGIWSSLGDRPLYIAPSESADSDKRLVSEKDIVSVYDFDNVVVNQKGKQQLVMNSRSITREVLAVMGDWQINTVTAEKLDEKQYLKLMNEKNTVLLGYPDQVVGSLVESRLNLGIGLTDDDRVDRVQLPLSGKGQVRFFNDRTRDVYTASIMTPGTSLDDIKWPKNMTDVNFEWRQNRLRMNYLSETKLKTKSYLLDESKRADVVATAFKSARVTPYLVDTPDDKVEYTDGDTRRLVLNKQSGNVEMTEYDSKTMPRAMSSNMTHAYDTLVALKQVPENMYYFEELEDGMKLSYRLYVEGLPMFMSENFDFGTISVTYESNRQTVDYSVYGIQVPLPDKNEKTITLDNTETVMEKLTDAGVDTKKVQGLTMGYSWLENDEEGYITLQPAWFVQMKDEWLPVTFYTGAV
>NZ_CP007588.1|WP_009495681.1|85998_86358_+|type-II-toxin-antitoxin-system-PemK/MazF-family-toxin
MGKEVEVKRGDVFFINLDPVVGSEQGGQRPAVIIQNNVGNRYSPTVIVAPITARISKPKMPTHVALPAETKLTGVNRNSVILCEQIRTIDKQRLQDKIGMLPGKIVTELNKAIAVSVNV
>NZ_CP007588.1|WP_009495680.1|86418_88713_+|AAA-family-ATPase
MEEQEWQLERQRLVVVNEELATQLVDSELEYEKAHAETSAVERNYGANTSINTLEEDDSMETNAEIQQQRNIVARVTETENIMQKKLQTLKTLTGSPYFGRVNLVEDGYKEKLYIGLASLQGEDGDFLINDWRAPISGVYYNGVLGKVTYPTPVGEQEAFLEKKRQFTIEDGEIVNMFDTDVTIGDEMLQYTLGQQNDDTMHNIVATIQQEQNRIIRDTESDLLVVQGVAGSGKTSAILQRIAFLLFHAREELNSDQIVLFSPNRLFSSYIADVLPSLGERNMRQVTLHEFLSARLQGLQVQTLFERYEHADEVVQTARQAMTTAIEAPELYDCLVNYLSQVRPQEVRFADVYFDDEIWFSADEFKEVFASFPAAYSFVERMKMTQEVFLERLTEQYTELIHDEWVELGLDALSNQEYQALRLNQDGDLMDDEDTHAIHEEVAQRYVAERLRSVDDAVYNFAFVDVYAQYADFLVALGDMQYATLNADWWALKAERYSQQLELHKIDYEDAIPVLYLRDLMTGAGTNQYMQYIFVDEMQDYTQLQMLYLKHAFPRAKFTLLGDAEQALFRAVETPSELLGKYKTIFGDQRVSFVQLNKSYRSTTEIMDFAKALLPDGDEIVSFERHGAKPELSVLSMDDISEELATLIGDIQTRQQTVAVVTKTQQDAHIVGEALRRFEIQHQVIENEDRTRDEHVLVLPIYLAKGLEFDAVVGYDVSAENYPDDESVGLLYTLASRAMHELHLISKGPATPLLETVMSYITLK
>NZ_CP007588.1|WP_009495679.1|88792_89809_+|tryptophan--tRNA-ligase
MTNKKVLLTGDRPTGQLHIGHYVGSLKNRVAMQNSGDYTPFIMIADKQAFTDNARDPEKVHNSVLQVALDYLAIGIDPSKTTIFIQTSVPALSELTEYFLNLVTVARLQRNPTVKAEIQQKGFGSSIPAGFFTYPVSQAADIALFKGEVVPVGDDQEPMIEQSREIIRTFNNYYGDILVEPEAVFPPKGHGRIPGLDGDAKMSKSLGNAIYLADDEETLWTKVKSMYTDPTHLHVEDPGHVEGNMVFTYLDIFDPDTEKVAELKAQYQAGGLGDMKIKKYLFEVLNNELGPIRERRAKLAENPEAVMQMLAEGSAKARAAAEVTMQEVRDAMGINYWN
>NZ_CP007588.1|WP_009495678.1|89825_90758_+|exopolyphosphatase
MGSYLAIVDLGSNSTRMVVEELQGDGEFRELKRRKIDTRLAEGMQENAGALTTDAINRVLDALREFQDVYMQYPNVKVRGIATAAVREATNQSEFLAHVKQAINLDIQVLSGDEEAYYDYLGVVTSLPDVEDAWLLDTGGASVELADIVSQADQNLTSLPFGAVNLSEKFNLNLETVELSSVESAMKSVQQQYFDLGWIKPQGDRPVVLLGGANRVLARLDRERKGLSNSNDFHGYRMQAADIIQIFKEMVLMPCSERRVLLNKDANRADIMLGGLVPLVVLLNQTGAKEVLFSSSGVREGLLQEYKKQY
>NZ_CP007588.1|WP_038566597.1|91211_93971_+|LPXTG-cell-wall-anchor-domain-containing-protein
