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_CP024592	Porphyromonas gingivalis strain KCOM 2803 chromosome, complete genome	9 crisprs	cas5,cas3,cas8b6,cas7,cas4,cas1,cas2,cmr1gr7,cas10,cmr3gr5,cmr4gr7,cmr5gr11,cmr6gr7,DEDDh,Csx28,cas9	3	13	1	1

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP024592_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP024592_1

95305-95401

Unclear

Consensus_repeat	Method
TTTTGGAGCCCTTCATCGTATAGTTCAGAC	CRISPRCasFinder

1 spacers

cas6,cas5,cas3

The CRISPR arrays of NZ_CP024592_1

>merge|NZ_CP024592|1|95305-95401|CRISPRCasFinder
TTTTGGAGCCCTTCATCGTATAGTTCAGACTTTGCAAGGGAAAACGCAGCGGCAGCCAAGCGGTCGATTTTGGAGCCCTTCATCGTATAGTTCAGAC

>NZ_CP024592|1|1|95305-95401|CRISPRCasFinder
TTTTGGAGCCCTTCATCGTATAGTTCAGAC	TTTGCAAGGGAAAACGCAGCGGCAGCCAAGCGGTCGA
TTTTGGAGCCCTTCATCGTATAGTTCAGAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP024592.1\|WP_099840425.1\|88906_89698_-\|sulfide/dihydroorotate-dehydrogenase-like-FAD/NAD-binding-protein	unknown	unknown	gnl\|CDD\|235747
NZ_CP024592.1\|WP_077094158.1\|103916_104888_+\|methionyl-tRNA-formyltransferase	unknown	unknown	gnl\|CDD\|234567
NZ_CP024592.1\|WP_077094241.1\|91587_91779_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_099840428.1\|105052_107596_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|370572
NZ_CP024592.1\|WP_099840429.1\|107599_109531_+\|LTA-synthase-family-protein	unknown	unknown	gnl\|CDD\|293739
NZ_CP024592.1\|WP_130267223.1\|109867_110104_+\|DUF1661-domain-containing-protein	unknown	unknown	gnl\|CDD\|285160
NZ_CP024592.1\|WP_077094242.1\|90607_91519_+\|ion-transporter	unknown	unknown	gnl\|CDD\|366146
NZ_CP024592.1\|WP_099840426.1\|91911_92997_-\|IS5-family-transposase	unknown	unknown	gnl\|CDD\|377531
NZ_CP024592.1\|WP_077094153.1\|93738_94179_-\|histidinol-phosphate-phosphatase	unknown	unknown	gnl\|CDD\|273496
NZ_CP024592.1\|WP_077094163.1\|111449_113582_+\|CRISPR-associated-helicase/endonuclease-Cas3	cas3	COG1203_cas3_CAS-I	gnl\|CDD\|224124
NZ_CP024592.1\|WP_099840424.1\|84864_87378_-\|primosomal-protein-N'	unknown	unknown	gnl\|CDD\|235514
NZ_CP024592.1\|WP_077094162.1\|110851_111457_+\|hypothetical-protein	cas5	mkCas0069_cas5_CAS-I-B	unknown
NZ_CP024592.1\|WP_005874422.1\|93148_93598_-\|N-acetylmuramoyl-L-alanine-amidase	unknown	unknown	gnl\|CDD\|177282
NZ_CP024592.1\|WP_099840867.1\|97678_97906_+\|DUF1661-domain-containing-protein	unknown	unknown	gnl\|CDD\|285160
NZ_CP024592.1\|WP_077094155.1\|95752_97270_-\|redoxin-family-protein	unknown	unknown	gnl\|CDD\|239264
NZ_CP024592.1\|WP_099840427.1\|98256_103371_+\|Arg-gingipain-RgpA	unknown	unknown	gnl\|CDD\|199211
NZ_CP024592.1\|WP_004583676.1\|87411_88884_-\|NADPH-dependent-glutamate-synthase	unknown	unknown	gnl\|CDD\|237200
NZ_CP024592.1\|WP_053444560.1\|89898_90576_+\|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD	unknown	unknown	gnl\|CDD\|234581
NZ_CP024592.1\|WP_077094161.1\|110179_110845_+\|CRISPR-associated-endoribonuclease-Cas6	cas6	cd09652_cas6_CAS-I:CAS-III	gnl\|CDD\|273848
NZ_CP024592.1\|WP_013815313.1\|84442_84838_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|176856

Protein	Function_ID	Function_description	E-value
NZ_CP024592.1\|WP_099840425.1\|88906_89698_-\|sulfide/dihydroorotate-dehydrogenase-like-FAD/NAD-binding-protein	gnl\|CDD\|235747	PRK06222, PRK06222, sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein.	2.29362e-163
NZ_CP024592.1\|WP_077094158.1\|103916_104888_+\|methionyl-tRNA-formyltransferase	gnl\|CDD\|234567	PRK00005, fmt, methionyl-tRNA formyltransferase; Reviewed.	3.16285e-146
NZ_CP024592.1\|WP_099840428.1\|105052_107596_+\|hypothetical-protein	gnl\|CDD\|370572	pfam09586, YfhO, Bacterial membrane protein YfhO. This protein is a conserved membrane protein. The yfhO gene is transcribed in Difco sporulation medium and the transcription is affected by the YvrGHb two-component system. Some members of this family have been annotated as glycosyl transferases of the PMT family.	1.41903e-05
NZ_CP024592.1\|WP_099840429.1\|107599_109531_+\|LTA-synthase-family-protein	gnl\|CDD\|293739	cd16015, LTA_synthase, Lipoteichoic acid synthase like. Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.	2.52151e-65
NZ_CP024592.1\|WP_130267223.1\|109867_110104_+\|DUF1661-domain-containing-protein	gnl\|CDD\|285160	pfam07877, DUF1661, Protein of unknown function (DUF1661). This is a family containing bacterial proteins of unknown function. Many of the proteins in this family are hypothetical.	1.62527e-05
NZ_CP024592.1\|WP_077094242.1\|90607_91519_+\|ion-transporter	gnl\|CDD\|366146	pfam00520, Ion_trans, Ion transport protein. This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.	9.14244e-32
NZ_CP024592.1\|WP_099840426.1\|91911_92997_-\|IS5-family-transposase	gnl\|CDD\|377531	pfam05598, DUF772, Transposase domain (DUF772). This presumed domain is found at the N-terminus of many proteins found in transposons.	1.17768e-23
NZ_CP024592.1\|WP_077094153.1\|93738_94179_-\|histidinol-phosphate-phosphatase	gnl\|CDD\|273496	TIGR01201, HU_rel, DNA-binding protein, histone-like, putative. This model describes a set of proteins related to but longer than DNA-binding protein HU. Its distinctive domain architecture compared to HU and related histone-like DNA-binding proteins justifies the designation as superfamily. Members include, so far, one from Bacteroides fragilis, a gut bacterium, and ten from Porphyromonas gingivalis, an oral anaerobe. [DNA metabolism, Chromosome-associated proteins].	6.15024e-50
NZ_CP024592.1\|WP_077094163.1\|111449_113582_+\|CRISPR-associated-helicase/endonuclease-Cas3	gnl\|CDD\|224124	COG1203, COG1203, CRISPR-associated helicase Cas3 [Defense mechanisms].	4.36426e-60
NZ_CP024592.1\|WP_099840424.1\|84864_87378_-\|primosomal-protein-N'	gnl\|CDD\|235514	PRK05580, PRK05580, primosome assembly protein PriA; Validated.	1.62216e-134
NZ_CP024592.1\|WP_005874422.1\|93148_93598_-\|N-acetylmuramoyl-L-alanine-amidase	gnl\|CDD\|177282	PHA00447, PHA00447, lysozyme.	6.16338e-42
NZ_CP024592.1\|WP_099840867.1\|97678_97906_+\|DUF1661-domain-containing-protein	gnl\|CDD\|285160	pfam07877, DUF1661, Protein of unknown function (DUF1661). This is a family containing bacterial proteins of unknown function. Many of the proteins in this family are hypothetical.	6.01354e-07
NZ_CP024592.1\|WP_077094155.1\|95752_97270_-\|redoxin-family-protein	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	2.67566e-09
NZ_CP024592.1\|WP_099840427.1\|98256_103371_+\|Arg-gingipain-RgpA	gnl\|CDD\|199211	cd10913, Peptidase_C25_N_gingipain, gingipain subgroup of the Peptidase C25 family N-terminal domain. Gingipain, produced by Porphyromonas gingivalis, exemplifies the Peptidase family C25, a unique class of cysteine proteases. P. gingivalis is one of the primary gram-negative pathogens that causes periodontitis, a disease also associated with other diseases such as diabetes and cardiovascular disease. The gingipain subgroup contains extracellular Arg- and Lys-specific proteinases called Arg-gingipain (Rgp) and Lys-gingipain (Kgp); RgpA and RgpB are homologous Arg-specific gingipains encoded by two closely related genes, rgpA and rgpB, while Lys-specific gingipain is encoded by the single kgp gene. Mutant studies have shown that, among the large quantities of proteolytic enzymes produced by P. gingivalis, these three proteases are major virulence factors of this bacterium. All three genes encode an N-terminal pre-pro fragment, followed by the protease domain; however, rgpA and kgp also encode additional C-terminal HA (hemaglutinin/adhesion) subunits which consist of several sequence-related adhesion domains. Although unique, their cysteine protease active site residues (His and Cys) forming the catalytic dyad, are well-conserved, cleaving the C-terminal peptide bond with Arg or Lys residues. Gingipains are evolutionarily related to other highly specific proteases including caspases, clostripain, legumains, and separase. Gingipains function by dysregulating host defense and inflammatory responses, and degrading host proteins, e.g. tissue, cells, matrix, plasma and immunological proteins. It has been suggested that they enhance gingival crevicular fluid (GCF) production through activation of the kallikrein/kinin pathways, thus increasing vascular permeability and causing gingival inflammation, a distinctive feature of periodontitis. RgpA and RgpB are also able to cleave and activate coagulation factors IX and X in order to activate prothrombin to produce thrombin, which in turn increases production of GCF. The gingipains also play a pivotal role in the survival of P. gingivalis in the host by attacking the host defense system through cleavage of several immunological molecules, while at the same time evading the host-immune response by dysregulating the cytokine network.	1.94747e-131
NZ_CP024592.1\|WP_004583676.1\|87411_88884_-\|NADPH-dependent-glutamate-synthase	gnl\|CDD\|237200	PRK12778, PRK12778, bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase.	0
NZ_CP024592.1\|WP_053444560.1\|89898_90576_+\|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD	gnl\|CDD\|234581	PRK00026, trmD, tRNA (guanine-N(1)-)-methyltransferase; Reviewed.	2.84621e-139
NZ_CP024592.1\|WP_077094161.1\|110179_110845_+\|CRISPR-associated-endoribonuclease-Cas6	gnl\|CDD\|273848	TIGR01877, CRISPR-associated_endoribonuclease_Cas6_1, CRISPR-associated endoribonuclease Cas6. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This broadly distributed, highly divergent Cas family is now characterized as an endoribonuclease that generates guide RNAs for host defense against phage and other invaders. The family contains a C-terminal motif GXGXXXXXGXG, where the each X between two Gly is hydrophobic and the spacer XXXXX contains (usually) one Arg or Lys. The seed alignment for the current version of this model has gappy columns removed. Members of this protein family are found associated with several different CRISPR/cas system subtypes, and consequently we designate this family Cas6.	2.16452e-35
NZ_CP024592.1\|WP_013815313.1\|84442_84838_+\|hypothetical-protein	gnl\|CDD\|176856	cd07814, SRPBCC_CalC_Aha1-like, Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins. This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.	1.13782e-06

>NZ_CP024592.1|WP_077094153.1|93738_94179_-|histidinol-phosphate-phosphatase
MINGQPAKIRYAQTLKTGDMDLSEICDLTSKISAVSEGDVRSIINTVTGLVITGLKQGRAISLGELGRFRISLSSKAAKEGEEFTVENIRRARVLFLPGGDIRRACRQIRLKGINMLRPGEQQGGTPSVPDSPEGGGEQGSGGGGL
>NZ_CP024592.1|WP_005874422.1|93148_93598_-|N-acetylmuramoyl-L-alanine-amidase
MNTIKYIVIHCSATRSNMTYTSLQLDRDHRARGFRSAGYHFYIRRNGDTEALRPTTEPGAHAKGYNHCSIGVCYEGGLDAAAKPADTRTPQQKTALRRLLMELRNLYPQASIVGHRDLSYDRNYDGSITPDEWMKACPCFDAHAEYSRL
>NZ_CP024592.1|WP_099840426.1|91911_92997_-|IS5-family-transposase
MAYQSKNTDEHVTFADALLSKRYRKAQNDFLNQVDTLIDWRPIRTPINKKYTKRQNAIGAPAYDVILLFKMLLLETWYNLSDCALEERINDSITFSRFLGLKMEEVSPDHSTISRFRSALTELGLMDKLLAQFNKQLSRHHISVREGVLVDASLVETPHKPDGSITIEVADDRQDNRSEAEKEAEEDYQKQVVRQRKGTDEEARWVYKQKRYHYGYKKHCPANVQGIVQKVITTAANRSDTKEFIPLLQGANIPQGTAVLADKGYACGENRSYLQTHHLQDGIMHKAQRNRALTEEEKQRNKAIGPIRSTIERTFGSIRRWFHGGRCRYRGLAKTHTQNILESIAFNLYRTPEIIMSSSVG
>NZ_CP024592.1|WP_077094241.1|91587_91779_-|hypothetical-protein
MLQRSRLVGLLLLFIGFFVPPVGEIDSSVLIAYGEVSTFAGSLLGIDYRYRYKYGGYGKKSDP
>NZ_CP024592.1|WP_077094242.1|90607_91519_+|ion-transporter
MKMIEWLTSKLPDRAHVRSIIFGMNTPTGRLFDILLLCLILLSVIVVSAESTVGLSHSTRNFLHWCEWVITIVFTIEYILRIYCLHKPWRYILSFYGIIDLISILPSYIALIYSGAQVLMVFRILRLLRIFRILSLNNLVSAGDMLVRSIRASMAKIMVFMLFLLLLVTVLGSVMYLIEGRGNPNFSSIPKSIYWAIVTLTTVGYGDITPVTAVGQLVSTIVMLLGYSIIAVPTGIISAEMTKSNRTDSMVAFDTPIRCPRCNKRIRRHKARYCDQCGYSLFTHGHTVVPNTYKPEGDTGSNE
>NZ_CP024592.1|WP_053444560.1|89898_90576_+|tRNA-(guanosine(37)-N1)-methyltransferase-TrmD
MRIDIITVLPEMIENTLNCSIIGRAQERGLLELKLHQLRDYSTDKWKRVDDYPFGGEPGMVMQIEPIDRIITELKTQREYDEVIFTSPDGERFDQPMANELSLLSNLIILCGHYKGIDYRIREHLITREISIGDYVLTGGELAAAVMTDAIARLIPGVLNDAGSALSDTFQDNLLAPPVYTRPAEYKGWRVPDILLSGHEANIAKWRLEQAVERTKRLRPDLIKD
>NZ_CP024592.1|WP_099840425.1|88906_89698_-|sulfide/dihydroorotate-dehydrogenase-like-FAD/NAD-binding-protein
MNKIVSKEYFSANVIKLEVEALRIAKSRRAGHFVIIRVGEKGERIPLTIAQADIKRGTITLVVQAVGKSSKKLAELEVGDYITDVVGPLGQSTHIEKVGTVVCAGGGVGVAPLLPIVEAFHKAGNRVIVVLAARTKDLVILEEQMRANSDEVIIMTDDGSYGTKGLVTDGVESVIKRETVDLCVTIGPAVMMKFVSLLTKRYEIPTIASLNTIMVDGTGMCGACRISVGGQTKFVCVDGPEFDAHQVDFDEMIMRLGAYREME
>NZ_CP024592.1|WP_004583676.1|87411_88884_-|NADPH-dependent-glutamate-synthase
MTTEELIRLRRSEPWREELRNALKNKERMSRPRAEMPELDPLYRSSKINEEVNRGLSREAAMAEASRCLDCPQPSCMEGCPVSINIPTFIKQIEVGDILAAASTLRETSSLPAVCGRVCPQEKQCESRCIYTKMNKPAVAIGFLERFAADYEREQGALKVPEMAPRNGIKVAVIGSGPAGLSFSGDMAKLGYDVTVFEALHEIGGVLKYGIPEFRLPNSIVDSEINLLEEMGVRFETNTIVGRTIAYDDLHEAGFRGVFVGSGAGLPNFMNIPGENLVGVMSSNEYLTRVNLMHASQADSDTPVFKGKNVAVIGGGNTAMDSVRTAKRLGAERAMIVYRRSEEEMPARLEEVKHAKEEGIEFLTLHNPIEYIGNERGRVTAMRLQKMELGEPDAGGRRRPVAITGAIEEIPVDEVIVSIGVSPNPLVPRTISGLEVTSKGTIVVNESNQTALPDVFAGGDIVRGGATVILAMGDGRKAAAAMHEYLKAES
>NZ_CP024592.1|WP_099840424.1|84864_87378_-|primosomal-protein-N'
MRYAEVLIPLALEGSFHYRLAEGLAEKAIVGMRCVVPFGAKRYYTGIIIGLSDKRPNLQISFKEVLFLPDDKPSVTASQLSLWQWLSAYYICTQGEVLRAALPAALLPESHTVIHYNTDFEADSRLSRDEEELLDILESAKGRTYTLDALQKAVGKRAIRAFTSLVERGAIRLEEEVKSHYKPKAEVFVRLAEPFRTEKTFASLLDSLHRAPKQSALLLHWAELITEHSLPYSSPMPQRLLAESDPHATVTLSALKKKGIFLSESVTHSVMYSAGGGEYRLWKQPQEEEKAIQSEESSTDSAVSASLPQKPLSLLYTHDFRRKEKQLLEWTEEVVRSGGQVLYLSPEANKRGGSDTLSTRMAERLGSCLLSYHAFESDAKRVEVWNRLAATEYPCVVLGVRSALFLPFRRLRLIIVDEEQEYLYKQQDPAPRFHTRQVAARLGRIHDCPVVLASVTPSAEVLHQVRHKACELITWPDDRVRPRFDLEVIDMGKMRRQRQVGAGELLSFPLLSAIEETIRQKKMAVVLQNRRGFAPYIICSSCGEKLRCIHCDVSLTYHKHSGMLVCHYCGYSRPLPRICPSCKRASGVGEPSSLQPVGYGAERIEEELKRRFPSVSILRMDSDMAMSRTKMDEALARLEAKEVDILVGTQLIKGQAYNEHVGLVAVTQLDSILGFPDFRAYERAYQLLYQLMLRSGASRLYVQTNNPANSFPDLLREGDYKAFIGKQLEERQMLFFPPFSRLIRIEFRAGEESLVERIASDYAASLAAHLPEQSLSPILVPPISRLRNAFIRELLLRLPLSSSVSATRNVLDTIRTTLQTRTQEYKRVRILFDVDPL
>NZ_CP024592.1|WP_013815313.1|84442_84838_+|hypothetical-protein
MEKNKLQLEYVFDRVSTRSLWRYLSTPDGLSEWFAYDVRLEDNGDFYFQWDKNSGEKASILEQREGERIRFQWHREQDQNACFEFVIHHSELTGGKSLEVIDYIAPEEVADMEHFWNNLISRLRLSLGAPE
>NZ_CP024592.1|WP_077094155.1|95752_97270_-|redoxin-family-protein
MMKPSLFLTLVAVFFMATIKGLAKPQIDKEVDPITKLTLRNPQNGGSGVLWTNIPCSADSDLAGLVTPIFFENGEVTISIPLKRSVCIQFAGNQLFPKSKIILCPGDHLILTADNSSGKWSFGATGDNASGNLYLLDSTLFAGYRWLNEYLTILRTGKGKAELIDQVDSMLDMELESFLSMEKQGDISDAFLSAVKAEMQQMVLYAAGLAVRNIEETNRLRQKAKELYFYYLERYSPLAEMYKGSEMSLHNAGTATLRGHKNLAGGKRIDIGLWDGSKEFFHEYCYLPDDVQIRLFISKIQLLHFVVGAITTPQYVEKVALLGKVVGSSRYLELLRSFIDLNDPSGKNYSRGLFFYDHKFDKLEEVGKEVGENLPEVIKRFFPDKWVLVDVWATWCSPCKKEFGYNKQLHTFLEEKGIAMLYCSVDEPENSDNWRNNLSAFDLTGYHYYITSKAEKELLKIPDFRMLIPRYLLFDNKGKLVHANLPRPSSEKALYEEIEKLMQGN
>NZ_CP024592.1|WP_099840867.1|97678_97906_+|DUF1661-domain-containing-protein
MVREVKKLRAKTKKFSRRFLRIHRPQSEHFRFVIHRRDRFYRIEIRERISVILISEVKRYGTLIEELIGLVGETF
>NZ_CP024592.1|WP_099840427.1|98256_103371_+|Arg-gingipain-RgpA
MKNLNKFVSIALCSSLLGGMAFAQQTELGRNPNVRLLESTQQSVTKVQFRMDNLKFTEVQTPKGMAQVPTYTEGVNLSEKGMPTLPILSRSLAVSDTREMKVEVVSSKFIEKKNVLIAPSKGMIMRNEDPKKIPYVYGKSYSQNKFFPGEIATLDDPFILRDVRGQVVNFAPLQYNPVTKTLRIYTEITVAVSETSEQGKNILNKKGTFAGFEDTYKRMFMNYEPGRYTPVEEKQNGRMIVIVAKKYEGDIKDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNNLTYVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENVIANLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLANYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVACVNGDFLYNVPCFAEALMRAQKDGKPTGTVAIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGVTMNGMFAMVEKYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPAQINLTDASVNVSCDYNGAIATISANGKMFGSAVVENGTATINLTGLTNKSTLTLTVVGYNKETVIKTINTNGEPNPYQPVSNLTATTQGQKVTLKWDAPSTKTNATTNTARSVDGIRELVLLSVSDAPELLRSGQAEIVLEAHDVWNDGSGYQILLDADHDQYGQVIPSDTHTLWPNCSVPANLFAPFEYTVPENADPSCSPTNMIMDGTASVNIPAGTYDFAIAAPQANAKIWIAGQGPTKEDDYVFEAGKKYHFLMKKMGSGDGTELTISEGGGSDYTYTVYRDGTKIKEGLMATTFEEDGVAAGNHEYCVEVKYTAGVSPKVCKDVTVEGSNEFAPVQNLTGSAVGQKVTLKWDAPNGTPNPNPNPNPNPGTTTLSESFENGIPASWKTIDADGDGHGWKPGNAPGIAGYNSNGCVYSESFGLGGIGVLTPDNYLITPALDLPNGGKLTFWVCAQDANYASEHYAVYASSTGNDASNFTNALLEETITAKGVRSPEAIRGRIQGTWRQKTVDLPAGTKYVAFRHFQSTDMFYIDLDEVEIKANGKRADFTETFESSTHGEAPAEWTTIDADGDGQGWLCLSSGQLGWLTAHGGTNVVASFSWNGMALNPDNYLISKDVTGATKVKYYYAVNDGFPGDHYAVMISKTGTNAGDFTVVFEETPNGINKGGARFGLSTEADGAKPQSVWIERTVDLPAGTKYVAFRHYNCSDLNYILLDDIQFTMGGSPTPTDYTYTVYRDGTKIKEGLTETTFEEDGVATGNHEYCVEVKYTAGVSPKKCVNVTVNSTQFNPVKNLKAQPDGGDVVLKWEAPSAKKTEGSREVKRIGDGLFVTIEPANDVRANEAKVVLAADNVWGDNTGYQFLLDADHNTFGSVIPATGPLFTGTASSNLYSANFEYLIPANADPVVTTQNIIVTGQGEVVIPTGVYDYCITNPEPASGKMWIAGDGGNQPARYDDFTFEAGKKYTFTMRRAGMGDGTDMEVEDDSPASYTYTVYRDGTKIKEGLTETTYRDAGMSAQSHEYCVEVKYAAGVSPKVCVDYIPDGVADVTAQKPYTLTVVGKTITVTCQGEAMIYDMNGRRLAAGRNTVVYTAQGGYYAVMVVVDGKSYVEKLAVK
>NZ_CP024592.1|WP_077094158.1|103916_104888_+|methionyl-tRNA-formyltransferase
MKKEELRLIFMGTADFAVPALRALVENGYQVKAVVTMPDKPMGRGHKVSPSMVKLYAQELGLPILQPDNLNEESFLDELRTYQPHLQIVVAFRMLPRSVWQMPPMGTINLHGSLLPMYRGAAPINHAIRHGDTETGVTTFRLRHEIDTGEVLLQEKLPIGHEETFGELYERMATLGASVLVRTVDLFLEGEPVSIPQEQLPGYVGARPAPKIFKDDCRIDWDKPAEVVHNFIRSISPAPTAWTKLHRPRMESIVLKIYRTQVIEREPRHRGRFGSIIWDKKNLDVMTRKGVIRILSLQMPGKKQMDAASFLNGFALSSDMYIE
>NZ_CP024592.1|WP_099840428.1|105052_107596_+|hypothetical-protein
MKENEKPTAAAGTVTTTDKTKHDWRKILPYAAVVLLFIALALAYFYPASFDGRVLFQGDVAGASGTAQDVRDWEAQTGEHSYWTNSLFGGMPMYQISPSYPSTHTLQTIQDVLTLRKPFYLLGTYAWMLFAMMGGFFLFLRSLRIRILPAVIGSIAWAFSSYFLILIMAGHIWKLTAMCFIPPTLAGMIWIYNGRWLAGGSVMAFFTALQVLANHVQMSYYFLFVMFFMVLAFLAEAIRTKRIRHVFLSSAVVVIAGLVGVAVNSTNLFHTYQYGKETMRGGSELTLKQSGAPTDQVTHENKSGLDKAYITQWSYGIGETWSLLIPDIKGGSSGYLGYDEKVMETVNPSYAQAIARMNRYWGDQPFTAGPVYVGAFVLFLFVLGCFIVKGPVKWALLAATILSILLSWGHNMMWLTSFFIDHFPLYDKFRTVSSILVIAEFTIPALAVMALVEIIKEGKPLLKRERTAWVAATLLTLGASLLFALVPSLLGLLSGQEEAMFQEAAGHPEAAAIKTTLVNVRSGILASDAWRSFGILAVCGILLWLFFQKRLKATALLVSLAVITLVDLWTVDKRYLNDEHFIDPELVSQRAAPLTEADKQILADKSLGYRVLNLTVDTYNDATTSRWHRSIGGYHAAKLQRYQDLIEHQLSKGNREVVNMLNTKYIIVPGENNRPSPMSNPDAYGPAWPAGSIRWVGNANEEMMALDSNRLTRDIAVVDERFSSESLKRLPALTDSTASISLKEYAPNRQVYEAVSTQPMLGIFSEIYYPHGWTATIDNQAVPIIRANYILRALEVPAGRHKIEFRFDPKSLHITEAIAKTALALLLLGIVWAIARPFFLRGKRPTA
>NZ_CP024592.1|WP_099840429.1|107599_109531_+|LTA-synthase-family-protein
MKTLFERGELLFRKRSGFCYVIGVFVLFLLYFLFQKVIFLLVYSGRLAGIGTSSGDIAAIFLYGLRHDAAVAAYLTVLPLLFAGINAIAGWGEKKIGRILRQILKHYYTLISFFVGLIYTADLMLFGYWGFRLDATPLFYLRQPQEAMASVTAPQLLIGLLITVVFVCIPAFVLHRFHRRYFPTKVVAHPHIADIWKPVVGGAFLFLLIRGGVGVATLNVGSVFHSPKQLHNQAAVNPVFSFLYTCMHSEEDYSNYQFLSEEDCIKAFEQLRLYGCSDGSEVRESASDSTERILSTDRPNIVLILLESFSANAVGCLGGTPGHTPCIDSLAQNGILFSQAFASSFRTDRGTVATLSGYPSQPNSSIIKYPNKVRNLPGIAASLRTVGYSTHHLYGGDADFTNVRSYLYATGYDEVTDVSSFPIKTRLSKWGTPDHISFPRLLDDCRRLEKEKKPYFYSFLTLSSHEPFDVPSQHHPDPYLNSVFYTDSCFGDYIRGMQQSPQWKNTLIITVSDHGYPYPADQAMPDQPGRYGIVMLWTGGAILRPIRFEEVVSQSDLPATLLAQLGLAHDEFVFSKDVFRRNSPHFAYFSFPGLVGLATSEGTTIYDFAGDKIVYGHEAPLADQRAIAAKVMLQSVMKDMLSR
>NZ_CP024592.1|WP_130267223.1|109867_110104_+|DUF1661-domain-containing-protein
MRPRKTWRVNFFVVVREIKNSRATTKNFLLRFFRKHAPQSEHFRLVFYTPALAPSLFSVRFSQNCSERWMLYIRFPRK
>NZ_CP024592.1|WP_077094161.1|110179_110845_+|CRISPR-associated-endoribonuclease-Cas6
MRIELSIKADDSLVSFSHQHLLVGTLQKWLGENDMHGKSISYSFSRLNGGKFVSELNSILFADWANMFVSAHDPELIRRMLAGIRQDPEMFKSLCVREVTVIEDPDMTDREIFFPASPILLKRWREDNGFDHIVYTDEAANALLTENLRKKLQAVGIDDPTATASFVPDQGKAKVMLIDYRGVKNKASWCPIRIIGNAETKLFAWNAGIGNSTGIGFGAIK
>NZ_CP024592.1|WP_077094162.1|110851_111457_+|hypothetical-protein
MEDKIFFVVHYTGPFGYIKPWSAVRDIETYSQQFLTPSIIEGMEKKLFPEMLIKKGIRKIARHKLSCMSMSVQQEKTQTQAWEGKGKGKGRTYTRPQSILKRGVMLHPSLYLAFTSEEDAVIAARQHLCLCRNEDVVLPDTEILKMDEETFNALPGFELRFGKDYPDAFMVGFNRFDENTPMYGRIEIGGEAVLAPPKSNE
>NZ_CP024592.1|WP_077094163.1|111449_113582_+|CRISPR-associated-helicase/endonuclease-Cas3
MNDLRLILAKSDGTPLIQHLKDVAMVAEVLAHHLGLSVEIARKGAHLHDIGKTSCIFQQKLVGINPPFKKSFRHEIASLFFLSLLQDKEERCAVIEMVAAHHRSICNDMPKRGLLGLLDLEDKYPHCFELHSEGFEQWSQEALGILHELGWETHPITMDEARSNYQEAVDYCSSLGRNCSQWKGLLMAADHFASGLDGQTEDTLRKLFIIPDLSYYRNRRSELYPLSLLSADDERKHTLVTAPTGAGKTDFLLRRCRGRVFYTLPFQASINAMYDRLKADLQDTDAQIYPLHAASILKLNGDYERILSRHVGASIKVLTPHQIAALAFGLKGYEVTALDIRGCDVILDEIHTYRKETQAMVLKIVEILIALGCRIHIGTATMPTDLYTGLLRLLGGETAVYEVKLPKEVLKGFDRHTIHKVGSMEDVGPVIQKAVEQGQKILMVCNQVKRAQQLYQDVIGKYPAIPTLLVHSRFKRGHRAQLELELKERYNQCQGPCIVVSTQVVEVSLDISFDLMLTECAPIDALIQRFGRINRKRSLETIGQTKSIYVIAPPENEKEALPYELEILQRSYSSLPHCEVLHEADVQQLLDSVYPEVMALDIDMLTVFQEGKWVMKKLKHNPKSALFETLDINSACCLMEKDREVYENGSFAERTLLEIPVARSITQRNNLTPITCGVHPFLIPDQAYDSKLGLLEEFAAPRYYNSFEII

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Crispr_ID: NZ_CP024592_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP024592_2

118104-118994

Unclear

Consensus_repeat	Method
ATTTCAATTGCACCATACAGGAATTAAAAC	PILER-CR
ATTTCAATTGCACCATACAGGAATTAAAAC	CRISPRCasFinder
ATTTCAATTGCACCATACAGGAATTAAAAC	CRT

13 spacers

cas2,cas1,cas4,cas7,cas8b6,cas3,cas5,cas6

The CRISPR arrays of NZ_CP024592_2

>merge|NZ_CP024592|2|118104-118994|PILER-CR,CRISPRCasFinder,CRT
ATTTCAATTGCACCATACAGGAATTAAAACGACGGCACGCTCGGCGGGGATAGAGACCTCGGGGGATTTCAATTGCACCATACAGGAATTAAAACGCGGCAGATAGCCTCGCCTCCGGCCAAAGGCGGGGGGCGGATTTCAATTGCACCATACAGGAATTAAAACATCTTAGCACCTTGTGCTTGTTTTCCAGCTGCTTCATATTTCAATTGCACCATACAGGAATTAAAACAGGGTGATATTATGTGCATTTACACTGCCCTGAAGAATTTCAATTGCACCATACAGGAATTAAAACACAGCTAACCTCGCTGCCAGCAAGCTGAAAGCGGAATTTCAATTGCACCATACAGGAATTAAAACCGCGCACAAGTCCGGCAACTCGATAGTACGCCAAATTTCAATTGCACCATACAGGAATTAAAACAACCTTGACAGTTCGACAGGTATGTAATTGATACAAATTTCAATTGCACCATACAGGAATTAAAACCTTTATACGTGATATCAAATTCATGAGTTGTTGAAAAATTTCAATTGCACCATACAGGAATTAAAACCAAAAGGACGTAAAAGGCAAATAGCACATTTGCTGGAATTTCAATTGCACCATACAGGAATTAAAACCTATTTGCGCGAGCAAAGCCGCTTCCCCTCCGTCCGATTTCAATTGCACCATACAGGAATTAAAACGGAAGGAGGAGAGCAATGAGAACTACAAACAGTTTCTATTTCAATTGCACCATACAGGAATTAAAACAGGAGGCAATTCGTCGGAGATCACCCCGTCATGCGATTTCAATTGCACCATACAGGAATTAAAACGATACGCAAGCATCGATCGTTTACAGCGAGGATAACATTTCAATTGCACCATACAGGAATTAAAAT

>NZ_CP024592|2|1|118104-118994|PILER-CR
ATTTCAATTGCACCATACAGGAATTAAAAC	GACGGCACGCTCGGCGGGGATAGAGACCTCGGGGG
ATTTCAATTGCACCATACAGGAATTAAAAC	GCGGCAGATAGCCTCGCCTCCGGCCAAAGGCGGGGGGCGG
ATTTCAATTGCACCATACAGGAATTAAAAC	ATCTTAGCACCTTGTGCTTGTTTTCCAGCTGCTTCAT
ATTTCAATTGCACCATACAGGAATTAAAAC	AGGGTGATATTATGTGCATTTACACTGCCCTGAAGA
ATTTCAATTGCACCATACAGGAATTAAAAC	ACAGCTAACCTCGCTGCCAGCAAGCTGAAAGCGGA
ATTTCAATTGCACCATACAGGAATTAAAAC	CGCGCACAAGTCCGGCAACTCGATAGTACGCCAA
ATTTCAATTGCACCATACAGGAATTAAAAC	AACCTTGACAGTTCGACAGGTATGTAATTGATACAA
ATTTCAATTGCACCATACAGGAATTAAAAC	CTTTATACGTGATATCAAATTCATGAGTTGTTGAAAA
ATTTCAATTGCACCATACAGGAATTAAAAC	CAAAAGGACGTAAAAGGCAAATAGCACATTTGCTGGA
ATTTCAATTGCACCATACAGGAATTAAAAC	CTATTTGCGCGAGCAAAGCCGCTTCCCCTCCGTCCG
ATTTCAATTGCACCATACAGGAATTAAAAC	GGAAGGAGGAGAGCAATGAGAACTACAAACAGTTTCT
ATTTCAATTGCACCATACAGGAATTAAAAC	AGGAGGCAATTCGTCGGAGATCACCCCGTCATGCG
ATTTCAATTGCACCATACAGGAATTAAAAC	GATACGCAAGCATCGATCGTTTACAGCGAGGATAAC
ATTTCAATTGCACCATACAGGAATTAAAAT

>NZ_CP024592|2|2|118104-118994|CRISPRCasFinder
ATTTCAATTGCACCATACAGGAATTAAAAC	GACGGCACGCTCGGCGGGGATAGAGACCTCGGGGG
ATTTCAATTGCACCATACAGGAATTAAAAC	GCGGCAGATAGCCTCGCCTCCGGCCAAAGGCGGGGGGCGG
ATTTCAATTGCACCATACAGGAATTAAAAC	ATCTTAGCACCTTGTGCTTGTTTTCCAGCTGCTTCAT
ATTTCAATTGCACCATACAGGAATTAAAAC	AGGGTGATATTATGTGCATTTACACTGCCCTGAAGA
ATTTCAATTGCACCATACAGGAATTAAAAC	ACAGCTAACCTCGCTGCCAGCAAGCTGAAAGCGGA
ATTTCAATTGCACCATACAGGAATTAAAAC	CGCGCACAAGTCCGGCAACTCGATAGTACGCCAA
ATTTCAATTGCACCATACAGGAATTAAAAC	AACCTTGACAGTTCGACAGGTATGTAATTGATACAA
ATTTCAATTGCACCATACAGGAATTAAAAC	CTTTATACGTGATATCAAATTCATGAGTTGTTGAAAA
ATTTCAATTGCACCATACAGGAATTAAAAC	CAAAAGGACGTAAAAGGCAAATAGCACATTTGCTGGA
ATTTCAATTGCACCATACAGGAATTAAAAC	CTATTTGCGCGAGCAAAGCCGCTTCCCCTCCGTCCG
ATTTCAATTGCACCATACAGGAATTAAAAC	GGAAGGAGGAGAGCAATGAGAACTACAAACAGTTTCT
ATTTCAATTGCACCATACAGGAATTAAAAC	AGGAGGCAATTCGTCGGAGATCACCCCGTCATGCG
ATTTCAATTGCACCATACAGGAATTAAAAC	GATACGCAAGCATCGATCGTTTACAGCGAGGATAAC
ATTTCAATTGCACCATACAGGAATTAAAAT