MINKMKISGRLMTVVVTVVLGLFVGTHVQANVIDASPFMDKVSTNVKEFHPRETGEITIEFSEKNGHTFKPGDEIVFKLPAELKGFGQNMWLDDFAQVRVLKDRVVVKFTGKIHDRKNTKIKISFGVKGSEDVARGSHRDVPLHLGTAMADYPSVLVHGYPEENNQQQGDVDFAYKGGSVNEDDARLIDWYIVVNPMNLQVADDVFIRDVLGFGHELVPGSIMIDGEPVPEKQDVLNAKKRSFDLVLSQSFVNGRGVGIFYQTRLNSVGESMKNLTNSFTADFQIKNARKDQITDSASVSNVLMSGSLGGDMVEHHANQDEEVIPDESGNLETLEDVESGNATETEVENHATENVETNQPEIHVDVREEEIPDESDKWEELEEIETNNATETEVENHATENVETNQPEIHVDVREEEIPDESDKWEELEEIETNNATETEVENHATENVETNQPEIHVDVREEEKADESDKLEELEEIETNNATETEVENHATENVETNQPEIHVDVREEENVDESDKLEELEEIETNNATETEVENHATENVETNQPEIHVDVREEENADESDKLEELEEIETNNATETEVENHATENVETNQPEIHVDVREEENADESDKLEELEEIETNNATETEVENHATENVETNQPEIHVDVREEENVDESDKLEEFDESGNLKDLEDYTTGEDDNLGVHLETHEELLDESDKLEELEEIETNNATETEVENHATENVETNQPEIHVDVREEENADESDKLEELEGIETNNATETEVENHATENVETNQPENHVDVREEENADESDKLEELEAIETNNATETEVENHTTENVETNQPEIHVDVREEENADESDKLEELEAIETNNTTETEVENHATENVETNQPEIHVDVREEDENVTGHEELPMTGSKSNYWIVLLGVLMMFGLLFKRRILK
>NZ_CP007588.1|WP_009495675.1|94583_96287_+|LPXTG-cell-wall-anchor-domain-containing-protein
MKNAMITRPIWVVMAVFSFVIAMFVGVSAHASVIDSSPFVDKITSSQNVFQPREIGEISMEFSEKEGHEFQPGDELVFTLPEEFKGFANKMMLEDYAEVIVEANRVRVIFNDKVTKKNHIKGSLKFSIKATENIERGTSKEVNLDLGTKANPFPNVTVHGYPVANEGDGGNQTAPDFAYKGGNVNENDAELIDWYIVVNAGRLQVSGDTLVRDTLGKGHEFVEGSITINGQPLTAEQGKLVVNGNSFEMTLRDAAVSGNTIGINYQTRLTEDGKKQKTLSNDFKADYQILNESPTSIEGASSVKNVLMSGAIEGDEEEEKTPTEETEEIPFEEVEELEEVTPDHGNVTEEEDNMHNVDEPKKEEIHVDETEEEVPFEELEELEEVTPDHGNVTEEEDNMHNVDGSKEEEIHVDGTEENVPFEEVEELEEVTPENGNVTEQENNANESAEVTQPEVHVAPEETKPTPEVIEPKKEEKVTPKKENKTTPKVTAPKKENKTTPKTVKAIVPAKKEEKTVAPVSKKTVAKSETVKAAELPNTGSEDNKLFAVVGLVLMAFAGLLFRRRSAK
>NZ_CP007588.1|WP_009495674.1|96472_97897_+|dipeptidase-PepV
MTTEQGKWLSNSLKYEDALLTDLKEMLAIESVRDDAAATELAPLGPGPAAALDKFVALAERDGFRTGMFKNLVAYAEMGPEDAEESVAVIGHLDVMPAGDGWTKDPFTPTIEDGRLYARGASDDKGPTFTAYYAMKMLKDMGVPLKRKITFVVGIDEESDWTGMDEFFAEYGEPTMGFSPDAEFPIINGEKGNVSVVTRFSGENGSGDYLVSFAAGERPNMVPGTAIAVVKTDAAAAMVESMEAYLAAETRVTGEASVDGDQVTFKFFGRQVHGAKPETGLNAGTFLANFLQTKNFDADAAGFLALLGDKLHDDTVAEKIGAATHDDLMGDLSMNVGIQRFAANEDGFIDANFRYPQNITAAQIEADLRDALPAKFAASVAIEGHGMTPHYVPGNDPLVETLLRVYREQTGLPAGELVIGGGTFGRLLKRGVAFGAMFEGVPDTMHQADEFYPVADLTRSMAIFAQSMNDLANY
>NZ_CP007588.1|WP_009495673.1|98036_99008_+|DUF1002-domain-containing-protein
MWKKVGTIVLTTVVLGGLVGTSHVSAMATGEQQRALNKPYVVYGDAAQQKHQIAQTLGVTSNYTQLTTKGSDAAYLGLQGVSDSVMISSVALAPGKAGAGTLVNIEAFEAKNNITQVTAQQYAMAATMAGVKDVIITVTANVPVSGEAALAGVYKALEADGVDLNNENTTAANDVLSSTSAAISENANDGKYAGKLTSAVTQTTSDLAADKQAGKNITINIIIDKLIVNLDKQGIKDQTGEANINAIANSIQLVNNAPISDSADFVKSANNLADTLSNSAGDLMAKAKDFANSQDAKEVANWFTINIWEPVKNFFSGLFGGNQ
>NZ_CP007588.1|WP_038528011.1|99075_99663_+|guanylate-kinase
MEREKVKNLQRRVFVVTGNTGTGKTTVTKYLNEFYEMPKVITHTTRPPREGEEDGVDYYFESNDSFDRNHFLEEVSYSGYKYGSSVEGLERAWEKNQLITIVLDPMGAVTYLQDLPEGEVVVIYLDVSERADLLERLEKRGDDVEAIAQRLNSEEYQRDLMILPGLKERAHVVMNDDWDAARSEIDEIVQSAIRV
>NZ_CP007588.1|WP_009495671.1|99681_100062_+|hypothetical-protein
MKKRTPPFITPVALLSLIIALSAGNAVVNVSTNTRNGAPVKETSEKKDTSSLSTESANEETTSNNTTSETSSAVSKSPNDISESESTVSGQSNSESSVLPSESSSSVTSSSSSSEVVADVAKKEAE