>NZ_CP024592|2|1|118104-118994|CRT
ATTTCAATTGCACCATACAGGAATTAAAAC	GACGGCACGCTCGGCGGGGATAGAGACCTCGGGGG
ATTTCAATTGCACCATACAGGAATTAAAAC	GCGGCAGATAGCCTCGCCTCCGGCCAAAGGCGGGGGGCGG
ATTTCAATTGCACCATACAGGAATTAAAAC	ATCTTAGCACCTTGTGCTTGTTTTCCAGCTGCTTCAT
ATTTCAATTGCACCATACAGGAATTAAAAC	AGGGTGATATTATGTGCATTTACACTGCCCTGAAGA
ATTTCAATTGCACCATACAGGAATTAAAAC	ACAGCTAACCTCGCTGCCAGCAAGCTGAAAGCGGA
ATTTCAATTGCACCATACAGGAATTAAAAC	CGCGCACAAGTCCGGCAACTCGATAGTACGCCAA
ATTTCAATTGCACCATACAGGAATTAAAAC	AACCTTGACAGTTCGACAGGTATGTAATTGATACAA
ATTTCAATTGCACCATACAGGAATTAAAAC	CTTTATACGTGATATCAAATTCATGAGTTGTTGAAAA
ATTTCAATTGCACCATACAGGAATTAAAAC	CAAAAGGACGTAAAAGGCAAATAGCACATTTGCTGGA
ATTTCAATTGCACCATACAGGAATTAAAAC	CTATTTGCGCGAGCAAAGCCGCTTCCCCTCCGTCCG
ATTTCAATTGCACCATACAGGAATTAAAAC	GGAAGGAGGAGAGCAATGAGAACTACAAACAGTTTCT
ATTTCAATTGCACCATACAGGAATTAAAAC	AGGAGGCAATTCGTCGGAGATCACCCCGTCATGCG
ATTTCAATTGCACCATACAGGAATTAAAAC	GATACGCAAGCATCGATCGTTTACAGCGAGGATAAC
ATTTCAATTGCACCATACAGGAATTAAAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP024592.1\|WP_010956473.1\|117593_117857_+\|CRISPR-associated-endonuclease-Cas2	cas2	cd09725_cas2_CAS-I:CAS-II:CAS-III:CAS-V	gnl\|CDD\|187856
NZ_CP024592.1\|WP_077094162.1\|110851_111457_+\|hypothetical-protein	cas5	mkCas0069_cas5_CAS-I-B	unknown
NZ_CP024592.1\|WP_077094166.1\|116577_117594_+\|type-I-B-CRISPR-associated-endonuclease-Cas1	cas1	cd09722_cas1_CAS-I-B	gnl\|CDD\|274695
NZ_CP024592.1\|WP_077094164.1\|113593_114892_+\|hypothetical-protein	cas8b6	mkCas0111_cas8b6_CAS-I-B	unknown
NZ_CP024592.1\|WP_077094165.1\|116068_116581_+\|CRISPR-associated-protein-Cas4	cas4	pfam01930_cas4_CAS-I	gnl\|CDD\|366863
NZ_CP024592.1\|WP_099840430.1\|119168_120917_-\|phospho-sugar-mutase	unknown	unknown	gnl\|CDD\|100092
NZ_CP024592.1\|WP_099840868.1\|114900_116010_+\|CRISPR-associated-protein-Cas7	cas7	mkCas0088_cas7_CAS-I-B	unknown
NZ_CP024592.1\|WP_099840429.1\|107599_109531_+\|LTA-synthase-family-protein	unknown	unknown	gnl\|CDD\|293739
NZ_CP024592.1\|WP_077094163.1\|111449_113582_+\|CRISPR-associated-helicase/endonuclease-Cas3	cas3	COG1203_cas3_CAS-I	gnl\|CDD\|224124
NZ_CP024592.1\|WP_130267223.1\|109867_110104_+\|DUF1661-domain-containing-protein	unknown	unknown	gnl\|CDD\|285160
NZ_CP024592.1\|WP_099840433.1\|130621_131248_+\|signal-peptidase-I	unknown	unknown	gnl\|CDD\|274044
NZ_CP024592.1\|WP_077094455.1\|120989_121727_-\|DNA-repair-protein-RecO	unknown	unknown	gnl\|CDD\|376822
NZ_CP024592.1\|WP_054191491.1\|129234_130632_+\|signal-peptidase-I	unknown	unknown	gnl\|CDD\|182787
NZ_CP024592.1\|WP_099840431.1\|122296_124798_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP024592.1\|WP_099840432.1\|128502_129219_+\|4-hydroxy-tetrahydrodipicolinate-reductase	unknown	unknown	gnl\|CDD\|234595
NZ_CP024592.1\|WP_021664493.1\|127098_128442_+\|deoxyguanosinetriphosphate-triphosphohydrolase-family-protein	unknown	unknown	gnl\|CDD\|273571
NZ_CP024592.1\|WP_077094161.1\|110179_110845_+\|CRISPR-associated-endoribonuclease-Cas6	cas6	cd09652_cas6_CAS-I:CAS-III	gnl\|CDD\|273848
NZ_CP024592.1\|WP_004583655.1\|125094_125454_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_077094457.1\|125962_126955_+\|putative-sulfate-exporter-family-transporter	unknown	unknown	gnl\|CDD\|225411
NZ_CP024592.1\|WP_099840434.1\|131268_131907_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|378083

Protein	Function_ID	Function_description	E-value
NZ_CP024592.1\|WP_010956473.1\|117593_117857_+\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|187856	cd09725, Cas2_I_II_III, CRISPR/Cas system-associated protein Cas2. 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; Cas2 is present in majority of CRISPR/Cas systems along with Cas1; RNAse specific to U-rich regions; Possesses an RRM/ferredoxin fold.	2.04042e-30
NZ_CP024592.1\|WP_021664493.1\|127098_128442_+\|deoxyguanosinetriphosphate-triphosphohydrolase-family-protein	gnl\|CDD\|273571	TIGR01353, dGTP_triPase, deoxyguanosinetriphosphate triphosphohydrolase, putative. dGTP triphosphohydrolase (dgt) releases inorganic triphosphate, an unusual activity reaction product, from GTP. Its activity has been called limited to the Enterobacteriaceae, although homologous sequences are detected elsewhere. This finding casts doubt on whether the activity is shared in other species. In several of these other species, the homologous gene is found in an apparent operon with dnaG, the DNA primase gene. The enzyme from E. coli was shown to bind coopertatively to single stranded DNA. The biological role of dgt is unknown. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions].	4.95914e-160
NZ_CP024592.1\|WP_077094166.1\|116577_117594_+\|type-I-B-CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|274695	TIGR03641, cas1_HMARI, CRISPR-associated endonuclease Cas1, subtype I-B/HMARI/TNEAP. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is 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 Cas1 subgroup that includes Cas1 proteins of the related HMARI and TNEAP subtypes of CRISPR/Cas system.	8.82054e-165
NZ_CP024592.1\|WP_099840431.1\|122296_124798_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	2.57331e-42
NZ_CP024592.1\|WP_099840430.1\|119168_120917_-\|phospho-sugar-mutase	gnl\|CDD\|100092	cd05799, PGM2, This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.	0
NZ_CP024592.1\|WP_077094455.1\|120989_121727_-\|DNA-repair-protein-RecO	gnl\|CDD\|376822	pfam02565, RecO_C, Recombination protein O C terminal. Recombination protein O (RecO) is involved in DNA repair and pfam00470 pathway recombination.	1.15752e-18
NZ_CP024592.1\|WP_077094163.1\|111449_113582_+\|CRISPR-associated-helicase/endonuclease-Cas3	gnl\|CDD\|224124	COG1203, COG1203, CRISPR-associated helicase Cas3 [Defense mechanisms].	4.36426e-60
NZ_CP024592.1\|WP_130267223.1\|109867_110104_+\|DUF1661-domain-containing-protein	gnl\|CDD\|285160	pfam07877, DUF1661, Protein of unknown function (DUF1661). This is a family containing bacterial proteins of unknown function. Many of the proteins in this family are hypothetical.	1.62527e-05
NZ_CP024592.1\|WP_099840433.1\|130621_131248_+\|signal-peptidase-I	gnl\|CDD\|274044	TIGR02227, Inactive_signal_peptidase_IA., signal peptidase I, bacterial type. This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking].	1.23001e-11
NZ_CP024592.1\|WP_099840429.1\|107599_109531_+\|LTA-synthase-family-protein	gnl\|CDD\|293739	cd16015, LTA_synthase, Lipoteichoic acid synthase like. Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.	2.52151e-65
NZ_CP024592.1\|WP_054191491.1\|129234_130632_+\|signal-peptidase-I	gnl\|CDD\|182787	PRK10861, PRK10861, signal peptidase I.	8.2325e-17
NZ_CP024592.1\|WP_077094165.1\|116068_116581_+\|CRISPR-associated-protein-Cas4	gnl\|CDD\|366863	pfam01930, Cas_Cas4, Domain of unknown function DUF83. This domain has no known function. The domain contains three conserved cysteines at its C-terminus.	2.08403e-68
NZ_CP024592.1\|WP_099840432.1\|128502_129219_+\|4-hydroxy-tetrahydrodipicolinate-reductase	gnl\|CDD\|234595	PRK00048, PRK00048, dihydrodipicolinate reductase; Provisional.	1.11726e-51
NZ_CP024592.1\|WP_099840434.1\|131268_131907_+\|hypothetical-protein	gnl\|CDD\|378083	pfam08889, WbqC, WbqC-like protein family. This family of proteins are functionally uncharacterized. However it is found in an O-antigen gene cluster in E. coli and other bacteria suggesting a role in O-antigen production. Feng et al. suggest that wbnG may code for a glycine transferase.	1.71749e-44
NZ_CP024592.1\|WP_077094161.1\|110179_110845_+\|CRISPR-associated-endoribonuclease-Cas6	gnl\|CDD\|273848	TIGR01877, CRISPR-associated_endoribonuclease_Cas6_1, CRISPR-associated endoribonuclease Cas6. CRISPR is a term for Clustered, Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR-Associated) proteins. This broadly distributed, highly divergent Cas family is now characterized as an endoribonuclease that generates guide RNAs for host defense against phage and other invaders. The family contains a C-terminal motif GXGXXXXXGXG, where the each X between two Gly is hydrophobic and the spacer XXXXX contains (usually) one Arg or Lys. The seed alignment for the current version of this model has gappy columns removed. Members of this protein family are found associated with several different CRISPR/cas system subtypes, and consequently we designate this family Cas6.	2.16452e-35
NZ_CP024592.1\|WP_077094457.1\|125962_126955_+\|putative-sulfate-exporter-family-transporter	gnl\|CDD\|225411	COG2855, COG2855, Predicted membrane protein [Function unknown].	7.13383e-54

>NZ_CP024592.1|WP_010956473.1|117593_117857_+|CRISPR-associated-endonuclease-Cas2
MYIILVYDIGEKRVGKMLKLCRKYLNWIQNSVFEGEISEVKLLELKSRAAGIMEKEEDSLIIFSSRQERWLEKEIIGKERSATDIFL
>NZ_CP024592.1|WP_077094166.1|116577_117594_+|type-I-B-CRISPR-associated-endonuclease-Cas1
MKKTYYLFNPGELSRKDNTIRFVPIQEGENGQEQAGQARYIPVEGISDFYVFGSLRANSSLYNFLGSNDIAVHFFDYYENYTGSFMPRDFLLSGKMLLAQASAYKNKKKRLFLARKFIEGAASNMQKNLAYYNNRGKDMQPMMELIDKYSLRLEETTTIEALMGIEGNIRQAYYDAFNLIIDPFEMGVRSKQPPQNEVNALISFGNMMCYTLCLKAIHQSQLNPTISFLHTPGERRYSLCLDISEVFKPILVDRTIFKVMNKRIIQAKHFDKQLNKCILNPSGKKLFVQAFEERLSETIRHRKLNRSVSFRHLVKLECYKIAKDILGIEEYQPFKMYW
>NZ_CP024592.1|WP_077094165.1|116068_116581_+|CRISPR-associated-protein-Cas4
MAIITGTHFNYHQVCRRKLWLFSAGITMEHTSDLVYEGKLIHETTYPQRPERYQELELDGIKIDFYDAKNRVVHEVKKSNKISPAHRLQLLYYLYVLERNGVSGATGILEYPTLRKKEEVILSDIDRERIREIEQEILQIISREDCPPVIDSGICKNCSYYEFCFSGEEQ
>NZ_CP024592.1|WP_099840868.1|114900_116010_+|CRISPR-associated-protein-Cas7
MQPVLYLRGLKNVSYSVFAVDKGQKFYRDPLFSSHTHIGKKLPFSSGQQVKRCIIDALLSNLNVERAPVTFVFEQKNLKEGEVLSLCDPNYPDQLLGGWMLANSKKEKTKKKEKEIKDEDSDENSDGSIKKRRSPLSISALTPLHPLLAEYNTENISFDRSDNKSLHRVIIRDDKGNLLSDEETKMILEGTHRDLYRKWIQDSGRTTGLFVYDVAIDLRTLFSVSIYDVPNNIKLDEKKWKRGKNAFGECWTLCKSDREKLIPALAHALVNWRITSNQARTFSLMETLAIAIGDNANAQAGAIRARLIDDESGKPKATLVLDENAGANLYITPPCAAHILLNNEDVEALRKAEKHLIEVMLAFDYDNQF
>NZ_CP024592.1|WP_077094164.1|113593_114892_+|hypothetical-protein
MLTSVIGKIFLEAYNKQNNRQYTPKEFFLEVYYPIFFGHEKYLIWVQNSAVVQKLNKTEIPSEKFEGAIRQKEIIKIKKKKLIDKIENAISFDASIAVGYKAEGYTATTSGQTCIHNHKMKKDDAYFSWIGAGLGIRIGGAIILFDKPQLLLDIAEGWGKYRELINSRPNLGGNKIEAWNAIWINRKYEQIDHSLDLNQYIKENNDSIELKTISWVQLFIHICKHFKDPKMMGYFYDLGKTNKTFGFVPIVLSSIRKSYEFTNQIFRDYDSIILDELFQSWKTEYGLDIACRRGVIGLYAMEPKDLWSYLYSNKKSPKKKDKIELLTYQNWLLAMLNNKQLWEKSMHVAELLHAYRQGQSKDRTNRDNALKELLSHPYQSSFMRNIPKILEEIEDKKDLMEICRIINSMPSDSVPYFVSLIKIHYINIAGKL
>NZ_CP024592.1|WP_077094163.1|111449_113582_+|CRISPR-associated-helicase/endonuclease-Cas3
MNDLRLILAKSDGTPLIQHLKDVAMVAEVLAHHLGLSVEIARKGAHLHDIGKTSCIFQQKLVGINPPFKKSFRHEIASLFFLSLLQDKEERCAVIEMVAAHHRSICNDMPKRGLLGLLDLEDKYPHCFELHSEGFEQWSQEALGILHELGWETHPITMDEARSNYQEAVDYCSSLGRNCSQWKGLLMAADHFASGLDGQTEDTLRKLFIIPDLSYYRNRRSELYPLSLLSADDERKHTLVTAPTGAGKTDFLLRRCRGRVFYTLPFQASINAMYDRLKADLQDTDAQIYPLHAASILKLNGDYERILSRHVGASIKVLTPHQIAALAFGLKGYEVTALDIRGCDVILDEIHTYRKETQAMVLKIVEILIALGCRIHIGTATMPTDLYTGLLRLLGGETAVYEVKLPKEVLKGFDRHTIHKVGSMEDVGPVIQKAVEQGQKILMVCNQVKRAQQLYQDVIGKYPAIPTLLVHSRFKRGHRAQLELELKERYNQCQGPCIVVSTQVVEVSLDISFDLMLTECAPIDALIQRFGRINRKRSLETIGQTKSIYVIAPPENEKEALPYELEILQRSYSSLPHCEVLHEADVQQLLDSVYPEVMALDIDMLTVFQEGKWVMKKLKHNPKSALFETLDINSACCLMEKDREVYENGSFAERTLLEIPVARSITQRNNLTPITCGVHPFLIPDQAYDSKLGLLEEFAAPRYYNSFEII
>NZ_CP024592.1|WP_077094162.1|110851_111457_+|hypothetical-protein
MEDKIFFVVHYTGPFGYIKPWSAVRDIETYSQQFLTPSIIEGMEKKLFPEMLIKKGIRKIARHKLSCMSMSVQQEKTQTQAWEGKGKGKGRTYTRPQSILKRGVMLHPSLYLAFTSEEDAVIAARQHLCLCRNEDVVLPDTEILKMDEETFNALPGFELRFGKDYPDAFMVGFNRFDENTPMYGRIEIGGEAVLAPPKSNE
>NZ_CP024592.1|WP_077094161.1|110179_110845_+|CRISPR-associated-endoribonuclease-Cas6
MRIELSIKADDSLVSFSHQHLLVGTLQKWLGENDMHGKSISYSFSRLNGGKFVSELNSILFADWANMFVSAHDPELIRRMLAGIRQDPEMFKSLCVREVTVIEDPDMTDREIFFPASPILLKRWREDNGFDHIVYTDEAANALLTENLRKKLQAVGIDDPTATASFVPDQGKAKVMLIDYRGVKNKASWCPIRIIGNAETKLFAWNAGIGNSTGIGFGAIK
>NZ_CP024592.1|WP_130267223.1|109867_110104_+|DUF1661-domain-containing-protein
MRPRKTWRVNFFVVVREIKNSRATTKNFLLRFFRKHAPQSEHFRLVFYTPALAPSLFSVRFSQNCSERWMLYIRFPRK
>NZ_CP024592.1|WP_099840429.1|107599_109531_+|LTA-synthase-family-protein
MKTLFERGELLFRKRSGFCYVIGVFVLFLLYFLFQKVIFLLVYSGRLAGIGTSSGDIAAIFLYGLRHDAAVAAYLTVLPLLFAGINAIAGWGEKKIGRILRQILKHYYTLISFFVGLIYTADLMLFGYWGFRLDATPLFYLRQPQEAMASVTAPQLLIGLLITVVFVCIPAFVLHRFHRRYFPTKVVAHPHIADIWKPVVGGAFLFLLIRGGVGVATLNVGSVFHSPKQLHNQAAVNPVFSFLYTCMHSEEDYSNYQFLSEEDCIKAFEQLRLYGCSDGSEVRESASDSTERILSTDRPNIVLILLESFSANAVGCLGGTPGHTPCIDSLAQNGILFSQAFASSFRTDRGTVATLSGYPSQPNSSIIKYPNKVRNLPGIAASLRTVGYSTHHLYGGDADFTNVRSYLYATGYDEVTDVSSFPIKTRLSKWGTPDHISFPRLLDDCRRLEKEKKPYFYSFLTLSSHEPFDVPSQHHPDPYLNSVFYTDSCFGDYIRGMQQSPQWKNTLIITVSDHGYPYPADQAMPDQPGRYGIVMLWTGGAILRPIRFEEVVSQSDLPATLLAQLGLAHDEFVFSKDVFRRNSPHFAYFSFPGLVGLATSEGTTIYDFAGDKIVYGHEAPLADQRAIAAKVMLQSVMKDMLSR
>NZ_CP024592.1|WP_099840430.1|119168_120917_-|phospho-sugar-mutase
METDKLLDQVRAKARIWLGTEYDDSTRKAVQAMLDNTDTTELVDAFYRDLEFGTGGLRGIMGAGTNRMNRYTVGAATQGLSNYLLREFAGSSDISVVIGYDCRNNSRFFADTAAAVFSANGIRVYLFEELRPTPEISYAIRHLGCKSGVMITASHNPKEYNGYKAYWEDGAQIIAPHDRNIIAEVNRIRSVDEIKFEAKPELIRMIGENIDSAFIAEVKALSLSPESIARHRDMKIVYTPIHGTGSTVVPRALREYGFANIIHVPEQDVVSGDFPTVHSPNPEEPAALALAIAKAEETGADLVLASDPDADRIGVAVRNNEGRIVLINGNEICSLLIYYSIMRRKELGDLHPDDYIVKTIVTTELIRDIAKKEHVSMFDCYTGFKWIAAVIRENEGRRRYIGGGEESYGFLWEDFIRDKSSVSACALFCEMAAWALDRGMSVYRLIRSIYLEYGLYYEKGLSVVRKGKSGAEEIEAMMRNYREYAPVELGGSPVQEILDYASLEGKDFTRGEKFSLDMPTTSNVLQYKTEDGTKVSIRPSGTEPKIKFYIGVHFSVANEQELDRAYIVAEEKIATILHDLGV
>NZ_CP024592.1|WP_077094455.1|120989_121727_-|DNA-repair-protein-RecO
MIIVSRAIVLHNTAYNDSYSIAHLFSRESGRVSYLIPRSSKRGKSGGSLRLLISPLNELEITAEHKQHRDLHFIKEAKLCSLHGRIQSDPVRNSIALFLAEFLYLILRLPEADTNLYDFVAFSIDKLEEMDGPMANFHLAFLFRLLVPLGLIPDLQFGGSVIPRWFDPADGRFVPNAPAHGRGIPPHQSTYLQLFNRITFDNMKAFRLSRAERRQVLDYLVDYYRFHLPPFPLLKTPDILSTLFD
>NZ_CP024592.1|WP_099840431.1|122296_124798_-|TonB-dependent-receptor
MKQLNIISFIIAFLFLGTSASAQQSGGSVTGTVVDKSSKEPIAYVQVFVKGTTLGTSTDANGNYSIKGIPSGNQTIVARLMGYSTCEEKVHIEKGGSRHVDLYLTEEILSLDGVVVSANRNETFRRQAPSLVTVLSPELFLKTNSTNLSQGLKFQPGLRVEDNCQNCGFNQVRINGLEGAYSQILIDSHPIFSSLAGVYGLEQMPANMIERVEVIRGGGSALFGSNAVGGVINVITKEPLRNSAEISHSTMTFDHAKGWGSFQNTTQFNGSMLTEDRKAGVMVFGQHNYRPGQDIDGDNFTELPNLRNRSLGFRSYYKTGLYSKATLEYHSMQEYRRGGDRLDNPPFEAQIAEYLQHYINGGSFKFDQGFSGGKDFFSLYASAQDVQRRSYYGGGDYTENLLNGAVQSGSTESDEYNDAFTALTSYGTTKGFDLQGGGMYRHTFGENWDFTGGLEYIYGQLDDRSGYRPSKIDQNTSTFSQYDQLEYKTEKLSALIGARIDYVLLNQDGKRYIDPLFIFSPRANVRYNPNKNLSFRLSYSEGFRAPQYFDEDLHVELAGGTPISRVLSPNLKEERSRSISASFDYYHRADEWQFNIMGEAFSTFISNQFKPSDKVETTSDGKEWIIRTIYNDKDGVSKVYGVNLEGRIAYNKSFDLQLGCTWQRSRYGSIYTAVEADKTTGQAEISVKDYVRTPNLYGYFVATVRPTEHFAINLSGTFTGKMNVVHEAYEGDIPAEHIAPDGSFDFEMNGQQFKGLAEGHAKLVKTPAFADIDLKLSHDFHLASTMTLELNAGIQNIFNSYQKDTDKGPGRASTYVYGPMQPRRIFVGTKINF
>NZ_CP024592.1|WP_004583655.1|125094_125454_-|hypothetical-protein
MKERLNQTVRYFLPILFAVYAGLVISFTHVHIINGVIIVHSHVQWGDNESDPQDNPHSDSELILYNQLSAIFTTYLDTPAIDLKEPVRVVGVVPFFCDNLIALISELTPSNHLRAPPVA
>NZ_CP024592.1|WP_077094457.1|125962_126955_+|putative-sulfate-exporter-family-transporter
MNTDNPKSHISRIAYPAIIVFLILTLLGSLVEKFHPFTSWLTPPVALLMGLAYALIFGSTHRRANKLGSKVLLQYSVVGLGFGMNLGESLASGRDGMMFTIISVFGTLLLGWFIGRKILQMNRNTSALISAGTAICGGSAIAAVGPILKAEEHEMSVALGTVFLLNAVALFIFPSIGHWLALDQQQFGTWAAIAIHDTSSVVGAGSAYGEEALRVATTIKLTRALWIVPLTLVFSFVYKTKGAKRFPVPLFILFFIGAIILNTYLLEAYFPEVGRFVASLARKGLTLSLFFIGASLTKEVIASVGVRALLQGLFLWILISVGSLAFILLI
>NZ_CP024592.1|WP_021664493.1|127098_128442_+|deoxyguanosinetriphosphate-triphosphohydrolase-family-protein
MTMMQWERLLSDKRVGMEHYHQPKQSAQPWERTDFERDYDRMVFSSPFRRLQNKAQVFPLAGNIFVHNRLTHSLEVSCVGRSLGNNITRGLKARYGELPWESGAISAIVSAACLAHDMGNPPFGHSGERAISAYFREGKGRVWEDAVRKEGGRWEDFLHFEGNANAFRLLTHQFEGRRKGGFALTYSTVASIVKYPYSSEMAGKAGKFGFFATEEDTFLMIAEELGMLCRNEHPVKYARYPLVYLVEAADDICYQIMDIEDAYKLRILTYAETENLFLAFCPEEELGHIRGVLDHITDANEQIAYLRSRVISLLVESCTRVFLDHEDEILSGTFSGTLIGAMEPRLKEAYGACARMAYSKIYVARDVVDVELAGHQIFGALIDKMMQALTNPDHAYSRTLLSRVSTQYNIREESLYGKIQCTLDYISGMTDIYALDLYRKITGMNLR
>NZ_CP024592.1|WP_099840432.1|128502_129219_+|4-hydroxy-tetrahydrodipicolinate-reductase
MKIVLIGYGKMGHVIERIACSRGHEVVLTIDAGEEDRFDSIAFRLADVAIEFTRPDAAYANCSRCMDKSVPVVCGTTGWTERLPELEERCRREGKTLFWASNFSIGVNLFFSLGRMFARLMSRHDQYRPHLTEIHHVHKLDAPSGTAITLAEGLIAESPSLDAWRLTETPEENELPITSIREGEVPGTHSISYTSEVDRLTICHEAFGREGFALGAVLAAEYAATHKGFLTMNDLISL
>NZ_CP024592.1|WP_054191491.1|129234_130632_+|signal-peptidase-I
MTFHWKDLTPWRRIKGVAITILYLLFCIWAGPFWLIFLPLIVDYYFFHIIKWGWYKNIRNKTLRIICSWVADIIYCVVAVTFIFAFLFQNFAIPTSSLEKTLLIGDYLFVSKLSYGPRSPMTPLGVPLTHNTMPLTGGKSFSDKPLLPYKRLKGFGHVKEGDLVVFNFPAGDTVAVKQPNPDYYMWKKLVGREELWSNPDFYGEIVYRPVDRRDHYVKRCVGMPGQELSIRNNQIYIDGKEQRNPRNMQLNYLVRMSREMSVDLIDELGISYDDVRAASSEELKASVGSNLIDSASNQPQIIYHLPLTQGMLDKLQAEPSFVKAVVEPTPIGPLYPLEYETGWTRDNYGPIVIPAKGMTVRLTPLNLALYSRCIRNFEGNKLVQKADGTVLINGRTADSYTFKMDYYFMMGDNRHNSADSRYWGFVPEDHIVGKPVFIWLSLNKDKSLFGGKIRFGRMMRTVNAD
>NZ_CP024592.1|WP_099840433.1|130621_131248_+|signal-peptidase-I
MQIKSRYRNRIFFIGLPAVVLLSAVLIRLFLVTTYRVRSDAMLPTYRSGKLLWINRIASPDRGDVLVIKYRQDGEADSRFYLARLIGLPGDTLFLSKGGVVANRQKLKLPTSLLPREPYKIIVPRNDRTYRLTPLSLLAYRRAIEEECSSNISFRRGKLYRDGAETAFFHFRRNYYWILADNPASGPDSRHLGIVPEESIEGVVMNAN
>NZ_CP024592.1|WP_099840434.1|131268_131907_+|hypothetical-protein
MNLLSPSDPIVLSTAYLPPIQYFTKLLHPEGVLLETAENFVKQSYRNRCHIAGPEGMQPLTIPVEKSPSPKAPIRDIRISEHGNWRHLHLNALISSYGSAPFFDHYMTEIEPFYRHKYTFLWDFNLDLLSVCLEWLDISPLIMFTSEYVEDCPNDFRYSIRPKQALEDESFRPRVYYRTFAHKYGFLPNLSIVDLIFHEGPSAIQTLKECIR

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Crispr_ID: NZ_CP024592_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP024592_3

151005-151552

TypeIII

Consensus_repeat	Method
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	CRISPRCasFinder
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	CRT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	PILER-CR

7 spacers

cas2,cas1,cmr6gr7,cmr5gr11,cmr4gr7,cmr3gr5,cas10,cmr1gr7

The CRISPR arrays of NZ_CP024592_3

>merge|NZ_CP024592|3|151005-151552|CRISPRCasFinder,CRT,PILER-CR
CTCACTATACATACACAGTCCGTAAGGCTATTAAGACTTTTTGTCTGAATTCAGACGATCTGCCTTTTGTCTCACTATACATACACAGTCCGTAAGGCTATTAAGACACGGGACACCCAGGAACAAGGGGATGGACTGTTTTTTCTCACTATACATACACAGTCCGTAAGGCTATTAAGACCTAGATTTCTCAAAGATGTGAATCTTTATACTACCAGCTCACTATACATACACAGTCCGTAAGGCTATTAAGACTTTTTTGCCCTAAAACCAAACAAATATATTTTCCTGTTACTCACTATACATACACAGTCCGTAAGGCTATTAAGACTTCAGGCAATGGAGTCGGGAAGTTCATGGTAACGGCTCACTATACATACACAGTCCGTAAGGCTATTAAGACACCAATGCCAGTTTTATTAGACGTATTCATTGATTTCTCACTATACATACACAGTCCGTAAGGCTATTAAGACCCTTTTCTTGTTCTTTCTCTAAATGCCGAATCGCTCTCACTATACATACACAGTCCGTAAGGCTATTAAGAC

>NZ_CP024592|3|3|151005-151552|CRISPRCasFinder
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	TTTTTGTCTGAATTCAGACGATCTGCCTTTTGT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	ACGGGACACCCAGGAACAAGGGGATGGACTGTTTTTT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	CTAGATTTCTCAAAGATGTGAATCTTTATACTACCAG
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	TTTTTTGCCCTAAAACCAAACAAATATATTTTCCTGTTA
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	TTCAGGCAATGGAGTCGGGAAGTTCATGGTAACGG
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	ACCAATGCCAGTTTTATTAGACGTATTCATTGATTT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	CCTTTTCTTGTTCTTTCTCTAAATGCCGAATCGCT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC

>NZ_CP024592|3|2|151005-151552|CRT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	TTTTTGTCTGAATTCAGACGATCTGCCTTTTGT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	ACGGGACACCCAGGAACAAGGGGATGGACTGTTTTTT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	CTAGATTTCTCAAAGATGTGAATCTTTATACTACCAG
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	TTTTTTGCCCTAAAACCAAACAAATATATTTTCCTGTTA
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	TTCAGGCAATGGAGTCGGGAAGTTCATGGTAACGG
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	ACCAATGCCAGTTTTATTAGACGTATTCATTGATTT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	CCTTTTCTTGTTCTTTCTCTAAATGCCGAATCGCT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC

>NZ_CP024592|3|2|151075-151552|PILER-CR
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	ACGGGACACCCAGGAACAAGGGGATGGACTGTTTTTT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	CTAGATTTCTCAAAGATGTGAATCTTTATACTACCAG
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	TTTTTTGCCCTAAAACCAAACAAATATATTTTCCTGTTA
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	TTCAGGCAATGGAGTCGGGAAGTTCATGGTAACGG
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	ACCAATGCCAGTTTTATTAGACGTATTCATTGATTT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC	CCTTTTCTTGTTCTTTCTCTAAATGCCGAATCGCT
CTCACTATACATACACAGTCCGTAAGGCTATTAAGAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP024592.1\|WP_012458602.1\|156563_157403_+\|DNA-adenine-methylase	unknown	unknown	gnl\|CDD\|273146
NZ_CP024592.1\|WP_099840441.1\|145379_146105_+\|type-III-B-CRISPR-module-RAMP-protein-Cmr4	cmr4gr7	cd09682_cmr4gr7_CAS-III-B	gnl\|CDD\|187813
NZ_CP024592.1\|WP_099840447.1\|154987_156040_-\|hemagglutinin	unknown	unknown	unknown
NZ_CP024592.1\|WP_099840446.1\|152618_154625_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_099840445.1\|150455_150746_+\|CRISPR-associated-endonuclease-Cas2	cas2	pfam09827_cas2_CAS-I:CAS-II:CAS-III	gnl\|CDD\|187856
NZ_CP024592.1\|WP_099840450.1\|162172_163171_+\|mechanosensitive-ion-channel	unknown	unknown	gnl\|CDD\|182386
NZ_CP024592.1\|WP_021677506.1\|164924_166331_-\|sugar-transferase	unknown	unknown	gnl\|CDD\|274398
NZ_CP024592.1\|WP_097555163.1\|141206_142478_+\|hypothetical-protein	cmr1gr7	mkCas0086_cmr1gr7_CAS-III-B	unknown
NZ_CP024592.1\|WP_099840443.1\|146538_147285_+\|type-III-B-CRISPR-module-RAMP-protein-Cmr6	cmr6gr7	cd09661_cmr6gr7_CAS-III-B	gnl\|CDD\|187792
NZ_CP024592.1\|WP_004583632.1\|163131_164928_-\|chloride-channel-protein	unknown	unknown	gnl\|CDD\|238233
NZ_CP024592.1\|WP_099840442.1\|146101_146542_+\|type-III-B-CRISPR-module-associated-protein-Cmr5	cmr5gr11	mkCas0098_cmr5gr11_CAS-III-B	unknown
NZ_CP024592.1\|WP_099840439.1\|142452_144153_+\|type-III-B-CRISPR-associated-protein-Cas10/Cmr2	cas10	cls000742_cas10_CAS-III	gnl\|CDD\|274208
NZ_CP024592.1\|WP_004585649.1\|157395_158685_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_099840444.1\|147340_150436_+\|CRISPR-associated-endonuclease-Cas1	cas1	cd09634_cas1_CAS-I:CAS-II:CAS-III:CAS-V	gnl\|CDD\|187766
NZ_CP024592.1\|WP_143733548.1\|151813_151921_-\|DUF1661-domain-containing-protein	unknown	unknown	gnl\|CDD\|285160
NZ_CP024592.1\|WP_012458620.1\|140954_141191_+\|hypothetical-protein	cmr1gr7	mkCas0102_cmr1gr7_CAS-III-B	unknown
NZ_CP024592.1\|WP_099840438.1\|139369_140953_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_099840449.1\|159778_160678_+\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP024592.1\|WP_099840440.1\|144154_145366_+\|type-III-B-CRISPR-module-associated-protein-Cmr3	cmr3gr5	cd09656_cmr3gr5_CAS-III-B	gnl\|CDD\|273855
NZ_CP024592.1\|WP_097626381.1\|161183_162071_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|274350

Protein	Function_ID	Function_description	E-value
NZ_CP024592.1\|WP_012458602.1\|156563_157403_+\|DNA-adenine-methylase	gnl\|CDD\|273146	TIGR00571, DNA_adenine_methylase, DNA adenine methylase (dam). All proteins in this family for which functions are known are DNA-adenine methyltransferases. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). The DNA adenine methylase (dam) of E. coli and related species is instrumental in distinguishing the newly synthesized strand during DNA replication for methylation-directed mismatch repair. This family includes several phage methylases and a number of different restriction enzyme chromosomal site-specific modification systems. [DNA metabolism, DNA replication, recombination, and repair].	1.52398e-117
NZ_CP024592.1\|WP_099840441.1\|145379_146105_+\|type-III-B-CRISPR-module-RAMP-protein-Cmr4	gnl\|CDD\|187813	cd09682, Cmr4_III-B, CRISPR/Cas system-associated RAMP superfamily protein Cmr4. 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; RAMP superfamily protein; This protein is a subunit of Cmr complex.	4.44027e-78
NZ_CP024592.1\|WP_097626381.1\|161183_162071_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|274350	TIGR02917, TPR_domain_protein, putative PEP-CTERM system TPR-repeat lipoprotein. This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.	1.12879e-14
NZ_CP024592.1\|WP_099840450.1\|162172_163171_+\|mechanosensitive-ion-channel	gnl\|CDD\|182386	PRK10334, PRK10334, small-conductance mechanosensitive channel MscS.	4.06596e-59
NZ_CP024592.1\|WP_021677506.1\|164924_166331_-\|sugar-transferase	gnl\|CDD\|274398	TIGR03025, EPS_sugtrans, exopolysaccharide biosynthesis polyprenyl glycosylphosphotransferase. Members of this family are generally found near other genes involved in the biosynthesis of a variety of exopolysaccharides. These proteins consist of two fused domains, an N-terminal hydrophobic domain of generally low conservation and a highly conserved C-terminal sugar transferase domain (pfam02397). Characterized and partially characterized members of this subfamily include Salmonella WbaP (originally RfbP), E. coli WcaJ, Methylobacillus EpsB, Xanthomonas GumD, Vibrio CpsA, Erwinia AmsG, Group B Streptococcus CpsE (originally CpsD), and Streptococcus suis Cps2E. Each of these is believed to act in transferring the sugar from, for instance, UDP-glucose or UDP-galactose, to a lipid carrier such as undecaprenyl phosphate as the first (priming) step in the synthesis of an oligosaccharide "block". This function is encoded in the C-terminal domain. The liposaccharide is believed to be subsequently transferred through a "flippase" function from the cytoplasmic to the periplasmic face of the inner membrane by the N-terminal domain. Certain closely related transferase enzymes, such as Sinorhizobium ExoY and Lactococcus EpsD, lack the N-terminal domain and are not found by this model.	3.91045e-129
NZ_CP024592.1\|WP_099840443.1\|146538_147285_+\|type-III-B-CRISPR-module-RAMP-protein-Cmr6	gnl\|CDD\|187792	cd09661, Cmr6_III-B, CRISPR/Cas system-associated RAMP superfamily protein Cmr6. 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; RAMP superfamily protein; This protein is a subunit of Cmr complex.	6.87494e-69
NZ_CP024592.1\|WP_099840439.1\|142452_144153_+\|type-III-B-CRISPR-associated-protein-Cas10/Cmr2	gnl\|CDD\|274208	TIGR02577, thermophile-specific_DNA_repair_system, CRISPR-associated protein Cas10/Cmr2, subtype III-B. This model represent a Crm2 family of the CRISPR-associated RAMP module, a set of six genes recurring found together in prokaryotic genomes. This gene cluster is found only in species with CRISPR repeats, usually near the repeats themselves. Because most of the six (but not this family) contain RAMP domains, and because its appearance in a genome appears to depend on other CRISPR-associated Cas genes, the set is designated the CRISPR RAMP module. This protein, typified by TM1794 from Thermotoga maritima, is designated Crm2, for CRISPR RAMP Module protein 2.	2.85465e-76
NZ_CP024592.1\|WP_099840444.1\|147340_150436_+\|CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|187766	cd09634, Cas1_I-II-III, CRISPR/Cas system-associated protein Cas1. 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; Cas1 is the most universal CRISPR system protein thought to be involved in spacer integration; Cas1 is metal-dependent deoxyribonuclease, also binds RNA; Shown to possess a unique fold consisting of a N-terminal beta-strand domain and a C-terminal alpha-helical domain.	5.04063e-68
NZ_CP024592.1\|WP_143733548.1\|151813_151921_-\|DUF1661-domain-containing-protein	gnl\|CDD\|285160	pfam07877, DUF1661, Protein of unknown function (DUF1661). This is a family containing bacterial proteins of unknown function. Many of the proteins in this family are hypothetical.	0.000634986
NZ_CP024592.1\|WP_004583632.1\|163131_164928_-\|chloride-channel-protein	gnl\|CDD\|238233	cd00400, Voltage_gated_ClC, CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function.	9.43748e-102
NZ_CP024592.1\|WP_099840445.1\|150455_150746_+\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|187856	cd09725, Cas2_I_II_III, CRISPR/Cas system-associated protein Cas2. 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; Cas2 is present in majority of CRISPR/Cas systems along with Cas1; RNAse specific to U-rich regions; Possesses an RRM/ferredoxin fold.	9.80316e-16
NZ_CP024592.1\|WP_099840449.1\|159778_160678_+\|T9SS-type-A-sorting-domain-containing-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.	6.38864e-11
NZ_CP024592.1\|WP_099840440.1\|144154_145366_+\|type-III-B-CRISPR-module-associated-protein-Cmr3	gnl\|CDD\|273855	TIGR01888, Hypothetical_protein_SSO1730, CRISPR type III-B/RAMP module-associated protein Cmr3. CRISPR is a term for Clustered Regularly Interspaced Short Palidromic Repeats. A number of protein families appear only in association with these repeats and are designated Cas (CRISPR associated) proteins. This highly divergent family is found in at least ten different archaeal and bacterial species as part of the CRISPR RAMP modulue but is not a member of the RAMP superfamily itself. A typical example is TM1793 from Thermotoga maritima.	3.33819e-72

>NZ_CP024592.1|WP_099840445.1|150455_150746_+|CRISPR-associated-endonuclease-Cas2
MNDKKLPVAYDISSNRRRRKVARILEQCGIRINKSVFICSLRELTMDKLVEAVTSQTAKRDKVFFLPLCQHCYTAAWMSGHPTLPKSRRKRKSIVG
>NZ_CP024592.1|WP_099840444.1|147340_150436_+|CRISPR-associated-endonuclease-Cas1
MPLSTDSLPIFLSDFTAYHFSVRFRAERAIAFERKWYFMPRFALGNALKNSEQYAYLYGQIFKPQEEDTDESKGPGNTSRLIIRADKPSRKSLEAGEAMDLYITVVTRDPLLVGDFLSFLPEWQAYNFFRENDLTYDSYRLYNPTTQKYESGLRVEDAALTVDFFSRQAIRWGEILSVRFLSPASIKVDQILSAEIPYSRLMNRLSRRLYELYTQYLSRGETSVERYIFPDHDGLIYSQISMPRKATIKENRQYDMSGILGQLFYRVPYDPVAALMLSMAHWVHIGNHTIVGNGQIESTPGNDTLYRKWLSSLAADRDLPMAEAERQDLLEALRICSYIPQPYHSVNIPKGDGSYRQLHIPSAVDLHLQRSLAGILYPITESLSIAQSYAYRKGKGAVAAVRRVQHLLDSLDENYTVVRCDIDNFFDSIPVASLLQKVQRTTEDPLLTRMLSLWMKSGVVDRKQQYAPASSGIPQGSPLAPLLSNLYLEDTDRYIAGHITTEFIRYADDLLLFLPEKVDPLNALQDLSEHLKYRKGLKLNRDFVVSSIKSSFSFLGITFCADGSRSMSRDKKEGLKRKITLALHRDTENFSALSETIHGMEQYYRKLLEKVDIEAIDEVAATVYATHIASLPTSEARKSAKDNLLRLGFLSSETAKQTLREAMRQTEVSSADNFPIKKESEILREQQKRQLQEREEIFDLVVTEPGAFIGISRNHVLVRKYGKTICKQPAAQIEQISIISDGVSLSSNVTKYCRKKNIRVIFYNATGQAYASLNGMNTILPSVMEAQMRLSEEKKREFVLTLIKNKVRNQGKLLRYYHKYYRHDKELKEPLSNAIAELKQLEGIPIAEGSSLADFRQHAMLHEARCAQVYWRAFALLVHRSGHEFEGREHKGAEGLVNQMLNYGYAILRSYVMKTIDLWQLNPNIGILHSTQDNKPALCFDLMEQYRAFVVDRSILALLAKGEDVGQNNKGLLDMPTRSRIISKINERWFATESYRSGEKLFSDIMKLQTKDVRAFCCGKVKRIKFYTPKW
>NZ_CP024592.1|WP_099840443.1|146538_147285_+|type-III-B-CRISPR-module-RAMP-protein-Cmr6
MNFGHWYYREYFNTINLDSKGIVTNFSTFNKGENDKLIKGAALPPYDKVNDIKDVTSFELKTCYPGLLCGVGYHHEINNPKNEPKEDDAPEVYNLGMYFDYTSGLPVIPGSSIKGMLRSAIEEWDFLADYELNNGVTREEIIEKVFVGKEYSIYDRDIFLDAIPIRVDNTLFGEDYITHHPNPLQNPNPVRFLRVEPGVTYQFRFILKDHGEKLTVDFKTKLFKAIICTFGLGAKTNVGYGQFVEPEK
>NZ_CP024592.1|WP_099840442.1|146101_146542_+|type-III-B-CRISPR-module-associated-protein-Cmr5
MNKKTIQDLIPKAMQAIEGVGIVGKDKKFKKVHEGYINALGPNIIQSGLLPTLIFYNKDKRELWLRALYYMAVGEEDEMTDESSTVIIRLIIGKEGGRIENLKPKAKEWERKILEYAVALKLALRTFVAEEPETSNTEQQQEGGAQ
>NZ_CP024592.1|WP_099840441.1|145379_146105_+|type-III-B-CRISPR-module-RAMP-protein-Cmr4
MKTAAYMIHCLTNMHVGKGDATYEVVDKCVQRDVTTGMPCIYSSSLKGALRQFFSKQGFADIKYVFGSDVSRDVKDESKGNESDNSNEENPKEHSVGNFTFFQANLLAYPVQTTQEGATYILKTNKALQESIKELAKLLSAPFDIEKILPKETKKDLSNEALEQLPVIARNQLDNGKSENLWYEEVVPAESRFVFFVSYDDEEIFAKFDKIIQEKVIQIGANGSIGYGFCKIANVTNPFKK
>NZ_CP024592.1|WP_099840440.1|144154_145366_+|type-III-B-CRISPR-module-associated-protein-Cmr3
MSTYLIKLTPLDKFFFGQKKTFGDDNANYFVYSSHFPQQTTLLGLLRYQLLQIAGEEVFKDNKIQDEHKAGELIGKQSFSPFVKDKLQFGIIQSLSPVFIIDKKKDEGKEEYFLPVGKRFQKKKEKAPYSLLHLSCEDECPPIFESRESQKEKEEAYDPKKGLASCWLSSKSHTLLNEEDFFTKDERIGIRKDYEGATNDDAFFCQRYYRFKNFKKVVEDEEGNECKQPPVRVHDFCFATVLETEKAIEHEKLNGRIVYLGGERQPFLMEVSEETFKLNIESSTLTSDEKHYTVVLLSDAMIDPDHLSKVRFASTEVKDFACLLTHVGTQKFYNKENKRQEHYLKESATALSLQKELYARGSVFYFDTKEQANQFCEDLEKVPNFHTIGYNHAIIIEPTKTKE
>NZ_CP024592.1|WP_099840439.1|142452_144153_+|type-III-B-CRISPR-associated-protein-Cas10/Cmr2
MNSKEVKNNAYTAITIGPIGKTLAKARSVKSFWTASYLFSWIMRELLKKLPEENFEVLSPHRAGKDVSEETSKKVGLFPDRLFAKGELEEKEFKRIKREIFGELAEKFKNAFQDEKDDIARKIDTERDPKRKRELEEIKSRYSNATSKSEDIRKYLENYLSISSITVELSSDCSILEQLNKYLDTQELFNKASSHTDEDYMELFIEASKNSFLEDYSKENTSSSGSNKDLKESSTKKRAFPSTSEIAVSGWEQNPPKDANGEVDYSKLTSKTGFRNCYKYLAVIKADGDGFGTYIKELKVDEEKEIKENGEKENELTRFTKSFFEFSVEVANELIQKTKAIPVYIGGDDLFLFAPVLEGNVEKDVFNLIKEIDDLFIQKEIGEGLSMSYGVSIFYYKSPMSEAIDIADSMLRKAKEEKEEKEKKKDTVAISIQKHSGQKIEFLLPCKHSTDKCKQETGLYKKATELIRAFKEDDSMLNSLIYWIEDMYETIFTDEVTLYQERINAVFDNFFDEEIHKENEVFFDLLKKFIHSMHHSEDTPRKLKDKKKLLHGILRYCQFVTAKKEK
>NZ_CP024592.1|WP_097555163.1|141206_142478_+|hypothetical-protein
MYKLEFELEQHTPIIHFQARDAGATLRASEVKPKLDKFILKEYKEKLPKSVIKEREEDKEKKEDKEVRKSLDYKMRIIARNVDSEDIDAKSAPMYFGNIKAIKPKRLVTAKSVQIIILVKNEVLKDCIEESIVRFFQLHNFGTRQSKGYGSFTIKVDGKKKIRDVYKYSFDVSGSDYKEVMNRINYFYKSLRSGINEYRGKGEKKRSILYFKSALHYYVTTVLEEQWDKKSIKEYFFPQQLEEEKTKHKVEDISSKEKNDFRDLLGFSTDEAWGKEYQIKKTCKKETDKGEEEFSRLKSPIQFKPIRFDKGFTVFFDVFPEYSGWNNFLGREICVEAFQVKKEDITGKEKDTTGKKTLIPIKKEPLTLKVPTDIDLKDVLRYIFLNMDPEQRKLKATKESEDIFNDIKATYNKLHNELERSKK
>NZ_CP024592.1|WP_012458620.1|140954_141191_+|hypothetical-protein
MEIETLILLSLAVAGFTTIIVVAIVWYSKFKIRKEELEHQRLVEQEREKAKELNNSFAKSLLATNKEIIEVYCKNNTK
>NZ_CP024592.1|WP_099840438.1|139369_140953_+|hypothetical-protein
MGAETYSRHIFIFPFQWDYIEKRRYASYNERTDIKKFDKLFSEVSPLKRQYFEIGASEERYNEYTYFHPFARRALFGTKENPSVYHYELSDTQGTYNISVKIGGVSTTYSLQLEKIAVSVFDTGVGTVAYFLRNDKHTSFEDILRINDSGRRIYPQYMAKGDRLAAKNSFLADRIYGSLGVLDFDDDFRQFEEDISHTNIFLPPDHIRQVFGYNKMDRTEDDGCQKFVFHQESERKDIIRISPVMDDRMFFITYYHSPYYAKKLRSKPKIFRRKREYNIYEEGHFGDLWFRYLFGDGGDKTVANTSVQREDVRRTTYARWSGSGTLFGLTKDSLVGISDWYLIGDHITTMYYQMATLSLVQRSTILRFSNEIASITQLILDKKTKRKTEKQVKELYGNYIRFLNETYFREVTPQIQGIEMYDMLQSNMNIEKDAKALDEEMGELFNYTTLEEQGVLNKTANLYLPITLLVGFLGINTFVEKGCITRFFNIGDPCPSTWGLLGGDIITLIVFAICLYFPIRHYFKYRK
>NZ_CP024592.1|WP_143733548.1|151813_151921_-|DUF1661-domain-containing-protein
MAREFFTSRTKTKKFPRHVFQSIDSLLQRVRYPLL
>NZ_CP024592.1|WP_099840446.1|152618_154625_+|hypothetical-protein
MRLLPAVVCAIILLSLPLGGQTVVPEWDEYIAEQIESGAIGEDEGAEFLERWMVQKQHPLDINTLTREDLEQFPFLNEFQIRRFLLYQHAHPEGFDCIWVLNEIAGWDRRTCLLLWPMLTVQKRSEPAAASFREILSYARHDVSVHTDAILQRQEGYRPDSRHPYRGDPWGGGLRWSYAMGNRFSLGLTASKDRGEPAFDKRRKGFDSYSAHFFMEGKGAVRAVALGDYRIGMGYGLLVNQASFMGMAYAYPRGGTTLRRAFTYAEDNFMRGAATALAQGRWALTAFYSHKGVDATVTEDGAIKAIYHTGLHRTDAEIARRNAATMTTAGTSVCYTDDRLRLTFNLLHLHWDGLRLLRAVGTQGIASLTDLERFSLVSADYSYLFGQGEAELFGEFAGAANGAVGTINGLRYTHPVGGSYMLVGRYIPADYWSYYRGAFARHSRPGNEWGVMGRAAWELPSDWTVRAFADYYGSFVPRFGRKEKTEALYWMFEGEKRLSALSWSCRIRGTGDKRYRRSLAVRLRGRYTFDERWRLMASLQWSRSNSFDRELQTWQAPTGGKSFALRADYSGGKLLRVCSMDAVAFDTDSFADRLYEAVHNPRHHYSSAFFYGRGVRLGVFVRIAPLPHVEVESRIDHLLRRDTDTIGSAGELIRGQARTHLLMTVRYR
>NZ_CP024592.1|WP_099840447.1|154987_156040_-|hemagglutinin
MTVENLRLQRLQNLEHYRFAKNVLTLCRTANIAKLNPKLPELEKAIEMEDLALNPPVANELTPQVIALDEERDRAYQALMSRVRSYAFDEDSQLRNAAARIEDVAARYGNVIRMNYDKETAAIENFLTDLKGENIRPLVTKLGVTALVDRLEKANKAFADFFLRRLSTDQRGKYDVKALRAETDRTLVAVVRRMDSIDDMEPSPEIRALIELYNRLVANRRALLARRASYGEAAVEKRRAEIAEMLRPLLARIVEEKKTAVFAGRTLGTGKNRHYLITFVAENGDEEDRWYRIDGERLVYVPEDELPKPKKKKKPASSTDTPSEPPVLPDPSQGGSSSGGGEQGSTGGGL
>NZ_CP024592.1|WP_012458602.1|156563_157403_+|DNA-adenine-methylase
MAKNKLIAPFLKWVGGKRQLIPEIKNLLPKGILSHPYYEPFIGGGALLFELQPKNATINDYNEELINVYKVIRDNPHELIEDLKKHKNTAEYFYEIRAIDRNPLFINLTDIERASRIIYLNKTCYNGLYRVNNAGEFNSPFGKYKNPNIVNEPVIKAVSKYLNTAKIQIFNGDYQTILKDIPRSSFVYLDPPYHPISQSANFTGYVQGGWDEKDQIRLRNVCNTLNERGIKFLLSNSSSDFIKEIYSDYNIYVVQATRAVNSDSSKRGQVSEFLINNYE
>NZ_CP024592.1|WP_004585649.1|157395_158685_+|hypothetical-protein
MSKSKNDLAWEAIFERYSLLDELAKNGRVSISSEKINEFRESRLMTKFDHRSQLPDLFGKHKLSILPTSRGTYEIGPFETFCDFNKDEIGIMSMPFRSDLESIDYKDITSESAAINCAFVCSILQDFTGEEALFPTVSGRMGSSSFEFTINSGAKKVKIDVENSQIEIDGGYEGENSLALIEAKNYISDDFLIRQLYYPYRLWSNKITKRVRPIFLTYSNGIFHLREYEFSAPELYNSIRLVQHKKYAIQEGGISINTETIQDILGIVSVVKEPQIPFPQADSFERVINLCELLKQRGFISKYDITQNYDFDHRQTDYYSNAAKYLGLIKDARENRNIGYTLTQKGLQVFNPSISIVNRQLEFVKLILEHAAFQETLKLYFDKGEVPTKDEVVVIMKNNGLYKIDSDTTYKRRAATIISWINWILGLIE
>NZ_CP024592.1|WP_099840449.1|159778_160678_+|T9SS-type-A-sorting-domain-containing-protein
MAFAQVPKGNDKSKDEHILTWALPEEPESDEGILLIYNSFLTPFNGMTMACASFFDVQDLLPYVGYTINRIDFHPTADEKNYEQVAASKFYICIWGNKEQTEVLYEQALPTIHKEDLSYGHGVDGEENYYDEPMYLAELETPFVIPAGKALYIGCRVETQEGHAVGFGLDDGPAKKGKGDLVGVYLPGAAPMPFVPLSDIPARSMDANFFIYSRISLGSGTQDILLHRMKVYPNPATTELHVEALSAWVGEQAAVYDMRGRRVSARTVDSEKLCIDIASLPAGVYMLRIGSYSAKFEKR
>NZ_CP024592.1|WP_097626381.1|161183_162071_-|tetratricopeptide-repeat-protein
MTDRFLRILRLSALCLLFSALLPPLFGQPTTARQDSLPADYTRLIDRSFEALGQGNLELAEQALRQAIKAYPDLPSGYALMNNLGAIQQRQGKPEEALLTYSAALQKLPDDKLLRTNRAMLLTEMGRTDEAIFDYNELLRAEPDNEIFHYGRAMLYLAKGMYGDAESDLEEILRINDSSLKARLGIALVATMKGEYDKAERLYNYVIDKLPKNAAAYEGRARLFLNKGMKGYALRDINKAFEYATPPAASLFVLRGEINAAIGDKKAAADDYAAAESRGYSKESLDLLRAALRKQ
>NZ_CP024592.1|WP_099840450.1|162172_163171_+|mechanosensitive-ion-channel
MGLKIFFPLQNLSVDTTKVNKIAEVVSPEALKQIKEIKPSQWTELLTQWGGKALTFGIKVLIALVAFYLGKLLLNVLIKWLDRIMVRRSFEPAARTFLRSFANIGGFVLLIVIIISTLGFQPVSLAALLASVGVAVGMGLSGQLQNLAGGLIVLLTKPFKVGDYIVSNNVEGVVDGVTLFHTTVMTFENKYIFIPNGLLSSNVIINYSRMAVRRNEWIIGIEYNEDFDRVKTLLLRLIDEEPRIIKEPLPTVVLKELADSSVRVMARAWCATDDLWNVYWDINERIYSEFNRQGIAFPFPQLTIHGSAAGQERRGKSTEAQSPENVSTNTSL
>NZ_CP024592.1|WP_004583632.1|163131_164928_-|chloride-channel-protein
MKDKETSRYGWFLHFLLWRERHINERLFLIILSLIIGILSAFAAVLLKNTIHIIQHFAFDRIRETSYLYLIFPVVGILITWLFVRYVVRDDIGHGVTKILFAISQRKSRIKPHNMWSSLAASSITIGFGGSVGAESPIVLTGAAIGSNLGRLFRMEQKTLMLLVGCGAAGAISGIFKAPITGLVFVIEVLLLDLTMSSVLPLLISSVSAAAVSYIITGQGAMFSFTLNDPFSMDRIPYALLLGVFCGLVSFYFSKVMFVFESKLKNFPHYRQRYLISAFILCGLIFLFPPLYGEGYDTINALLGGQYSSLMDGSLFEPYSNSYWVLFVFLGFIIITKVFASVATNSGGGCGGLFAPSLFMGALSGFIFAYALNFFPFIEVYLPQKNFALLGMAGVMAAVMHAPLTGIFLIAELTGGYNLFLPLMLVSTSSYATIRLFMPHSIYSLRLAQKGKLLTHQKDKAVLTLMTLDAVIEKDFEPVRPDMTLGDVVHVFGISHRNVFPVLDENNLLMGLVLLDNIRNIMFRPELYERFKVSRFMVSPPAKIVNTMSMETIMRIFDDTKAWNLPVIDEQGCYLGFVSKSKIFNSYREVLVETFSGD
>NZ_CP024592.1|WP_021677506.1|164924_166331_-|sugar-transferase
MTRMQLHRLRYLLADVFGIVASYLSYNTLRYLTEEQERIYSTLSEYLFNAKSLWVGILYLLFWLSLFALSGYYNKPIAKSRISELLTTVASVLVGSVVVFLLLVVDDIVHDTALYLRLFFMMVATVLPWVYFPRLWVTTFGIKERKKTKGYHRVLLIGSGTIAEETASWLKSVNDMATTRLHFVPPTMREGFEQSLKSFATLVAEAVQESKPHQIILAVDCPDASFISLLLYQLYPFHMPVCVPMRSMLFAGAKVNVQGMKGEPMVDMTATNMSECAKSIKWFADRLFSLLMLILLIPVYAVIAVLVKRSSRGPVFFGQERIGLHGRPFTIYKFRTMYLDAEKDGPSLSFDGDSRVTPIGRILRKYRMDELPQFWNVLRGDMSFVGPRPERAFYIRQLVERAPYYYLLHNVRPGITSWGMVRYGYASTPDEMLERLQYDFLYYENMSLRLDIEVLLYTCQTIFKGLGK

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Crispr_ID: NZ_CP024592_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP024592_4

453754-454185

TypeVI-B2

VI-B2

Consensus_repeat	Method
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	PILER-CR
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	CRISPRCasFinder
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	CRT

6 spacers

Csx28

The CRISPR arrays of NZ_CP024592_4

>merge|NZ_CP024592|4|453754-454185|PILER-CR,CRISPRCasFinder,CRT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAACTCCTCCGCCTTCCTTTCTATTTTCTTCTCTGTTGGATCTACCCTCTATTCGAAGGGTACACACAACGACTGCTCCGGGCTAAATTTCCCTGTCTCTGTTGGATCTACCCTCTATTCGAAGGGTACACACAACATCTCCCCATTCTCGACACGAAGTCCCTCTGTTGGATCTACCCTCTATTCGAAGGGTACACACAACCCTTTGATTTGAAGAAATCTTTAATAGAAGGTTGGATCTACCCTCTATTCGAAGGGTACACACAACTTTTTAGAAGATTTCCAATAAATTGTTTTGGTTGGATCTACCCTCTATTCGAAGGGTACACACAACTAGTCAAGCATCTTGCCAATCGTATCAACTGTTGGATCTACCCTCTATTCGAAGGGTACACACAAC

>NZ_CP024592|4|3|453754-454185|PILER-CR
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	TCCTCCGCCTTCCTTTCTATTTTCTTCTCT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	GACTGCTCCGGGCTAAATTTCCCTGTCTCT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	ATCTCCCCATTCTCGACACGAAGTCCCTCT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	CCTTTGATTTGAAGAAATCTTTAATAGAAG
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	TTTTTAGAAGATTTCCAATAAATTGTTTTG
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	TAGTCAAGCATCTTGCCAATCGTATCAACT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC

>NZ_CP024592|4|4|453754-454185|CRISPRCasFinder
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	TCCTCCGCCTTCCTTTCTATTTTCTTCTCT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	GACTGCTCCGGGCTAAATTTCCCTGTCTCT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	ATCTCCCCATTCTCGACACGAAGTCCCTCT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	CCTTTGATTTGAAGAAATCTTTAATAGAAG
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	TTTTTAGAAGATTTCCAATAAATTGTTTTG
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	TAGTCAAGCATCTTGCCAATCGTATCAACT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC

>NZ_CP024592|4|3|453754-454185|CRT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	TCCTCCGCCTTCCTTTCTATTTTCTTCTCT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	GACTGCTCCGGGCTAAATTTCCCTGTCTCT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	ATCTCCCCATTCTCGACACGAAGTCCCTCT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	CCTTTGATTTGAAGAAATCTTTAATAGAAG
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	TTTTTAGAAGATTTCCAATAAATTGTTTTG
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC	TAGTCAAGCATCTTGCCAATCGTATCAACT
GTTGGATCTACCCTCTATTCGAAGGGTACACACAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP024592.1\|WP_004584821.1\|448611_449181_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_080657698.1\|465193_466636_+\|exo-alpha-sialidase	unknown	unknown	gnl\|CDD\|271234
NZ_CP024592.1\|WP_077094290.1\|459141_460170_+\|UDP-glucose-4-epimerase-GalE	unknown	unknown	gnl\|CDD\|187558
NZ_CP024592.1\|WP_043898408.1\|452998_453544_+\|hypothetical-protein	Csx28	-	unknown
NZ_CP024592.1\|WP_005873799.1\|463173_464628_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380191
NZ_CP024592.1\|WP_021664579.1\|447689_448592_-\|tRNA-(adenosine(37)-N6)-dimethylallyltransferase-MiaA	unknown	unknown	gnl\|CDD\|234626
NZ_CP024592.1\|WP_077094289.1\|458526_459132_+\|YihA-family-ribosome-biogenesis-GTP-binding-protein	unknown	unknown	gnl\|CDD\|234770
NZ_CP024592.1\|WP_061156466.1\|439780_440683_-\|glutamate-formimidoyltransferase	unknown	unknown	gnl\|CDD\|226169
NZ_CP024592.1\|WP_039417386.1\|462308_463079_+\|HAD-IA-family-hydrolase	unknown	unknown	gnl\|CDD\|223710
NZ_CP024592.1\|WP_077070478.1\|445048_446008_-\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|133030
NZ_CP024592.1\|WP_077094285.1\|446035_447550_-\|glycosyltransferase-family-39-protein	unknown	unknown	gnl\|CDD\|224720
NZ_CP024592.1\|WP_004584828.1\|457832_458426_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_077094288.1\|456360_457830_-\|metallophosphoesterase-family-protein	unknown	unknown	gnl\|CDD\|277318
NZ_CP024592.1\|WP_099840505.1\|444129_445038_+\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|273359
NZ_CP024592.1\|WP_004584831.1\|460212_462309_+\|ATP-dependent-DNA-helicase-RecG	unknown	unknown	gnl\|CDD\|236794
NZ_CP024592.1\|WP_010955985.1\|464641_464902_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_077094287.1\|454998_456198_-\|methionine-gamma-lyase	unknown	unknown	gnl\|CDD\|168478
NZ_CP024592.1\|WP_099840504.1\|438408_439680_-\|imidazolonepropionase	unknown	unknown	gnl\|CDD\|236478
NZ_CP024592.1\|WP_021664582.1\|440731_441250_-\|DUF4496-domain-containing-protein	unknown	unknown	gnl\|CDD\|273496
NZ_CP024592.1\|WP_097596505.1\|441925_443902_+\|transcription-termination-factor-Rho	unknown	unknown	gnl\|CDD\|236490

Protein	Function_ID	Function_description	E-value
NZ_CP024592.1\|WP_080657698.1\|465193_466636_+\|exo-alpha-sialidase	gnl\|CDD\|271234	cd15482, Sialidase_non-viral, Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.	1.64633e-92
NZ_CP024592.1\|WP_077094290.1\|459141_460170_+\|UDP-glucose-4-epimerase-GalE	gnl\|CDD\|187558	cd05247, UDP_G4E_1_SDR_e, UDP-glucose 4 epimerase, subgroup 1, extended (e) SDRs. UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), is a homodimeric extended SDR. It catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup has the characteristic active site tetrad and NAD-binding motif of the extended SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. 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. 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. 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.	0
NZ_CP024592.1\|WP_005873799.1\|463173_464628_-\|hypothetical-protein	gnl\|CDD\|380191	NF033187, internalin_J, class 1 internalin InlJ. Internalins, as found in the intracellular human pathogen Listeria monocytogenes, are paralogous surface-anchored proteins with an N-terminal signal peptide, leucine-rich repeats, and a C-terminal LPXTG processing and cell surface anchoring site. See PMID:17764999 for a general discussion of internalins. Members of this family are internalin J (InlJ).	1.30429e-35
NZ_CP024592.1\|WP_021664579.1\|447689_448592_-\|tRNA-(adenosine(37)-N6)-dimethylallyltransferase-MiaA	gnl\|CDD\|234626	PRK00091, miaA, tRNA delta(2)-isopentenylpyrophosphate transferase; Reviewed.	4.99359e-126
NZ_CP024592.1\|WP_077094289.1\|458526_459132_+\|YihA-family-ribosome-biogenesis-GTP-binding-protein	gnl\|CDD\|234770	PRK00454, engB, GTP-binding protein YsxC; Reviewed.	6.74252e-98
NZ_CP024592.1\|WP_061156466.1\|439780_440683_-\|glutamate-formimidoyltransferase	gnl\|CDD\|226169	COG3643, COG3643, Glutamate formiminotransferase [Amino acid transport and metabolism].	1.05901e-150
NZ_CP024592.1\|WP_039417386.1\|462308_463079_+\|HAD-IA-family-hydrolase	gnl\|CDD\|223710	COG0637, COG0637, Predicted phosphatase/phosphohexomutase [General function prediction only].	5.59908e-38
NZ_CP024592.1\|WP_077070478.1\|445048_446008_-\|glycosyltransferase-family-2-protein	gnl\|CDD\|133030	cd04187, DPM1_like_bac, Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.	9.43495e-98
NZ_CP024592.1\|WP_077094285.1\|446035_447550_-\|glycosyltransferase-family-39-protein	gnl\|CDD\|224720	COG1807, ArnT, 4-amino-4-deoxy-L-arabinose transferase and related glycosyltransferases of PMT family [Cell envelope biogenesis, outer membrane].	1.33376e-33
NZ_CP024592.1\|WP_077094288.1\|456360_457830_-\|metallophosphoesterase-family-protein	gnl\|CDD\|277318	cd00839, MPP_PAPs, purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain. Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.	2.90429e-14
NZ_CP024592.1\|WP_099840505.1\|444129_445038_+\|DMT-family-transporter	gnl\|CDD\|273359	TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter. [Transport and binding proteins, Amino acids, peptides and amines].	3.13331e-12
NZ_CP024592.1\|WP_004584831.1\|460212_462309_+\|ATP-dependent-DNA-helicase-RecG	gnl\|CDD\|236794	PRK10917, PRK10917, ATP-dependent DNA helicase RecG; Provisional.	0
NZ_CP024592.1\|WP_077094287.1\|454998_456198_-\|methionine-gamma-lyase	gnl\|CDD\|168478	PRK06234, PRK06234, methionine gamma-lyase; Provisional.	0
NZ_CP024592.1\|WP_099840504.1\|438408_439680_-\|imidazolonepropionase	gnl\|CDD\|236478	PRK09356, PRK09356, imidazolonepropionase; Validated.	0
NZ_CP024592.1\|WP_021664582.1\|440731_441250_-\|DUF4496-domain-containing-protein	gnl\|CDD\|273496	TIGR01201, HU_rel, DNA-binding protein, histone-like, putative. This model describes a set of proteins related to but longer than DNA-binding protein HU. Its distinctive domain architecture compared to HU and related histone-like DNA-binding proteins justifies the designation as superfamily. Members include, so far, one from Bacteroides fragilis, a gut bacterium, and ten from Porphyromonas gingivalis, an oral anaerobe. [DNA metabolism, Chromosome-associated proteins].	1.16618e-52
NZ_CP024592.1\|WP_097596505.1\|441925_443902_+\|transcription-termination-factor-Rho	gnl\|CDD\|236490	PRK09376, rho, transcription termination factor Rho; Provisional.	0