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Crispr_ID: NZ_CP007588_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP007588_3

1313645-1313822

Orphan

Consensus_repeat	Method
TACCACTGTTTGCTTGTAGTTGGTTCAATCCACCAGCTAATGTTTGACCACCT	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP007588_3

>merge|NZ_CP007588|3|1313645-1313822|PILER-CR
ACCACTATTGGCTTGTAGTTGGTTCAATCCACCAGCTAATGTTTGACTACCTGCATTCAACTTACCACTGTTTGCTTGTAGTTGGTTCAATCCACCAGCTAATGTTTGACCACCTGCATTCAGCTTACCACTGTTTGCTTGTAGTTGGTTCAATCCACCAGCCAATGTTTGACCACCT

>NZ_CP007588|3|1|1313645-1313822|PILER-CR
ACCACTATTGGCTTGTAGTTGGTTCAATCCACCAGCTAATGTTTGACTACCTG	CATTCAACTT
ACCACTGTTTGCTTGTAGTTGGTTCAATCCACCAGCTAATGTTTGACCACCTG	CATTCAGCTT
ACCACTGTTTGCTTGTAGTTGGTTCAATCCACCAGCCAATGTTTGACCACCT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP007588.1\|WP_009765165.1\|1303813_1305631_+\|FAD/NAD(P)-binding-protein	unknown	unknown	gnl\|CDD\|379196
NZ_CP007588.1\|WP_009765176.1\|1319024_1320086_+\|tRNA-dihydrouridine-synthase	unknown	unknown	gnl\|CDD\|223120
NZ_CP007588.1\|WP_009765170.1\|1310814_1311300_-\|PTS-glucose-transporter-subunit-IIA	unknown	unknown	gnl\|CDD\|376324
NZ_CP007588.1\|WP_009765171.1\|1311313_1312027_-\|trehalose-operon-repressor	unknown	unknown	gnl\|CDD\|274116
NZ_CP007588.1\|WP_009765182.1\|1323812_1325159_-\|amino-acid-permease	unknown	unknown	gnl\|CDD\|224038
NZ_CP007588.1\|WP_009765177.1\|1320161_1321127_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_CP007588.1\|WP_009765166.1\|1305688_1306087_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP007588.1\|WP_009765180.1\|1322546_1322759_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP007588.1\|WP_009765175.1\|1316130_1318764_-\|cation-translocating-P-type-ATPase	unknown	unknown	gnl\|CDD\|319781
NZ_CP007588.1\|WP_009765168.1\|1306901_1309247_-\|glycoside-hydrolase-family-65-protein	unknown	unknown	gnl\|CDD\|224471
NZ_CP007588.1\|WP_009765183.1\|1325326_1326451_-\|AI-2E-family-transporter	unknown	unknown	gnl\|CDD\|223701
NZ_CP007588.1\|WP_009765163.1\|1302542_1302761_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP007588.1\|WP_009765167.1\|1306224_1306896_-\|beta-phosphoglucomutase	unknown	unknown	gnl\|CDD\|213672
NZ_CP007588.1\|WP_081580100.1\|1312309_1312576_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_CP007588.1\|WP_009765178.1\|1321300_1321645_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP007588.1\|WP_009765169.1\|1309295_1310798_-\|PTS-transporter-subunit-EIIC	unknown	unknown	gnl\|CDD\|273919
NZ_CP007588.1\|WP_009765179.1\|1321672_1322554_-\|YihY/virulence-factor-BrkB-family-protein	unknown	unknown	gnl\|CDD\|377085
NZ_CP007588.1\|WP_009765164.1\|1303145_1303805_+\|NAD(P)H-hydrate-epimerase	unknown	unknown	gnl\|CDD\|223140
NZ_CP007588.1\|WP_009765174.1\|1315464_1315920_-\|Rrf2-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224870
NZ_CP007588.1\|WP_009765181.1\|1322771_1323674_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223730