>NZ_CP024592.1|WP_043898408.1|452998_453544_+|hypothetical-protein
MMTMTICWTPICVQLIKLSGIFIAAYLAYRYAVRKLSKESIENIERCKYQAVLEAHRSFYKLLRFTTDTENADSILVWQKAKGGGAKTYYFRPACIRGFLSELTDEFYKNGNGIFLSKEIISRIFEYRSIVYGLLLSERQNSDERIVMNKPETAERMISIHQELTQTVREAIALKKRTLNF
>NZ_CP024592.1|WP_004584821.1|448611_449181_-|hypothetical-protein
MVFNFLIVSDEVEDFRREIAIDSEATFLDLQNAILDSVGYSHSELTSFFLCDEDWHKGQEITLMEMDTASDEDSYVMENTRLEEFIEDEHQRLVFEFDLMTERYFFIEVMDIVPGKSLSEPKLLTSEGLPPQQSSLDDLMDPTAIPTKQARGLDLEEDFFGDSEYNEDEIDREGFEGFDEITSDLSDNY
>NZ_CP024592.1|WP_021664579.1|447689_448592_-|tRNA-(adenosine(37)-N6)-dimethylallyltransferase-MiaA
METQDHTLYVLLGPTGVGKTDLSLDIAERLGSPIISADSRQIFRELPIGTAAPTPEQRARVPHLFVGTHSVRDYYSAGMYEVEVLEALKELFRKYRGVLLTGGSMMYIDAVCRGIDDIPDPFPEVREELYARYGAEGLDGILAQLRLLDPDYYAKVDRRNYKRVIHGLEICLSTGRPFSSFHRHEAKERPFRIVKIGLYREREELCRRIDARVLEMMEQGLEEEARAVYPLRHLNALNTVGYKEMFEYFDGSIDRAEAVRRIQRNSRVYARKQMTWFRRDSTIRWFHPEADKGTVLTLVT
>NZ_CP024592.1|WP_077094285.1|446035_447550_-|glycosyltransferase-family-39-protein
MKLSFQKKKAFSQTITSLIILVVLFLSCIPYFCKLDSLPIQLWDESRVSMNALCMYYNGDWGMTYYLDEPDMWNTKPPLLVWLQVIFMKLLGPGELAIRLPSALAAVATGILLFWTARKVYGNNLSGVIAAFILSTTPLFVNAHGMRTGDYDSLLLFWVSAFIFCSFFCSEAYRHERIKEAHRYLYIASLALSLAVLTKGVQALIVVPAVLAFVIFYGGPRRILKDKHLYFAFLLFVLIAGAWYLGREIKSAGYLQAIWENELGGRYFDSDSLLNRKSGYFYPTYLWEEYRWGTAIFGGCLLYAVLYGRKRSRVFALYLALCIVFYLSILSMSVTKIWWYMLPIVPPMTLIIAGIGVPVMYRLKKLYRPAVIAPVSLLLVVFFFAIPFAGIMKKIQTPESQDDLSNYLRRLTEIEDEKEIRTNPLILVYGEEYYQRAPLAFYVLQLQKRGIEVEYKKREELESGDFVCVAEQWAQEYVDARYRYEEVGREGKDIKFLRILGHRE
>NZ_CP024592.1|WP_077070478.1|445048_446008_-|glycosyltransferase-family-2-protein
MSINTSYTKDLSIVVPIYNEEKGIPELVRRLSAAAASITEDYELIFVNDGSRDGSMELLRSLCKGDDRFFYINLSRNFGHQIAVSAGLDHVRGKATVIIDGDLQDPPELIPELYAKYREGYEVVYAQRKHREGETWFKKATAKGFYRTMRKITSIDMPLDTGDFRLIDRKIVQCLREMPEQSKFLRGQIAWMGFRQTGVQFDRDERKYGQTNYPLRKMLALAIDGITGFSSRPLEWVAQLGAWVSLLSLFVIVYALISHFLLNKTVSGWTSVIVSSMFLGGVQLICLGVIGTYISKINKNIVARPLYLVAESNIAADER
>NZ_CP024592.1|WP_099840505.1|444129_445038_+|DMT-family-transporter
MTSSRLYGLAVGILSFATFGLIPLFTLPISAKGASFELILFYRFFFAAIAIGILHRLSGGSFKVSRADIGPLVLLGFLYAGTALFLFHGYGYMASGVATTIHFLYPLFVTALMLLFFGERLSPVPLTAIFIALIGVGLLMGLTGGGDRVGLTGFVIVAISALCYALYIVFVNRSRIRIMPGRRLTFYVFVAAAGFCLINVLVRQGEVAPLPDAASWGNILLLALVPTVISNLALVVAVRNIGSTLTSALGAMEPLTSVLVGVWVFDEVLGASAIVGMGCILIAVGLIVFSEPLELMLRRRRR
>NZ_CP024592.1|WP_097596505.1|441925_443902_+|transcription-termination-factor-Rho
MQKYTIVDLNEKAEAELAAIAGELGIANAGSMPKQELIYKILDEQAISVAGVRKEKQKTTEDRHTERRKPGRPRKNAEEEAPESKDVAAAPAEPNDEEAQAKRKRGRPRKAAEEIAEETREDVQQLVALAAAEETNATEKESAGRKPAAKTSTASPAKAPAKALPRPAETTPRVAPSPPSTTPVSEPAKDDAKPETPAPPPAIESITTTPAAGAVDEGGARRLVFRHKNSSSVLDQVLPYSSPQPPQRPKPAGAPVGSSPIRQRQPAGVPTPRREPQQPLYNFDGILECMGVLEIMPDGYGFLRSSDYNYLSSPDDVYVSQQQIKHNGLKTGDVVAGTIRPPREGEKYFPFVQLRSVNGRSPEEIRDRVPFDHLTPLFPEEKFTLEAPGIRAVNDKISVRVVDLFAPIGKGQRGLIVSQPKTGKTMLLKDIANAIAANHPEVYMIVLLIDERPEEVTDMARSVNAEVIASTFDEPAERHVKIAEIVLNKAKRMVECGHDVVILLDSITRLARAYNTVQPASGKVLSGGVDANALQKPKRFFGAARNIENGGSLTILATALTDTGSKMDEVIFEEFKGTGNMELQLDRRLSNKRIFPAVDIMSSSTRRDDLLQDETTLNRMWILRKYLSDMNPVEAMEFVRKQLENTHTNMEFLASMSN
>NZ_CP024592.1|WP_021664582.1|440731_441250_-|DUF4496-domain-containing-protein
MSLKYVIKKSVAKIGPKAGQTIYYAQPAAQDSVTFHSLCKRIAEESALTSADVKGILDRLVNILSEELPNGKTVRIGELGSFRLSFGSKQLDDPKNFSVDQIQKHRLVFIPSAELKSIPARGKLRPGSSALAFDYERVEPQPKKKPGTGDNQTPSPSTPDGGGGQGGTGGGL
>NZ_CP024592.1|WP_061156466.1|439780_440683_-|glutamate-formimidoyltransferase
MALSRIMECVPNFSEGRDREKIEKIVNPFRTREGVKLLNYSNDEDHNRLVVTVVGEPEPLREAVLEAVGIAVELIDLTKHTGQHPRMGAVDVIPFIPIKNVTAEDADTLAKEVGRTIGEKYGVPVFLYEKSATAPHRENLAKIRKGEFEGMAEKIHEADWHPDFGPADRHPTAGTVAVGARMPLVAYNVNLNTNDLSIADAIAKKVRFLGGGLRFCKAMGVELTDRGIVQVSMNLTDFTKTAVYRAHEMVRMEAARYGVSVVGSEVIGLVPMQALIDCAEYYLGIENFSMDQILESRIME
>NZ_CP024592.1|WP_099840504.1|438408_439680_-|imidazolonepropionase
MPNTPHTMNLYIKNIAQLVTCQGTEAKHGREAMGQIHTIEGPAAVVIRDGVIAFAGRMADVAPSMTEGCRELDATGRCVLPGFVDSHTHLVFGGYREDEFQWRLAGDSYMSIMERGGGIASTMRATRAESEDELKASARRHLSNMMKMGVTTVEAKSGYGMNLETELKQLRVVRDLQDEQPLDLYSTFMGAHDTAPEYKGRPTEFIEYLCREVLPEVVRQNLAECCDIFTEKGVFDHEQTRRMLTAAKEAGLSVKMHADEIVPFGGAELAAELGCLSADHLLRISDAGIKALAESNTVATLLPCTVFSLRADYAPARKMIDAGCAVALGSDLNPGSCFSASVPLMFALATLYMGMTVEEAITALTINGAAAIGRADTIGSIEPGKKGDLVVLQYPSYKFLSYHFGMNLVEHTVKGGRIVYTNS
>NZ_CP024592.1|WP_077094287.1|454998_456198_-|methionine-gamma-lyase
MKKEDLMRSGFATRAIHGGAIENAFGCLATPIYQTSTFVFDSAEQGGRRFAGEEDGYIYTRLGNPNCTQVEEKLAMLEGGEAAASASSGIGAISSAIWVCVKAGDHIVAGKTLYGCTFAFLTHGLSRYGVEVTLVDTRHPEEVEAAIRPNTKLVYLETPANPNMYLTDIKAVCDIAHKHEGVRVMVDNTYCTPYICRPLELGADIVVHSATKYLNGHGDVIAGFVVGKEDYIKEVKLVGVKDLTGANMSPFDAYLISRGMKTLQIRMEQHCRNAQTVAEFLEKHLAVEAVYFPGLPSFPQYELAKKQMALPGAMIAFEVKGGCEAGKKLMNNLHLCSLAVSLGDTETLIQHPASMTHSPYTPEERAASDISEGLVRLSVGLENVEDIIADLKHGLDSLI
>NZ_CP024592.1|WP_077094288.1|456360_457830_-|metallophosphoesterase-family-protein
MRKKRSNPYYKVSRRKFSKRNSGRRYSRKRRRNGRRRGLMISLLLLVALGIWIAKRYRAWFVSPAEVAYTVPHTIDRLTLTPGEDFLTQRTVSWRCDTLPQDSWLDYRSPDGADADTLLISLPAEGKEVVTRAGRNYYYHAKINGLKPGRTYTYRVKTGEQTSPWYRFSIPDSSAATDFIYIGDVQDPGNGGSQALLQRLRTLHPNPDFLALGGDQIEGPTDFYWEVWHRVIGDWTASTPVIAATGNHEYIKGLKRQLDPRWVPQYNYPANGPKGFERRSYYIDFPHMRLIVMDTNDIQWPASVFNHRTWLKNALETTVQPWKVVMFHHGVYSVRQGRMNPIIRYGFRSILEEGGADLVLQGHDHAYSRITTKTESGTKTTPVYIISSASPKHYRNGFSEQHDRIGSGLYLYQTIHVTPGEIRYRSTTFDNRPYDDLHLKKQGGRTTVKDNAEDWKEIFAFDNFADSKKGRKKRADYRQAAQERAAGHR
>NZ_CP024592.1|WP_004584828.1|457832_458426_-|hypothetical-protein
MNKSLIILIYTLVWVLLIVLQSLALESANPGTPSFWNTPSAYYSVWIVDAYIIALYYINYFLIAPFMIKRHLFRPYIVLSLALGGIGMLLPVVFHHAWQWTIPGTSEGQMPLYGEGFIASIAAIAVGLSVRGVREWVRLARRNTNLEIALKNKSIAYDRAEARLRSLEQPVSFHNPGTGAKAENAPSSTPVSPQTNE
>NZ_CP024592.1|WP_077094289.1|458526_459132_+|YihA-family-ribosome-biogenesis-GTP-binding-protein
MEIKKAAFVISNTDVRKCPDTRFPEYAFIGRSNVGKSSLINMLTGQKGLAMTSQKPGKTQLINHFIIDDSWYLVDLPGYGYARLGASNRESLRRIIETYILCREQLSSLFVLIDCRHEPQKIDLEFLQWLGENGIPFGIVFTKADKLSFSRLKENTEAYKQKLLETWEELPPVFITSSEKKTGKEELLDYIDSINQELATK
>NZ_CP024592.1|WP_077094290.1|459141_460170_+|UDP-glucose-4-epimerase-GalE
MKQKILVTGGTGYIGSHTTVELQQAGYRVVSVDNFSNSNAAVLDGIARITGVRPDFYEADCNDTEAMERVFTAHPDIAGVIHFAASKAVGESVQKPLLYYRNNILSLLNILELMERFGTRGIVFSSSCTVYGQPEVLPVTEEAPIQEALSPYGNTKQINEEIIRDAIHAGAGYKAILLRYFNPIGAHPTAHIGELPNGVPQNLIPYLTQTAAGIRAELSVFGDDYDTPDGSCIRDYIYVVDLAKAHVAAIERMLNEEKASDSIEVFNIGTGRGVSVLELIRTFERVTGVAVPHRIVGRREGDIEQVWAEPKKANEVLGWKALESLEDTLLSAWRWQQRLSEK
>NZ_CP024592.1|WP_004584831.1|460212_462309_+|ATP-dependent-DNA-helicase-RecG
MDILSTKITYLTGVGPKRAEVLKEEIEVRTYLDLLHYFPFRYVDRSRFYAIREIRSDMPYIQLRGVLRNFSEVGEGRRKRLTATFSDGTGSIELVWFKGIKYIRDKLQEGRRYIVFGKPVFFASGYNIAHPEIDAEEKAEQVAGGLTPIYHTTERMKSMGLGSKQLQQLLYVLLNQVSATLTETLPPYILSSYGFVSYQEAIRQIHFPQGVAQLEAARTRLKFEELFYVQLHLIGSKLERKARFQGIVFAQVGALFNTFYKEYLPFELTGAQKKVVREIRQDTLSGHQMNRLVQGDVGSGKTLVALLSMLLALDNGCQACLMAPTEILARQHHHTLSELLRPLGIEVGLLIGSCTARQRERLLPRLADGSLSIVVGTHALLEQGVAFHRLGMAVIDEQHRFGVQQRARLWEKNLDTLPHILIMSATPIPRTLAMTLYGDLDISIIDELPPGRKPIQTLHHFDNDMAPVFRFLRSQLAAGRQVYVVYPMIEGSETTDLKNLEDGFELFSSIFPDEGVTMVHGKMKAKEKEARMADFVSGRSRILLATTVIEVGVNVPNATVMVVENADRFGLSQLHQLRGRVGRGGEQSYCILITGTKTGEDSRRRIQVMVETNDGFEIAEEDMRLRGFGDLEGTRQSGRQISLRIANPARDTELIALSRSIAEQLLERDPELRHPDNQMLALRLNKLFPKEEDWSVIS
>NZ_CP024592.1|WP_039417386.1|462308_463079_+|HAD-IA-family-hydrolase
MEKKESMDYNNITEALQAFRTEKAYRHAPLRSCFFDMDGVLFDSMPAHARSWVEAAGECGIAAEPLDFYRWEGQKGSDTIKILFERGYGRLPTEKEIADMYGRKSQLFALYNSGSVIDDAPALVSDVCDRGLRIMLVTGSSQTDILQRLQRSYGDNFSPANMVTGADVHRGKPHPEPYLKALECVGMSPSEAFVVENAPLGVRAAVDAGIFTIAVNTGCLPDADLWDAGASLVLPSMAVLRSLLGELLTESLSSSA
>NZ_CP024592.1|WP_005873799.1|463173_464628_-|hypothetical-protein
MKRKPLFSALVILSGFFGSVHPASAQKVPAPVDGERIIMELSEADVECTIKIEAEDGYANDIWADLNGNGKYDSGERLDSGEFRDVEFRQTKAIVYGKMAKFLFRGSSAGDYGATFIDISNCTGLTAFDCFANLLTELDLSKANGLTFVNCGKNQLTKLDLPANADIETLNCSKNKITSLNLSTYTKLKELYVGDNGLTALDLSANTLLEELVYSNNEVTTINLSANTNLKSLYCINNKMTGLDVAANKELKILHCNNNQLTALNLSANTKLTTLSFFNNELTNIDLSDNTALEWLFCNGNKLTKLDVSANANLIALQCSNNQLTALDLSKTPKLTTLNCYSNRIKDTAMRALIESLPTITEGEGRFVPYNDDEGGEEENVCTTEHVEMAKAKNWKVLTSWGEPFPGITALISIEGESEYSVYAQDGILYLSGMEQGLPVQVYTVGGSMMYSSVASGSAMEIQLPRGAAYVVRIGSHAIKTAMP
>NZ_CP024592.1|WP_010955985.1|464641_464902_+|hypothetical-protein
MVCEKWLVFVLISCFQNLIANSAGGFVAAIIRGWKKKACLPFSFRRRATKESGWICFGLCAFLWIAPLFELRQYRGIILALGKANI
>NZ_CP024592.1|WP_080657698.1|465193_466636_+|exo-alpha-sialidase
MYRTLVKVALSESLPPDAKQIRIGFSLPKETEEKVTALYLLVSDSLAVRDLPDYKGRVSYDSFPISKEDRTTALSADLVAGRRFFYLAADIGPVASFSRSDTLTARVEEVAVDGRPLPLKELSPASRRLYRGYEALFVPGDGGSRNYRIPAILKTANGTLIAMADRRKYNQTDLPEDIDIVMRRSTDGGKSWSDPRIIVQGEGRNHGFGDVALVQTQAGKLLMIFVGGVGLWQSTPDRPQRTYISESRDEGLTWSPPRDITHFIFGKDCADPGRSRWLASFCASGQGLVLPSGRITFVAAIRESGQEYVLNNYVLYSDDEGDTWHLSDCAYRRGDEAKLSLMPDGRVLMSVRNQGRQESRQRFFALSSDDGLTWERAKQFEGIHDPGCNGAMLQVKRNGRDQVLHSLPLGPDGRRDGAVYLFDHTSGRWSAPVVVNSGSSAYSDMTLLADGTIGYFVEEDDEISLVFIRFVLDDLFDARQ

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Crispr_ID: NZ_CP024592_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP024592_5

797708-797804

Orphan

Consensus_repeat	Method
AGTAATAATCATACAAAGAATCATATAAAAAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP024592_5

>merge|NZ_CP024592|5|797708-797804|CRISPRCasFinder
AGTAATAATCATACAAAGAATCATATAAAAATCGTTCCGTGTCCTCTGACTACACGTCAAAGGATAGTAATAATCATACAAAGAATCATATAAAAAT

>NZ_CP024592|5|5|797708-797804|CRISPRCasFinder
AGTAATAATCATACAAAGAATCATATAAAAAT	CGTTCCGTGTCCTCTGACTACACGTCAAAGGAT
AGTAATAATCATACAAAGAATCATATAAAAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP024592.1\|WP_130266966.1\|797411_797576_-\|DUF1661-domain-containing-protein	unknown	unknown	gnl\|CDD\|285160
NZ_CP024592.1\|WP_099840570.1\|810898_812452_-\|DUF1858-domain-containing-protein	unknown	unknown	gnl\|CDD\|225301
NZ_CP024592.1\|WP_004585225.1\|799028_799541_+\|isochorismatase-family-protein	unknown	unknown	gnl\|CDD\|238493
NZ_CP024592.1\|WP_004585231.1\|809979_810639_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213222
NZ_CP024592.1\|WP_021677706.1\|785336_786425_+\|aminoglycoside-phosphotransferase-family-protein	unknown	unknown	gnl\|CDD\|366736
NZ_CP024592.1\|WP_077094424.1\|796549_797311_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187604
NZ_CP024592.1\|WP_012457729.1\|812936_814292_-\|aldehyde-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|143440
NZ_CP024592.1\|WP_012457717.1\|794864_796472_-\|indolepyruvate-ferredoxin-oxidoreductase	unknown	unknown	gnl\|CDD\|274526
NZ_CP024592.1\|WP_099840569.1\|807511_809887_+\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|274576
NZ_CP024592.1\|WP_143733817.1\|812599_812740_-\|DUF1661-domain-containing-protein	unknown	unknown	gnl\|CDD\|285160
NZ_CP024592.1\|WP_077094427.1\|790837_791977_+\|ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|238561
NZ_CP024592.1\|WP_099840567.1\|802728_805080_+\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|274576
NZ_CP024592.1\|WP_077094426.1\|791973_793044_+\|iron-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|376439
NZ_CP024592.1\|WP_012457723.1\|801117_802371_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_CP024592.1\|WP_077094422.1\|799743_801078_+\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_CP024592.1\|WP_005873542.1\|789838_790720_+\|heme-binding-protein	unknown	unknown	gnl\|CDD\|368778
NZ_CP024592.1\|WP_077094425.1\|793087_793846_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224045
NZ_CP024592.1\|WP_004585221.1\|794244_794838_-\|indolepyruvate-oxidoreductase-subunit-beta	unknown	unknown	gnl\|CDD\|180732
NZ_CP024592.1\|WP_099840565.1\|787536_789810_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_CP024592.1\|WP_099840568.1\|805118_807485_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|274576

Protein	Function_ID	Function_description	E-value
NZ_CP024592.1\|WP_130266966.1\|797411_797576_-\|DUF1661-domain-containing-protein	gnl\|CDD\|285160	pfam07877, DUF1661, Protein of unknown function (DUF1661). This is a family containing bacterial proteins of unknown function. Many of the proteins in this family are hypothetical.	0.00271467
NZ_CP024592.1\|WP_099840570.1\|810898_812452_-\|DUF1858-domain-containing-protein	gnl\|CDD\|225301	COG2461, COG2461, Uncharacterized conserved protein [Function unknown].	3.11688e-104
NZ_CP024592.1\|WP_004585225.1\|799028_799541_+\|isochorismatase-family-protein	gnl\|CDD\|238493	cd01011, nicotinamidase, Nicotinamidase/pyrazinamidase (PZase). Nicotinamidase, a ubiquitous enzyme in prokaryotes, converts nicotinamide to nicotinic acid (niacin) and ammonia, which in turn can be recycled to make nicotinamide adenine dinucleotide (NAD). The same enzyme is also called pyrazinamidase, because in converts the tuberculosis drug pyrazinamide (PZA) into its active form pyrazinoic acid (POA).	4.21836e-32
NZ_CP024592.1\|WP_004585231.1\|809979_810639_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213222	cd03255, ABC_MJ0796_LolCDE_FtsE, ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.	7.00946e-113
NZ_CP024592.1\|WP_021677706.1\|785336_786425_+\|aminoglycoside-phosphotransferase-family-protein	gnl\|CDD\|366736	pfam01636, APH, Phosphotransferase enzyme family. This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.	2.28754e-15
NZ_CP024592.1\|WP_077094424.1\|796549_797311_-\|SDR-family-oxidoreductase	gnl\|CDD\|187604	cd05346, SDR_c5, classical (c) SDR, subgroup 5. These proteins are members of the classical SDR family, with a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	5.28705e-149
NZ_CP024592.1\|WP_012457729.1\|812936_814292_-\|aldehyde-dehydrogenase-family-protein	gnl\|CDD\|143440	cd07122, ALDH_F20_ACDH, Coenzyme A acylating aldehyde dehydrogenase (ACDH), ALDH family 20-like. Coenzyme A acylating aldehyde dehydrogenase (ACDH, EC=1.2.1.10), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA . The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH and may be critical enzymes in the fermentative pathway.	0
NZ_CP024592.1\|WP_012457717.1\|794864_796472_-\|indolepyruvate-ferredoxin-oxidoreductase	gnl\|CDD\|274526	TIGR03336, IOR_alpha, indolepyruvate ferredoxin oxidoreductase, alpha subunit. Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.	1.37331e-175
NZ_CP024592.1\|WP_099840569.1\|807511_809887_+\|FtsX-like-permease-family-protein	gnl\|CDD\|274576	TIGR03434, ADOP, Acidobacterial duplicated orphan permease. Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.	5.83517e-33
NZ_CP024592.1\|WP_143733817.1\|812599_812740_-\|DUF1661-domain-containing-protein	gnl\|CDD\|285160	pfam07877, DUF1661, Protein of unknown function (DUF1661). This is a family containing bacterial proteins of unknown function. Many of the proteins in this family are hypothetical.	0.000315793
NZ_CP024592.1\|WP_077094427.1\|790837_791977_+\|ABC-transporter-substrate-binding-protein	gnl\|CDD\|238561	cd01141, TroA_d, Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.	8.4744e-24
NZ_CP024592.1\|WP_099840567.1\|802728_805080_+\|FtsX-like-permease-family-protein	gnl\|CDD\|274576	TIGR03434, ADOP, Acidobacterial duplicated orphan permease. Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.	1.7518e-21
NZ_CP024592.1\|WP_077094426.1\|791973_793044_+\|iron-ABC-transporter-permease	gnl\|CDD\|376439	pfam01032, FecCD, FecCD transport family. This is a sub-family of bacterial binding protein-dependent transport systems family. This Pfam entry contains the inner components of this multicomponent transport system.	3.28348e-68
NZ_CP024592.1\|WP_012457723.1\|801117_802371_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	3.45071e-33
NZ_CP024592.1\|WP_077094422.1\|799743_801078_+\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	7.14817e-41
NZ_CP024592.1\|WP_005873542.1\|789838_790720_+\|heme-binding-protein	gnl\|CDD\|368778	pfam06180, CbiK, Cobalt chelatase (CbiK). This family consists of several bacterial cobalt chelatase (CbiK) proteins (EC:4.99.1.-).	6.78901e-122
NZ_CP024592.1\|WP_077094425.1\|793087_793846_+\|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].	1.2126e-78
NZ_CP024592.1\|WP_004585221.1\|794244_794838_-\|indolepyruvate-oxidoreductase-subunit-beta	gnl\|CDD\|180732	PRK06853, PRK06853, indolepyruvate oxidoreductase subunit beta; Reviewed.	4.90894e-83
NZ_CP024592.1\|WP_099840565.1\|787536_789810_+\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.38577e-68
NZ_CP024592.1\|WP_099840568.1\|805118_807485_+\|ABC-transporter-permease	gnl\|CDD\|274576	TIGR03434, ADOP, Acidobacterial duplicated orphan permease. Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.	3.45469e-46

>NZ_CP024592.1|WP_130266966.1|797411_797576_-|DUF1661-domain-containing-protein
MPRHKTWCVNFFVLVREVKNSRATTKKFSRHFVQKTRATIRSFAVRISDKTDPD
>NZ_CP024592.1|WP_077094424.1|796549_797311_-|SDR-family-oxidoreductase
MNPIALITGATSGIGAASARRLASLGYNLIITGRRSERLQNIADEIRAEYPVEILPLSFDVRNREEVEAHLGNLPDPWQAVSVLVNNAGLAAGLDPIQSGDIEDWERMIDTNIKGLLYVTRTISPGMIARSAGHIINIGSIAGKEVYSNGNVYCATKHAVDALSKAMRIDMLPYGIKVTQICPGAVETEFSLVRFHDDQAKADAVYKGFTPLCANDIAECIAVVLNLPDNICINDMVVMPKAQAGSGHFFKQV
>NZ_CP024592.1|WP_012457717.1|794864_796472_-|indolepyruvate-ferredoxin-oxidoreductase
MQKQLLLGVEAIAQAALDAGISGVYAYPGTPSTEITEHIQNSRMAKERNVHREWAANEKTAMESALGMSYAGKRALVCMKHVGMNVAADCFMNAAITGANGGMVIVAADDPSMHSSQNEQDSRVYGQFAMIPVMEPSNQQEAYDMTRLAFDLSERLGTPVMMRITTRLAHSRAGVVPTEPIGENELHLPEDKRQYVLLPGIAKKRYRILLDKQTDFVRESENSPYTEYIDAADKSKGIVACGIAYNYLMEAFKAQVPYPVLKVTQYPIPHKQMERLLNECGDIVVMEEGYPVVEQLLKGFPGLERIKGRLDGTLPRDGELNPDHVAKAFNIPVVEGEPIPDLVAARPPALCKGCSHRDVYDALNEVLTEYPNGRVFSDIGCYTLGALPPYEAINSCVDMGASITMAKGAADAGLFPAVSVIGDSTFTHSGITGLLDAINENSNITVIISDNESISMTGGQHSSAYGKVEAICRGIGVDPDHIKELLPVPKNHDELCSIIREEINYEGVSVIIPRRVCIQKHARDAKAAKRAKAKE
>NZ_CP024592.1|WP_004585221.1|794244_794838_-|indolepyruvate-oxidoreductase-subunit-beta
MKTDIILAGVGGQGILSIAAAIGSAALTNNLYLKQAETHGMSQRGGDVQSFLRLSDAPIYSDLIPIGGADLILSVEPMEALRYLPYLKPDGYVVTNTVPFINIPNYPETTSVISKIESLPHHVLIDADSIARDEVGNVRASNFVMLGAASPFIEIPFDYLAGGIEAIFSRKGQEVVDMNLKALNAGREFALRYAAGK
>NZ_CP024592.1|WP_077094425.1|793087_793846_+|ABC-transporter-ATP-binding-protein
MEKSIELSRLAIGYRTKSGDRIVASGLEAHLHAGQFTALLGVNGAGKSTLMRTMAGFMKPLSGQIHLLGRSLDSYKEIEIAKRIGVVLTDNCRIAGMTAGELVALGRSPYTGFWGRLQKGDRKLVAEAVERVGIAPLINRELTTLSDGERQKVVIAKALAQQTPIIFLDEPTAFLDYPSKMELLHLLHSLAHDTGRTIFLSTHDLDAILPMADRVWLLDKERPFREGTPASLASALEDYFGYIHPSPTSEPV
>NZ_CP024592.1|WP_077094426.1|791973_793044_+|iron-ABC-transporter-permease
MTSVSHLRTISVAGILAALGGAVLILFGVNLFLGSVAIPMSEIFRHLFSDRPEGGEALVHYNILWKSRLPEALTAAFAGAGLSVSGLQMQTVFRNPLAGPSVLGISSGASLGVALVVLLSGSLGGVALSSLGYMGEVAMNIAATVGSLAVMGLIVFVSTKVRSHVTLLIIGVMIGYVATAVIGVFKFFSIEEDIRAYVIWGLGSFSRATDSQLSFFAILMLIFIPAGMLLVKQLNLLLLGESYARNLGLNTRRARLLVISSAGLLIAAVTAYCGPIGFLGMAVPHLARVIFHTSDHRILMPATCLIGSALALFCNIIARMPGFEGALPVNSVTALVGAPIIVTVLFRRRRFKEETD
>NZ_CP024592.1|WP_077094427.1|790837_791977_+|ABC-transporter-substrate-binding-protein
MKRYSVTFFLSAILFLIGAGCNRTRTQEQKATSAISSDSLHPQYAEGFRLDAGEGCYLLSIEDPQQESHKEYRFALVPKGTYPVIPEGYTAVTIPVERVVCMTTLQLSNFIALDAQSLVAGISSTRYLRDSVMKAQLQDGRTQKIGIEGNFDREVVMSLQPDLILISPFKRGGYDVLEQVSVPLIPHLGYKELTPLGQAEWVKLIGLLTGQYDKACRFFSEIETRYHTLTGYADEVTDRPIVFSGEMRGGNWYAVGGKSYLAQQIRDAGGEYFLKDDQRSGGVSLDFETVYSRSDSARYWRILNSYPREFGYEALKAEDSRYADFRAFKEKGVIYCNLRETAFYELMPMHPDWVLADLIAILHPGLLPDHQPHFYYLLQ
>NZ_CP024592.1|WP_005873542.1|789838_790720_+|heme-binding-protein
MKKLILATLGLMAIAMLSCSSNNKDLENKGEATLLVTFGSSYKAPRETYAKIEKTFAAAYPDQRISWTYTSSIIRKKLAQQGIYIDAPDEALEKLARLGYKKINVQSLHVIPGREYDEMIDFVNKFKAAHSDITVKVGAPLFDTDEDMREVAEILHKRFQQTIEKGEAIVFMGHGTEHAANDRYARINKIMKNYSKFMIVGTVESDPSINDVIAELKETGATAVTMMPLMSVAGDHATNDMAGDEDDSWKTLLTNAGYTVSIDKLDNGNFSALGDIEEIRNIWLKHMKATSAR
>NZ_CP024592.1|WP_099840565.1|787536_789810_+|TonB-dependent-receptor
MRTKTIFFAIISFIALLSSSLSAQSKAVLTGSASDAETGEPLAGARIEVKHTNIVAGADAGGHFEIKNLPAGQHTIICSLGGYGQKEEVVAIEAGQTKTISFALRLRTNNLEEVVVTGTGTRYRLVDAPVATEVLTAKDIASFSAPTSEALLQGLSPSFDFGPNLMGSFMQLNGLSSKYILILIDGKRVYGDVGGQADLSRISPDQIERIELVKGASSSLYGSDAIAGVINVITKKNTNRLSAYTSHRISKYNDRQTNTSLDINIGKFSSNTNYFFYHTDGWQNSPFEIKKKKGSGEPVLEETYKKTFRAQENQGVSQSLSYYATNNLSFSGNVQYNKRQIFTPTFSEKKAYDMDYRALTASLGTNYLFPNGLHTLSFDAVYDRFRFGYLYHDKDSSESLINNQGQTEQPTFFPGQLRNKNDQIRYTAEARGVFTLPYAQKLTGGLEYFREELISPYNLITDKADASTLSAYVQDEWKPLDWFNMTAGFRLVHHQEFGTRMTPKVSILAKYGPLNFRATYANGYKTPTLKELFARNELTTMGSHNLYLGNADLKPQMSDYYALGLEYNKGPISFSATVYDNELRNLISFIDIPTSPEHEAQGIKKTKQYANIGKARSRGLDVLCDASIGWGIKLGAGYSLVEAKNLQTDEWLEGAARHRANVHADWAHYWGQYRLGVSLFGRIQSERYYKDGNAPDYTLWRLATSHRFAHFRHIILDGTLGIDNLFDYVDDRPMGVNYATVTPGRTFFAQIAIRFNN
>NZ_CP024592.1|WP_021677706.1|785336_786425_+|aminoglycoside-phosphotransferase-family-protein
MKQLNEIVAHFHTEGSVAEIAPLGAGLINDTYKVATAEADAPDYVLQRINHTIFKDVEMLQANITAVTAHIRRKLTESGADDIERKVLTLVTSDGDKTYYYDGENYWRMMVFIPRAQTFEAVTPEYSRYAGQAFGSFQAMLSDLPDELGETIPDFHNMEFRLGQLHDALKTDPVGRAEEVRYYIDEIEKRAEEMCKAERLHREGKLPKRVCHCDTKVNNMLFDEDGHVLCVIDLDTVMPNFIFSDYGDFLRTGANTGEEDDKDLDHVNFDMEIFKAFTEGYLKGASSFLTDIEIENLPYAAALFPYMQCVRFLTDYINGDTYYKIKYPEHNLVRTRAQFRLLQSVEDCMLQMQAFIDQCLRY
>NZ_CP024592.1|WP_004585225.1|799028_799541_+|isochorismatase-family-protein
MVLLIVDPQVDFVSGSLAVEGAPKAMKALAEYMAAHRKEIKSIVVTMDQHPADHCSFVAQGGQWPSHCVRYTVGAAIEPCIAEALAACSAEGIPVEMIEKATTQERDAYSAFETEVPDSLRSAERIVVAGIAGDYCVRQSVLDLERHGLGERIELLKEGIAYIAEEENRP
>NZ_CP024592.1|WP_077094422.1|799743_801078_+|TolC-family-protein
MRFQHYLICTAAVAALAANPLTGQSNMTLEECIDYARRHSSAVALSAAELEQSKADYLQAVGNFLPRVSAGTGASWNFGRGLDAETNTYTDINSFNNSYSIHATMTLFDGLQSVYRLRMAHARREASRLSVREQQELAALGTTEAYYDLVYARQMQELAMQKYEESNRLHRQTARMEELGMKSRPDVLEMQSRMAGDRLALTQADNQCIIALIRLKEKMNFPIDDELVVDDMPADSLFADIAESDSSAGVFARAAHHHPVLLRAKLDEQAATDRLRAARGAFLPSVSVSGGWNTGFSRFLNGSDYTPFSEQFRNRRGEYISLNLSIPIFSGFSLVSNLRQARAERRAASVRRGEAERRLYSEIAQAMADRDAALASYRQAKEHADAMQATYEAVLQRYEEGLNTAIDLTTQANRLLDARVQRLRAAMTYRLKCKLIAYYGCLSD
>NZ_CP024592.1|WP_012457723.1|801117_802371_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MDRKIEKKKTLIPRKYYPYAGGAIVILALAAWAVFGNHSTKFRAERARISIDSVRRGEFNDYVRINGQVQPINSIQISAVEGGMVAEKTVEEGAMVHKGDIIVRLTNPMLNLNILDSEAQLAEKQNFLRNTQVTMEQDRLNLKRESLNLRLDIERKKRKAEQYARLYKEKLCSREEYLQAGEDYQYAVEGSRLVMERQRQDSLYRGIQVRQMEESLHNMRRNLEMVRARVEDLNVKAPADGQLGLLDVEIGQTVGAGSRIGQINVLSDYKVEAMIDEHYIDRVKAGLAASFERQGRDFSLRVRKVYPEVRDKQFRTDFVFDGERPDNIRTGQTYYINLRLGQPSEAIMIPRGAFYQNTGGRWIFVVTPDGKRAVRRDITIARQNPQYYEVTSGLHAGEMVITSSYDMFGDAEEIILN
>NZ_CP024592.1|WP_099840567.1|802728_805080_+|FtsX-like-permease-family-protein
MRTYFKFLSRNKLYTFVTIVGFALSLIFVLLLSFYVRREQQADRIHTDYKRIYQYNVESKNNWSGFICCYPAGTLIREQVPDVEEICRISEYNDKEYIFIGADKQNGLIASHLSVESNFFTFFDGYKLLEGDPKTVLSEQNSAVISSALAARIFGNVSPIGQEVSFFDYSKNKQTFRITGIMEPMADNCHIRPAELLFYQEPKENNYNRGNYALYLKAREGADLTAQLPAVQKAVQGKDVIFAFDEKAEVKLHPLEKCYPEPLFPNEYAKMVQKGNPARMRILIAITLLVLIIAIISYINLTLAQAGSRGNEVALRRLWGSSRLAIVRRLWFESLLLIFLSTLLAVFGMFAFEPVFDRLFDTHLYLARHISLTLIILLIGFILLLSIVCAALPAWFISRFRPIEVVSGKFRRVVKSSFSQIMVISQYAITMILLSCTMVMAVQIDYMTNSDMGYDYRNKLIIDVFGLDPQIASTMRTEIAKIPGITGIGLTRGTPLNEGNNNTSEYRGKQLSMQIFSMDSVALSLFDLKMKPNGRKADKPDRTLYLSRSAYNDFDVANLSDGVIHWGEAGEFYYCGDAPEVHFGGFKEPHPSYLFIPYPQSSAWSWSVLVGYSEGADPEQLIQSIQAVYSRITGQPYTEILRSEDIIASHSEEERSLSGFLLLFSILALVGTVMSVFAMAALRIRHKQKEIAIRKVVGAREVQILQIIGRRSLWNLLIAFAVASPASYLVMNRWLQGYTYHADMPWWVFPASLLFVSAVAMLSMLSMAMNAASSNPVDYLKNE
>NZ_CP024592.1|WP_099840568.1|805118_807485_+|ABC-transporter-permease
MRTYFKFLSRNKLYTFVTVFGFSVSLMFVIILGIYIRNEMSVDRFHSKSDRIYMLCSEEAANWSNLAPSYIQSILPDIESYCRVANRDVYVQMPSGERLKTPILLADSTFFTLFDFRLTNGIPSQVLNDRKSAVISRDFARKLFADQDPVGQSVFLYNFPHTITGVMEGIPSNSQFKKVDIVVNYHFLSDLSGENAFRWGNCSFMAYYLLKAGTDLESKARILEETFKKEAFMWLYHQGFHKEVHFVSLPDCYFDSRVVEANLENRANNMTKVKVLTGIVLLILVIAVLNYVNMTVAQAGFRGKESAIRRLLGGSRSGVIRKLLLESLVITLLTFIAGLLLAFTFEPFFNRVLETTLDLKHQFTPSTVIAIALFVVLLSFLSGILPAWIISRFKPIEVVKGTLRYRIKSTYSKVLIIFQYTIAVALLVCSLFMIRQTHYLIHSDLGFRTRGVLWISNTVDSVPKGILRAELEKIPGVEKVSYACGNPIQYLNNMSFTKDGVNVSTWEMVVDSVFFDFFEISPIPLTDEPVETFFDREKMRAARIIPEWGNMKMINAVRPDPETGIFTQGDDDNDEVKYRMVGRIPDLKYKPLNMEQSPLQIRPLYAREQPWVTLVRASDEADKSAVLAAVSDTYKRVTGAEDIEPLWAEDIILDRYKSQTNLSQLISAFALLTVLIMVMGVFAMSLYMIKQKEKEIALRKVNGATVATILAMLNTQSLRRFGIALLIALPVSWWAMDRWLQTFAFHIRLDWWVFVVAALIVLLLSLVSTSLQSWRAACANPVDYLKNE
>NZ_CP024592.1|WP_099840569.1|807511_809887_+|FtsX-like-permease-family-protein
MLPLKLAARRLFRQGEHSISKLLTLTLGLSVSVLLLSIVIYQRSYERDFPHHDRICIVKTHGTRQSQEGDKPEELDFSQVSGGVAPAIQEEIPGVELATRTTLYGTSKMILEDNKTYETKTLLAEPAFLDMFGVELIAGVRDSALRDNMTCLISESLARKMGGDVLGKRLRPAESKSDRAITIGGVFEDLPHNSSIQADMLLPITWMPAESLNNWIGNDRYIAYVRLRPGVSPESLDEALLEMQKRHQDMEVFRKAGVELHYSLTPFNRLRLEDPTLVNMLRIQQIVAIAVLLISLLNYVLMTLASMVNRRRVAAIRKCYGAMPVQIQGTMIWETFLYLFLSLVLALLTLILFRKPMEALIETPLLHLISWRVAAALAGVLAMATFFMGWIPGYSLSRTPVMNIFRKSVAHNRLWKLGLLAVEFVAASFLFGLLAITGLQYRHMIGQDAGYKAAGLYYVPIESLDQQQLPVVIEKLKALPEVEGYTLTTALPASSGQSGDNLIDPVTDRELINVADLFYVDEHYLKVYDIELLEGKNFDVATEKDREIMLSKKAATELARLMNWKDGVIGKNIILTSFGRVVIRGVYDDLMLRRQHLSPYPEKLPSAIVYGDDWLHYLTIRLRHDDARLLHRVNGILSEADPYKETSFLSVEMELLSRFEAAKTFRNTILFGSVVAILIALIGLVGYVNTEVNRRRKELAIRKINGAGEGDILRLFLRSIFRLSLPSVLAGLFVAYLFGRNWLEKFSYRIELNGRIFLLVGLFVLLIIALAVVINLRRIARRNPVNELRYE
>NZ_CP024592.1|WP_004585231.1|809979_810639_+|ABC-transporter-ATP-binding-protein
MIEISNLTKVFRTEEIETVALDGVSLKVDKGEFIAIMGPSGCGKSTLLNILGLLDNPTSGIYKLDGAEVGNLREKDRTAVRKGNIGFVFQSFNLIEEMTVSENVELPLVYLGVKASERKERVEEALRKMSISHRAGHFPNQLSGGQQQRVAIARAVVANPKLILADEPTGNLDSKNGADVMELLRGLNREGATIVMVTHSEHDARSAGRIINLFDGKIR
>NZ_CP024592.1|WP_099840570.1|810898_812452_-|DUF1858-domain-containing-protein
MQVIKTNETFDSLDKSKLERMLDIKEAHREGHLTLEEAKERMKKEVGSISPEEFAAAEQLFKERDQDECQNEDVRTMLQLFEGLINPIRPDLPFGHPIDAYLRENDKAKELLDQADALLERTFIPNPWIELMETLMGYKLHFARKQNQLYSTLEQKGFDRPSTTMWTYDDHIRDEMNKAMSLLREKDYDSFPAAYKEMAIVLRDLMEKEELILYPTSLKLISDKEFEEMKHGDREIGFFLIDMPELDAPAKQSKEAHGQSFMAELGALLAKHGMGTGGQDDKAILDVAEGKLTLEQINLLFRHLPVDISFVDENELVCFYTDTKHRVFPRSKGVIGREVRNCHPPKSVHIVEEIIDKFRRGEQDRAEFWINKPGVFIYIVYVAIRDADGRFRGVMEMMQDCTRIRSLEGSRTLLTWDEEQSPAQGSKESESDTVGEDGIRPDTKLKSLLQRYPQLMDDLPTISSKFTLLRSPMAKVILPVATIKMMSERADIPSDMLIGKLESLIASYNKPDRSEEK
>NZ_CP024592.1|WP_143733817.1|812599_812740_-|DUF1661-domain-containing-protein
MWHVNFLLLAWEKKKSETKTKKISRLFFTKHRPQSEHFRLVFLLEA
>NZ_CP024592.1|WP_012457729.1|812936_814292_-|aldehyde-dehydrogenase-family-protein
MEIKEMVSLARKAQKEYQATHNQEAVDNICRAAAKVIYENAAILAREAVDETGMGVYEHKVAKNQGKSKGVWYNLHNKKSVGILNIDERTGMIEIAKPIGVVGAVTPTTNPIVTPMSNIIFALKTCNAIIIAPHPRSKKCSAHAVRLIKEAIAPFNVPEGMVQIIEEPSIEKTQELMGAVDVVVATGGMGMVKSAYSSGKPSFGVGAGNVQVIVDSNIDFEAAAEKIITGRAFDNGIICSGEQSIIYNEADKEAVFTAFRNHGAYFCDEAEGDRARAAIFENGAIAKDVVGQSVAFIAKKANINIPEGTRILVVEARGVGAEDVICKEKMCPVMCALSYKHFEEGVEIARTNLANEGNGHTCAIHSNNQAHIILAGSELTVSRIVVNAPSATTAGGHIQNGLAVTNTLGCGSWGNNSISENFTYKHLLNISRIAPLNSSIHIPDDKEIWEL

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Crispr_ID: NZ_CP024592_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP024592_6

1474874-1474970

Orphan

Consensus_repeat	Method
CTTTCAAATAGAGAATGATACATAACTAAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP024592_6

>merge|NZ_CP024592|6|1474874-1474970|CRISPRCasFinder
CTTTCAAATAGAGAATGATACATAACTAACCCTGTATGGTGCAATTGAAATGAGTCAAGGTCGATGCCTTTCAAATAGAGAATGATACATAACTAAC

>NZ_CP024592|6|6|1474874-1474970|CRISPRCasFinder
CTTTCAAATAGAGAATGATACATAACTAAC	CCTGTATGGTGCAATTGAAATGAGTCAAGGTCGATGC
CTTTCAAATAGAGAATGATACATAACTAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP024592.1\|WP_021664688.1\|1488010_1488514_+\|DNA-binding-protein	unknown	unknown	gnl\|CDD\|273496
NZ_CP024592.1\|WP_080657388.1\|1466828_1468343_-\|Rne/Rng-family-ribonuclease	unknown	unknown	gnl\|CDD\|273254
NZ_CP024592.1\|WP_077095062.1\|1461895_1462201_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|369563
NZ_CP024592.1\|WP_012458242.1\|1469577_1471974_-\|anaerobic-ribonucleoside-triphosphate-reductase	unknown	unknown	gnl\|CDD\|235937
NZ_CP024592.1\|WP_099840706.1\|1462429_1463665_-\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|274034
NZ_CP024592.1\|WP_077094973.1\|1484293_1485223_-\|amidinotransferase	unknown	unknown	gnl\|CDD\|227211
NZ_CP024592.1\|WP_099840494.1\|1481634_1482537_+\|IS982-like-element-IS195-family-transposase	unknown	unknown	gnl\|CDD\|372648
NZ_CP024592.1\|WP_077095042.1\|1488814_1490080_+\|nucleotide-sugar-dehydrogenase	unknown	unknown	gnl\|CDD\|185104
NZ_CP024592.1\|WP_005874016.1\|1491596_1492517_+\|3-phosphoglycerate-dehydrogenase	unknown	unknown	gnl\|CDD\|240651
NZ_CP024592.1\|WP_077094974.1\|1482585_1484217_-\|L-glutamate-gamma-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|143441
NZ_CP024592.1\|WP_077095059.1\|1466208_1466832_-\|recombination-protein-RecR	unknown	unknown	gnl\|CDD\|234616
NZ_CP024592.1\|WP_004584585.1\|1468663_1468942_-\|integration-host-factor-subunit-beta	unknown	unknown	gnl\|CDD\|259858
NZ_CP024592.1\|WP_005874020.1\|1490413_1491496_+\|phosphoserine-transaminase	unknown	unknown	gnl\|CDD\|235428
NZ_CP024592.1\|WP_077094978.1\|1487772_1487988_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_005874739.1\|1465674_1466202_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379112
NZ_CP024592.1\|WP_099840709.1\|1485229_1486459_-\|ornithine--oxo-acid-transaminase	unknown	unknown	gnl\|CDD\|273853
NZ_CP024592.1\|WP_077095060.1\|1463677_1465687_-\|NAD-dependent-DNA-ligase-LigA	unknown	unknown	gnl\|CDD\|236137
NZ_CP024592.1\|WP_004584586.1\|1469053_1469545_-\|anaerobic-ribonucleoside-triphosphate-reductase-activating-protein	unknown	unknown	gnl\|CDD\|274161
NZ_CP024592.1\|WP_004585684.1\|1486908_1487475_+\|elongation-factor-P	unknown	unknown	gnl\|CDD\|234788
NZ_CP024592.1\|WP_099840707.1\|1472408_1473311_-\|IS982-family-transposase	unknown	unknown	gnl\|CDD\|372648

Protein	Function_ID	Function_description	E-value
NZ_CP024592.1\|WP_021664688.1\|1488010_1488514_+\|DNA-binding-protein	gnl\|CDD\|273496	TIGR01201, HU_rel, DNA-binding protein, histone-like, putative. This model describes a set of proteins related to but longer than DNA-binding protein HU. Its distinctive domain architecture compared to HU and related histone-like DNA-binding proteins justifies the designation as superfamily. Members include, so far, one from Bacteroides fragilis, a gut bacterium, and ten from Porphyromonas gingivalis, an oral anaerobe. [DNA metabolism, Chromosome-associated proteins].	3.20735e-63
NZ_CP024592.1\|WP_080657388.1\|1466828_1468343_-\|Rne/Rng-family-ribonuclease	gnl\|CDD\|273254	TIGR00757, Ribonuclease_E/G-like_protein, ribonuclease, Rne/Rng family. This model describes ribonuclease G (formerly CafA, cytoplasmic axial filament protein A), the N-terminal domain of ribonuclease E in which ribonuclease activity resides, and related proteins. In E. coli, both RNase E and RNase G have been shown to play a role in the maturation of the 5' end of 16S RNA. The C-terminal half of RNase E (excluded from the seed alignment for this model) lacks ribonuclease activity but participates in mRNA degradation by organizing the degradosome. [Transcription, Degradation of RNA].	1.02173e-131
NZ_CP024592.1\|WP_077095062.1\|1461895_1462201_+\|hypothetical-protein	gnl\|CDD\|369563	pfam07863, CtnDOT_TraJ, homologs of TraJ from Bacteroides conjugative transposon. Members of this family have been implicated in as being involved in an unusual form of DNA transfer (conjugation) in Bacteroides. The family has been named CtnDOT_TraJ to avoid confusion with other conjugative transfer systems.	1.62447e-19
NZ_CP024592.1\|WP_012458242.1\|1469577_1471974_-\|anaerobic-ribonucleoside-triphosphate-reductase	gnl\|CDD\|235937	PRK07111, PRK07111, anaerobic ribonucleoside triphosphate reductase; Provisional.	0
NZ_CP024592.1\|WP_099840706.1\|1462429_1463665_-\|FtsX-like-permease-family-protein	gnl\|CDD\|274034	TIGR02212, releasing_system_transmembrane_protein_lolC., lipoprotein releasing system, transmembrane protein, LolC/E family. This model describes the LolC protein, and its paralog LolE found in some species. These proteins are homologous to permease proteins of ABC transporters. In some species, two paralogs occur, designated LolC and LolE. In others, a single form is found and tends to be designated LolC. [Protein fate, Protein and peptide secretion and trafficking].	1.74502e-39
NZ_CP024592.1\|WP_077094973.1\|1484293_1485223_-\|amidinotransferase	gnl\|CDD\|227211	COG4874, COG4874, Uncharacterized protein conserved in bacteria containing a pentein-type domain [Function unknown].	2.31809e-115
NZ_CP024592.1\|WP_099840494.1\|1481634_1482537_+\|IS982-like-element-IS195-family-transposase	gnl\|CDD\|372648	pfam13612, DDE_Tnp_1_3, Transposase DDE domain. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contains three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction.	5.14725e-101
NZ_CP024592.1\|WP_077095042.1\|1488814_1490080_+\|nucleotide-sugar-dehydrogenase	gnl\|CDD\|185104	PRK15182, PRK15182, Vi polysaccharide biosynthesis UDP-N-acetylglucosamine C-6 dehydrogenase TviB.	9.59831e-165
NZ_CP024592.1\|WP_005874016.1\|1491596_1492517_+\|3-phosphoglycerate-dehydrogenase	gnl\|CDD\|240651	cd12174, PGDH_like_3, Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains. Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.	1.34079e-112
NZ_CP024592.1\|WP_077094974.1\|1482585_1484217_-\|L-glutamate-gamma-semialdehyde-dehydrogenase	gnl\|CDD\|143441	cd07123, ALDH_F4-17_P5CDH, Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17. Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.	0
NZ_CP024592.1\|WP_077095059.1\|1466208_1466832_-\|recombination-protein-RecR	gnl\|CDD\|234616	PRK00076, recR, recombination protein RecR; Reviewed.	5.05987e-109
NZ_CP024592.1\|WP_004584585.1\|1468663_1468942_-\|integration-host-factor-subunit-beta	gnl\|CDD\|259858	cd13836, IHF_B, Beta subunit of integration host factor (IHFB). This subfamily consists of the beta subunit of integration host factor (IHF) and IHF-like domains. IHF is a nucleoid-associated protein (NAP) that binds and sharply bends many DNA targets in a sequence specific manner. It is a heterodimeric protein composed of two highly homologous subunits IHFA (IHF-alpha) and IHFB (IHF-beta). It is known to act as a transcription factor at many gene regulatory regions in E. coli. IHF is an essential cofactor in phage lambda site-specific recombination, having an architectural role during assembly of specialized nucleoprotein structures (snups). IHF is also involved in formation as well as maintenance of bacterial biofilms since it is found in complex with extracellular DNA (eDNA) within the extracellular polymeric substances (EPS) matrix of many biofilms.	3.05457e-33
NZ_CP024592.1\|WP_005874020.1\|1490413_1491496_+\|phosphoserine-transaminase	gnl\|CDD\|235428	PRK05355, PRK05355, 3-phosphoserine/phosphohydroxythreonine transaminase.	0
NZ_CP024592.1\|WP_005874739.1\|1465674_1466202_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	1.54508e-19
NZ_CP024592.1\|WP_099840709.1\|1485229_1486459_-\|ornithine--oxo-acid-transaminase	gnl\|CDD\|273853	TIGR01885, Ornithine_aminotransferase, ornithine aminotransferase. This model describes the final step in the biosynthesis of ornithine from glutamate via the non-acetylated pathway. Ornithine amino transferase takes L-glutamate 5-semialdehyde and makes it into ornithine, which is used in the urea cycle, as well as in the biosynthesis of arginine. This model includes low-GC bacteria and eukaryotic species. The genes from two species are annotated as putative acetylornithine aminotransferases - one from Porphyromonas gingivalis (OMNI\|PG1271), and the other from Staphylococcus aureus (OMNI\|SA0170). After homology searching using BLAST it was determined that these two sequences were most closely related to ornithine aminotransferases. This model's seed includes one characterized hit, from Bacillus subtilis (SP\|P38021).	0
NZ_CP024592.1\|WP_077095060.1\|1463677_1465687_-\|NAD-dependent-DNA-ligase-LigA	gnl\|CDD\|236137	PRK07956, ligA, NAD-dependent DNA ligase LigA; Validated.	0
NZ_CP024592.1\|WP_004584586.1\|1469053_1469545_-\|anaerobic-ribonucleoside-triphosphate-reductase-activating-protein	gnl\|CDD\|274161	TIGR02491, Anaerobic_ribonucleoside-triphosphate_reductase, anaerobic ribonucleoside-triphosphate reductase activating protein. This enzyme is a member of the radical-SAM family (pfam04055) and utilizes S-adenosyl methionine, an iron-sulfur cluster and a reductant (dihydroflavodoxin) to produce a glycine-centered radical in the class III (anaerobic) ribonucleotide triphosphate reductase (NrdD, TIGR02487). The two components form an alpha-2/beta-2 heterodimer. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism, Protein fate, Protein modification and repair].	1.40709e-63
NZ_CP024592.1\|WP_004585684.1\|1486908_1487475_+\|elongation-factor-P	gnl\|CDD\|234788	PRK00529, PRK00529, elongation factor P; Validated.	3.23865e-100
NZ_CP024592.1\|WP_099840707.1\|1472408_1473311_-\|IS982-family-transposase	gnl\|CDD\|372648	pfam13612, DDE_Tnp_1_3, Transposase DDE domain. Transposase proteins are necessary for efficient DNA transposition. This domain is a member of the DDE superfamily, which contains three carboxylate residues that are believed to be responsible for coordinating metal ions needed for catalysis. The catalytic activity of this enzyme involves DNA cleavage at a specific site followed by a strand transfer reaction.	6.63648e-97

>NZ_CP024592.1|WP_099840707.1|1472408_1473311_-|IS982-family-transposase
MKTNIVDVFCIIDDFSKLFDEAIKKKTLEEADKKRRNRKFKMSDSEVMTILILFHLSRYRDLKAFYLQYITHSCRSEFPHLVSYNRFVELQSRVGFKLIAFLNMCCLGQCTGISFIDSTPLKACHIKRAHGHRTMRGWAQKGKSTMGWFYGFKLHIVINDRGEIINYQITPGNRDDREPLKDGTFTKNLFGKLIADRGCISQNLFDRLFVDDIHMITKIKKNMKNSLMHLYDKVLLRKRALIETVNDMLKNLCPIEHTRHRSVNNFVTNLISGIIAYNILPKKPELNIEIIRNPNFPISA
>NZ_CP024592.1|WP_012458242.1|1469577_1471974_-|anaerobic-ribonucleoside-triphosphate-reductase
MEEVILRIVKRDGHVQSFDPEKIRQAIIKAYRAGGVHEEAARIDNIVQSVTDFARQSGELVTVEQIQDRVEEELMRLNPFIAKKYIIYREWRTVERDKRTSMKHTMDGIVTIEKNDVNLGNANMSSHTPAGQMMTFASEVTKDYASKYLLSLRYSRAHRAGDIHIHDLDYYPTKTTTCVQYDIADLYERGFRTKNGSIRTPQNIHSYATLATIIFQTNQNEQHGGQAIPAFDFFMAPGVRKSFVTHLIERLRFVLELRQPTNTDLSTTLPKAIRNLTPLLTDSPQEAGRLYEGLCSASFPFSSTEVEIALATAFRKTRKDTHQAMEGFIHNLNTMHSRGGNQVVFSSINYGTDTSPEGRMVMEELLRATEEGLGHGEVPIFPIQIFKVKEGINYSEADVKSALENFDDAMAGKVLFSAPNFDLLLKACATTAKALFPNFVFLDTPFNLHEDWRADDPKRYLQEVATMGCRTRVFDNVNGPKSSIGRGNLSFTSMNLPRLAIEARHEAEENCPDGDKETIRSEARLLFLESVRRMSTLIADQLYDRYCYQRTALARQFPFMMGNDVWKGGAALEPNEEVGDVIKSGTLGIGFIGGHNAMVAIYGEGHAHNKAAWNTLYDAISVMNDVAQEYKRKYHLNYSVLATPAEGLSGRFTRMDRKRYGIIPGVTDLDYYVNSFHVDVREPIGIAEKIKCEAPFHAITGGGHITYVELDGEAKKNVSVILKIVKMMKDENIGYGSINHPVDTCKGCGFKGVIYDKCPVCGSDRIARLRRITGYLTGSLDTWNSAKQAEEHDRVKHL
>NZ_CP024592.1|WP_004584586.1|1469053_1469545_-|anaerobic-ribonucleoside-triphosphate-reductase-activating-protein
MSESIESYGIRLLNVYRETICDGPGLHYSIYLAGCRHACPGCHNPSSWDPEAGVLMTDSILGNIIREINANPLLDGITLSGGDPFYNPAGLTCLLQRLRASCTLPIWCYTGYTLEQLETDPMLSAPLALIDVLVDGPFVRELFDPTLLWRGSSNQCIIRLHEN
>NZ_CP024592.1|WP_004584585.1|1468663_1468942_-|integration-host-factor-subunit-beta
MTKADVVNAIAKSTGIDKETTLKVVESFMDTIKDSLSEGDNVYLRGFGSFIVKERAEKTARNISKQTTIIIPKRNIPAFKPSKIFMSQMKQD
>NZ_CP024592.1|WP_080657388.1|1466828_1468343_-|Rne/Rng-family-ribonuclease
MAVLEDGKLVELQREPRNLSFAVGDIYLGKVKKVMPGLNAAFVDVGYKKDAFLHYLDLGLTFDAQQKMMEMMTKSKSIPSLSKVPLGSDLPKEGKIADVLKAGQQILVQIAKEPISTKGPRLTAELSFAGRSLVLVPFADKVSVSQKIRSAEERARLRQLIISIKPKNFSVIIRTSAEGKRASELDKELQSLLRRWDDNIKKLLRAKAPSIVYEEASRTLGLLRDNFNPSYQSIIVNDKAFRDSLSDYVELIAPGREEIVQYYQGELPIFDHFAITKQIKALFGRTVTYKSGAYLIIEQTEAMHVVDVNSGNRSRGSTEQEATAVDVNMAAAEELARQLRLRDMGGIIVVDFIDMSEAQHRQQLYEHMVKLMSADRARHNILPLSKFGVMQITRQRVRPAMVIHTEECCPTCLGTGKVESSILFTDQLEEKVAKMVMEHQVKQFVLHVHPYVAAYLKKGFLSSILKKWKLKYAKGIKLIPDESLGFLDYTFYDYDGNELDILDE
>NZ_CP024592.1|WP_077095059.1|1466208_1466832_-|recombination-protein-RecR
MIQKYPSRLLEKAIDQFATLPGVGRKTALRLALYLLHQPVENTRQFAAALVDLREHISYCRRCHNISDSDVCTICADPTRDQSTLCVVENIRDVMAIENTSQYRGLYHVLGGVISPMDGIGPGDLQIDSLVHRVASEQIHEVILALSTTMEGDTTNFFLFRKLEPTGVRISVIARGIAIGDEIEYADEITLGRSILNRTDFSDSVKF
>NZ_CP024592.1|WP_005874739.1|1465674_1466202_-|GNAT-family-N-acetyltransferase
MTDLFSSEQVRLRALEPEDLDFLYLWENDAELRESGNMLVPIGRNRLKEYIEKSSEGLMELGMMRLVICLSDDDKPVGAIDLYEYDAFHRRVAVGLFVIPEYRRLGIAVESLRKISHYVLDYLRLHQIIAYVLEDNKPSRMLFEAAGFEHTATLRQWMWHAGDYSDVLLYQLWKR
>NZ_CP024592.1|WP_077095060.1|1463677_1465687_-|NAD-dependent-DNA-ligase-LigA
MEKIVPPAVRIEELRRNLREHEYRYYVLSSPTIDDFEYDAMMKQLEELEREYPEWDSPDSPTHRVGSDKTEGFASVRHDRPMLSLSNTYNYDEIGDFYRRVSEGLQGAPFEIVAELKFDGLSISLIYEDGMLVRAVTRGDGIMGDDVTANVRTIRSVPLRLRGDDYPHMLEVRGEILLPFKEFDRINAQREAEGEPLFANPRNAASGTIKQLDPRIVAGRNLDAYFYYLYSDEPLAENHYDRLMQARQWGFKVSDAVTLCCSREDVYAFIDRFDTERLTLPVATDGIVLKVNAPAQQDLLGFTAKSPRWAIAYKYQAERVRTRLQHVSYQVGRTGAVTPVANLDPVLISGTVVRRASLHNADFIAEKDLHEGDFVYVEKGGEIIPKIVGVDTDARSIDGRPIVFTVLCPDCATPLVREQGEAAYYCPNAEGCPQQQKGRLEHYCGRKAADINIGPETIELLYSRNMIRNVADFYALTEEQLLTLPGFKKRAAAKLLDSIEASKARPYQAILFGLGIRFVGETVAKKLAAVYPSIDALAAATSEELVQIDEIGERIAAAVLHFFSLRQNRELIERLRLAGVSLEAETVSVPVSNRLAGKTVVISGTFEKRSRDEYKAMVEDNGGRMAGSVSSKTSFILAGSDMGPSKREKAEKLGVRLMSEEEFLRLIEE
>NZ_CP024592.1|WP_099840706.1|1462429_1463665_-|FtsX-like-permease-family-protein
MKIDFFLAGRLFRGGGKEGKGIAPIVRLSVIGIMLSLMVMLITVSIAGGFKQNIRSLVYGYTGHLCIAPVAGTSDHFNAPVGMLEAITSVGGVDRVVPTIEMTGVAKTDSAFAGILLMGDNSLRTRNLLFGQTVSGNYPSFSSADTVPNPILLPQVTADKLHLKIGDKLRIYFAGTERMRLRAFTVAGVYSGGKMDMPVGLVSADVLRRVGGLGADDVSRLLIYASDPDETDLIVTRVFDRLSETLYVGEQRLTINTATEQNPMIMDWLSALDTNVAILLTLMGLVGGFTMIAGLIVLVMDKTQFIGMLKALGCGEGSLRRIFLYLAMMLVGRGMIWGNVLALILCLLQQHFRWLRLLDPDIYYMDYVPVQVDWLVWILVNLGTLLVTFLMLLAPSHIISRISPVKALRFE
>NZ_CP024592.1|WP_077095062.1|1461895_1462201_+|hypothetical-protein
MRLHSSEFLLIGIVGCYCVMTLAGWIIGAGGGIGLYGRNVNQTAQRGTQGAYTGSKAMIGGAQVLLPVMSFDVSKGHSLKGSKFPPVEKEVSTCGNPACTK
>NZ_CP024592.1|WP_099840494.1|1481634_1482537_+|IS982-like-element-IS195-family-transposase
MKTNIVDVFCIIDDFSKLFDEAIKKKTLEEAGKKRRNRKFKMSDSEVMTILILFHLSRYRDLKAFYLQYITHSCRSEFPHLVSYNRFVELQSRVGFKLIAFLNMCCLGQCTGISFIDSTPLKACHIKRAHGHRTMRGWAQKGKSTMGWFYGFKLHIVINDRGEIINYQITPGNCDDREPLKDGTFTKNLFGKLIADRGYISQNLFDRLFVDDIHMITKIKKNMKNSLMHLYDKVLLRKRALIETVNDMLKNVCQIEHTRHRSVNNFVTNLISGIIAYNILPKKPELNIETIRNPNFPISA
>NZ_CP024592.1|WP_077094974.1|1482585_1484217_-|L-glutamate-gamma-semialdehyde-dehydrogenase
MNNSHFAFAKPVNEPVYGYAPGSPERKKLKEELQRQLSTPIEIPIIIGGKEIRTGDTGIVVMPHNHAVRLATYHRVGEKEVQQAIEAAEKARQDWSRLPWTERASVMLRIGELISTKYRYQLAASVMLGQSKNPMQAEIDAPCELIDFLRFGAYYAGQIYADQPISEKGILNRVEYRSLEGFVLAVTPFNFTSIASNLNLAPAMMGNTTIWKPSTTALHSNYLLMKIFQEAGLPDGVVNFLPGQGSLIGRVATANEHLAGFHFTGSTATFNTLWKSIAGNIDRYRGYPRIVGETGGKNFVMVHPSAEAREVATALVRGAFEYQGQKCSAASRAYIPRSLWPSVKEVMGDMLDSIKMGDVMEFDNFVNAVIDEASFDNIMNYLAAAKRDSDAKIIFGGEGDKSVGYFIRPTVIETTNPHYATMTDELFGPVLTVYVYEDKDFADTLRLCDSTGRYGLTGSIFSRDRYAIEQALDALRFSAGNFYINDKPTGAVVGQQPFGGARASGTNDKAGGPLNLMRWCNPRTVKETFVPPTDYPYPFLAKD
>NZ_CP024592.1|WP_077094973.1|1484293_1485223_-|amidinotransferase
MALICKQATNRVLMVRPALFGFNAETARNNSFQKETGVPEAVAREAKKEFDNYVNLLREYGVDVWVIQDSKTPHTPDSIFPNNWFSTHVTGELVLYPMYAPNRQQERKLPVLATVGEMEGVDRIINLSGYERDNCFLEGTGSMVLDRVNRIAYCCSSERTNPKVLEEFCRELDYKGLIFTATDANGAPIYHTNVMMCVASRYAIVCLECIRDEAERSMVVNSLTANGHRIIAISTEQVEHFAGNMLEVESETGQSLLVMSAEARRSLTKEQVAEIEGFSTIIAPELTTIEKNGGGSARCMLAEIFLPQG
>NZ_CP024592.1|WP_099840709.1|1485229_1486459_-|ornithine--oxo-acid-transaminase
MVLSEKAKYYVDLEHRYGAHNYHPLEVVLSRGLGAYVWDVDGKRYFDFLSAYSAVNQGHCHPKIIAALKEQAEKICLTSRAFYNDCLGEYEEFMHHYFGYDKMLPMNSGAEAVETALKLSRRWGYRVKGIPEEKAIIIVCDGNFHGRTISIVSMSSDPDSYTDYGPYTPGFVNIPYNNIEALEKALEEHKDHVAAFVVEPIQGEAGVFVPDDGYIRRAAELCRKYHALFVADEVQTGIARTGRMLCCDHDDVRPDIVVLGKAISGGVLPVSCVLADDEVMLTIKPGEHGSTFGGFPLACKVAMAALTVVKEEGLPERAEELGQYFRGELLKIKSPLLKLVRGRGMLNAIVIEPHNGHEAWDVCEAMAERGLLAKPTHRHIIRLAPPLCITREELAQAVEIIKESIKVLE
>NZ_CP024592.1|WP_004585684.1|1486908_1487475_+|elongation-factor-P
MATTADFRNGMCLEIEGQYYFIVEFLHVKPGKGPAFVRTKLKNVATGRILDKTWNSGVKVEEVRIERRPYQYLYQDEMGYNFMHPETFEQITIPGASIDGVQFLKDGDMVEAMVHATSETVLTCELPPHVKLRVTYTEPGLKGDTATNTLKPATVETGAEVRVPLFIQEGELIEVDTRDGSYIGRVKE
>NZ_CP024592.1|WP_077094978.1|1487772_1487988_+|hypothetical-protein
MLRSLCPRNTEAVLYIKRKALFVVENFFPQNIWTIGFFTLIFAVQTERRGWRRIDLSIAIIKLMDRKSPHY
>NZ_CP024592.1|WP_021664688.1|1488010_1488514_+|DNA-binding-protein
MLFFKRRQSCIAHKATGKKLWYPQTVINGSTASTLHIAEQISELSGASPGDVFGILRDLGIVMRRELASGKKIKLDGIGCFRLIAQAKGSGVEKKEDVKASQFNSVRVNFRAECRYNTVTRERDCTLIAPDLKFAEYGKPLPAGASANAGDSNSQTGGGDQGSGGGL
>NZ_CP024592.1|WP_077095042.1|1488814_1490080_+|nucleotide-sugar-dehydrogenase
MNNIRIAIIGLGYVGLPLARLFSTKFPTIGFDINPNRVEELMSGYDSTGEIGNELLQEALQKGLLCTTKIEEIGDCNFYIVTVPTPIDHNHTPDLRPLLAASETIGKVIDQGDVVVYESTVYPGVTEDECIPIIEKVSGLKYNVDFFAGYSPERINPGDKVHTVENIKKVTSGSTPEIADYVDRMYNTVLVNGTHKASSIKVAEASKIIENAQRDVNIAFMNEIAKIFNAMEIDTREVLEAAATKWNFLPFQPGLVGGHCIGVDPYYLIQRAQVYGVYPRVLMSARRLNDSMGSYIASQTIKQMNKAGIMVKDARILILGFTFKENCPDIRNTKVIDTYSTLQEYTKNIIVHDPWANPSIAEQVYGIKIHNEFPKGKFDAIIIAVAHRDFSNIDLEKSSTANTIIYDVKGILPQGKKCHKL
>NZ_CP024592.1|WP_005874020.1|1490413_1491496_+|phosphoserine-transaminase
MKKHNFTAGPCILNDLVLKDAASACLNFAGTGLSVLEVSHRDKEFDAVMLEARNLFKELLDVPEGYEVLFLGGGASLQFYQVPLNLLKKKAAFINTGTWATNAIKQAKIMTQVYGGEVEVLASSEDKNFSYIPKDFVIPEDVDYFHFTTNNTIYGTEIRKDFDTKTRLVADMSSDIFSRPIDVSKYDLIYGGAQKNIGPAGATFVLVKTDVLGQVDRPLPDMLNYQIHIKKDSMFNTPPVFPVYVALQTMKWYKELGGVKVLEKMNLDKAALIYDAIDSSKIFRGTVNPEDRSIMNACFVMKDEYKELEKEFATFAASRGMVGIKGHRSVGGFRASLYNALPIESVQSLVSVMKEFEAKH
>NZ_CP024592.1|WP_005874016.1|1491596_1492517_+|3-phosphoglycerate-dehydrogenase
MTKVLVATEKPFAKVAVDGIKRIIEEAGLEFALLEKYTDKKQLLDAVKDANAIIIRSDQIDAEVLDAAKELKIVVRAGAGYDNVDLAAATAHNVCVMNTPGQNSNAVAELVMGMLVFMYRNLFNGASGSELMGKKLGILAYGNVGRNVARIAKGFGMEIYAYDQFVSAADIEKEGVKAVASRDALFETCDIVSLHIPKTPETVKSINAELLSKMPKGACLINTARQEVIDEEGICKFMAERTDFKYATDIKPTNDAEMAKFEGRYFTTPKKMGAQTAEANINAGLAAARQIVDFIKNGNEKFRVNK

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Crispr_ID: NZ_CP024592_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP024592_7

1749813-1750770

orTypeII

Consensus_repeat	Method
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	PILER-CR
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	CRISPRCasFinder

12 spacers

cas2,cas1,cas9

The CRISPR arrays of NZ_CP024592_7

>merge|NZ_CP024592|7|1749813-1750770|PILER-CR,CRISPRCasFinder
ACGGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCAAGTTTTTTCTCTTTTAGCTTATCCGTATCACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCCCGCTTCAGCTCGTTGGTGTCGACTGTTTCACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCGCGGAGGTTCGGACGGTTTCACACCTTCGCACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCGCCTATCACAGCAATGATGCCAAAGACCAGACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCATAATCGACCTCCTGCGAATTAGATTCCAGACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCCAATAAATGGATCAACAACGAGCGTTGGGAACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCTGGGGAAAGAATTTCTTTGATAATTCTCTTACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCACCGCCCCGGATATAAAATGTAGGTCGTTTACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCAGCCGTGAAGTTTTACCTCGCCTGCGGCCTACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCAGTCGCGACGACACAACCATCCTCTCGGCTACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCGTTCTTCGTACACGGGGATACCTCTATTGGACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGCAATGGCTTTCCACGCTTCCTCAATTACGAGACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC

>NZ_CP024592|7|4|1749813-1750770|PILER-CR
ACGGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	AAGTTTTTTCTCTTTTAGCTTATCCGTATC
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	CCGCTTCAGCTCGTTGGTGTCGACTGTTTC
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	GCGGAGGTTCGGACGGTTTCACACCTTCGC
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	GCCTATCACAGCAATGATGCCAAAGACCAG
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	ATAATCGACCTCCTGCGAATTAGATTCCAG
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	CAATAAATGGATCAACAACGAGCGTTGGGA
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	TGGGGAAAGAATTTCTTTGATAATTCTCTT
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	ACCGCCCCGGATATAAAATGTAGGTCGTTT
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	AGCCGTGAAGTTTTACCTCGCCTGCGGCCT
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	AGTCGCGACGACACAACCATCCTCTCGGCT
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	GTTCTTCGTACACGGGGATACCTCTATTGG
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	AATGGCTTTCCACGCTTCCTCAATTACGAG
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC

>NZ_CP024592|7|7|1749813-1750770|CRISPRCasFinder
ACGGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	AAGTTTTTTCTCTTTTAGCTTATCCGTATC
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	CCGCTTCAGCTCGTTGGTGTCGACTGTTTC
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	GCGGAGGTTCGGACGGTTTCACACCTTCGC
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	GCCTATCACAGCAATGATGCCAAAGACCAG
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	ATAATCGACCTCCTGCGAATTAGATTCCAG
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	CAATAAATGGATCAACAACGAGCGTTGGGA
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	TGGGGAAAGAATTTCTTTGATAATTCTCTT
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	ACCGCCCCGGATATAAAATGTAGGTCGTTT
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	AGCCGTGAAGTTTTACCTCGCCTGCGGCCT
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	AGTCGCGACGACACAACCATCCTCTCGGCT
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	GTTCTTCGTACACGGGGATACCTCTATTGG
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC	AATGGCTTTCCACGCTTCCTCAATTACGAG
ACTGGGAATAGCTTTCAGATTTAGTATTTTTGTTGCAACGCACAGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP024592.1\|WP_077094668.1\|1745889_1747305_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293810
NZ_CP024592.1\|WP_004584080.1\|1758453_1759296_+\|carboxylating-nicotinate-nucleotide-diphosphorylase	unknown	unknown	gnl\|CDD\|238806
NZ_CP024592.1\|WP_077083412.1\|1738548_1739418_-\|glucose-1-phosphate-thymidylyltransferase-RfbA	unknown	unknown	gnl\|CDD\|130274
NZ_CP024592.1\|WP_021664465.1\|1737943_1738534_-\|dTDP-4-dehydrorhamnose-3,5-epimerase	unknown	unknown	gnl\|CDD\|376414
NZ_CP024592.1\|WP_099840762.1\|1763170_1764154_+\|VWA-domain-containing-protein	unknown	unknown	gnl\|CDD\|238744
NZ_CP024592.1\|WP_058018757.1\|1760342_1761338_+\|MoxR-family-ATPase	unknown	unknown	gnl\|CDD\|223786
NZ_CP024592.1\|WP_004584079.1\|1759315_1760242_+\|quinolinate-synthase-NadA	unknown	unknown	gnl\|CDD\|236489
NZ_CP024592.1\|WP_021679367.1\|1750928_1751231_-\|CRISPR-associated-endonuclease-Cas2	cas2	COG3512_cas2_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|226043
NZ_CP024592.1\|WP_099840757.1\|1737089_1737947_-\|dTDP-4-dehydrorhamnose-reductase	unknown	unknown	gnl\|CDD\|367904
NZ_CP024592.1\|WP_061156509.1\|1762217_1763174_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_099840761.1\|1761348_1762221_+\|DUF58-domain-containing-protein	unknown	unknown	gnl\|CDD\|224635
NZ_CP024592.1\|WP_099840886.1\|1748268_1748907_-\|Crp/Fnr-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223736
NZ_CP024592.1\|WP_004584081.1\|1756865_1758422_+\|L-aspartate-oxidase	unknown	unknown	gnl\|CDD\|223108
NZ_CP024592.1\|WP_023847137.1\|1751269_1752208_-\|type-II-CRISPR-associated-endonuclease-Cas1	cas1	cd09720_cas1_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|274694
NZ_CP024592.1\|WP_077094666.1\|1752220_1756507_-\|type-II-CRISPR-RNA-guided-endonuclease-Cas9	cas9	cd09643_cas9_CAS-II-A:CAS-II-B:CAS-II-C	gnl\|CDD\|187774
NZ_CP024592.1\|WP_077094669.1\|1745533_1745917_-\|rhodanese-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|238089
NZ_CP024592.1\|WP_099840759.1\|1741572_1742811_-\|3-deoxy-D-manno-octulosonic-acid-transferase	unknown	unknown	gnl\|CDD\|224436
NZ_CP024592.1\|WP_099840758.1\|1739532_1741488_-\|alkaline-phosphatase-family-protein	unknown	unknown	gnl\|CDD\|293739
NZ_CP024592.1\|WP_099840760.1\|1742835_1744356_-\|glutamate--tRNA-ligase	unknown	unknown	gnl\|CDD\|234953
NZ_CP024592.1\|WP_077094667.1\|1747397_1748204_-\|sulfite-exporter-TauE/SafE-family-protein	unknown	unknown	gnl\|CDD\|376667