Protein	Function_ID	Function_description	E-value
NZ_CP007588.1\|WP_009765165.1\|1303813_1305631_+\|FAD/NAD(P)-binding-protein	gnl\|CDD\|379196	pfam13454, NAD_binding_9, FAD-NAD(P)-binding.	1.91192e-32
NZ_CP007588.1\|WP_009765176.1\|1319024_1320086_+\|tRNA-dihydrouridine-synthase	gnl\|CDD\|223120	COG0042, COG0042, tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis].	3.99509e-70
NZ_CP007588.1\|WP_009765170.1\|1310814_1311300_-\|PTS-glucose-transporter-subunit-IIA	gnl\|CDD\|376324	pfam00358, PTS_EIIA_1, phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 1.	7.39594e-56
NZ_CP007588.1\|WP_009765171.1\|1311313_1312027_-\|trehalose-operon-repressor	gnl\|CDD\|274116	TIGR02404, Trehalose_operon_transcriptional_repressor, trehalose operon repressor, B. subtilis-type. This family consists of repressors of the GntR family typically associated with trehalose utilization operons. Trehalose is imported as trehalose-6-phosphate and then hydrolyzed by alpha,alpha-phosphotrehalase to glucose and glucose-6-P. This family includes repressors mostly from Gram-positive lineages and does not include the TreR from E. coli. [Regulatory functions, DNA interactions].	1.23345e-73
NZ_CP007588.1\|WP_009765182.1\|1323812_1325159_-\|amino-acid-permease	gnl\|CDD\|224038	COG1113, AnsP, Gamma-aminobutyrate permease and related permeases [Amino acid transport and metabolism].	2.14769e-178
NZ_CP007588.1\|WP_009765177.1\|1320161_1321127_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	2.44521e-16
NZ_CP007588.1\|WP_009765175.1\|1316130_1318764_-\|cation-translocating-P-type-ATPase	gnl\|CDD\|319781	cd02089, P-type_ATPase_Ca_prok, prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL and Listeria monocytogenes LMCA1. Ca(2+) transport ATPase is a plasma membrane protein which pumps Ca(2+) ion out of the cytoplasm. This prokaryotic subfamily includes the Ca(2+)-ATPase Synechococcus elongatus PacL, Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1) which has a low Ca(2+) affinity and a high pH optimum (pH about 9) and may remove Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH, and the Bacillus subtilis putative P-type Ca(2+)-transport ATPase encoded by the yloB gene, which is expressed during sporulation. 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
NZ_CP007588.1\|WP_009765168.1\|1306901_1309247_-\|glycoside-hydrolase-family-65-protein	gnl\|CDD\|224471	COG1554, ATH1, Trehalose and maltose hydrolases (possible phosphorylases) [Carbohydrate transport and metabolism].	0
NZ_CP007588.1\|WP_009765183.1\|1325326_1326451_-\|AI-2E-family-transporter	gnl\|CDD\|223701	COG0628, yhhT, Predicted permease, member of the PurR regulon [General function prediction only].	3.49862e-61
NZ_CP007588.1\|WP_009765167.1\|1306224_1306896_-\|beta-phosphoglucomutase	gnl\|CDD\|213672	TIGR01990, bPGM, beta-phosphoglucomutase. This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides].	8.36791e-81
NZ_CP007588.1\|WP_081580100.1\|1312309_1312576_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	9.46399e-15
NZ_CP007588.1\|WP_009765169.1\|1309295_1310798_-\|PTS-transporter-subunit-EIIC	gnl\|CDD\|273919	TIGR01995, beta-glucosides_PTS_EIIBCA, PTS system, beta-glucoside-specific IIABC component. This model represents a family of PTS enzyme II proteins in which all three domains are found in the same polypeptide chain and which appear to have a broad specificity for beta-glucosides including salicin (beta-D-glucose-1-salicylate) and arbutin (Hydroquinone-O-beta-D-glucopyranoside). These are distinct from the closely related sucrose-specific and trehalose-specific PTS transporters.	6.39418e-126
NZ_CP007588.1\|WP_009765179.1\|1321672_1322554_-\|YihY/virulence-factor-BrkB-family-protein	gnl\|CDD\|377085	pfam03631, Virul_fac_BrkB, Virulence factor BrkB. This family acts as a virulence factor. In Bordetella pertussis, BrkB is essential for resistance to complement-dependent killing by serum. This family was originally predicted to be ribonuclease BN, but this prediction has since been shown to be incorrect.	3.34103e-31
NZ_CP007588.1\|WP_009765164.1\|1303145_1303805_+\|NAD(P)H-hydrate-epimerase	gnl\|CDD\|223140	COG0062, COG0062, Uncharacterized conserved protein [Function unknown].	4.71446e-55
NZ_CP007588.1\|WP_009765174.1\|1315464_1315920_-\|Rrf2-family-transcriptional-regulator	gnl\|CDD\|224870	COG1959, COG1959, Predicted transcriptional regulator [Transcription].	9.43537e-21
NZ_CP007588.1\|WP_009765181.1\|1322771_1323674_-\|alpha/beta-hydrolase	gnl\|CDD\|223730	COG0657, Aes, Esterase/lipase [Lipid metabolism].	5.08034e-23

>NZ_CP007588.1|WP_081580100.1|1312309_1312576_+|helix-turn-helix-transcriptional-regulator
MNHTKLLRSLQKSLLPKSPHGMSQTSHFDKNMRYFRLQSQLRKKELAALLNVDTSTISNYERGRRRPNFDTLIQLSDIFDVTIDELLR
>NZ_CP007588.1|WP_009765171.1|1311313_1312027_-|trehalose-operon-repressor
MDKYQNIYRDMLDDIKSGKYTSGEFLPSDTKLVMKYNVSRETVRKAMVNLAHDGYVQRLKGKGTIVLDRQRVAIPMSQLKSYREVMVEGNITSTNDVLFLEENHEVPENLRIESAIDSDLMSTKLIRRRNVGGEATVIDYDYINQAVVDHLPREAAAESIFNYFEHDLGLQIDYAIKHMTIEPANQQDHKGLGVAIGSPVVVIRSETHLTDNRLLSFTESRHRADRFSNVEFSRRRN
>NZ_CP007588.1|WP_009765170.1|1310814_1311300_-|PTS-glucose-transporter-subunit-IIA
MFGFGKKKDVVVDDKLYAPVNGTVIDLTVVPDPVFSGKLMGDGFAIEPTSARVVSPVSGEVTMVQGHALGFKRADGLEILMHMGIDTVSLDGAPFEMMVKEGDVVEAGEAVANVDWDQITAAGLPTTTMIVITNTADKLAALNVTTGDVTAGAIVGEATAN
>NZ_CP007588.1|WP_009765169.1|1309295_1310798_-|PTS-transporter-subunit-EIIC
MAKKDYSALVAEIIENVGGKDNVDNAIHCVTRLRFYLKDPSKAQTEKIEALDGVAGAVYNEQLGQYQVVIGQAVADVYEELAEQLGLSPDEEPEKTGDKKPHSIGGMFQALVGTITGSMIPIIGLLAAGGMINGLLTLMSEPTLLNWIDSGSDTYVILSSMAMAPFYFLPVLVGFSAAKQLKSDPYVVAAIGGFMIHPAVQALTTPHIAGDTIVKPEILGTLFGVPLNATYMGLSINIPNYAYTIFPIIFAAWLARPVGNFFKNHLPLALRPILQPMFTLFIVGSIVLIGVGPVISIVSSGIAALITGLINLNLAIASFIIGGLYQVLVIFGLHWMVIPILTQQIAETGQSNINMIVSFTMLAQGAGALAVFFKAKNAALKALAGSGALSAFAGVTEPAMYGVNLKYGRVFITSSIGAAFGAGLAGLLDLHMYGFSGSLIGFPNFASPADNPNNFMVFWLATAVTMIISFTLTYFFGFKNDGVVKEDVAKKNVFKDAVEK
>NZ_CP007588.1|WP_009765168.1|1306901_1309247_-|glycoside-hydrolase-family-65-protein
MAEKAWRLMYNGLETEKRAYGQESLLTLGNGYVGWRGASVFQSFDEHNYPGLYVAGVFNQTRTEVANKDVVNEDMVNLPNPQLFKLTLDDQPVVINHDTITHREAGVDFQNGLFTEELTVAVPQGQLTLRTVKAVDPKQYHMLGIQLAITADFSAQLQVESIIDGTLLNQNVARYRAFDSREFNVTEIAGDILTAKTRSTDIDIVVGAETTSDVMTFQNVEGPADMQVSTGEVTLQTNQTVQIDKLIAIGTSYELSEPLVFVQAALATHSVDKVIESSTAYWQEVWETADIQLDSDDPDMQLMIRMNIFHIRQAAQHEANKDLDASVGSRGLTGEGYRGHIFWDEIFVVPYYAANDPETARDILRYRIKRIDAAKKNAILDGEAGAMFPWQSGMYGDEQSQFIHLNTVNNEWEPDNSRLQRHVSLTIAYNIWVYTQITGDTSLLREGGLELLLETTKFWLNKAEEDADGRYHIAGVMGPDEYHEAYPGTEAGGIKDNAYTNLMLTWSLNWLLELAETQTEMFESVAHETDFGSDWLNLAKNVSKGLALEISPEGIIAQYAGYFDLEAVDFAAYEAKYGDIHRIDRLLKAEGLSPDDYQVAKQADTLMTIYNLGNRHMAKLVAQLGYDLPENWLALNKDYYLARTVHGSTTSRPVFAGIDVTLNNMDEALDYLTTAIGSDYYDIQGGTTAEGVHIGVMGETLEVIQNEFGGVMLRDGLVSIAPNLPTSWHRLAFTQKYRGTMLTFEMTPEAVTVMADAPLDVEVYGQPVSLAANTAQTFTKG
>NZ_CP007588.1|WP_009765167.1|1306224_1306896_-|beta-phosphoglucomutase
MTFENIKGFAFDMDGVLADTAKFHSIAWRQIAEEVGTTWTPELAENLKGIDRMGSLDLILTTGGMADEYDLAAREALATKKNDNYRNLISELTPDDALPGMREFLAELKAAGYKMSIASASKNAGFIVDRLGISDYFEAIVDPASVAAGKPDPAIFKAAADVLNLAPEEVIGLEDSGAGIQSINGAGEMSVGIGDADALSDADILFASTKDVTLANIKANWPK
>NZ_CP007588.1|WP_009765166.1|1305688_1306087_-|hypothetical-protein
MMIKKKWASLLPFQQNLVALVVGVFIVTLVSNIITGREVWYNMSFVIMLIGMYVTWMLLEKFTRTSVQRFVIPFVIVWVGLSISSFFDGSYCDYTTFIVTGAVAAFVAVMMMLGAKLVETQLAEHEKESNDD