Protein	Function_ID	Function_description	E-value
NZ_CP024592.1\|WP_077094668.1\|1745889_1747305_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293810	cd07724, POD-like_MBL-fold, ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain. Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.	1.15709e-74
NZ_CP024592.1\|WP_004584080.1\|1758453_1759296_+\|carboxylating-nicotinate-nucleotide-diphosphorylase	gnl\|CDD\|238806	cd01572, QPRTase, Quinolinate phosphoribosyl transferase (QAPRTase or QPRTase), also called nicotinate-nucleotide pyrophosphorylase, is involved in the de novo synthesis of NAD in both prokaryotes and eukaryotes. It catalyses the reaction of quinolinic acid (QA) with 5-phosphoribosyl-1-pyrophosphate (PRPP) in the presence of Mg2+ to produce nicotinic acid mononucleotide (NAMN), pyrophosphate and carbon dioxide. QPRTase functions as a homodimer with two active sites, each formed by the C-terminal region of one subunit and the N-terminal region of the other.	4.94643e-147
NZ_CP024592.1\|WP_077083412.1\|1738548_1739418_-\|glucose-1-phosphate-thymidylyltransferase-RfbA	gnl\|CDD\|130274	TIGR01207, Glucose-1-phosphate_thymidylyltransferase_1, glucose-1-phosphate thymidylyltransferase, short form. Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides].	1.02128e-179
NZ_CP024592.1\|WP_021664465.1\|1737943_1738534_-\|dTDP-4-dehydrorhamnose-3,5-epimerase	gnl\|CDD\|376414	pfam00908, dTDP_sugar_isom, dTDP-4-dehydrorhamnose 3,5-epimerase. This family catalyze the isomerisation of dTDP-4-dehydro-6-deoxy -D-glucose with dTDP-4-dehydro-6-deoxy-L-mannose. The EC number of this enzyme is 5.1.3.13.	2.44934e-102
NZ_CP024592.1\|WP_099840762.1\|1763170_1764154_+\|VWA-domain-containing-protein	gnl\|CDD\|238744	cd01467, vWA_BatA_type, VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation protein von Willebrand factor (vWF). Typically, the vWA domain is made up of approximately 200 amino acid residues folded into a classic a/b para-rossmann type of fold. The vWA domain, since its discovery, has drawn great interest because of its widespread occurrence and its involvement in a wide variety of important cellular functions. These include basal membrane formation, cell migration, cell differentiation, adhesion, haemostasis, signaling, chromosomal stability, malignant transformation and in immune defenses. In integrins these domains form heterodimers while in vWF it forms multimers. There are different interaction surfaces of this domain as seen by the various molecules it complexes with. Ligand binding in most cases is mediated by the presence of a metal ion dependent adhesion site termed as the MIDAS motif that is a characteristic feature of most, if not all A domains. Members of this subgroup are bacterial in origin. They are typified by the presence of a MIDAS motif.	6.89462e-74
NZ_CP024592.1\|WP_058018757.1\|1760342_1761338_+\|MoxR-family-ATPase	gnl\|CDD\|223786	COG0714, COG0714, MoxR-like ATPases [General function prediction only].	2.28724e-92
NZ_CP024592.1\|WP_004584079.1\|1759315_1760242_+\|quinolinate-synthase-NadA	gnl\|CDD\|236489	PRK09375, PRK09375, quinolinate synthase NadA.	1.71066e-166
NZ_CP024592.1\|WP_021679367.1\|1750928_1751231_-\|CRISPR-associated-endonuclease-Cas2	gnl\|CDD\|226043	COG3512, COG3512, CRISPR-associated protein, Cas2 homolog [Defense mechanisms].	4.13745e-28
NZ_CP024592.1\|WP_099840757.1\|1737089_1737947_-\|dTDP-4-dehydrorhamnose-reductase	gnl\|CDD\|367904	pfam04321, RmlD_sub_bind, RmlD substrate binding domain. L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.	1.22358e-126
NZ_CP024592.1\|WP_099840761.1\|1761348_1762221_+\|DUF58-domain-containing-protein	gnl\|CDD\|224635	COG1721, COG1721, Uncharacterized conserved protein (some members contain a von Willebrand factor type A (vWA) domain) [General function prediction only].	6.3775e-43
NZ_CP024592.1\|WP_099840886.1\|1748268_1748907_-\|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].	9.5284e-27
NZ_CP024592.1\|WP_004584081.1\|1756865_1758422_+\|L-aspartate-oxidase	gnl\|CDD\|223108	COG0029, NadB, Aspartate oxidase [Coenzyme metabolism].	0
NZ_CP024592.1\|WP_023847137.1\|1751269_1752208_-\|type-II-CRISPR-associated-endonuclease-Cas1	gnl\|CDD\|274694	TIGR03639, cas1_NMENI, CRISPR-associated endonuclease Cas1, subtype II/NMENI. The CRISPR-associated protein Cas1 is virtually universal to CRISPR systems. CRISPR, an acronym for Clustered Regularly Interspaced Short Palindromic Repeats, is a prokaryotic immunity system for foreign DNA, mostly from phage. CRISPR systems belong to different subtypes, distinguished by both nature of the repeats, the makeup of the cohort of associated Cas proteins, and by molecular phylogeny within the more universal Cas proteins such as this one. This model is of type EXCEPTION and provides more specific information than the EQUIVALOG model TIGR00287. It describes the Cas1 variant of the NMENI subtype of CRISPR/Cas system.	6.59513e-104
NZ_CP024592.1\|WP_077094666.1\|1752220_1756507_-\|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.	6.11164e-39
NZ_CP024592.1\|WP_077094669.1\|1745533_1745917_-\|rhodanese-like-domain-containing-protein	gnl\|CDD\|238089	cd00158, RHOD, Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.	4.38819e-24
NZ_CP024592.1\|WP_099840759.1\|1741572_1742811_-\|3-deoxy-D-manno-octulosonic-acid-transferase	gnl\|CDD\|224436	COG1519, KdtA, 3-deoxy-D-manno-octulosonic-acid transferase [Cell envelope biogenesis, outer membrane].	2.03385e-63
NZ_CP024592.1\|WP_099840758.1\|1739532_1741488_-\|alkaline-phosphatase-family-protein	gnl\|CDD\|293739	cd16015, LTA_synthase, Lipoteichoic acid synthase like. Lipoteichoic acid (LTA) is an important cell wall polymer found in Gram-positive bacteria. It may contain long chains of ribitol or glycerol phosphate. LTA synthase catalyzes the reaction to extend the polymer by the repeated addition of glycerolphosphate (GroP) subunits to the end of the growing chain.	2.25209e-64
NZ_CP024592.1\|WP_099840760.1\|1742835_1744356_-\|glutamate--tRNA-ligase	gnl\|CDD\|234953	PRK01406, gltX, glutamyl-tRNA synthetase; Reviewed.	0
NZ_CP024592.1\|WP_077094667.1\|1747397_1748204_-\|sulfite-exporter-TauE/SafE-family-protein	gnl\|CDD\|376667	pfam01925, TauE, Sulfite exporter TauE/SafE. This is a family of integral membrane proteins where the alignment appears to contain two duplicated modules of three transmembrane helices. The proteins are involved in the transport of anions across the cytoplasmic membrane during taurine metabolism as an exporter of sulfoacetate. This family used to be known as DUF81.	1.11029e-28

>NZ_CP024592.1|WP_099840886.1|1748268_1748907_-|Crp/Fnr-family-transcriptional-regulator
MKFAPKKQIEDISEFRSSPELVDKLYKHGILKVYKAGSVILNENAHVRSIPIVIKGVMRVIRTEEDGREILLYYIKAGESCIMSFLGGLHNETSKVKVEIEDDAEILFLPVDKVSLFMKEHPEWLNYIFRSYHKRFEELLDTVNAIAFKKMDERLLALIQKKAELVEGNTIQITHEQLANELGTARAVVSRLLKQLEESGIVRLGRNKITLM
>NZ_CP024592.1|WP_077094667.1|1747397_1748204_-|sulfite-exporter-TauE/SafE-family-protein
MLIAGYLASILIGLSLGLIGGGGSILTVPVLVYLMGIDPVLGTAYSLFIVGATSVVGSISYFRRSLVDVRTAVLFGLPSIFAVFLTRAYLVPAIPEYVLSPGSFAIDRNMLLMLLFAVLMLTASVSMIRPAKMQEKASQRPPKPKQPRYALILLEGIVVGTLTGLVGAGGGFLIIPALVFLGGLPMKQAIGTSLVIISAKSLLGFLGENNPAGLDWGLLLSVTAFAIIGIFIGMKFSQYIDGDKLKPAFGWFVFVMGLYIILKETILV
>NZ_CP024592.1|WP_077094668.1|1745889_1747305_-|MBL-fold-metallo-hydrolase
MKVEQIYTGCLAQGAYYITSMGEAAIIDPLREITPYLERLKRDGVKLKYILETHFHADFVSGHLDLSRATGAPIVYGPTAKPGFDAIVAEDNQIFELGNVKIRVLHTPGHTMESSCFLLIDENGRETALFSGDTLFLGDVGRPDLAQKAANLTQEELAGLLYDSLYTKILPLSDDIIVYPAHGAGSACGKNMMQETVDSLGNQKRVNYALNQPSKEAFIASVIEGLLPPPAYFGGNVVMNKMGYDSIDNVMERGLSALSATDFEAIAETSDALVLDTRAPGVFAQGFIPRSINIGLDGDFAPWVGTMIVDVKQPLLLVADPGREQEVITRLSRVGFDQVLGYLDGGFDTWNTSGKEIDHVECITANEFAERFCPEESLVFDVRKESEYAAEHVEGAYSRPLAYINDWIQDIPRDRHFYLHCIGGYRSMIASSILLSRGYRNFTDIEGGFASIAQTGVPKTDYVCQSKVSKK
>NZ_CP024592.1|WP_077094669.1|1745533_1745917_-|rhodanese-like-domain-containing-protein
MSKQSVKKIISFSLTIIIAIVMLGLLKNLFSQPDDKALTEAIRNSAFLVDVRTPGEFASGSVAEAVNIPLDRIASRLNELKNKKTIIVFCRSGNRSSQAKSILERNGFSNVLDGGTWGHVASLKGDQ
>NZ_CP024592.1|WP_099840760.1|1742835_1744356_-|glutamate--tRNA-ligase
MDTINRRIRVRFAPSPTGPLHIGGVRTALYNYLFARQHGGDMILRIEDTDSNRFVPGAEAYIIEAMEWLGIKFDEGVGYGGRFGPYRQSERRDIYRTYVRQLLDSGQAYIAFDTPEELEARRAEVPNFQYDATTRGQMRNSLTLPAEEVERLVAEGTQYVVRFLVEPNVDVEVNDLIRGRVVINSSILDDKVLYKSADDLPTYHLANIVDDHLMEVSHVIRGEEWLPSAPLHVLLYRAFGWEDTMPRFAHLALLLKPEGNGKLSKRDGDRLGFPVFPLEWKDPQTGDISKGYRESGYLPEAVVNFLALLGWNPGNDQDVMSMDELIRLFDIEKCSKAGAKFDYEKGRWFNHQYIQRKDNAELAELFRPILRENGVVATDEKTAHVISLVKERVNFIGELWEQAGFFFIAPSYDEKTVKKRWKEDTAKQLGELAELLDSHRSFAAEATEPTVKNWIETNGYHLGNIMNATRLALVGESKGPHIFDIMEVLGREETVGRIRRAIEILG
>NZ_CP024592.1|WP_099840759.1|1741572_1742811_-|3-deoxy-D-manno-octulosonic-acid-transferase
MRFLFSLIGLVYSSLIKLAVPFNPKARMMVRGRWKVWRQLREGIVPGGRYIWFHAASLGEFEQGRPMIERIRSEYPDYRIVLTFFSPSGYEVRKNYEGADVIVYLPADRLSRVRKFLDLVKPEMAIFIKYDFWPCFLTELERKQIPTYLVSSIFRPSQLFFRWYGGAYKRLLHCFTHIFVQDEASRLLLEKHGIDHVSVAGDTRFDRVISVYEARKSLSLIERFAASVPEDGLVIVGGSSWPPDEEILVRYFNRNPKIKLILAPHEIDKEHLLQIISHIRRPFIRLSEATESDIARQDCLIVDSFGLLSSIYRYGQVAFIGGGFGKGIHNTPEAAVYGIPVIFGPRYEKFKEARELIDVGGGFSVSSAEEFGNLIKRIQTDKAYRDAASHAAADYIRSNAGATEYIVHRIMK
>NZ_CP024592.1|WP_099840758.1|1739532_1741488_-|alkaline-phosphatase-family-protein
MNICKRTIRTNSWWAFAYRMALAYFLFGIARGLFYLFNYRFFADMTAEQVWRAWMGGLRFDTASVLYLNALFILLSFLPFRFRAKRSYRILTDWTFFVPNALGLAAGLADCIYYPYTLKRTSSTVFSEFSHEGGGLIWHLLLNYWYMSLLAIVLVAAMVWLYHRVKPVRTYAEAKDSLHYYTVHIVALVAAIAFIVWGIRGGSFAKSWRPMTMSYANLSVDKVEHRALVLNTPYSIIRTIGKQGLEEKRFYTSEKELEQVFNPIHHLAMDTTARFGQLRGRNVMVIIIESFARQYVGRLNQDIPDYNGYTPCFDSISQKGYLFEQAFANGRKSIDAMPSILSSLPSLRSHFITSHYSGNEIEGLGTALGRIGYHSIFLHGAPNGSMGFDAFVKQAGYKRYFGKTEYAHDEDFDGVWGIWDEPFLLHAVDELSRMKQPFVGTLFTLSSHEPFHIPSHREGLFPNEGEPLVQCIGYTDHALGEFFRKASRQTWFENTLFVITADHASGDLRPEYRSAVGRYAIPILFYAPGSDLIGFDRTTTVQQADILPTVLSLLGYSAPVLAFGNNMFSRQAPHFAVTDYDGTLQLLEDGLVLQHDGNHPLALYDYLNDKELRTNLLKTQAARADSMTCRIEAVIQSFNHRMNTNRLVADK
>NZ_CP024592.1|WP_077083412.1|1738548_1739418_-|glucose-1-phosphate-thymidylyltransferase-RfbA
MKGIILAGGSGTRLYPITRGVSKQLLPVYDKPMIYYPLSTLMLAGIRDVLIISTPQDLSMFQRLLGDGRDLGVRLEYAEQPSPDGLAQAFIIGREFVGDDCACLVLGDNIFYGHGFSQMLRSAVADAEKGMATIFGYYVNDPERYGVAEMDATGKVISLEEKPENPKSNYAVVGLYFYPNDVLDVAADVKPSARGELEITSVNQEFMLRKQLHLQQLGRGFAWLDTGTHESLTDASVFVSVIEKRQGLKIACLEEIAYNNGWLTKEDLARVAEPMKQNQYGKYLLGLIK
>NZ_CP024592.1|WP_021664465.1|1737943_1738534_-|dTDP-4-dehydrorhamnose-3,5-epimerase
MNFIPTEIPEVVILEPRLFRDDRGYFFESFSRQEIEMGIRPINFVQDNESASRYGVLRGLHFQKPPHAQSKLVRVVRGCVIDYAVDIRFGSPTFGKYVAVELSDTNFRQLFIPRGFAHGFVVLSDEVVFQYKCDNYYAPQSEGAIAWNDPNLDIEWKIPAEDIILSAKDQANPSWTELISSEDFRNLFPYNQDLYE
>NZ_CP024592.1|WP_099840757.1|1737089_1737947_-|dTDP-4-dehydrorhamnose-reductase
MNRILVTGADGQLGSELRLLASADSRFVFTDLAELDIRDKDAVLRFMEEYNIGIIINCAAYTAVDKAEDDEASAEKVNHQAAAHLAAAAAKYDALLIHISTDYVFDGTANIPYREDIPTAPLGAYGRTKLKGEQAVLAADCRYMILRTSWLYSSFGNNFVKTMLRLTAERDTLNVVFDQVGTPTYAADLAAFIHRLAIGQLPVKTGLYHFSNEGVCSWFDFAVAIARMSGHTACRISPCHSDEYPTRVRRPHYSVLDKTLIKNTFDISIPHWQDSLAACLNLLKH
>NZ_CP024592.1|WP_021679367.1|1750928_1751231_-|CRISPR-associated-endonuclease-Cas2
MWVMVFFDLPTETAADRKRAAIFRKNLIKDGFEMFQFSIYIRHCASRENAETHCRRVRSAIPEKGKIGLMTITDKQFSAMEIICGKGREYYQPPLQLELF
>NZ_CP024592.1|WP_023847137.1|1751269_1752208_-|type-II-CRISPR-associated-endonuclease-Cas1
MIKRTLYFGSPAYLSLKLGQLEVRLPEVEQTDSLPEHIKKAGRQSIPIEDLGIVVLDHKQITITQALLSALIKNGCAIISCDDSHHPTGMMLSFLGHSELGERVQDQIGASLPLKKQMWQQTIRAKIANQAVALSQTTKQSHSNMHAWIDLVKSGDTDNIEARAAAYYWANIFPELPSFKRDREGDWTNKLLNYGYAIVRAMAARAITAAGLLPSVGIFHHNKYNHFCLADDLMEPYRPYVDILVYRLIQKDIKNPPLSLSSEDKRELLSLPVIDTIIDDKAHPMSIAMHHSATSLYQCFAGKERRILYPHM
>NZ_CP024592.1|WP_077094666.1|1752220_1756507_-|type-II-CRISPR-RNA-guided-endonuclease-Cas9
MKKILGLDLGTASIGSAYVLEAEKSADQTKIVYLGTRIILSSADAENFSKGLSCSPTTDRTFKRSMRRRLQRYKQRRSSLIQQFKKIGIITNTEQIIREPISETHELLRIRSKAVSERVSLEEFARILLTINKRRGYKSNRKTSKSTEEDGKLVDAMAVTKELIKLKKTPGQYMFERFKRGKYAEIDFYPFDLINELKQIWEVQGQKYPDVLTEDLLSSLLKQKTGKAKELIYSKSDLNPAEVPIDYQKGKKLRKTILNKYFAYESRSLAVTNIIPVEQAITAIVAICKQINNSSGYLGAIGDRSRVLYANNQTIGQYLYERIKANPHDRIRGEVFYRQDYLDEFDRIWECQQNYYPAILTNDRKQYIRNRIIFYQRPLKSKKSELAFCEFESREVEHNGKKYTEGLHVAPKSSPVFQHFRLWQRLGQIEVSPLRKWDKQSNELFEQQNNADREGILNTEAKQKLFSYLNLLDHLTDNEILNILGYSPDKWKINFREIIGNRTNNLMMKAFFSMKEMTDGEQIDWEKNLTKITNGQSLISPEQIVDLIRQFFEREGITTSLLYFDPATDNFREQSHYSLWHLLYSYEDDNSPTGTTSLCKTLAKRYGIPHELCPLLASLTFERQYGSLSTKAMRKLLPFMQEKRYDEACKLAGYRHSAWITKEENAKRTLKNKLPLLRKGSLRNPVVEKILNQMTHVINTHIAEYGNPDEIRIEMARDMQANSKQRKAMTATITEATKRNTQFIEEIQKEFGFNPSKNDLIKYKLWKELAPLGNKTLYSNIYIPKEELFTAKFEIEHIIPRALFYDDSFSNKTLELNSVNKLKGNKTALDYLDTLGQEKANDYILRVEELKKIGAITQAKYKKLLIREKDLGDDFTNRDLTNTRYIIRHAADMLLQVTPSIVHTNGSITAILRRDWGLLDILKELNLPTYESIDRKISDPEEKLTQSVDRKDGQAIKMIKDWSKRDDHRHHAMDALITALTTRKHVQYLNGNSGAEETDKAQKLEQLKALRKQLIGSDGHFIPPMHDIRVQAKEALSRVIISTKVKGKVTTPNTNIICSRDKTTGRKIYVRQTTLTPRGALHLDTKYGINRYYQEREVSIGSKLTQEEIRLVSSPHIQSILLERLRAFDNNPKSAFTGRNSVDKKPLEDKNKKLVYTDKKVKQTILANRFVKRDRVNSKLDLDKVIDTGIKRILERRLKQYGGKYETAFSDLENNPIWLNEEKGIAIKSVRIRGKNNTITIRQTNTCRIKYVANDNNHHLAVYALPDGSIKDDIVSFFDAVERSRKRLPIIDKHKNQSLGWKYLFSIKQNEYFLLPQQVEKIDIDTGEISMQTTFSPKDLSHEYIMNPDNYAELASHIFRVQSISKTPQGNRDVRIYLFKQQYISGSQKDSLHLKGITHRQISSAKDLAELVKIRVNHLGRIVSVGEK
>NZ_CP024592.1|WP_004584081.1|1756865_1758422_+|L-aspartate-oxidase
MNRFDYIVVGGGLAGLYTAFKASKHGRVALITKADIHESNSYFAQGGVAAVTAADDAPDNHYNDTVEAGRGLCEDEAVRVLAEEAPERIDELIRWGMRFDTEADGLLALGLEGGHHHKRILHAGGDSTGRMLTSFMIDSVLQTSAIEIFVNHQAVELLIDDLGCRGVRTWDWGHGREVVFYGKHTVMATGGSAAIYRRSTNPQGTLGDGIALCYHAGCEVRDMEFVQFHPTALYNPKGEAFLISEAVRGEGAHLYNSRGERFMQGVHELGELAPRDVVARRIFLEMRRLGDEYVYLDLRHLDPDHIRKRFPTICARCAELGLDLTDRIPVAPAAHYTVGGISTDLNGCTAVPHLYAVGEVASTGIMGANRLASNSLIECLVFGHRVVADTIASDSIDYPTMPLSVVGYPKPKDASLYHKVKEQLSRLMTDYVGIIRNEEGLLSVDRKIEELRRTLLGTEDLYACFAEQLLTVGQLIVRGAIARRESRGGHYREDYPDTSEAYRKHSSYTLAGGAGNTK
>NZ_CP024592.1|WP_004584080.1|1758453_1759296_+|carboxylating-nicotinate-nucleotide-diphosphorylase
MTHEEMLLEKLIDLAIAEDIADGDISSNAIIPQSEGAAATMVMKADGIISGMEVARRVFERFEAVTWTPYVSDGDSVKRGQVILRVEGSYRALLQAERLALNFLQRMSGIATMTARYAEALKGTAVRLLDTRKTAPGMRITDKMAVRHGGGHNHRMGLYDMIMLKDNHIKVAGGIPQAIEAARRALPLSIKLEVETSNLAEVEEAVRYGADIIMLDNMDNDTMCEAVRLIAGRARTEASGNMTLERLQSVAETGVDYISVGALTHSVTAMDISMNFLLTQ
>NZ_CP024592.1|WP_004584079.1|1759315_1760242_+|quinolinate-synthase-NadA
MQTKDILKEIELLKKERNAIILAHYYARPEVQDIADYIGDSLGLSRQAADTEADTILFCGVHFMAETASIISPQKTILAPTKYAGCSLAEGASAEGLRRWKEQNPDGLIVSYVNTTAEVKAWTDYCCTSSNALKVVESLPRDRKILFGPDRNLGAYISRKTGREMELWNASCFVHERITEESILEAMELYPDADILIHPESEGSHSPRVLSSDRCFMYSTAGILSHARESDKKMFVIATEPETLHVLRKENPGKTFIAIQPDNRCFHMKQTGLWEVLEALRHNRYEVKVPAEIREKALLSIERMLAVG
>NZ_CP024592.1|WP_058018757.1|1760342_1761338_+|MoxR-family-ATPase
MSETIDIKALTELIEQKSSFVNLITHGMAQNIVGQNHLVESLLIGLLADGHILLEGVPGLAKTLAIKTLAGLISAKYNRIQFTPDLLPADVVGTMMYSQKREEFQVKQGPIFANFILADEINRAPAKVQSALLEAMQERQVTIGETTFKLPEPFLVMATQNPIEQEGTYQLPEAQVDRFMMKVLIDYPQKKEEMQIIRQNIGGRSAEIRPVITTEEILEARQVIRQVYLDEKIEQYIVDIVFATRYPEQFGLNALKDMISFGASPRASINLALAARAYAFIKHRGYVIPEDVRAVCHDVMRHRIGLSYEAEANSLTPDAVVNEILNKVEVP
>NZ_CP024592.1|WP_099840761.1|1761348_1762221_+|DUF58-domain-containing-protein
MQTSDLLKKVRRIEIKARGLSRQIFAGQYHSAFRGRGMAFSEVREYTVGDDVRDIDWNVTARYARPYVKVFEEERELTVMLMVDMSGSLSFGTEVETKRELTAEVAATLAFSAIQNNDKIGVLFFTDRIEKYVPPAKGKKHILYIIRELLEFRPQSRATDLSVPLSYLTRLVKKRCTAFLISDFQSEEDSYEKTLLMSARKHDIVAIRIFDRREADLPNVGLMRFRDAETGQTHWVDTANSSVRKAYADAYERRQVALAVLLKRCGVDTTEIRTGQDFVQQLLILFKKRS
>NZ_CP024592.1|WP_061156509.1|1762217_1763174_+|hypothetical-protein
MRHSLAIRFVLSAFCMLFVSSFLKAQELSIIGKLDRAEMQIGEQAVIDITIRTADLAHTHLQIPTDSTMSRIEILAFGITDTVVVKDPIVEIKAKMVITSFDSTLLEIPPFIVTDGQDQVMSKSLFLKVTMPEIDLSKPDSIYDIKEPWGVSYTWSDIFNIMLRHPLTWTILATFLAVLSYLFYKRYKENQARRPVVIPETPAIPAYDRAIAALESLRAKKLVEAGLYKEYFTELTDLLRSYIAETREIDAREMTSSEILQALQRIELPEKGSRLLHGILQTADLAKFAKYKPIHGEDVEAIRDARAFLDEVHNIRES
>NZ_CP024592.1|WP_099840762.1|1763170_1764154_+|VWA-domain-containing-protein
MTFAYPELLWLLILLPLIATWYILQARKTSATMTISSLKPFEGGRRGLRVYLRHSLPILRALSVGFLIIALARPQNTNSWQKDSIEGIDIMLAMDVSGSMQTMDFKPNRLEAAKDVAISFINNRPNDNIGMVTFAGESFTQCPLTTDHTVLLNMVQDLQMGVLDDGTAIGMGLATAVNRLKDSKAKSRVVILLTDGSNNMGDITPRMAADIARTFGIRVYTVGVGTRGEAPFPIQTEFGVRIQNVPVDIDEPTLDGIAEVSGGKYFRAVDNETLNEIYKEIDKLEKTRLMTKSFKAYEEKYFVYALIAFLLLLTEFLLRNTLLRSNP

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Crispr_ID: NZ_CP024592_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP024592_8

1976937-1977030

Orphan

Consensus_repeat	Method
GAAAAAGCCGGAATACGGTTGGAAAAGACG	CRISPRCasFinder

1 spacers

DEDDh

The CRISPR arrays of NZ_CP024592_8

>merge|NZ_CP024592|8|1976937-1977030|CRISPRCasFinder
GAAAAAGCCGGAATACGGTTGGAAAAGACGCGTCCTCGGTGTCACGGGGAGTATCGCAGCCTACGAAAAAGCCGGAATACGGTTGGAAAAGACG

>NZ_CP024592|8|8|1976937-1977030|CRISPRCasFinder
GAAAAAGCCGGAATACGGTTGGAAAAGACG	CGTCCTCGGTGTCACGGGGAGTATCGCAGCCTAC
GAAAAAGCCGGAATACGGTTGGAAAAGACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP024592.1\|WP_012457433.1\|1978300_1979686_+\|DNA-repair-protein-RadA	unknown	unknown	gnl\|CDD\|236994
NZ_CP024592.1\|WP_004583881.1\|1970888_1971512_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_021663839.1\|1987293_1987761_+\|DNA-binding-protein	unknown	unknown	gnl\|CDD\|273496
NZ_CP024592.1\|WP_099840803.1\|1966776_1967445_-\|uracil-DNA-glycosylase	unknown	unknown	gnl\|CDD\|235376
NZ_CP024592.1\|WP_023847381.1\|1984535_1985444_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_099840806.1\|1982622_1983261_+\|MarC-family-protein	unknown	unknown	gnl\|CDD\|225006
NZ_CP024592.1\|WP_099840802.1\|1965021_1965837_+\|noncanonical-pyrimidine-nucleotidase,-YjjG-family	unknown	unknown	gnl\|CDD\|162788
NZ_CP024592.1\|WP_099840805.1\|1979747_1982441_+\|transglutaminase-domain-containing-protein	unknown	unknown	gnl\|CDD\|376628
NZ_CP024592.1\|WP_099840804.1\|1969070_1970672_-\|S41-family-peptidase	unknown	unknown	gnl\|CDD\|223864
NZ_CP024592.1\|WP_021679987.1\|1967478_1968999_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_021662654.1\|1963271_1963973_+\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	unknown	unknown	gnl\|CDD\|381175
NZ_CP024592.1\|WP_004583877.1\|1976129_1976792_-\|fructose-6-phosphate-aldolase	unknown	unknown	gnl\|CDD\|234947
NZ_CP024592.1\|WP_023847380.1\|1985450_1986119_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_099840801.1\|1964017_1964872_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274008
NZ_CP024592.1\|WP_043901003.1\|1986430_1986658_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|379402
NZ_CP024592.1\|WP_023847382.1\|1983264_1983756_+\|3'-5'-exonuclease	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|99834
NZ_CP024592.1\|WP_077094895.1\|1974834_1976133_-\|DUF1343-domain-containing-protein	unknown	unknown	gnl\|CDD\|377768
NZ_CP024592.1\|WP_099840807.1\|1987870_1988185_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_077094896.1\|1977328_1978255_+\|amidinotransferase	unknown	unknown	gnl\|CDD\|224747
NZ_CP024592.1\|WP_077094894.1\|1972290_1974756_+\|PKD-domain-containing-protein	unknown	unknown	gnl\|CDD\|349483

Protein	Function_ID	Function_description	E-value
NZ_CP024592.1\|WP_012457433.1\|1978300_1979686_+\|DNA-repair-protein-RadA	gnl\|CDD\|236994	PRK11823, PRK11823, DNA repair protein RadA; Provisional.	0
NZ_CP024592.1\|WP_021663839.1\|1987293_1987761_+\|DNA-binding-protein	gnl\|CDD\|273496	TIGR01201, HU_rel, DNA-binding protein, histone-like, putative. This model describes a set of proteins related to but longer than DNA-binding protein HU. Its distinctive domain architecture compared to HU and related histone-like DNA-binding proteins justifies the designation as superfamily. Members include, so far, one from Bacteroides fragilis, a gut bacterium, and ten from Porphyromonas gingivalis, an oral anaerobe. [DNA metabolism, Chromosome-associated proteins].	1.79845e-52
NZ_CP024592.1\|WP_099840805.1\|1979747_1982441_+\|transglutaminase-domain-containing-protein	gnl\|CDD\|376628	pfam01841, Transglut_core, Transglutaminase-like superfamily. This family includes animal transglutaminases and other bacterial proteins of unknown function. Sequence conservation in this superfamily primarily involves three motifs that centre around conserved cysteine, histidine, and aspartate residues that form the catalytic triad in the structurally characterized transglutaminase, the human blood clotting factor XIIIa'. On the basis of the experimentally demonstrated activity of the Methanobacterium phage pseudomurein endoisopeptidase, it is proposed that many, if not all, microbial homologs of the transglutaminases are proteases and that the eukaryotic transglutaminases have evolved from an ancestral protease.	7.66175e-17
NZ_CP024592.1\|WP_099840803.1\|1966776_1967445_-\|uracil-DNA-glycosylase	gnl\|CDD\|235376	PRK05254, PRK05254, uracil-DNA glycosylase; Provisional.	2.07461e-136
NZ_CP024592.1\|WP_099840806.1\|1982622_1983261_+\|MarC-family-protein	gnl\|CDD\|225006	COG2095, MarC, Multiple antibiotic transporter [Intracellular trafficking and secretion].	3.26513e-24
NZ_CP024592.1\|WP_099840802.1\|1965021_1965837_+\|noncanonical-pyrimidine-nucleotidase,-YjjG-family	gnl\|CDD\|162788	TIGR02254, hydrolase_haloacid_dehalogenase-like_family, noncanonical pyrimidine nucleotidase, YjjG family. This HAD superfamily includes including YjjG from E. coli and YfnB from B. subtilis. YjjG has been shown to act as a house-cleaning enzyme, cleaving nucleotides with non-canonical nucleotide bases. This family is a member of the haloacid dehalogenase (HAD) superfamily of hydrolases which are characterized by three conserved sequence motifs. By virtue of an alpha helical domain in-between the first and second conserved motif, this family is a member of subfamily IA (TIGR01549).	2.05363e-121
NZ_CP024592.1\|WP_023847382.1\|1983264_1983756_+\|3'-5'-exonuclease	gnl\|CDD\|99834	cd06130, DNA_pol_III_epsilon_like, an uncharacterized bacterial subgroup of the DEDDh 3'-5' exonuclease domain family with similarity to the epsilon subunit of DNA polymerase III. This subfamily is composed of uncharacterized bacterial proteins with similarity to the epsilon subunit of DNA polymerase III (Pol III), a multisubunit polymerase which is the main DNA replicating enzyme in bacteria, functioning as the chromosomal replicase. The Pol III holoenzyme is a complex of ten different subunits, three of which (alpha, epsilon, and theta) compose the catalytic core. The Pol III epsilon subunit, encoded by the dnaQ gene, is a DEDDh-type 3'-5' exonuclease which is responsible for the proofreading activity of the polymerase, increasing the fidelity of DNA synthesis. It contains three conserved sequence motifs termed ExoI, ExoII and ExoIII, with a specific Hx(4)D conserved pattern at ExoIII. These motifs are clustered around the active site and contain four conserved acidic residues that serve as ligands for the two metal ions required for catalysis. The epsilon subunit of Pol III also functions as a stabilizer of the holoenzyme complex.	3.2279e-76
NZ_CP024592.1\|WP_099840804.1\|1969070_1970672_-\|S41-family-peptidase	gnl\|CDD\|223864	COG0793, Prc, Periplasmic protease [Cell envelope biogenesis, outer membrane].	3.53973e-90
NZ_CP024592.1\|WP_021662654.1\|1963271_1963973_+\|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase	gnl\|CDD\|381175	cd11648, RsmI, Ribosomal RNA small subunit methyltransferase I (RsmI), also known as rRNA (cytidine-2'-O-)-methyltransferase. RsmI is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.	9.00399e-123
NZ_CP024592.1\|WP_004583877.1\|1976129_1976792_-\|fructose-6-phosphate-aldolase	gnl\|CDD\|234947	PRK01362, PRK01362, fructose-6-phosphate aldolase.	4.79442e-143
NZ_CP024592.1\|WP_099840801.1\|1964017_1964872_+\|hypothetical-protein	gnl\|CDD\|274008	TIGR02168, Chromosome_partition_protein_Smc, chromosome segregation protein SMC, common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].	0.00010613
NZ_CP024592.1\|WP_043901003.1\|1986430_1986658_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|379402	pfam13936, HTH_38, Helix-turn-helix domain. This helix-turn-helix domain is often found in transferases and is likely to be DNA-binding.	2.05433e-10
NZ_CP024592.1\|WP_077094895.1\|1974834_1976133_-\|DUF1343-domain-containing-protein	gnl\|CDD\|377768	pfam07075, DUF1343, Protein of unknown function (DUF1343). This family consists of several hypothetical bacterial proteins of around 400 residues in length. The function of this family is unknown.	2.29623e-173
NZ_CP024592.1\|WP_077094896.1\|1977328_1978255_+\|amidinotransferase	gnl\|CDD\|224747	COG1834, COG1834, N-Dimethylarginine dimethylaminohydrolase [Amino acid transport and metabolism].	2.45563e-26
NZ_CP024592.1\|WP_077094894.1\|1972290_1974756_+\|PKD-domain-containing-protein	gnl\|CDD\|349483	cd18173, M14_CP_bacteria, bacterial peptidase M14 carboxypeptidase, uncharacterized. This family contains only bacterial carboxypeptidase (CP) members of the M14 family of metallocarboxypeptidases (MCPs), mostly of which have yet to be characterized. The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. The N/E subfamily includes eight members, of which five (CPN, CPE, CPM, CPD, CPZ) are considered enzymatically active, while the other three are non-active (CPX1, PCX2, ACLP/AEBP1) and lack the critical active site and substrate-binding residues considered necessary for CP activity. These non-active members may function as binding proteins or display catalytic activity towards other substrates. Unlike the A/B CP subfamily, enzymes belonging to the N/E subfamily are not produced as inactive precursors that require proteolysis to produce the active form; rather, they rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavages that would otherwise damage the cell. In addition, all members of the N/E subfamily contain an extra C-terminal domain that is not present in the A/B subfamily. This domain has structural homology to transthyretin and other proteins and has been proposed to function as a folding domain. The active N/E enzymes fulfill a variety of cellular functions, including prohormone processing, regulation of peptide hormone activity, alteration of protein-protein or protein-cell interactions and transcriptional regulation.	1.10352e-157