>NZ_CP007588.1|WP_009765165.1|1303813_1305631_+|FAD/NAD(P)-binding-protein
MQIALIGAGPRNLILTERLITYANQSIMPVTITLFDPFPIGGRVWSPEQNPTFIANTIASHATLFSDDTIPSVYGGLRGPNWFDWLQTDAKAFIQDQNYTHAASFLETIDTITPNTYPARALFGAYSAWAFQQIKAHAKTHVNVEHRRISVSALNTTNTVFELTLDNGELFSADKVVLTPGQLPNAPTAEEINFATAAETNQLIYLPVGHPGEAALEELPAKAPVIMRGLGLSFFDYMAALTIGRGGKFIRQESGALTYEASGQEPHIIAGSRRGQLAHARGVNQKTAHVSYEPKIFTTARLTETVPASFDTFFRLIKAEMQLVYYTNLLREQPDIYSGNHANFLQTLIDSPDVEQAVKDFDFPVEYRYDWDHVFPHTTSSDALQMSQLLQLDIMDAKQGNAFGPYSASYEVVKDLRALIRKYLANGIFDGTNYEAFLTEFGPFNNTVAVGPPLERIEQLDALIQAEVMTITGPELKVSVQDNQYLAQDSTGEHWQAQALVEARLPTTNLNKVIDPLMSQLRETHAVQEYTMSREDGSTYQIPATDVNIQTLQVQTPTGQLDNFFIWGLPTEGKRWFTTFLPRPDDGDLNMRDAETIAQTMFQNS
>NZ_CP007588.1|WP_009765164.1|1303145_1303805_+|NAD(P)H-hydrate-epimerase
MVEAITAQEMQLLERYTIDEIGVSPLVLMERTAMSVIEVLGAGDFDLSNVLVLCGLGNNGGDGIAIARLLIQKGINVDLLILGDEKRASPRTLNQLNIARNYGIEVKQRASDFRSYTAIVDALFGIGLSKPVPAKLGDVIKRINSANVPVVSVDTPSGLDATTGEILGSSIRAAATVTFGYAKTGLLKNEGLKRAGNIYVKDIGVYKYPDFDAEQASAE
>NZ_CP007588.1|WP_009765163.1|1302542_1302761_+|hypothetical-protein
MKNPLIWPAAKLAFNNTSIALGWSFLIFLVASLFFPNVMMMVQKSNVFLIIFFIASFTGDFSRAYRKAKNEA
>NZ_CP007588.1|WP_009765174.1|1315464_1315920_-|Rrf2-family-transcriptional-regulator
MQLKQSFEEAICIVLLLAAEKTRDRRMNSAEIVEKLGTSQSYIKKILGQLVHANIISSGAGKNGGFFINKALEELTLLDVYYAIEGRETMYRPKHIADRFVSDKHYIREKEADIVQIFNDAEQAYCEKLSTFKLSNILDVDGDVMKKVRQP
>NZ_CP007588.1|WP_009765175.1|1316130_1318764_-|cation-translocating-P-type-ATPase
MKEYQKPLNDVLVDYKVDPETGLDAQQVEMHRKEYGANTFVEPAKPSLARKILISLNDVATIILLVAAVISFITAYMENTGNYFESMLIIGIVIINSTLSIVQEGKAESSLAALQGLNKSKVKVLRNGKPEFIDGDDIVVGDILLIDNGSSIAADARLIDSAELQAEESPLTGESVPATKNADVVLSGDVDLGERANMVYRGTTIVNGHARAVVTGVGMQSEMGIIAGLLNSEAKTPLTPLQQRLVQLGKNISIIAVISAAFVMALGLYQGMDLMHIFLTAISLAVAVVPETLAVIVTMTLALGVQRMAKKHAIIRRLPAVETLGTTSVIASDKTGTLTQNKMTVREVWANENNHLTYLDNGMDASAENVLSIAAISTNVDVREVEGETVYDGLPTEVAIVRAMQPVKPRTELLKEWPVVDQIPFNSTKKRMTTVHQDPDGGFVAITKGAFDVLLPMVENGDKERALEINKGFGQDALRVLTITAKHFDEMPAEPTAEFYEQHLSLIGLIGIIDPPRPESAPAVAKAAAAGIKTVMITGDHLETASAIAREIGIMRDGDKGMTGAELAELSDDQLDERVKEYAVYARVTPTDKIRIVKSWQRNGAIIAMTGDGVNDAPALKAADVGISMGETGTDVARGASDIILTDDNFATIVDAVSEGRGVYVKVRKTINFLLSANMSEILVIIIAMLLGWGSPLLPVHLLFINLVSDGLPGFALSREPMLTNVMNQPPMDKDEKLFADGLGKQIGLNAILFMIVTLLAIWVGRDMTLGGMLPSAEIGQTMAFIVLSLTSIFHVFNIRSEKSLFTNKYSDNPTLVNMALLATVITLVIALIPLTAGLFGLTQLSIMHWVVVAILSLIPTVVLEVWKQIQPSFFRV
>NZ_CP007588.1|WP_009765176.1|1319024_1320086_+|tRNA-dihydrouridine-synthase
MVQAKSAYWQNIVDAAQNHPEVEGIETLPFFTLAPMEAVTDTVFRRVVAQAAAPEAFYTEFTNARSMSHPKAKFTVQGRLCFVPEEHSIPIAQLWGDRPIDFELGVADLKERGFEAVDINMGCPDSTVIKNGGGSDLIRNPEKAAELIQAAKLAGLPVSVKTRLGFNKIDTFREWLPFLLKQDVQVLTVHLRTRKEMSKVEAHYEYIDEILAMRDEISPNTLIQFNGDIKDRAQGLALAKEHPGIDGIMIGRGVFEDPYTFEDTPTEHTLEESLALLRLQLDLHDEFDKEFGPTNFQKLKRFFKIYVRGFSYASDLRVALMETKTTDDARDILAEFDEQWQERVKAEAENTPS
>NZ_CP007588.1|WP_009765177.1|1320161_1321127_-|helix-turn-helix-transcriptional-regulator
MSFDQDMKQLRKDKGMTQQDLADALHVSRQTVSTWETGKNYPSLDVLKSISDLFDVSFEHLLFGGHEEMVRKQENVAQAIDNDVKLKGRYKKTTIFLSTIISIVVIGLITLGVGYVKGIDTIDRVNPFLQYKTGYAKLPSEKYVKPFNKTNDGYWTEWFADDDMGTEWTKLTLATGMNPGIKDPYVMAYHKGSYVKEARIVPGAVISQMSKHNADTVREYFETGWGSKELKDESQKLNNQIHLGSVISQIRRLNVEKIREYFETGWNSKGWDYESQKLNNRIHLGSEISSAVFPGHMESDDEEQDNKDDFDKLEKKSSEKK
>NZ_CP007588.1|WP_009765178.1|1321300_1321645_-|hypothetical-protein
MKRKLLPLINRLFPKKVIHYLVNIVDDILNEDVEQLNLTDFERQKLREYKHALVDSKDYYLKSNLVFVQTMSPVILRGEANSEVQFLYSEILRLNPQLMSQRLGNELLLKKFFR
>NZ_CP007588.1|WP_009765179.1|1321672_1322554_-|YihY/virulence-factor-BrkB-family-protein
MDKVKAWLAPIQAKWEKFATWSHFPQFLTFVDRAQVGMVAPTVAYYTIVSLVPLIMSIGVILGFVGINVTEMNAFISQQLPDTIGDVLIPIVDSVLKGSVSVLSFSVIVVIWTASGILSTFRKIFNDIYGREQAENGLITRVMSFLWFMGFLVAAVIIGLFSSLFPAIMKNLPHVDGWIQTFAQQTWIYALVLVWIILTIFNYALPAVKIRWKSVIFGSGIAALGLSLLNAGFGLYAQFAMRNVDFYRSLGSLLALLIYFNLVATIIVMGQVFIAWFETFQTEKDAKKDSVTV
>NZ_CP007588.1|WP_009765180.1|1322546_1322759_-|hypothetical-protein
MLALKQSIFHATPRQLMFSLIVDALFLILLRPSTPLSITVYIIFLPGFDLVSAVVSYWNYVQAYKQASHG
>NZ_CP007588.1|WP_009765181.1|1322771_1323674_-|alpha/beta-hydrolase
MTERFIDLKYTHIPAKTEGITRKWLDVPYMDGERHGMDIYLPNTGEGPYPVIIDIYGGGLYRGEKSSMKLDASLKLLREHGYAVVSPNYSMLWQAPYPTQIHEVKAAIRFLRANAAEYQLDMSRVALVGESSGAQLAVTVAATANVDEMMDKTFGAYREESEKVDAVIALYGPYEFDQFEKQFAEEGITSKFPETGTAISFQGQLFGERAPKDVPELVEAYNPATYFAAGMPAILGFAGTADPVVPYHQTVNMMTSARAVLGEDKTPYHLIDGGVHGPANYMTPEWTAVKADFLAQELNQ
>NZ_CP007588.1|WP_009765182.1|1323812_1325159_-|amino-acid-permease
MNGEETKLERGLSARHVEMIALGGTIGTGLFLGAGRSISTAGPAILLVYIITGLFMFWMMRALGELLLTDPDKPTFVAFIEKYLGKRTGFVIGWTYWLGWITIAMAEVTAISAYMKYWFPDIPGWIWAIVFLAVLFSINIFAVGAFGETEFWFSMIKIVAILAMIATGAIMIATRAETSAGVTSLSNLWTHGFFANNGSGILSAFQMVFFAFLGIEFVGMTAAESKDPDYVIPKAINSIIIRILIFYIGSLIAIMSIQPWMNYNANESPFVQVFAGIGITAAAGIINFVVLTAAASALNSAIFTTGRMLFALTSQGESKSRFGRLNKRALPMNALVASTLLIGLAAVINFLFPSEAFEVITSVASAAFIGIYATLVFAHVKYRRTDDFKNGEKKFLMPLAPFSDYLTLGFMGMVFLVLLFTPATQVTTIFAIIWFVVMALLSRRYASK
>NZ_CP007588.1|WP_009765183.1|1325326_1326451_-|AI-2E-family-transporter
MQNVTHSKTFYWTLEILAIATLFWVLSQLGFILTPMGQFIGGVFVPLLISGFLYYLMNPIVELICKVPLGKYKVPRGISITIVMLLFLGIIVFAVGSFIPTLAEQVSRLLASVPQYVHKTQMWFDSLSRETWFRDYVQAIDMSKLQQTIEKYGETVVMGTASGFGSVLGTVTSVTIAAITIPVMTIYMLADGKKFVPFAQRVMPKRFSGDVAELLGRLNKTLSRYISGQALEMLFVGVFTTIGYMVIGQRYALLLGVIAGITNMIPYVGPYIGYIPALFIGLMQGPMEAVSITIVVLIVQQIDSNILYPRIIGSTLSIHPLTILVILLAAGNIAGIPGMILAVPLYAVVRTIVVYIAEVWKVDRQSKAEESITK