>NZ_CP024592.1|WP_004583877.1|1976129_1976792_-|fructose-6-phosphate-aldolase
MKFFIDTANLDQIREANDMGVLDGVTTNPSLMAKEGISGKDNCMRHYLAICEIVDGDVSAEVIATDYEGMIREGEELAALHPQIVVKVPCTAEGIKAIKYFSDKGIRTNCTLIFTVGQALLAAKAGASYVSPFVGRLDDIASDGIKLVENIVAMFGFYRYETEVLAASIRHTQHIIQCLEAGADVATCPLNAIKGLLKHPLTDSGLKAFLEDHRRVNEGK
>NZ_CP024592.1|WP_077094895.1|1974834_1976133_-|DUF1343-domain-containing-protein
MIPRFFRKYSIALACISGLMSFSAYTGCQVAGAAHSSRSEEVGSQTAHSEQEISVATPREEVRVVVGAERTELLLPLLRDKRVALVANATSVVGMEREHLLDNLLRQGVNVVKILGPEHGFRGDADAGATVKDERDVRTGIPIVSLYGKNKKPTPRMLADVDVLLFDMQDVGTRFFTYISTLHYVMEACAEEQKKLIVTDRPNPNDYVDGPILQDDCRSFVGVDPLPILHGLTIGELANMINGEGWLGKKEMKCDLTVVPMLGWKHGQEYALPVKPSPNLPTANAIAWYPSLCLFEATIMSVGRGTDFPFEVLGYPKKVFGSFVFVPRPIRGMDSNPLYKGRHCYGVDLRGEKAPRGLSLQLLIRYYRTARREGIKFVNRRQMFNLLAGTKELAQQIEKGRTEEQIRASWQSDLDKYHKLRKKYLLYPTPTE
>NZ_CP024592.1|WP_077094894.1|1972290_1974756_+|PKD-domain-containing-protein
MKKKNFLLLGIFVALLTFIGSMQAQQAKDYFNFDERGEAYFSFKVPDRAVLQELALIMSIDEFDPVTNEAIAYASEEEFEAFLRYGLKPTFLTPPSMQRAVEMFDYRSGEKYEWNAYPTYEAYISMMEEFQTKYPSLCTTSVIGKSVKDRKLMICKLTSSANTGKKPRVLYTSTMHGDETTGYVVLLRLIDHLLSNYESDPRIKNILDKTEVWICPLTNPDGAYRAGNHTVQGATRYNANNVDLNRNFKDDVAGDHPDGKPWQPEATAFMDLEGNTSFVLGANIHGGTEVVNYPWDNKKERHADDEWYKLISRNYAAACQSISASYMTSETNSGIINGSDWYVIRGSRQDNANYFHRLREITLEISNTKLVPASQLPKYWNLNKESLLALIEESLYGIHGTVTSTANGQPLKCQILIENHDKRNSDVYSDATTGYYVRPIKAGTYTVKYKAEGYPEATRTITIKDKETVIMDIALGNSVPLPVPDFTASPMTISVGESVQFQDQTTNNPTNWEWTFEGGQPAMSTEQNPLVSYSHPGQYDVTLKVWNASGSNTITKEKFITVNAVMPVAEFVGTPTEIEEGQTVSFQNQSTNATNYVWIFDGGTPATSEDENPTVLYSKAGQYDVTLKAISASGETVKTKEKYITVKKAPVPAPVANFEGTPRKVKKGETVTFKDLSTNNPTSWLWVFEGGSPATSTEQNPVVTYNETGKYDVQLTATNEGGSNVKKAEDYIEVILDDSVEDIVAQTGIVIRPQNGTKQILIEANAPIKAIVLYDINGRVVLKTTPNQLRSTVDLSILPEGIYTINIKTEKSARTEKIHIG
>NZ_CP024592.1|WP_004583881.1|1970888_1971512_+|hypothetical-protein
MKRMLLLLVVLLYGIAGRLAAQDVIRPWSLQVGAGYSDTENIPGGFTYGFYLGKRMGSFLEVGLSMYNSTRQTANNADSFASNEGDGSFQVNMSSPNEKWSFFDAGSANCYMIVVGVNPLHLFWQNSRHNLFLAVQAGLSNKHNIHFIYGDKGAKVSIYTNSNTYIGYGARVAYEYQIHKNVGAGAAVMYDHGNKMLTAMATLSTHF
>NZ_CP024592.1|WP_099840804.1|1969070_1970672_-|S41-family-peptidase
MNKASKSIILLLLLGCSASAQKLSSSMKEALRKLETAVYAISSLYVDSVDNNKLTEYAIRGVLSELDPHSVYSDAEETKSELEPLNAGFDGIGVQFNMLTDTVYVVQVIAGGPSEKAGLLAGDRIVSVDDTVIAGVKMKTNDVMKRLRGPRGSKVKLGVWRGNDRLNITVKRGLVPVHSREACYMVDERTGYIRLSRFSRTTYDEFAEGIALLRGRGMQQLVLDLRFNGGGILDQAVEMAGTFLPEGSTVLTVRNNRMPRISERMEATSNNLLPKDLPLVVLVNEFSASASEILAGAIQDWDRGVVIGRRTFGKGLVQRPLPFQDGSMIRLTIARYYTPSGRSIQKPYAKGNFKAYEQELIGRFKHGESIHSDSIRFPDSLRYKTLVTGRTVYGGGGIMPDLFIPTDTALFNKLHRELLNKGIFNRAVLKYVDAHRQKLRQRFPDRQSYATFSVPKELTESLKAFAEAEKITWSTELFAEAEELIKCQLHAYIARDILGENDFFYFFNRMDKEYIKALDLLNDPDEYKRLLGK
>NZ_CP024592.1|WP_021679987.1|1967478_1968999_-|hypothetical-protein
MKEISRLTAVILLAVGFVLANGSCSDDFDKYAESPEDRAEFSADTIKFDTLFSRVSSSTRTFMVYNRLNRSLRLSEVELVGGKSRGYRVNVDGHVGTKFSDLTILPKDSMFIFVEATFPEGESDDPVEVKDSLRFLINGRTDYVLLQGFRQNVDEVTALVIDRDTIFGAQRPTLLLDSLVVQQGATLTLPAGCRLLMANKAHIKVRGRLMAEGNPAKRVMIENLRHDLLVQDVPYTLVPGQWGGILFSEESRGNELRYTTIRNGRWGIIAEGGKDVTTPKLLLEGCMVTNTKGSGLAASGGYIRILNSEISNTLGYTVALFGSVCELTQSTVCNFYRWDNRQGEALRYVTAFAPDVAGGSYTPSSDSRLILSNSIVDGSRSVVKQGDKESGGEISLSDGSPSDNEASVLARLTIRNSYVRARSSILNVGYNVMEADKNNPADSIYYSVGYDLIKKKYNFRYDYHPLPNAPFVGKADPAIIALFPHDLTGEPRRTATVGAFEVKPRP
>NZ_CP024592.1|WP_099840803.1|1966776_1967445_-|uracil-DNA-glycosylase
MKEVRIEAGWKKVLQEEFDKFYFEKLTDFVREEYRQSPIYPPARFIFRAFDTCPFDRVKVVILGQDPYHEPGQAEGLAFLVPTGIPIPPSLRNICEEIRTDTGQPAHIDGGSLLPWVEQGVLLLNATLTVRASQAGSHQGHGWETFTDAAIEALAKRREHLVFLLWGSYARRKSAMIDPRCHLILEAPHPSPLSAHRGFFGCKHFSRTNAYLRQHGIAPIVW
>NZ_CP024592.1|WP_099840802.1|1965021_1965837_+|noncanonical-pyrimidine-nucleotidase,-YjjG-family
MFVSQAVELHTAASAVLPLLLSSGTSGLAASSSTHSVFSMIKHLFIDLDDTLWDTYHNNKSSLEELYHTHAWDRYFDSFETFFSIYLPHNEALWSEYRYGQIDKPTLTLERFRRPFTGYLTLSDEQILTWNVEFLSITGQKTRLCPHALEVMEYLHRYYKVYILSNGFREIQHAKLTNSGLAPYIDRVILSEDAGINKPNKKIFDFALVKAKARKTESIMIGDSWEADIVGAANAGLASVWYNPNRHILPDDGVRAPMHIISSLSELMQIF
>NZ_CP024592.1|WP_099840801.1|1964017_1964872_+|hypothetical-protein
MKKKLFIATALTLALVSCGKNSSAYKELKMQYDSIAAVNSQHESELAEMDSIISGVLTNFQEISAMEGMINLNPLSGDIRASQRDRINDNMRLINEKLQANRKSIDDLTEKLQKSGRENSRLMKTLTQLRQQLEAKTQEVNQLREELERKNIAIGMLDSTVISQGAQLESSARENATLAEQNARQDRELNTVRYCIGTSSDLKEMNIVRRGQALTEGHNDTYFTKADMRNLKVIPLMAKKANVLTSHPASSYELIRGTDKMLTLRIKDPQAFWKNSKMLVIQTN
>NZ_CP024592.1|WP_021662654.1|1963271_1963973_+|16S-rRNA-(cytidine(1402)-2'-O)-methyltransferase
MEGRLTVVPTPIGNLEDITLRALKVLREADLILAEDTRTSSVLLHHYDIHCPLQSHHKFNEHRTAKSLAERISGGERIALISDAGTPGISDPGFLLVRACAELGVVVECLPGPTALIPALVASGLPADRFVFEGFLPVKKGRQTRMKELAEELRTMIFYESPHRVLRTLIQFVETFGLDRPAAACRELSKLHEEVIRGTLAELLAHFENHPPRGEFVLIVGGAAPKGRKEEKQ
>NZ_CP024592.1|WP_077094896.1|1977328_1978255_+|amidinotransferase
MMKILPHVINETAPLRTVVLGLPDSTGGAPALADTYDAKSYESVLRGTYPSDEDIKIEMDAVLDVLVRHGIEVLRPEPIANYNQIFARDVAFAIDDKLFVSNLIADRARESEAFSPIWDCVGESHLVRLSEDIHAEGGDILLYDDILFIGTYLQKDYPSFKTARTNARAVDFFREFFPHKTIIPIELIKHDTDPMRSVLHLDCAFQPVGRGRAIVYRQGFLHSESFGLITEIFGGRDNLFEITPEEAYMMNTNIFSISPDTVISERNFVRLNNHLREAWGMTVEEVPYAEISKQGGLLRCSTMPLVRE
>NZ_CP024592.1|WP_012457433.1|1978300_1979686_+|DNA-repair-protein-RadA
MAKEKTIYVCRSCGTKYAKWQGNCNACGEWNCIDEEKVPAPASGKHAAKSFMPREQDNRPRLLQDVESGDEERIRLGDEEFDRVLGGGIVKGAFVLLGGEPGIGKSTLILQTVLRLPQLRTLYVSGEESARQLKMRAERLGQAMNECYVYCETNIERILSRAEELTPDLLVIDSIQTVYTEEMESSAGSVGQIRECAALLLKYCKTTGIPVIVIGHITKEGSIAGPKVLEHIVDTVLLFDGDKHHLYRILRGQKNRYGSTSELGIYEMRQDGLRGVENPSEHLITRNREDLSGIAIAVAMEGIRPILIEAQALVSSAIYANPQRSATGFDIRRMNMLLAVLEKRAGFKLIQKDVFLNIAGGIKIADPATDLAVISAVLASSLDIVIPPAVCMTGEVGLSGEIRPVSRIEQRITEARRIGFKEILVPADNFRQEDAGRFGIRLVPVRKVEEAFRHLFSKGRE
>NZ_CP024592.1|WP_099840805.1|1979747_1982441_+|transglutaminase-domain-containing-protein
MKENKLFRIGILAIVALLLTGCKGSDTHFITDADFRKQVQEDLRVKREALSEGNLFEVLERDSLRTEEREALEFLYAYMTLPDIVDYSGDFYLQNVRESFRAREEMSWGKEVPELLFRHFVLPIRVNNENLDSSRMVFYAELKERVKGMSMKEAALEVNHWCHEKATYSPSDPRTRSPLATVKNALGRCGEESTFTVAALRLVGIPARQVYTPRWAHTDDNHAWVEVWVDGKWYFIGACEPAAELNDAWFNSSVVRAMLTHTRVFGRYEGPEEKLFRTANYTEINCIDNYAPTEMIEVKVTDRSGAVVEGADIRFCIYNYSEFYPVVTKQSDAQGQASLRVGKGDMLIWAAKDGLFGYALSKADDRKPLTIALDSFEVQPEWADFKIVPPAGDPIPTTCSPQQISTNDTRLLREDSIRAAYEATFATAEQSAALAAELGVDAPALTGILQTSRGNHADIEGFLRSVEAGKARQRAMDLLQTVSPKDLTDTPESLLKVIFRDMAEPAPEAASGEAYRRHLRYVASPRIYTEMLSSFVPTLRSILTAKEQEAMRQDPAELVRWVSSNIRLDTLYNTQYTTITPVGVWRAKRADLRSMGIFFVAMARTLGIPARYDEVTGKIQYSKELMPLRWSDVNLRESKTALKEQGSLALDYTPTALAPNPNYYSRFTVAELQPSGIIRTLYYDENEPTDLKTLFDRPKEMNAGHYFLVTGTRMASGSVLCRMRKFTVEAGKTTRQPLELLHDSTDIQVIGSINAEQLYHDLSHAEDRSLLSTTGRGYFAMAILGAGQEPTNHALKDLEKVKADFEQWGRKLILLFPDADGYKRYKPADFPSLPETAVFGLDIQGRNAAMIREAANLPDATNLPIVIIADSFGRVVFVRQGYTIGLGEQMMQVIRRL
>NZ_CP024592.1|WP_099840806.1|1982622_1983261_+|MarC-family-protein
MDFLDKVLQDLSLIDLKEIIGSFVILFVAIDIIGAIPVVLSLKDRGQSFHSGKATTFSCVMMLAFLFIGEPMLNFFGVDVSSFGVAGAIVLFVMAVEMIFGVQIFKDDGPAGSATIVPLVFPLFAGAATFTTILTLRADGIAMTNIAIAILINVAMIYLMLRFVNQLERFFGKGGIYILRKFFGVILLAISVKFFTGNIVKIIEAMNEALQK
>NZ_CP024592.1|WP_023847382.1|1983264_1983756_+|3'-5'-exonuclease
MLDFAAIDFETANAERTSVCSVGIIVVRGGEIVHRYYSLIRPEPDYYNYHNTRVHGLTAADTESARIFPDVWAEVEPLIAGLPLVAHNKPFDEGCLKAVFRMYRMDYPDYPFFCTLQAARRQLRHLSDHRLPTVAQCCGYILAQHHQALTDAEACAAIALKLL
>NZ_CP024592.1|WP_023847381.1|1984535_1985444_+|hypothetical-protein
MKKNILFLAAMILILGILPSCSKDEFSLDALQTANNAISRASKSDQALDSLMVAIDKYNAAFIGGNRNAALQSMLLASNSNTQRGFWGILKKICKVVIADAAGTSGGVIVGTASSIVAIIDQFGLDPANAKSLTLPTTCPFLSSRETGSIKGEAHNKVAYQVIKNNPNFAKMNEVNLYNAVVLEYQKLYDKTSLPSFAFASNLLNNVRTHLLENELNDEASWYIAWQQITQNQPKISKLVVDFALNVVNIRENDDVRSYVKGYSKIVENSKVSTAEKSIIFDGISVAANSRILWNASLSNME
>NZ_CP024592.1|WP_023847380.1|1985450_1986119_+|hypothetical-protein
MKHWFKSISLLLCAFLFVGTNALAQENESEKSRFDFSVSLGQGFLTNSTTGLMHGYTPVHDGLMSGAIYLGWTATKRENAMGVTFRMLTPSPGYSVDAFGKENTLNHTFYVAALYDRSVIPIHPIKNLNFVFSIEAGAVWLNRVEQIYNSTSQNWDKQSRTRVGIEAAIGMHLQYQINKSVYLIAGTNLTSCIFRKKINEYQQKDKTHIGLVDNSIGIGLNF
>NZ_CP024592.1|WP_043901003.1|1986430_1986658_+|helix-turn-helix-domain-containing-protein
MEKTKYKRLTLDNRKTIANCIGLGKSVTEIAQILSVHKSTISREIRRLGELQDYRPLKAHKPGQTHQKFRENTSC
>NZ_CP024592.1|WP_021663839.1|1987293_1987761_+|DNA-binding-protein
MLNLSVKSQIMKIGKHKGKTMYYAQVDKPRVIEYEDVIKDIAEMSSLTTGDVRNAIDRLAYYLQRELTEGNTVKLGQIGTFRVAVPSKYVETEKEVNASILKKAKIQFYINRTLSAVAENIRFAVYRNGQKVDTTTSPSTPSEGGGEQPGGSGGL
>NZ_CP024592.1|WP_099840807.1|1987870_1988185_+|hypothetical-protein
MKNYLMKRYDLTNKEGYKIAIQDFRLITFAAVSLCLWAILNPSRKKQKQTAEELIKQGKLNGVKEMEIIMEDRTGLHLDVPIKDVNIKTGIGSEGKTVVKVTYK

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Crispr_ID: NZ_CP024592_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP024592_9

2165384-2165479

Orphan

Consensus_repeat	Method
CTTGCGACTGCTCTATGATCTCACAGCAGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP024592_9

>merge|NZ_CP024592|9|2165384-2165479|CRISPRCasFinder
CTTGCGACTGCTCTATGATCTCACAGCAGATTTGAATTAAAGAATTCTTTTCTATCTTCGTTGTCACTTGCGACTGCTCTATGATCTCACAGCAGA

>NZ_CP024592|9|9|2165384-2165479|CRISPRCasFinder
CTTGCGACTGCTCTATGATCTCACAGCAGA	TTTGAATTAAAGAATTCTTTTCTATCTTCGTTGTCA
CTTGCGACTGCTCTATGATCTCACAGCAGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP024592.1\|WP_077094379.1\|2151226_2152816_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP024592.1\|WP_077094381.1\|2157703_2158816_-\|2-iminoacetate-synthase-ThiH	unknown	unknown	gnl\|CDD\|131404
NZ_CP024592.1\|WP_005873709.1\|2169972_2170782_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293819
NZ_CP024592.1\|WP_021678830.1\|2167519_2168098_-\|30S-ribosomal-protein-S16	unknown	unknown	gnl\|CDD\|237744
NZ_CP024592.1\|WP_004584649.1\|2175393_2175837_-\|DUF4494-domain-containing-protein	unknown	unknown	gnl\|CDD\|379718
NZ_CP024592.1\|WP_023846863.1\|2163439_2163640_-\|sulfur-carrier-protein-ThiS	unknown	unknown	gnl\|CDD\|273754
NZ_CP024592.1\|WP_004584669.1\|2158828_2159608_-\|thiazole-synthase	unknown	unknown	gnl\|CDD\|234687
NZ_CP024592.1\|WP_143733577.1\|2166541_2166703_+\|DUF1661-domain-containing-protein	unknown	unknown	gnl\|CDD\|285160
NZ_CP024592.1\|WP_077094387.1\|2176386_2176968_+\|DUF3575-domain-containing-protein	unknown	unknown	gnl\|CDD\|371897
NZ_CP024592.1\|WP_077094380.1\|2153581_2155204_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	gnl\|CDD\|275036
NZ_CP024592.1\|WP_077082551.1\|2156146_2156707_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_157763414.1\|2155385_2155781_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP024592.1\|WP_099840837.1\|2168882_2169854_+\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP024592.1\|WP_004584668.1\|2159666_2161610_-\|thiamine-phosphate-synthase	unknown	unknown	gnl\|CDD\|280703
NZ_CP024592.1\|WP_099840838.1\|2172513_2173524_+\|type-I-glyceraldehyde-3-phosphate-dehydrogenase	unknown	unknown	gnl\|CDD\|177912
NZ_CP024592.1\|WP_077094386.1\|2174722_2175397_-\|YggS-family-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|143483
NZ_CP024592.1\|WP_077094385.1\|2173663_2174611_-\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|378964
NZ_CP024592.1\|WP_043898385.1\|2156901_2157585_+\|PorT-family-protein	unknown	unknown	gnl\|CDD\|372635
NZ_CP024592.1\|WP_023846862.1\|2161606_2163370_-\|phosphomethylpyrimidine-synthase-ThiC	unknown	unknown	gnl\|CDD\|236451
NZ_CP024592.1\|WP_021663757.1\|2170834_2171914_-\|asparaginase	unknown	unknown	gnl\|CDD\|214873

Protein	Function_ID	Function_description	E-value
NZ_CP024592.1\|WP_077094379.1\|2151226_2152816_-\|T9SS-type-A-sorting-domain-containing-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.	1.15279e-11
NZ_CP024592.1\|WP_077094381.1\|2157703_2158816_-\|2-iminoacetate-synthase-ThiH	gnl\|CDD\|131404	TIGR02351, ThiH_protein, thiazole biosynthesis protein ThiH. Members this protein family are the ThiH protein of thiamine biosynthesis, a homolog of the BioB protein of biotin biosynthesis. Genes for the this protein generally are found in operons with other thiamin biosynthesis genes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine].	0
NZ_CP024592.1\|WP_005873709.1\|2169972_2170782_-\|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.	4.97043e-40
NZ_CP024592.1\|WP_021678830.1\|2167519_2168098_-\|30S-ribosomal-protein-S16	gnl\|CDD\|237744	PRK14521, rpsP, 30S ribosomal protein S16; Provisional.	2.86457e-73
NZ_CP024592.1\|WP_004584649.1\|2175393_2175837_-\|DUF4494-domain-containing-protein	gnl\|CDD\|379718	pfam14902, DUF4494, Domain of unknown function (DUF4494). This family of proteins is found in bacteria. Proteins in this family are typically between 154 and 172 amino acids in length. There are two conserved sequence motifs: VDA and EAE. There is a single completely conserved residue E that may be functionally important.	1.3233e-68
NZ_CP024592.1\|WP_023846863.1\|2163439_2163640_-\|sulfur-carrier-protein-ThiS	gnl\|CDD\|273754	TIGR01683, thiamine_biosynthesis_protein_ThiS, thiamine biosynthesis protein ThiS. This model represents ThiS, a small, ubiquitin-like thiamine biosynthesis protein related to MoaD, a molybdenum cofactor biosynthesis protein. Both proteins are involved in sulfur transfer. ThiS has a conserved Gly-Gly C-terminus that is modified, in reactions requiring ThiI, ThiF, IscS, and a sulfur atom from Cys, into the thiocarboxylate that provides the sulfur for thiazole biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine].	1.12281e-20
NZ_CP024592.1\|WP_004584669.1\|2158828_2159608_-\|thiazole-synthase	gnl\|CDD\|234687	PRK00208, thiG, thiazole synthase; Reviewed.	6.97979e-152
NZ_CP024592.1\|WP_143733577.1\|2166541_2166703_+\|DUF1661-domain-containing-protein	gnl\|CDD\|285160	pfam07877, DUF1661, Protein of unknown function (DUF1661). This is a family containing bacterial proteins of unknown function. Many of the proteins in this family are hypothetical.	1.30863e-05
NZ_CP024592.1\|WP_077094380.1\|2153581_2155204_-\|T9SS-type-A-sorting-domain-containing-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.	1.26346e-10
NZ_CP024592.1\|WP_077094387.1\|2176386_2176968_+\|DUF3575-domain-containing-protein	gnl\|CDD\|371897	pfam12099, DUF3575, Protein of unknown function (DUF3575). This family of proteins are functionally uncharacterized. This family is only found in bacteria. Proteins in this family are typically between 187 to 236 amino acids in length.	1.51247e-95
NZ_CP024592.1\|WP_099840837.1\|2168882_2169854_+\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	2.51976e-31
NZ_CP024592.1\|WP_004584668.1\|2159666_2161610_-\|thiamine-phosphate-synthase	gnl\|CDD\|280703	pfam02581, TMP-TENI, Thiamine monophosphate synthase. Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes 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. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.	1.4624e-66
NZ_CP024592.1\|WP_099840838.1\|2172513_2173524_+\|type-I-glyceraldehyde-3-phosphate-dehydrogenase	gnl\|CDD\|177912	PLN02272, PLN02272, glyceraldehyde-3-phosphate dehydrogenase.	0
NZ_CP024592.1\|WP_077094386.1\|2174722_2175397_-\|YggS-family-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|143483	cd00635, PLPDE_III_YBL036c_like, Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins. This family contains mostly uncharacterized proteins, widely distributed among eukaryotes, bacteria and archaea, that bear similarity to the yeast hypothetical protein YBL036c, which is homologous to a Pseudomonas aeruginosa gene that is co-transcribed with a known proline biosynthetic gene. YBL036c is a single domain monomeric protein with a typical TIM barrel fold. It binds the PLP cofactor and has been shown to exhibit amino acid racemase activity. The YBL036c structure is similar to the N-terminal domain of the fold type III PLP-dependent enzymes, bacterial alanine racemase and eukaryotic ornithine decarboxylase, which are two-domain dimeric proteins. The lack of a second domain in YBL036c may explain limited D- to L-alanine racemase or non-specific racemase activity.	1.82325e-103
NZ_CP024592.1\|WP_077094385.1\|2173663_2174611_-\|AraC-family-transcriptional-regulator	gnl\|CDD\|378964	pfam12833, HTH_18, Helix-turn-helix domain.	5.82627e-19
NZ_CP024592.1\|WP_043898385.1\|2156901_2157585_+\|PorT-family-protein	gnl\|CDD\|372635	pfam13568, OMP_b-brl_2, Outer membrane protein beta-barrel domain. This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.	3.50265e-14
NZ_CP024592.1\|WP_023846862.1\|2161606_2163370_-\|phosphomethylpyrimidine-synthase-ThiC	gnl\|CDD\|236451	PRK09284, PRK09284, thiamine biosynthesis protein ThiC; Provisional.	0
NZ_CP024592.1\|WP_021663757.1\|2170834_2171914_-\|asparaginase	gnl\|CDD\|214873	smart00870, Asparaginase, Asparaginase, found in various plant, animal and bacterial cells. Asparaginase catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma..- if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die.	1.52643e-126

>NZ_CP024592.1|WP_023846863.1|2163439_2163640_-|sulfur-carrier-protein-ThiS
MQVTINNQPITCPEGMGLATLLEAERIQVDRTAIAVNGEVVPRASWADFRLSEDDEILIIQATYGG
>NZ_CP024592.1|WP_023846862.1|2161606_2163370_-|phosphomethylpyrimidine-synthase-ThiC
MKEFKVTTGPLPGSEKIYVEGERFPFLRVPMRRIRMSDTILENGECEKNEDVVVYDTSGPYTDTSYEVNLHRGVPKIREQWIEDRGDTVRLEGLSSEYGRIRQSDASLEKLRYEHVCTRPRAAKDGCATQLYYARQGIVTPEMEFVAIRENQLIDQVRTRYRAEEGEPLGAVIPRKITPEFVRDEIAAGRAILPANINHPESEPMIIGRNFLVKINANIGNSPISSTIEEEVEKAVWSIRWGADTVMDLSTGDHIHETREWIIRNSPVPIGTVPLYQTLEKVQGDVTKLNWEIFRDTLIEQAEQGVDYFTIHAGLRWHHVPLTLRRLTGIVSRGGSIIANWCTTHKRESFIYEHFEEICQILARYDVAISLGDGLRPGCIHDANDAAQIAELKTLGELTEIAWKYNVQTIIEGPGHVPMHKIRENMEIQLEACHGAPFYTLGPLVSDVAAGYDHITSAIGAAQIGWFGTAMLCYVTQKEHLGLPNREDVREGVVTYRLAAHAADLAKGHPTAYWRDYMMSKARFEFRWKDQFHLSLDPEKAIQFHDATLPDEGHKEAHFCSMCGEHFCSMRANKNFRKLLNEEAVSK
>NZ_CP024592.1|WP_004584668.1|2159666_2161610_-|thiamine-phosphate-synthase
MKPWLITPERLTSEQIGLLDYFFDRGLERLHLRLPGAGEEDYSQVIEAVAACYRRRVVVHDHPRLVGRYGLCGLHLPEQVWKGMTDRPQLPDGCTVSASCHTIGDIESFPFRIDYCFLSPIFDSLCKVGYAGRFSPDSLGDRLQRLHLPVVALGGITPDRLPQLRRAGFASAAALGYVWLVEGRELMRWQELCTPAVICVGGVDPSAGAGITADVRTAENMGVRAYTVATAITFQGSGSYRGERWLDPADIIRQIETLSAEMEPAVAKIGLIRDSDTLSFVVDCLKKVFPSIRIVWDPVLRASADSSAGQADRFNLEDITALSRIDFITPNLPEARHLLGCEPDDETLLDFYRRSGVGLVLKGGHAGESVVTDRIVYDDRCEALRLLRGGTEKHGTGCAHSTAFAAALALEQEPFTAAGMAQLYVSRLRERASGLLAMHKDLPVDPVVRLMSEIDLQFITHRQPDLSELEEAEAVCRMGVRWVQLRMKEASDEEMLRTACAVKAVCRHYGSLFVVNDRVEIARQVDADGVHLGKEDMAIVEARRILGSNKIIGLTCNTMEDVRRAYAEGADYVGIGPYRYTETKQRLAPVLGLEGYKAIAACMQTEGIRLPAFAIGGIEDADIPLIRDCGIGGIAVSGSLIRKIKKN
>NZ_CP024592.1|WP_004584669.1|2158828_2159608_-|thiazole-synthase
MEMLQIAGKTFESRLFVGTGKFASSDLMEAAVLASQSRMVTVALKRVEIGRGEEDDIISRIVRHPEITLLPNTSGVRSAKEAILAAELAREALQTNWLKLEVHPDPRYLLPDPIETLRATEELVRRGFIVLPYVQADPVLCKHLEEAGAATVMPLGAPIGSNRGLKTREMIRIIIEQSRVPVVIDAGIGAPSQAAEAMEMGADAVLVNTAIAVAEDPVSMATAFRLAVEAGRMAFEAKLGSVRSEAEASSPFTSFLNLK
>NZ_CP024592.1|WP_077094381.1|2157703_2158816_-|2-iminoacetate-synthase-ThiH
MTFYDHLHASPYTWERVGNLLADTTAADVERSLAHRRRTIQDFITLISPAAIPYLEQMALQAHTLTVERFGRTMQLYIPLYLSNICSNACVYCGFSRSNKIHRRRLTAEEVDREAEAILRLGYKHLLLVSGESEKATPASYYEEMTRRLRPLFSQLSLEVQPLTTEEYARLHEAGIGAVYVYQETYNEQAYPTYHPAGRKADYRYRLETPDRIGRANMQKIGIGALLGLENWRVDSVFTALHLRYLEQTYWKSKFSISLPRLRPATGGWEPKDPIDDVGMVQLITAFRLLDKDVEISLSTRESREFRDHVMPLGITSVSAGSKTEPGGYAEENADLEQFAINDARSPAEMAADLRRLGYEPVWKDWDAFM
>NZ_CP024592.1|WP_043898385.1|2156901_2157585_+|PorT-family-protein
MKMKKMILIAAMILAAVGALSAQGRIAFRADAAVGFSTGDYKVESIGDLTGKSIVGYRISGGLDIPIGYGLYVNPSLAFHSKGMKTNLEGVALGALGLNSSLKVKTHYIEIPVHLGYRLSLLNLVSVAVQAGPYFSYAIKGDGTVVRKDGQETTFDIYKDGLKEMINAKRFDVGLGAAAMVGYSNFYLLIGADFGLINTVKDIKPETKNLEATLKNTSFHVGLGIRL
>NZ_CP024592.1|WP_077082551.1|2156146_2156707_+|hypothetical-protein
MEFWLIFAGTFTKKRTNMRMMKLTAMMLALLSALAFSSCKKDEPTTLEKTQWERMLTGAEINKIIALMDGEIDADSQLPESAKLKLELDFFSQTDANLNVDIMITPGITIKMKMKMPYMYNASTKSVLLRLSKSQVLSVEPMFPAFEGIDLSEAEDVTGVVDWKNKTMKLTMQGENHPVHIELTQK
>NZ_CP024592.1|WP_157763414.1|2155385_2155781_-|hypothetical-protein
MRKTSLLFFFSCFFRPPWSEHSASLSDSELADLFSLQKDTSPRSKKTSEKSFLALVLVISSLLVFYAFFLCAICPKRRCFLLSPYCQMRDLSKKMRDLSKYISSPLRSFVAEKAEHAFRVVRIADFDFGHS
>NZ_CP024592.1|WP_077094380.1|2153581_2155204_-|T9SS-type-A-sorting-domain-containing-protein
MKTKVLRKFVVAAFAVATLCPLAQAQTMGGDDVKVVQYNQEKLVQTRMSVADNGWIYVMTHSGYDTGNSNVKIFRSKDQGATYQKLRDWDPSDDYQFQDFDIVVTGKNESDIKIWSVELMNKPGGYKSRVAVFSRDANAQNAKLVYKEDFSNVQLYDVDIASNYRSPSSHNNGGNPFALAFAYTGFNNTHKISFVDYVFSLNGGQDFNKNLLFSQDGEKKIDKVDLSLGSTSGSMGHNAWPLMGVVFEMNKQGGKSDIGFLSNFVDNDPEFQWSGPIKVSENDMSFDPKIQMLLDEDNNTINGESCHNFMITYSNYDSEYSDWDIRYVYPKKSFKYEKGKTPTMDDLVEGFLTASYQSETNSGLGYDKNANHYLITYAKKEENGTNTLKYCWANYDKIHNKGLWSDTFTYTSSANALYTPQVDINPTKGLVCWSWVEYLPGKRIVWSDTQWTHANGVEDIVMQEGNMKLYPNPAQEYAVISLPTAANCKAVVYDMQGRVVAEASFSGNEYRLNVQHLAKGTYMLKVVSDTERFVEKLIVE
>NZ_CP024592.1|WP_077094379.1|2151226_2152816_-|T9SS-type-A-sorting-domain-containing-protein
MKTKALLKFIVAVFAAAICSPQLTQAQAMGGDDVLISSFSAMQPEGESRLAVADNGWIYVMAHYKDGTDTQVKIFRSVDGGATYQQLKHWYPEGGYQYADFDIVVTGKNASDIRVWSVELLVKDSDSKVVIFRRDADMANSARIYDETLPNVELYDVAMASNYRAPSPTGAGGNPFALGIAVCGYNKAASPKHSFLDYIFSLDGGATFTKSRVYTQNGTRQIKDVDISIGSTTGDLLNTWPIMGIVFAKDDYSSVGFISNFVDNDPGFAWSSPITLAASGNLSRPRIQMMLDHDSENTIGGKSCHNFMIVYETQNTIKYAYPKESFGYLSEPSVDDLTVTTLVSNARYPALSYDKVGNHYLFTYATEEDGVRKLKYQWAQYDNLHKPDTWSTKYVYASEDNDNYYFTQPLVDIDPSKLKACWIWFIESQGGCDLWGDTEWVHANGVEDIVMQEGSMKLYPNPAQEYAVISLPTAANCKAVVYDMQGRVVAEASFSGNEYRLNVQHLAKGTYMLKVVSDTERFVEKLIVE
>NZ_CP024592.1|WP_143733577.1|2166541_2166703_+|DUF1661-domain-containing-protein
MTLLKTWRGNFLVLARKAKNSHATTKKISFHFFRKFKPKPVHFWFGPMNLDVY
>NZ_CP024592.1|WP_021678830.1|2167519_2168098_-|30S-ribosomal-protein-S16
MATKIRLQRHGRKGYAFYKIVVADSRAPRDGKFIERIGSYNPNTNPATIDLNFERALYWIGVGAQPTDTARNILSREGVLMMKHLLGGVKKGAFDQAAAESKFEAWLKGKKDALNNMKAKVKEAAVADNKVKLEAEKAVNKARAEAVAEKKATEAKAKAEAEAAAAAEEAAETEETPVEAAAEEAPAAESAE
>NZ_CP024592.1|WP_099840837.1|2168882_2169854_+|Gfo/Idh/MocA-family-oxidoreductase
MHNFAIIGVAGYIAPRHLRAIKDTGNRLVSAMDKFDSVGIMDSYFQKAAFFTEQELFDRHNSKLRGTDQAIDHVSVCTPNYLHDAHCRYGLRLGADVICEKPLVLNPWNIDALQEIEQETGHRIYNILQLRLHESIVALKRKIESGPADKIYDVTLTYITSRGNWYYTSWKGDERKSGGIATNIGVHFYDMLSWIFGSVRHNVVHVCVHDRAAGYLELERARVRYFLSINEELLPENAVQGEKRTFRTIEIDGESFEFSEGFTELHTESYRRILAGEGFGLDEARNSIQIVHDIRNASPVGLKGEYHPFARLPLASHPFGWRR
>NZ_CP024592.1|WP_005873709.1|2169972_2170782_-|MBL-fold-metallo-hydrolase
MIKFMSIASGSSGNCYYLSNGNQALLIDAGIPLRSISKALKDHQLPIEGNVVGVLVTHDHADHIRTIGCLGEKFHLPVFATERVHNGINSSRYMDHLPLLSRRNILQEETFRLAGFDITAFPIPHDATENVGYHITAPGFSFTLCTDVGHITDTISHYASKADYLVMEANYDCEMLLSGPYPEFLKERVSGPNGHLSNQETGDFLARTFHPGMKHVWLCHLSKDNNHPDLCWKSIEYRLFSEGIRVGKDMELTVLKRTSPSSLYTLLED
>NZ_CP024592.1|WP_021663757.1|2170834_2171914_-|asparaginase
MQTKSASGRSAILLIYTGGTIGMIENPETKVLEAFDFKYLETNVPELKNFGFKIDSIQFDPPIDSAAISPDLWVRLADTIRENYRAYDGFVILHGTDTMAYTASALSFMLDDLQKPVILTGSQLPIGTLRTDGKENLITAIEIAAAKQNGYARVPEVCIFFDNYLMRGNRTSKVSADQFDAFASYNFSPLAYAGIDIRYEDALIADRGADAALSVQTEMDRNVVILKIFPGITREVVESILGIPSLKGVVLETYGSGNAPMEPWFLNALEKAVQRGIVIVNVTQCVSGYVDMHRYETGHQLENIGLISGYDSTTECAIIKLMYLFGRGYTPERVKAEMKRSLKGEISVGEGYENNKCRC
>NZ_CP024592.1|WP_099840838.1|2172513_2173524_+|type-I-glyceraldehyde-3-phosphate-dehydrogenase
MTKVGINGFGRIGRLVFRAAQTQNRSDIEIVAINDLIDVEYMAYMLKYDSVHGRFNGTVEVKDGQLIVNGKAIRVTAEKNPADLKWDQVGVEYVVESTGLFLTKEKSEAHLAAGAKYVVMSAPSKDDTPMFVCGVNTDKYVKGTKIVSNASCTTNCLAPIAKVLNDNWGMVGGLMTTVHATTATQKTVDGPSAKDWRGGRAAGGNIIPSSTGAAKAVGKVIPELNGKLTGMSFRVPTLDVSVVDLTCQLAKPAKYEDICAAMKKTSEGELKGILGYTDEEVVSSDFIGETRTSVFDAKAGIALTDTFVKIVSWYDNEIGYSNKVLDLIAYMAKVNA
>NZ_CP024592.1|WP_077094385.1|2173663_2174611_-|AraC-family-transcriptional-regulator
MDSMQFPISKFSFMTIPLKVFSINELAGYLGGKMNTLGDRVLLCNDKRSLPAAAVATPFLFESMLFSVCTRGYARLLIDSREIEVKEGELLVVMPRKTIEVIESSCFRAFHLCLDKEILALSAIRISGFISIINKLHSNEPFRPERMEKDFLTATLDLIRNTLQNGGRHQEEIVIYLISSLFLFLDDMIADEAEKDCKHTRSETICRDFLLLVSEHHKEQHTVKFYADRLCLSSKHLALTIKTVMGQSASKVINSFIIQQAKSLLRYTDKTVQEIGYELNFSTQSFFGKYFKQHTGMSPGEYRSQEARNRHSEES
>NZ_CP024592.1|WP_077094386.1|2174722_2175397_-|YggS-family-pyridoxal-phosphate-dependent-enzyme
MTLIAERLVPILRSLPQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKMEAMPDDVEWHFIGPLQTNKVKYIVPFISMIQSVSSLKLFDEISRQASKAGRTVPVLLEVYIASEDTKSGFTPEELPQVLEAVLARGSDTGVKIAGLMGMATFTDDREQIRREFRRLASLFREMKERFFSDSADFCELSMGMSGDFELAIEEGSTIVRIGTTIFGERRY
>NZ_CP024592.1|WP_004584649.1|2175393_2175837_-|DUF4494-domain-containing-protein
MAAWFECKVTYEKVADNGMPKKVVESYLVDADSFTLAEAKMIEEITPFVSMGEFNISNIRKVNYAELFLNEDDKCDRYYRCKVLYVTIDEKNGVEKKTPAFMLVKSDSLPNAVAELEKQMGKGLADYEIASVAETALMDVFQYVPAQ
>NZ_CP024592.1|WP_077094387.1|2176386_2176968_+|DUF3575-domain-containing-protein
MKRKIRLLIIGIILFAGLIPTLRAQQIGLKTNLLYWGTTTPNAGLEFRMGKKWTLDVSGGYNPFTFSHHRKLKHWLVAPELRYWTCEAFSGHFFGLHGIGGEYNVNDIDIPIGRLKKLNNYRYEGYAIGAGLTYGYQWLLGKRWNLEASISGGFVRFDYDKFECAKCGKKIAEGKYDYFGVTKATLSLIYIIK

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP024592_1	1.1\|95335\|37\|NZ_CP024592\|CRISPRCasFinder	95335-95371	37	NZ_CP024592.1	1083842-1083878	0	1.0
NZ_CP024592_8	8.1\|1976967\|34\|NZ_CP024592\|CRISPRCasFinder	1976967-1977000	34	NZ_CP024592.1	266102-266135	0	1.0
NZ_CP024592_2	2.7\|118531\|36\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	118531-118566	36	NZ_CP024592.1	1420697-1420732	2	0.944

1. spacer 1.1|95335|37|NZ_CP024592|CRISPRCasFinder matches to position: 1083842-1083878, mismatch: 0, identity: 1.0

tttgcaagggaaaacgcagcggcagccaagcggtcga	CRISPR spacer
tttgcaagggaaaacgcagcggcagccaagcggtcga	Protospacer
*************************************

2. spacer 8.1|1976967|34|NZ_CP024592|CRISPRCasFinder matches to position: 266102-266135, mismatch: 0, identity: 1.0

cgtcctcggtgtcacggggagtatcgcagcctac	CRISPR spacer
cgtcctcggtgtcacggggagtatcgcagcctac	Protospacer
**********************************

3. spacer 2.7|118531|36|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to position: 1420697-1420732, mismatch: 2, identity: 0.944

aaccttgacagttcgacaggtatgtaattgatacaa	CRISPR spacer
aacattgacagttcgacaggtctgtaattgatacaa	Protospacer
*** ***************** **************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NC_022111	Prevotella sp. oral taxon 299 str. F0039 plasmid, complete sequence	190899-190928	4	0.867
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NC_006297	Bacteroides fragilis YCH46 plasmid pBFY46, complete sequence	9030-9059	5	0.833
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	NC_010418	Clostridium botulinum A3 str. Loch Maree plasmid pCLK, complete sequence	187296-187325	6	0.8
NZ_CP024592_7	7.1\|1749859\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749859-1749888	30	MW149103	Microvirus sp. isolate gila14, complete genome	608-637	6	0.8
NZ_CP024592_7	7.2\|1749935\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749935-1749964	30	MN234174	Mycobacterium phage Efra2, complete genome	39486-39515	6	0.8
NZ_CP024592_7	7.2\|1749935\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749935-1749964	30	MN234165	Mycobacterium phage Yunkel11, complete genome	39226-39255	6	0.8
NZ_CP024592_7	7.2\|1749935\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749935-1749964	30	MN234201	Mycobacterium phage Guanica15, complete genome	39227-39256	6	0.8
NZ_CP024592_7	7.4\|1750087\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750087-1750116	30	NZ_CP045419	Pseudoalteromonas sp. THAF3 plasmid pTHAF3_a, complete sequence	10580-10609	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP010616	Phaeobacter inhibens strain P92 plasmid pP92_f, complete sequence	6501-6530	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP010635	Phaeobacter inhibens strain P78 plasmid pP78_f, complete sequence	6501-6530	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP041231	Bacteroides xylanisolvens strain H207 plasmid unnamed1, complete sequence	37315-37344	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP041397	Bacteroides ovatus strain 3725 D1 iv plasmid unnamed2, complete sequence	30229-30258	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP054001	Bacteroides fragilis strain FDAARGOS_763 plasmid unnamed1, complete sequence	50001-50030	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP010755	Phaeobacter inhibens strain P70 plasmid pP70_f, complete sequence	6501-6530	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP010713	Phaeobacter inhibens strain P66 plasmid pP66_h, complete sequence	6500-6529	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP032820	Butyricimonas faecalis strain H184 plasmid unnamed, complete sequence	37274-37303	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP010740	Phaeobacter inhibens strain P72 plasmid pP72_e, complete sequence	6501-6530	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP018939	Bacteroides fragilis strain Q1F2 plasmid Q1F2-p2, complete sequence	16666-16695	6	0.8
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP018939	Bacteroides fragilis strain Q1F2 plasmid Q1F2-p2, complete sequence	58867-58896	6	0.8
NZ_CP024592_4	4.1\|453790\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453790-453819	30	NZ_CP012100	Bacillus thuringiensis strain HS18-1 plasmid pHS18-1, complete sequence	60007-60036	7	0.767
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	KU645528	Acidianus tailed spindle virus isolate 1, complete genome	51767-51796	7	0.767
NZ_CP024592_4	4.5\|454054\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	454054-454083	30	NZ_CP014853	Bacillus thuringiensis strain HD12 plasmid pHD120345, complete sequence	159456-159485	7	0.767
NZ_CP024592_4	4.5\|454054\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	454054-454083	30	NZ_CP010090	Bacillus thuringiensis serovar galleriae strain 4G5 plasmid pBMB426, complete sequence	162120-162149	7	0.767
NZ_CP024592_4	4.6\|454120\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	454120-454149	30	MN855765	Myoviridae sp. isolate 14, complete genome	30509-30538	7	0.767
NZ_CP024592_7	7.1\|1749859\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749859-1749888	30	NZ_CP016791	Bacillus flexus strain KLBMP 4941 plasmid unnamed1, complete sequence	50576-50605	7	0.767
NZ_CP024592_7	7.1\|1749859\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749859-1749888	30	NC_022111	Prevotella sp. oral taxon 299 str. F0039 plasmid, complete sequence	1212294-1212323	7	0.767
NZ_CP024592_7	7.4\|1750087\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750087-1750116	30	NZ_CP022523	Pseudoalteromonas sp. NC201 plasmid pNC201, complete sequence	1033547-1033576	7	0.767
NZ_CP024592_7	7.7\|1750315\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750315-1750344	30	NZ_LR215032	Mycoplasma gallopavonis strain NCTC10186 plasmid 2	218367-218396	7	0.767
NZ_CP024592_7	7.10\|1750543\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750543-1750572	30	NZ_CP022991	Paraburkholderia aromaticivorans strain BN5 plasmid pBN1, complete sequence	438507-438536	7	0.767
NZ_CP024592_4	4.1\|453790\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453790-453819	30	MT430910	Streptococcus phage smHBZ8, complete genome	9000-9029	8	0.733
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	MN694120	Marine virus AFVG_250M1160, complete genome	33639-33668	8	0.733
NZ_CP024592_4	4.5\|454054\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	454054-454083	30	NZ_CP039041	Piscirickettsia salmonis strain Psal-072 plasmid unnamed1, complete sequence	60135-60164	8	0.733
NZ_CP024592_4	4.5\|454054\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	454054-454083	30	NZ_CP039048	Piscirickettsia salmonis strain Psal-073 plasmid unnamed2, complete sequence	101186-101215	8	0.733
NZ_CP024592_7	7.1\|1749859\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749859-1749888	30	NZ_CP021876	Enterococcus wangshanyuanii strain MN05 plasmid unnamed3	25691-25720	8	0.733
NZ_CP024592_7	7.1\|1749859\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749859-1749888	30	HG531805	Clostridium phage CDMH1 complete genome	8174-8203	8	0.733
NZ_CP024592_7	7.1\|1749859\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749859-1749888	30	NZ_CP021875	Enterococcus wangshanyuanii strain MN05 plasmid unnamed2	10859-10888	8	0.733
NZ_CP024592_7	7.2\|1749935\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1749935-1749964	30	MK279857	Mycobacterium phage IronMan, complete genome	20255-20284	8	0.733
NZ_CP024592_7	7.7\|1750315\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750315-1750344	30	MN101223	Klebsiella phage KOX10, complete genome	113124-113153	8	0.733
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NC_003527	Bifidobacterium pseudocatenulatum plasmid p4M, complete sequence	112-141	8	0.733
NZ_CP024592_7	7.12\|1750695\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750695-1750724	30	NZ_CP041205	Rhizobium sp. NIBRBAC000502774 plasmid pMK-2, complete sequence	69091-69120	8	0.733
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	NZ_CP045273	Bacillus megaterium strain FDU301 plasmid pFDU301A, complete sequence	1009637-1009666	9	0.7
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	NC_003042	Clostridium perfringens str. 13 plasmid pCP13, complete sequence	42737-42766	9	0.7
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	NZ_CP015809	Borrelia mayonii strain MN14-1539 plasmid lp54	31439-31468	9	0.7
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	NZ_CP015795	Borrelia mayonii strain MN14-1420 plasmid lp54, complete sequence	31455-31484	9	0.7
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	NC_023917	Clostridium perfringens plasmid pCP-OS1 DNA, complete sequence, strain: OS1	42958-42987	9	0.7
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	NC_023918	Clostridium perfringens plasmid pCP-TS1 DNA, complete sequence, strain: TS1	42940-42969	9	0.7
NZ_CP024592_4	4.4\|453988\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453988-454017	30	NZ_MK275619	Clostridium perfringens strain JXJA17 plasmid p1, complete sequence	20069-20098	9	0.7
NZ_CP024592_7	7.6\|1750239\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750239-1750268	30	NZ_CP032328	Azospirillum brasilense strain MTCC4035 plasmid p7, complete sequence	133967-133996	9	0.7
NZ_CP024592_7	7.6\|1750239\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750239-1750268	30	NZ_CP032342	Azospirillum brasilense strain MTCC4038 plasmid p3, complete sequence	489561-489590	9	0.7
NZ_CP024592_7	7.6\|1750239\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750239-1750268	30	NZ_CP033321	Azospirillum brasilense strain Cd plasmid p3, complete sequence	275319-275348	9	0.7
NZ_CP024592_7	7.6\|1750239\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750239-1750268	30	NZ_CP033315	Azospirillum brasilense strain Sp 7 plasmid p3, complete sequence	244899-244928	9	0.7
NZ_CP024592_7	7.9\|1750467\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750467-1750496	30	NZ_CP050098	Rhizobium leguminosarum bv. trifolii strain 9B plasmid pRL9b4, complete sequence	582133-582162	9	0.7
NZ_CP024592_7	7.9\|1750467\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder	1750467-1750496	30	NZ_CP053440	Rhizobium leguminosarum bv. trifolii strain CC275e plasmid pRltCC275eF, complete sequence	653497-653526	9	0.7
NZ_CP024592_4	4.3\|453922\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453922-453951	30	NC_014549	Glutamicibacter arilaitensis Re117 plasmid pRE117-1, complete sequence	27547-27576	10	0.667
NZ_CP024592_4	4.3\|453922\|30\|NZ_CP024592\|PILER-CR,CRISPRCasFinder,CRT	453922-453951	30	NC_001415	Corynebacterium glutamicum strain 22243 R-plasmid pAG1, complete sequence	10722-10751	10	0.667

1. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NC_022111 (Prevotella sp. oral taxon 299 str. F0039 plasmid, complete sequence) position: , mismatch: 4, identity: 0.867

aatggctttccacgcttcctcaattacgag	CRISPR spacer
aatggctttccacgcttcctcaatgagtat	Protospacer
************************ *  *

2. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NC_006297 (Bacteroides fragilis YCH46 plasmid pBFY46, complete sequence) position: , mismatch: 5, identity: 0.833

aatggctttccacgcttcctcaattacgag	CRISPR spacer
aattgctttccatgcttcctcaataataag	Protospacer
*** ********.*********** *..**

3. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NC_010418 (Clostridium botulinum A3 str. Loch Maree plasmid pCLK, complete sequence) position: , mismatch: 6, identity: 0.8

-----cctttgatttgaagaaatctttaatagaag	CRISPR spacer
gagttcctttgat-----gaaatctttaataaaag	Protospacer
     ********     *************.***

4. spacer 7.1|1749859|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to MW149103 (Microvirus sp. isolate gila14, complete genome) position: , mismatch: 6, identity: 0.8

aagttttttctcttttagcttatccgtatc	CRISPR spacer
atgtttttcctcttttagcttatcagaaaa	Protospacer
* ******.*************** * *

5. spacer 7.2|1749935|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to MN234174 (Mycobacterium phage Efra2, complete genome) position: , mismatch: 6, identity: 0.8

ccgcttcagctcgttggtgtcgactgtttc	CRISPR spacer
ccgcgtctgctcgttggtgtcgaggcattc	Protospacer
**** ** ***************    ***

6. spacer 7.2|1749935|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to MN234165 (Mycobacterium phage Yunkel11, complete genome) position: , mismatch: 6, identity: 0.8

ccgcttcagctcgttggtgtcgactgtttc	CRISPR spacer
ccgcgtctgctcgttggtgtcgaggcattc	Protospacer
**** ** ***************    ***

7. spacer 7.2|1749935|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to MN234201 (Mycobacterium phage Guanica15, complete genome) position: , mismatch: 6, identity: 0.8

ccgcttcagctcgttggtgtcgactgtttc	CRISPR spacer
ccgcgtctgctcgttggtgtcgaggcattc	Protospacer
**** ** ***************    ***

8. spacer 7.4|1750087|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP045419 (Pseudoalteromonas sp. THAF3 plasmid pTHAF3_a, complete sequence) position: , mismatch: 6, identity: 0.8

gcctatcacagcaatgatgccaaagaccag	CRISPR spacer
cgctatgacagcaatgatgccaaagatgac	Protospacer
  **** *******************. *

9. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP010616 (Phaeobacter inhibens strain P92 plasmid pP92_f, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
gagagctttccacgcttcatcaatgacgat	Protospacer
.* .************** ***** ****

10. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP010635 (Phaeobacter inhibens strain P78 plasmid pP78_f, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
gagagctttccacgcttcatcaatgacgat	Protospacer
.* .************** ***** ****

11. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP041231 (Bacteroides xylanisolvens strain H207 plasmid unnamed1, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
tatggctttccatgcttcttcaattattaa	Protospacer
 ***********.*****.*******. *.

12. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP041397 (Bacteroides ovatus strain 3725 D1 iv plasmid unnamed2, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
tatggctttccatgcttcttcaattattaa	Protospacer
 ***********.*****.*******. *.

13. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP054001 (Bacteroides fragilis strain FDAARGOS_763 plasmid unnamed1, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
tatggctttccatgcttcttcaattattaa	Protospacer
 ***********.*****.*******. *.

14. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP010755 (Phaeobacter inhibens strain P70 plasmid pP70_f, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
gagagctttccacgcttcatcaatgacgat	Protospacer
.* .************** ***** ****

15. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP010713 (Phaeobacter inhibens strain P66 plasmid pP66_h, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
gagagctttccacgcttcatcaatgacgat	Protospacer
.* .************** ***** ****

16. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP032820 (Butyricimonas faecalis strain H184 plasmid unnamed, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
tatggctttccatgcttcttcaattattaa	Protospacer
 ***********.*****.*******. *.

17. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP010740 (Phaeobacter inhibens strain P72 plasmid pP72_e, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
gagagctttccacgcttcatcaatgacgat	Protospacer
.* .************** ***** ****

18. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP018939 (Bacteroides fragilis strain Q1F2 plasmid Q1F2-p2, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
tatggctttccatgcttcttcaattattaa	Protospacer
 ***********.*****.*******. *.

19. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP018939 (Bacteroides fragilis strain Q1F2 plasmid Q1F2-p2, complete sequence) position: , mismatch: 6, identity: 0.8

aatggctttccacgcttcctcaattacgag	CRISPR spacer
tatggctttccatgcttcttcaattattaa	Protospacer
 ***********.*****.*******. *.

20. spacer 4.1|453790|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP012100 (Bacillus thuringiensis strain HS18-1 plasmid pHS18-1, complete sequence) position: , mismatch: 7, identity: 0.767

tcctccgccttcctttctattttcttctct	CRISPR spacer
tcatttaaattcctttctactttcttctct	Protospacer
** *...  **********.**********

21. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to KU645528 (Acidianus tailed spindle virus isolate 1, complete genome) position: , mismatch: 7, identity: 0.767

cctttgatttgaagaaatctttaatagaag	CRISPR spacer
tctttgagttgaagaattctttaatggttt	Protospacer
.****** ******** ********.*

22. spacer 4.5|454054|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP014853 (Bacillus thuringiensis strain HD12 plasmid pHD120345, complete sequence) position: , mismatch: 7, identity: 0.767

tttttagaagatttccaataaattgttttg	CRISPR spacer
gttttagattatttccaataaattgtgaaa	Protospacer
 *******  ****************   .

23. spacer 4.5|454054|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP010090 (Bacillus thuringiensis serovar galleriae strain 4G5 plasmid pBMB426, complete sequence) position: , mismatch: 7, identity: 0.767

tttttagaagatttccaataaattgttttg	CRISPR spacer
gttttagattatttccaataaattgtgaaa	Protospacer
 *******  ****************   .

24. spacer 4.6|454120|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to MN855765 (Myoviridae sp. isolate 14, complete genome) position: , mismatch: 7, identity: 0.767

tagtcaagcatcttgccaatcgtatcaact	CRISPR spacer
tcgtcaagcatcttgccaattgtttttaag	Protospacer
* ******************.** *. *

25. spacer 7.1|1749859|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP016791 (Bacillus flexus strain KLBMP 4941 plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.767

aagttttttctcttttagcttatccgtatc	CRISPR spacer
aagatttttatcttttagcttatcacaaga	Protospacer
*** ***** **************   *

26. spacer 7.1|1749859|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NC_022111 (Prevotella sp. oral taxon 299 str. F0039 plasmid, complete sequence) position: , mismatch: 7, identity: 0.767

aagttttttctcttttagcttatccgtatc	CRISPR spacer
gagctttttcccttttagcttatcgccatt	Protospacer
.**.******.*************  .**.

27. spacer 7.4|1750087|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP022523 (Pseudoalteromonas sp. NC201 plasmid pNC201, complete sequence) position: , mismatch: 7, identity: 0.767

gcctatcacagcaatgatgccaaagaccag	CRISPR spacer
cgctatgacagcaatgatgcgaaagatgat	Protospacer
  **** ************* *****. *

28. spacer 7.7|1750315|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_LR215032 (Mycoplasma gallopavonis strain NCTC10186 plasmid 2) position: , mismatch: 7, identity: 0.767

tggggaaagaatttctttgataattctctt	CRISPR spacer
ttaaataataatttcttagataattctctt	Protospacer
* ... ** ******** ************

29. spacer 7.10|1750543|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP022991 (Paraburkholderia aromaticivorans strain BN5 plasmid pBN1, complete sequence) position: , mismatch: 7, identity: 0.767

agtcgcgacgacacaaccatcctctcggct	CRISPR spacer
tttagcgacgacacaaccgtcctcttgatt	Protospacer
  * **************.******.*..*

30. spacer 4.1|453790|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to MT430910 (Streptococcus phage smHBZ8, complete genome) position: , mismatch: 8, identity: 0.733

tcctccgccttcctttctattttcttctct	CRISPR spacer
attgtctatttcctttctattttcttctct	Protospacer
 .. .*  .*********************

31. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to MN694120 (Marine virus AFVG_250M1160, complete genome) position: , mismatch: 8, identity: 0.733

cctttgatttgaagaaatctttaatagaag	CRISPR spacer
aactgtatatggagaaatctttaatagaat	Protospacer
  .*  ** **.*****************

32. spacer 4.5|454054|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP039041 (Piscirickettsia salmonis strain Psal-072 plasmid unnamed1, complete sequence) position: , mismatch: 8, identity: 0.733

tttttagaagatttccaataaattgttttg	CRISPR spacer
tttttataagatttccaataatctgcaact	Protospacer
****** ************** .**.  .

33. spacer 4.5|454054|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP039048 (Piscirickettsia salmonis strain Psal-073 plasmid unnamed2, complete sequence) position: , mismatch: 8, identity: 0.733

tttttagaagatttccaataaattgttttg	CRISPR spacer
tttttataagatttccaataatctgcaact	Protospacer
****** ************** .**.  .

34. spacer 7.1|1749859|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP021876 (Enterococcus wangshanyuanii strain MN05 plasmid unnamed3) position: , mismatch: 8, identity: 0.733

aagttttttctcttttagcttatccgtatc	CRISPR spacer
aagatttttcttttttagcttatattctgc	Protospacer
*** *******.*********** . .  *

35. spacer 7.1|1749859|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to HG531805 (Clostridium phage CDMH1 complete genome) position: , mismatch: 8, identity: 0.733

aagttttttctcttttagcttatccgtatc	CRISPR spacer
tagttttttctctattatcttatcaacttg	Protospacer
 ************ *** ****** .. *

36. spacer 7.1|1749859|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP021875 (Enterococcus wangshanyuanii strain MN05 plasmid unnamed2) position: , mismatch: 8, identity: 0.733

aagttttttctcttttagcttatccgtatc	CRISPR spacer
aagatttttcttttttagcttatattctgc	Protospacer
*** *******.*********** . .  *

37. spacer 7.2|1749935|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to MK279857 (Mycobacterium phage IronMan, complete genome) position: , mismatch: 8, identity: 0.733

ccgcttcagctcgttggtgtcgactgtttc	CRISPR spacer
ctgcttcagctcgtcggtgtcgataccggc	Protospacer
*.************.********.  .  *

38. spacer 7.7|1750315|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to MN101223 (Klebsiella phage KOX10, complete genome) position: , mismatch: 8, identity: 0.733

tggggaaagaatttctttgataattctctt	CRISPR spacer
gaaccaaataatttctttgatgattctcct	Protospacer
 ..  *** ************.******.*

39. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NC_003527 (Bifidobacterium pseudocatenulatum plasmid p4M, complete sequence) position: , mismatch: 8, identity: 0.733

aatggctttccacgcttcctcaattacgag	CRISPR spacer
catggctttccatgcttccttaatctcaga	Protospacer
 ***********.*******.***. *...

40. spacer 7.12|1750695|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP041205 (Rhizobium sp. NIBRBAC000502774 plasmid pMK-2, complete sequence) position: , mismatch: 8, identity: 0.733

aatggctttccacgcttcctcaattacgag	CRISPR spacer
gtgggctttccccgcctcctcaattatgga	Protospacer
.  ******** ***.**********.*..

41. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP045273 (Bacillus megaterium strain FDU301 plasmid pFDU301A, complete sequence) position: , mismatch: 9, identity: 0.7

cctttgatttgaagaaatctttaatagaag	CRISPR spacer
agaactatttgaagaaatctttaagagaca	Protospacer
    . ****************** *** .

42. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NC_003042 (Clostridium perfringens str. 13 plasmid pCP13, complete sequence) position: , mismatch: 9, identity: 0.7

cctttgatttgaagaaatctttaatagaag	CRISPR spacer
tatttgatttgaaaaaatcttttattagct	Protospacer
. ***********.******** ** ..

43. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP015809 (Borrelia mayonii strain MN14-1539 plasmid lp54) position: , mismatch: 9, identity: 0.7

cctttgatttgaagaaatctttaatagaag	CRISPR spacer
aattggattttaagaaatctttaatctctt	Protospacer
  ** ***** **************

44. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NZ_CP015795 (Borrelia mayonii strain MN14-1420 plasmid lp54, complete sequence) position: , mismatch: 9, identity: 0.7

cctttgatttgaagaaatctttaatagaag	CRISPR spacer
aattggattttaagaaatctttaatctctt	Protospacer
  ** ***** **************

45. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NC_023917 (Clostridium perfringens plasmid pCP-OS1 DNA, complete sequence, strain: OS1) position: , mismatch: 9, identity: 0.7

cctttgatttgaagaaatctttaatagaag	CRISPR spacer
tatttgatttgaaaaaatcttttattagct	Protospacer
. ***********.******** ** ..

46. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NC_023918 (Clostridium perfringens plasmid pCP-TS1 DNA, complete sequence, strain: TS1) position: , mismatch: 9, identity: 0.7

cctttgatttgaagaaatctttaatagaag	CRISPR spacer
tatttgatttgaaaaaatcttttattagct	Protospacer
. ***********.******** ** ..

47. spacer 4.4|453988|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NZ_MK275619 (Clostridium perfringens strain JXJA17 plasmid p1, complete sequence) position: , mismatch: 9, identity: 0.7

cctttgatttgaagaaatctttaatagaag	CRISPR spacer
tatttgatttgaaaaaatcttttattagct	Protospacer
. ***********.******** ** ..

48. spacer 7.6|1750239|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP032328 (Azospirillum brasilense strain MTCC4035 plasmid p7, complete sequence) position: , mismatch: 9, identity: 0.7

caataaatggatcaacaacgagcgttggga	CRISPR spacer
gtcgcgctggatcaaccgcgagcgttggga	Protospacer
     . ********* .************

49. spacer 7.6|1750239|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP032342 (Azospirillum brasilense strain MTCC4038 plasmid p3, complete sequence) position: , mismatch: 9, identity: 0.7

caataaatggatcaacaacgagcgttggga	CRISPR spacer
gtcgcgctggatcaaccgcgagcgttggga	Protospacer
     . ********* .************

50. spacer 7.6|1750239|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP033321 (Azospirillum brasilense strain Cd plasmid p3, complete sequence) position: , mismatch: 9, identity: 0.7

caataaatggatcaacaacgagcgttggga	CRISPR spacer
gtcgcgctggatcaaccgcgagcgttggga	Protospacer
     . ********* .************

51. spacer 7.6|1750239|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP033315 (Azospirillum brasilense strain Sp 7 plasmid p3, complete sequence) position: , mismatch: 9, identity: 0.7

caataaatggatcaacaacgagcgttggga	CRISPR spacer
gtcgcgctggatcaaccgcgagcgttggga	Protospacer
     . ********* .************

52. spacer 7.9|1750467|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP050098 (Rhizobium leguminosarum bv. trifolii strain 9B plasmid pRL9b4, complete sequence) position: , mismatch: 9, identity: 0.7

agccgtgaagttttacctcgcctgcggcct	CRISPR spacer
gcgtctgaagtcttacctcgccggcggcgg	Protospacer
.  . ******.********** *****

53. spacer 7.9|1750467|30|NZ_CP024592|PILER-CR,CRISPRCasFinder matches to NZ_CP053440 (Rhizobium leguminosarum bv. trifolii strain CC275e plasmid pRltCC275eF, complete sequence) position: , mismatch: 9, identity: 0.7

agccgtgaagttttacctcgcctgcggcct	CRISPR spacer
gcgtctgaagtcttacctcgccggcggcgg	Protospacer
.  . ******.********** *****

54. spacer 4.3|453922|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NC_014549 (Glutamicibacter arilaitensis Re117 plasmid pRE117-1, complete sequence) position: , mismatch: 10, identity: 0.667

atctccccattctcgacacgaagtccctct	CRISPR spacer
tgtgccccatcctcgacacgaagtcgagga	Protospacer
  . ******.**************

55. spacer 4.3|453922|30|NZ_CP024592|PILER-CR,CRISPRCasFinder,CRT matches to NC_001415 (Corynebacterium glutamicum strain 22243 R-plasmid pAG1, complete sequence) position: , mismatch: 10, identity: 0.667

atctccccattctcgacacgaagtccctct	CRISPR spacer
tgtgccccatcctcgacacgaagtcgagga	Protospacer
  . ******.**************

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

961522 : 1024426

uncultured_Caudovirales_phage(35.71%)

protease,plate,integrase,transposase

attL 984547:984565|attR 1028420:1028438

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_099840600.1\|961522_962608_-\|transposase	IS5 family transposase	A0A077K814	Ralstonia_phage	8.4e-19	27.7
WP_081392945.1\|963016_965413_-	hypothetical protein	NA	NA	NA	NA
WP_077095117.1\|965472_966363_-	PKD domain-containing protein	NA	NA	NA	NA
WP_081392944.1\|966359_966845_-	type VI secretion system transmembrane protein TssO	NA	NA	NA	NA
WP_077095115.1\|966873_967380_-	hypothetical protein	NA	NA	NA	NA
WP_077095114.1\|967393_968353_-	hypothetical protein	NA	NA	NA	NA
WP_099840602.1\|968372_969506_-\|plate	type VI secretion system baseplate subunit TssK	NA	NA	NA	NA
WP_099840603.1\|969518_970382_-	TssN family type VI secretion system protein	NA	NA	NA	NA
WP_077095111.1\|970390_972232_-	type VI secretion system protein TssF	NA	NA	NA	NA
WP_077095110.1\|972249_972690_-	GPW/gp25 family protein	NA	NA	NA	NA
WP_077095107.1\|974032_975220_-	hypothetical protein	NA	NA	NA	NA
WP_077095106.1\|975228_975639_-	hypothetical protein	NA	NA	NA	NA
WP_077084003.1\|975657_976083_-	type VI secretion system needle protein Hcp	NA	NA	NA	NA
WP_077095105.1\|976086_978582_-\|protease	ATP-dependent Clp protease ATP-binding subunit	H6X3M6	Enterobacteria_phage	1.8e-104	33.5
WP_099840605.1\|978706_978973_-	hypothetical protein	NA	NA	NA	NA
WP_099840606.1\|979186_979789_-	hypothetical protein	NA	NA	NA	NA
WP_077095102.1\|979793_980147_-	DUF2380 domain-containing protein	NA	NA	NA	NA
WP_099840608.1\|980510_980819_-	RHS repeat protein	NA	NA	NA	NA
WP_143734001.1\|980948_981557_-	hypothetical protein	NA	NA	NA	NA
WP_157765255.1\|981564_982539_-	hypothetical protein	A0A1P8CWI7	Bacillus_phage	7.1e-25	46.8
WP_099840610.1\|982804_983218_-	hypothetical protein	NA	NA	NA	NA
WP_039424033.1\|984466_984991_-	hypothetical protein	NA	NA	NA	NA
984547:984565	attL	NA	NA	NA	NA
WP_099840611.1\|985752_986163_-	hypothetical protein	NA	NA	NA	NA
WP_077095091.1\|986439_987336_-	RHS repeat-associated core domain-containing protein	A0A2H4JFP5	uncultured_Caudovirales_phage	7.0e-19	33.3
WP_077095090.1\|987482_987953_-	hypothetical protein	NA	NA	NA	NA
WP_077083156.1\|988095_988527_-	hypothetical protein	NA	NA	NA	NA
WP_099840880.1\|988537_989065_-	type IV secretion protein Rhs	A0A2H4JHK7	uncultured_Caudovirales_phage	7.5e-13	50.7
WP_018966114.1\|989505_990171_-	hypothetical protein	NA	NA	NA	NA
WP_099840612.1\|990182_991340_-	RHS repeat protein	A0A2H4JFP5	uncultured_Caudovirales_phage	5.1e-22	33.2
WP_099840613.1\|991486_991957_-	hypothetical protein	NA	NA	NA	NA
WP_014225733.1\|992120_992675_-	hypothetical protein	NA	NA	NA	NA
WP_099046124.1\|992679_993330_-	hypothetical protein	A0A2H4JFP5	uncultured_Caudovirales_phage	4.7e-09	48.5
WP_014225731.1\|993418_993979_-	hypothetical protein	NA	NA	NA	NA
WP_099840614.1\|993982_998194_-	hypothetical protein	A0A2H4JFP5	uncultured_Caudovirales_phage	1.9e-18	30.4
WP_077083133.1\|998217_999591_-	hypothetical protein	NA	NA	NA	NA
WP_077095087.1\|999598_1001431_-	hypothetical protein	NA	NA	NA	NA
WP_077083131.1\|1001483_1002878_-	type VI secretion system contractile sheath protein TssC	NA	NA	NA	NA
WP_018966016.1\|1002893_1003355_-	hypothetical protein	NA	NA	NA	NA
WP_077083130.1\|1003458_1003851_-	type VI secretion system needle protein Hcp	NA	NA	NA	NA
WP_077094648.1\|1005546_1005975_-	hypothetical protein	NA	NA	NA	NA
WP_157763398.1\|1005998_1006619_-	hypothetical protein	NA	NA	NA	NA
WP_077094649.1\|1006735_1007422_-	tetratricopeptide repeat protein	NA	NA	NA	NA
WP_077094646.1\|1007454_1008180_-	hypothetical protein	NA	NA	NA	NA
WP_005874619.1\|1008669_1009140_+	hypothetical protein	NA	NA	NA	NA
WP_099840616.1\|1009335_1009800_+	hypothetical protein	NA	NA	NA	NA
WP_099840617.1\|1009875_1010682_+	hypothetical protein	I3PUW5	Vibrio_phage	4.2e-31	40.1
WP_004342665.1\|1011356_1012157_+	23S ribosomal RNA methyltransferase Erm	E4ZFQ0	Streptococcus_phage	1.1e-15	28.4
WP_004342663.1\|1012261_1013080_-	nitroreductase	NA	NA	NA	NA
WP_004343809.1\|1013273_1014254_+\|transposase	IS30 family transposase	Q9MBM9	Staphylococcus_prophage	2.3e-31	34.0
WP_099777339.1\|1016289_1018503_+	peptidase domain-containing ABC transporter	W8CYL7	Bacillus_phage	1.3e-34	28.6
WP_088439428.1\|1018504_1018987_+	hypothetical protein	NA	NA	NA	NA
WP_088439430.1\|1019003_1019423_-	hypothetical protein	NA	NA	NA	NA
WP_088439434.1\|1019630_1020137_-	DUF3408 domain-containing protein	NA	NA	NA	NA
WP_088439436.1\|1020124_1020439_-	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_088439438.1\|1020459_1020729_-	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_088439799.1\|1021394_1021880_-	DUF1896 domain-containing protein	NA	NA	NA	NA
WP_088439440.1\|1021932_1023201_-\|integrase	site-specific integrase	H7BUI8	unidentified_phage	1.6e-24	37.8
WP_088439442.1\|1023205_1024426_-\|integrase	site-specific integrase	H7BUI8	unidentified_phage	9.8e-24	31.1
1028420:1028438	attR	NA	NA	NA	NA

Anti-CRISPR protein detection

Acr_ID: NZ_CP024592.1|WP_099840728.1|1611778_1612195_-|PcfK-like-protein

Click the colored protein region to show detailed information

Acr ID

Acr position

Acr size

Homology with known anti

Neighbor HTH/AcRanker

Neighbor Aca

In prophage

Protospacer in prophage

NZ_CP024592.1|WP_099840728.1|1611778_1612195_-|PcfK-like-protein

1611778_1612195_-

138 aa aa

hit_Aca_id	identity	query_coverage	hit_coverage
gnl\|BL_ORD_ID\|40	0.5886524822695035	1	1.0

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP024592

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

Click the colored protein region to show detailed information