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP007588_2	2.1\|84132\|28\|NZ_CP007588\|CRISPRCasFinder	84132-84159	28	KY499642	Vibrio phage pVa-21, complete genome	167841-167868	6	0.786

1. spacer 2.1|84132|28|NZ_CP007588|CRISPRCasFinder matches to KY499642 (Vibrio phage pVa-21, complete genome) position: , mismatch: 6, identity: 0.786

tggcggaaaccgtaatggtggacgcggt	CRISPR spacer
atgcggaaaccgcaatggtggaagccat	Protospacer
  **********.********* ** .*

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

562687 : 570034

Caulobacter_phage(16.67%)

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

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_009765412.1\|562687_564550_+	DNA primase	A0A0K1LMQ9	Caulobacter_phage	6.4e-51	35.8
WP_009765411.1\|564560_565694_+	RNA polymerase sigma factor RpoD	M4SMP8	Cyanophage	3.8e-38	34.8
WP_009765410.1\|565916_567140_+	MFS transporter	A0A2K5B2B5	Erysipelothrix_phage	8.6e-12	20.0
WP_009765409.1\|567240_567951_+	response regulator transcription factor	W8CYM9	Bacillus_phage	2.3e-33	32.8
WP_009765408.1\|567961_569335_+	PAS domain-containing protein	A0A1V0SGX0	Hokovirus	1.8e-18	28.8
WP_009765407.1\|569389_570034_+	uridine kinase	A0A1V0SAA3	Catovirus	3.3e-31	36.5

DBSCAN-SWA_2

759433 : 768053

Prochlorococcus_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_009765229.1\|759433_760021_-	phosphoribosylglycinamide formyltransferase	E3SNR5	Prochlorococcus_phage	1.2e-22	35.9
WP_009765228.1\|760005_761055_-	phosphoribosylformylglycinamidine cyclo-ligase	Q58MH8	Prochlorococcus_phage	6.2e-59	41.1
WP_038528405.1\|761088_762582_-	amidophosphoribosyltransferase	A0A0M3SGR2	Mollivirus	9.7e-50	33.5
WP_038528912.1\|762563_764774_-	phosphoribosylformylglycinamidine synthase subunit PurL	A6N228	Microbacterium_phage	9.4e-142	39.3
WP_009765225.1\|764800_765472_-	phosphoribosylformylglycinamidine synthase subunit PurQ	NA	NA	NA	NA
WP_009765224.1\|765475_765733_-	phosphoribosylformylglycinamidine synthase subunit PurS	NA	NA	NA	NA
WP_009765223.1\|765735_766458_-	phosphoribosylaminoimidazolesuccinocarboxamide synthase	A0A0E3ELR0	Synechococcus_phage	5.8e-32	33.2
WP_009765222.1\|766444_767572_-	5-(carboxyamino)imidazole ribonucleotide synthase	NA	NA	NA	NA
WP_009496497.1\|767564_768053_-	5-(carboxyamino)imidazole ribonucleotide mutase	A0A2P0VNU7	Tetraselmis_virus	4.6e-17	39.7

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP007588

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection