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_CP014226	Halomonas chromatireducens strain AGD 8-3 chromosome, complete genome	4 crisprs	DEDDh,WYL,DinG,csa3,cas14j,cas3,RT	1	1	0	0

Cas Category Instructions

Results visualization

1. NZ_CP014226

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP014226_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP014226_1

1352551-1352692

Orphan

Consensus_repeat	Method
AGTCCCGATAGCGCCGCGTCAGGTCGCCATAGGCGTCGATACGGCGGTCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP014226_1

>merge|NZ_CP014226|1|1352551-1352692|CRISPRCasFinder
AGTCCCGATAGCGCCGCGTCAGGTCGCCATAGGCGTCGATACGGCGGTCGCATCTGGTAGAGAGAGGCCAGATGCGCCGCGCATTGTCGTTAGTCCCGATAGCGCCGCGTCAGGTCGCCATAGGCGTCGATACGGCGGTCGC

>NZ_CP014226|1|1|1352551-1352692|CRISPRCasFinder
AGTCCCGATAGCGCCGCGTCAGGTCGCCATAGGCGTCGATACGGCGGTCGC	ATCTGGTAGAGAGAGGCCAGATGCGCCGCGCATTGTCGTT
AGTCCCGATAGCGCCGCGTCAGGTCGCCATAGGCGTCGATACGGCGGTCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP014226.1\|WP_066446497.1\|1347177_1348143_+\|tRNA-pseudouridine(38-40)-synthase-TruA	unknown	unknown	gnl\|CDD\|234577
NZ_CP014226.1\|WP_066446469.1\|1337089_1338166_-\|L,D-transpeptidase-family-protein	unknown	unknown	gnl\|CDD\|182294
NZ_CP014226.1\|WP_066446478.1\|1341715_1342795_+\|3-isopropylmalate-dehydrogenase	unknown	unknown	gnl\|CDD\|234832
NZ_CP014226.1\|WP_066446519.1\|1360713_1361142_+\|biopolymer-transporter-ExbD	unknown	unknown	gnl\|CDD\|376792
NZ_CP014226.1\|WP_066446553.1\|1368576_1369608_+\|acetyl-CoA-carboxylase-carboxyltransferase-subunit-beta	unknown	unknown	gnl\|CDD\|235547
NZ_CP014226.1\|WP_066446546.1\|1365553_1366219_+\|phosphoribosylanthranilate-isomerase	unknown	unknown	gnl\|CDD\|234923
NZ_CP014226.1\|WP_066446475.1\|1340796_1341450_+\|3-isopropylmalate-dehydratase-small-subunit	unknown	unknown	gnl\|CDD\|179314
NZ_CP014226.1\|WP_144439623.1\|1356215_1356962_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213222
NZ_CP014226.1\|WP_066446502.1\|1351448_1352396_+\|Nudix-family-hydrolase	unknown	unknown	gnl\|CDD\|236361
NZ_CP014226.1\|WP_066446527.1\|1361138_1362896_+\|lipid-A-export-permease/ATP-binding-protein-MsbA	unknown	unknown	gnl\|CDD\|131258
NZ_CP014226.1\|WP_066446494.1\|1344446_1347170_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225711
NZ_CP014226.1\|WP_144439624.1\|1366282_1367497_+\|tryptophan-synthase-subunit-beta	unknown	unknown	gnl\|CDD\|235288
NZ_CP014226.1\|WP_066446544.1\|1364449_1365550_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|275147
NZ_CP014226.1\|WP_066446510.1\|1354981_1356223_+\|lipoprotein-releasing-ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|274034
NZ_CP014226.1\|WP_066446492.1\|1343109_1344222_+\|aspartate-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|235839
NZ_CP014226.1\|WP_066446467.1\|1335910_1336525_+\|L,D-transpeptidase	unknown	unknown	gnl\|CDD\|377115
NZ_CP014226.1\|WP_043518089.1\|1336716_1336980_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP014226.1\|WP_066446508.1\|1353769_1354813_-\|agmatine-deiminase-family-protein	unknown	unknown	gnl\|CDD\|377332
NZ_CP014226.1\|WP_066446515.1\|1356992_1357532_-\|DUF2062-domain-containing-protein	unknown	unknown	gnl\|CDD\|378263
NZ_CP014226.1\|WP_144439622.1\|1348335_1350267_+\|asparagine-synthetase-B	unknown	unknown	gnl\|CDD\|238364

Protein	Function_ID	Function_description	E-value
NZ_CP014226.1\|WP_066446497.1\|1347177_1348143_+\|tRNA-pseudouridine(38-40)-synthase-TruA	gnl\|CDD\|234577	PRK00021, truA, tRNA pseudouridine(38-40) synthase TruA.	3.63625e-132
NZ_CP014226.1\|WP_066446469.1\|1337089_1338166_-\|L,D-transpeptidase-family-protein	gnl\|CDD\|182294	PRK10190, PRK10190, L,D-transpeptidase; Provisional.	5.11208e-57
NZ_CP014226.1\|WP_066446478.1\|1341715_1342795_+\|3-isopropylmalate-dehydrogenase	gnl\|CDD\|234832	PRK00772, PRK00772, 3-isopropylmalate dehydrogenase; Provisional.	0
NZ_CP014226.1\|WP_066446553.1\|1368576_1369608_+\|acetyl-CoA-carboxylase-carboxyltransferase-subunit-beta	gnl\|CDD\|235547	PRK05654, PRK05654, acetyl-CoA carboxylase carboxyltransferase subunit beta.	0
NZ_CP014226.1\|WP_066446546.1\|1365553_1366219_+\|phosphoribosylanthranilate-isomerase	gnl\|CDD\|234923	PRK01222, PRK01222, phosphoribosylanthranilate isomerase.	1.65713e-88
NZ_CP014226.1\|WP_066446475.1\|1340796_1341450_+\|3-isopropylmalate-dehydratase-small-subunit	gnl\|CDD\|179314	PRK01641, leuD, 3-isopropylmalate dehydratase small subunit.	1.15537e-136
NZ_CP014226.1\|WP_144439623.1\|1356215_1356962_+\|ATP-binding-cassette-domain-containing-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.	5.97929e-102
NZ_CP014226.1\|WP_066446502.1\|1351448_1352396_+\|Nudix-family-hydrolase	gnl\|CDD\|236361	PRK08999, PRK08999, Nudix family hydrolase.	1.65425e-146
NZ_CP014226.1\|WP_066446527.1\|1361138_1362896_+\|lipid-A-export-permease/ATP-binding-protein-MsbA	gnl\|CDD\|131258	TIGR02203, Lipid_A_export_ATP-binding/permease_protein_msbA., lipid A export permease/ATP-binding protein MsbA. This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other].	0
NZ_CP014226.1\|WP_066446494.1\|1344446_1347170_+\|hypothetical-protein	gnl\|CDD\|225711	COG3170, FimV, Tfp pilus assembly protein FimV [Cell motility and secretion / Intracellular trafficking and secretion].	1.16315e-40
NZ_CP014226.1\|WP_144439624.1\|1366282_1367497_+\|tryptophan-synthase-subunit-beta	gnl\|CDD\|235288	PRK04346, PRK04346, tryptophan synthase subunit beta; Validated.	0
NZ_CP014226.1\|WP_066446544.1\|1364449_1365550_+\|hypothetical-protein	gnl\|CDD\|275147	TIGR04352, hypothetical_protein_imdm_1353, HprK-related kinase A. A number of protein families resemble HPr kinase (see TIGR00679) but do not belong to that system. They include this family, which appears instead to be the marker for a different type of gene neighborhood, in which one of the conserved neighboring proteins resembles (but is distinct from) PqqD.	1.29959e-05
NZ_CP014226.1\|WP_066446510.1\|1354981_1356223_+\|lipoprotein-releasing-ABC-transporter-permease-subunit	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].	3.48949e-177
NZ_CP014226.1\|WP_066446492.1\|1343109_1344222_+\|aspartate-semialdehyde-dehydrogenase	gnl\|CDD\|235839	PRK06598, PRK06598, aspartate-semialdehyde dehydrogenase; Reviewed.	0
NZ_CP014226.1\|WP_066446467.1\|1335910_1336525_+\|L,D-transpeptidase	gnl\|CDD\|377115	pfam03734, YkuD, L,D-transpeptidase catalytic domain. This family of proteins are found in a range of bacteria. It has been shown that this domain can act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. This gives bacteria resistance to beta-lactam antibiotics that inhibit PBPs which usually carry out the cross-linking reaction. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue. Several members of this family contain peptidoglycan binding domains. The molecular structure of YkuD protein shows this domain has a novel tertiary fold consisting of a beta-sandwich with two mixed sheets, one containing five strands and the other, six strands. The two beta-sheets form a cradle capped by an alpha-helix. This family was formerly called the ErfK/YbiS/YcfS/YnhG family, but is now named after the first protein of known structure.	1.60715e-17
NZ_CP014226.1\|WP_066446515.1\|1356992_1357532_-\|DUF2062-domain-containing-protein	gnl\|CDD\|378263	pfam09835, DUF2062, Uncharacterized protein conserved in bacteria (DUF2062). This domain, found in various prokaryotic proteins, has no known function.	1.45173e-41
NZ_CP014226.1\|WP_066446508.1\|1353769_1354813_-\|agmatine-deiminase-family-protein	gnl\|CDD\|377332	pfam04371, PAD_porph, Porphyromonas-type peptidyl-arginine deiminase. Peptidyl-arginine deiminase (PAD) enzymes catalyze the deimination of the guanidino group from carboxy-terminal arginine residues of various peptides to produce ammonia. PAD from Porphyromonas gingivalis (PPAD) appears to be evolutionarily unrelated to mammalian PAD (pfam03068), which is a metalloenzyme. PPAD is thought to belong to the same superfamily as aminotransferase and arginine deiminase, and to form an alpha/beta propeller structure. This family has previously been named PPADH (Porphyromonas peptidyl-arginine deiminase homologs). The predicted catalytic residues in PPAD are Asp130, Asp187, His236, Asp238 and Cys351. These are absolutely conserved with the exception of Asp187 which is absent in two family members. PPAD is also able to catalyze the deimination of free L-arginine, but has primarily peptidyl-arginine specificity. It may have a FMN cofactor.	7.29668e-159
NZ_CP014226.1\|WP_066446519.1\|1360713_1361142_+\|biopolymer-transporter-ExbD	gnl\|CDD\|376792	pfam02472, ExbD, Biopolymer transport protein ExbD/TolR. This group of proteins are membrane bound transport proteins essential for ferric ion uptake in bacteria. The Pfam family consists of ExbD, and TolR which are involved in TonB-dependent transport of various receptor bound substrates including colicins.	5.34701e-29
NZ_CP014226.1\|WP_144439622.1\|1348335_1350267_+\|asparagine-synthetase-B	gnl\|CDD\|238364	cd00712, AsnB, Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.	9.53704e-42

>NZ_CP014226.1|WP_066446502.1|1351448_1352396_+|Nudix-family-hydrolase
MVKRRVHVAAAAIVSSDGDKALIARRPSNVDHGGLWEFPGGKLAPYETGLEGLKRELHEELGVEIKRAQPLIRIHHEYSDKHILLDVWQVHEFSGEPFGREGQAVRWVPLQELVNYPFPAANLPILQAVMLPTEYFITAEEADDAVFETRLARALVEDNVRLVQLRAKSLDEAAYLARAERALALCREHGARLLLNADPALLEQVDADGIHLTSERLMSLERRPISEAKWLAASTHDQKQLTQASRIGCDFVTLSPLRTTPSHPEVPPMGWHDFQQLVERAAMPVFALGGMTRFDANHARAVGAQGIASIRDFWK
>NZ_CP014226.1|WP_144439622.1|1348335_1350267_+|asparagine-synthetase-B
MSGICGIIHLNGRPVERNQLEQMAKRAAYRGPNGIDYHLVGPVGLACLSLDVTPDGTGACHLAREDRHGLLFLADARLDNREECAAGSNHFGGKSATDVELMLSTLVQAGEEGPSRLLGDFAYALWDGRHRRLHLARDAMGLRPLYYRVEENRILFASEAQQILSVPGVPRSLNERAVAWHLCCMQTPPGEVFYSGIDEVRPAEEVVIDASAVKRSRIFWQPDPEARIRYRDERDYAAHLRDILTTSVRARLRARDPVGISLSGGVDSTCVASVAGWLRQQGETLPSMRAYSWVFPENLAECDESETIYRIADHFRIPVTEIPAEHTYPFVDDDLNKPHEDDPFFSMFQPFMEMSLAAAGKDRVSTMFYGFRGDVVCGGSVEDVPGVLLGGRFSETRRVLARLARVHGLGRRQAVVRFLLRPLLYDQLKGRYQAVMLPPLFGEVEGEGSEKRVLPAPVRHAESHVSESFLGRVGLPAVEPHYEASRVWPRYAARDRLIHISSPLVARGVGYAERVTARHGIGLADPWSDRRIADFILACPQHLVGNVLASKRMARRAMVGIMPSQAIESIGKVSPESLYIEALRFKAHDKVMDLLTNSRCADLGCIDEVALKARFERFVRGEVPIFDLWPTLSLELWLRRYWA
>NZ_CP014226.1|WP_066446497.1|1347177_1348143_+|tRNA-pseudouridine(38-40)-synthase-TruA
MTLFRRLDERTPLSGRLALGVEYDGSAYCGWQRLKNAPSVQAELERALAKVASQPVTVHSSGRTDSGVHATRQIVHFDPPVPRSQKAWVFGVNANLSRDIAVRWVREVPDDFHARFKALARRYRYIILNQPSRPVLERANVTWCRDPLDAEAMHRAAQALVGEHDFSSFRAAGCQSKTPWRKVHFIEVHRHGPLVVVDVQGNAFLHHMVRNIVGALVTVGRGDRDDDYLAELMALKDRSLSDVTAPACGLHFVDSLYDDVWELPREPLGPNLLAFLGEWTGERALPDCPMVQFRRGRPVTEATLEEAALEKATLEEGSFRQ
>NZ_CP014226.1|WP_066446494.1|1344446_1347170_+|hypothetical-protein
MRRKLTIAMLLSLSASSLQALALGVGEAAVSSSLNAPLRATIPLTDTSGLEPELLRVSVAEPREFESAGLTRSPLAASVRTSVRVRDGQLMVDLITERAVREPWLDLMLSFEWPGGRQLREVTLLLDPPDYDQLPVLVGLPTGQPSSTAERSTTEPVQEAPAQPVTQSRDTQSGDPAWVSSGDTLWAVAGRLRPDSGISMDQMMVALVEANPDVFPSGNINAMRAGHTLVVPSRDAIVARSSQQAGDVVQAMNQAWASRGSGSPARVPLGTAEVAIAAPAAAQAAELADTAGEPEPASGSGESANGLVAGVEETAEPRLTLLSDADLAAEASESLDQPGEGGAGGGEMEASSLSEAGQSSESRLDPEVLASLDAEALAPQSESQRLESLERRWLESQSELEAVQAERDALQEELGDLRSEVNAMRDQLAALVAGGQGVDAPGGGGMVPPGGETFEAETPWWGAVYQDGLDRQLMLGGAGLAALLGLWLLIRRRRSRETASTKSFANMPNVTYGAPTESVSMPPASSTAPPVVTGMSVASADEAVERPAPMPQAEAISEADIFMAYGRYDQARESLLAGLAREPERDDLRLKLLTVHVEQGDWPSAEREAERLAEGGDPSMVAEASRLMAAHRAAASGGDDGRGRVPAEFVAARELPPQEFDSLLEPHGGEVEKDDEVDEVEKVDEVEKVEKVEKVEKVEKVEKVDEVEMQLPRFEAVKPSDSDDAEAQSGEPEPSPLDDTDKRAIVTPAADSAHAGESSTMDWDMIDYQPPTLDPEPGRREETPMQPSIDFPTTGAGKGEVADVFDGDGSRNAPENAGFLGEASLGERPRPEADEWEVEEVAFPPLERDNEGANDSVAGFDELEEARRLLGVGETDRAYALLQRLRDSAADPRIQTQAKELIIHYRL
>NZ_CP014226.1|WP_066446492.1|1343109_1344222_+|aspartate-semialdehyde-dehydrogenase
MLKVGFVGWRGMVGSVLMQRMQEDGDFEGIEPIFFTTSQVGKPGPDIGVDVPPLKDATDIEELKALDVVITCQGGDYTQQVYGDLRGGGWKGYWIDAASTLRMEDEATIILDPVNRKVIDDQLSRGARTFVGGNCTVSLMLMSLGGLFEADLIEWMTSMTYQAASGSGAKHMRELLNQMGALRDSVATELDDPASAILDIDRKVTAAMRSGDFPTDNFTAPLAGSLLPWIDVKRDNGQSKEEWKGTVETNKILGLQDNPIPIDGLCVRIGAMRSHSQAFTIKLKKDVPIDEIEDRLAKHNEWVKVIPNDKEATIAGLTPSVVTGTLTVPVGRLRKMQMGGEYLSAFTAGDQLLWGAAEPLKRMLKILREK
>NZ_CP014226.1|WP_066446478.1|1341715_1342795_+|3-isopropylmalate-dehydrogenase
MTRKILVLPGDGIGPEITAQASRILAACQAHGLDVEVEEGLVGGSAYDEHGEPLPAVTLDKAKAADAILLGAVGGPKWDKLEDLTKRPEKGLLGLRKNLGLFGNLRPAITYPQLASASSLKSELVAGLDIMIVRELTGGIYFGQPRGIEVRNGERVGFNTYIYSESEIERIGRVAFEMAQKRGKRLCSVDKANVLEVTILWREVMERLAPEYPDVELSHMYVDNAAMQLVRAPKQFDVMVTGNMFGDILSDAAAMLTGSIGMLPSASLNESGQGMYEPCHGSAPDIAGQNVANPLATILSVAMLLRYSLGEAALAERIEAAVGKVLDDGLRTADIASEGTRTVSTSEMGDAVLRAFDAI
>NZ_CP014226.1|WP_066446475.1|1340796_1341450_+|3-isopropylmalate-dehydratase-small-subunit
MNKFERTEGLVAPLDRANVDTDLIIPKQFLKSIKRTGFGVNLFDELRYLDEGQPGQDCSQRPLNPDFVLNQARYQGASVLLTRRNFGCGSSREHAPWALEDFGFRVVIAPSFADIFYNNAFKNGLLLVTLAEETIDRLFAEVEANEGYRLDVDLENQRVITPSGEIIEFEVDGFRKHCLLEGLDDIGLTLKDEDAIRAFEQRHRAARPWLFRESVQA
>NZ_CP014226.1|WP_066446469.1|1337089_1338166_-|L,D-transpeptidase-family-protein
MKNPTLAKRTLRAAALFGLVALLSATAYANESDEERTLPRGHFLLPEEGNMIGTAYTVTVDEGETLIDIGRRHNVGYDEIRMANPDVSIWAPFAGTEVVIPARYILPDAPREGIVINLSELRLYYYSSDDVVETYPISVGRDGFATPVGVTRTTVKVKDPHWSPPRSMREEAAARGEPPPAVVPPGPDNPLGRHAILLGLPSYLIHGTNMPDGVGMRASRGCIRMFPEDIESLYERVPSGTKVNIIDQPFKAAWSPDGILYAQSFPQLEENLGDFEPILNAIEVVARTFGEEKPPVDYAQLRRIVESPNGQMVSLLKVADEQPGEPRPRLDGIEEGLFSELELTQREGLIYELEIVQR
>NZ_CP014226.1|WP_043518089.1|1336716_1336980_+|hypothetical-protein
MTLKTTLKLTAAAASMAILAGCATNAALDEVRQTAESAQADAAEARSIATQAQNTANQAQRDAQAALQMSEQNREEMNRMFQRSMQK
>NZ_CP014226.1|WP_066446467.1|1335910_1336525_+|L,D-transpeptidase
MTSVSRRHFGLLALSAPLALLLPSSARANLIETLLARAQVPRHDDELWVLVEDERAVLSVFRGNTLVERFAPVSLGRAGAKPERLQGGNVTPMGEFRVNRFNNESDWHIFIGLDYPTPAHARMALESGLYTERDYEDYFAYYRRHGYPPQQTVLGGFIGIHGLGGADPDVHASYHWTQGCVAVTNEQIERLSELIEIGTRVVIR
>NZ_CP014226.1|WP_066446508.1|1353769_1354813_-|agmatine-deiminase-family-protein
MANRLLPEWHPQDAIQLTWPSATSDWAPLLERIEATMENIVVAVARYQSVVISVPSTATRHHLRRRFAYLGVPAERLHLIVAPADDTWTRDHGPIGIERDGSPALLDYIFNGWGGKFEAERDNGLTQRLADAGIYACAAESRDVILEGGAIETDGEGTLLTTEACLLNPNRNPQLDREAVEAMLTADFGIERVLWLANGHLDGDDTDSHIDTLARFCDPTTIAYVRCDDEADPHYPALAAMEAELQTFRRANGEPYRLVPLPWPRPCFDPVDGHRLPATYANFVIINGAVLVPTYGDAADSRALVALGDAFPGRDIVPIDCTSVIRQHGSLHCLTMQLPRGSLATHT
>NZ_CP014226.1|WP_066446510.1|1354981_1356223_+|lipoprotein-releasing-ABC-transporter-permease-subunit
MLDRLPLLIGLRYVRAKRRNHFISFISLTSMLGLMLGVAVLILVLSVMNGFDHELRTRILGMVPHAKIESRAGLVEWEALAEELMQRERVIGAAPFVEQQGMFSSAGRNEGAMVNGIHPEWEDRVSIIGRHMQQGSLDDLAPGEWNVVLGSLLARHLGVGVGDRVTLLVPEASITPAGVFPRLKRFTVSGIFSVGADLDANLAYANIEDMQTLARLGDAVGGLRLELDDLFVAASETRAIINQLGTGYRGTDWTFTHGNLFQAIQMEKRMIALLLTVIIAVAAFNIVSTLVMVVTDKHADIAILRTIGATPRSIMGIFMVQGMAIGVIGIAVGVGFGVLLALTISDLIGWVESALGIKFLDAGVYFISDLPSRLHWSDVRDIVAAAFGLTFLSTIYPAWRAARVQPAEVLRYE
>NZ_CP014226.1|WP_144439623.1|1356215_1356962_+|ATP-binding-cassette-domain-containing-protein
MNDPATVKESAMTQAANAKGKIMLACHDLTRIYREGPQDVTVLEGLELEVRAGERVAIVGSSGSGKTTLLNLLGGLDRPSRGEVRIADESLLDLGETALGRFRNRHIGFVYQFHHLLAEFTALENAALPLIVSGQRKKAAESRARELLIRVGIAERADHKPGELSGGERQRVAIARALVTDPSLVLMDEPTGNLDQTTAASILALMDELARTTACAFVIVTHDPAMAAHQDRVLKLDGGRLTEQHDPL
>NZ_CP014226.1|WP_066446515.1|1356992_1357532_-|DUF2062-domain-containing-protein
MPRRFLQRYMPHPETLRRQRSLRFVSHIIGDPGLWALSRRTVANAFSVGLFSAMLPIPFQMVVAAFGAWLLRCTLPLSVGLVWITNPLTMPLIFYGNYRLGAWLMNTPVREAPARVSTRWIADRMADILPALALGSVVSAIVFAIVGNVIIRLVWRWHVSRSWKLRAMRRRQARLDRED
>NZ_CP014226.1|WP_066446519.1|1360713_1361142_+|biopolymer-transporter-ExbD
MRFARRRRDPVEVNLTPLIDVVFLLLIFFMVSTTFETRQALELELPESVAGADLELSPVTLVVTEQGRYRLSERELSAAELNQALTAEAEQARMHGLVLEADARAMHADVVRALDQAGALGIRQVRIATREPQATPTQAETP
>NZ_CP014226.1|WP_066446527.1|1361138_1362896_+|lipid-A-export-permease/ATP-binding-protein-MsbA
MTRPGTQDSGWTLYKRLLGYVKPHWVSFGLAIVGYAIYAASSTALAEMMKRLIDGIQSPDAAFRLFLPLFVVGMFAARGLGTFLGTYFMSNVARNVVHALRCDVFNHMLHLPGRFFDSHSSGHLISRVTYHVEQVTGAATKAVTIVLREGLFVIGLLGYLMWTNWMLTLLFMTVTPLIAGVVRYASKRFRRISQRIQHSMGDVTHVASEALSGYRVVRTHGAEEYEKARFAEASNYNRQQSMKEALTKAISTPVIQLLVALSLAVLVWLAMSPALLDDMTPGEFVAFITAASLMAKPVRQLTEVNSEIQKGIAAAAELFGLLEVPPERDEGTREPGRLEGQVELQDVHFRYGDDQPEVLKGIDVTVKAGEMIAIVGRSGSGKSTLVGLLPRFYRPTAGRVLIDGVPIDEYRLAPLRRQIGLVSQQVTLFNASIADNIAYGVPDADPAAIEAAARAAHAHEFIEPLSQGYDTVVGDNGVMLSGGQRQRLAIARAIFKDAPLLILDEATSALDTESERYIQQALETVCRGRTTLVIAHRLSTIERADRILVMEQGRIVEQGSHDQLLARDGAYAALHRLQFQETPTP
>NZ_CP014226.1|WP_066446544.1|1364449_1365550_+|hypothetical-protein
MPPYRHVLYGFCLETDYCFRTPMTAAPPGRAHDLQFLLVRVAEPQKFEPVTCLFQSAEKNRFGESSVQGYALPTGIVMRFPRVADFWLCPGKIRCELHDPSLEFMVEVCLLGHVMAYYLELSGLAALHAGAVVHGEKAVLFAADRTGGKSTMVASLVKEGFPLLADDISALTAHDGTVYCRHGFPQMKLTPEQVERFVGDFDDFPLVHPSFAKLSVPASRVGEVQSTTLPVACIYLLERCLPGKPAGGAERVRIEPVAAGEAMIQLVRHAFLVQLLDAHADCRLLGQAHSSAKQGLKASRFHLLARITQSVPVKRLCYPSGYEYLPAVHRAIEADLAKPAADASVNRHKNEDVVLASASRWESALR
>NZ_CP014226.1|WP_066446546.1|1365553_1366219_+|phosphoribosylanthranilate-isomerase
MSPSDHHVNSRIKTRTRIKFCGLTREQDVDDAVAAGADALGFVFWPGSSRCVDDARLAALVDRVPAFVTRVGLFVDQSPELIMRVSRYLDLLQFHGNETPAYCAGFERPWVKALRMRDGLDLHAAAAAYSSAQALLLDAYRPGVPGGTGETFDWSRIPASLAKPVILAGGLTPANVAQAIDSVRPFAVDVSGGVEAARGCKAPELLKAFAAAVHGADGGCR
>NZ_CP014226.1|WP_144439624.1|1366282_1367497_+|tryptophan-synthase-subunit-beta
MSKFSDLTRLPDARGHFGAYGGRFVSETLSFALDDLEKAYLSLRDDPEFQAEFDYDLAHYVGRPSPLYHAERWSKQLGGAQIWLKREDLNHTGAHKVNNTIGQALLAKKSGKPRVIAETGAGQHGVATATVAARLGLKCDVYMGAEDVQRQKLNVYRMHLLGANVIPVESGTRTLKDAMNEALRDWVTNVDDTFYIIGTVAGPHPYPMLVRDFNAVVGREARRQSLEEFGRLPDALVACVGGGSNAMGLFYPFVEDDDVVMYGVEAGGDGVETGRHAAPLASNAPRGVLHGNRTYLMSDEGGQVSDTHSISAGLDYPGVGPEHALWKDVGRVNYVAANDKDVLEAFRELTRVEGIMPALESAHALAYAKVLAPTMRPDQNIVVNLSGRGDKDIMTVAKLDGIEF
>NZ_CP014226.1|WP_066446553.1|1368576_1369608_+|acetyl-CoA-carboxylase-carboxyltransferase-subunit-beta
MSWLDKIVPSMGRIQRKDRRASVPDGLWRKCPKCEAVLYLPELEKHHNVCPKCNHHMRLTARKRIDWFLDKEGREEISADLEPVDRLKFRDSKKYKDRLSAAQKETGEKDALIAMRGSLDGLPVVVVAFEFTFMGGSMGAVVGEKFVRAATLALEERIPLICFSASGGARMQEALFSLMQMAKTSAALERLREAGVPYISVLTDPVFGGVSASLAMLGDLNVAEPNALIGFAGPRVIEQTVREKLPEGFQRSEFLLEHGTVDMIVSRGDMRNRLGGVLRKLTHQPASGIDEEMLAEPDLVDMAEQIDEAEFEPLDASEPVDDQDISSQPVEPDSEADRSEPPR

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Crispr_ID: NZ_CP014226_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP014226_2

2166087-2166210

Orphan

Consensus_repeat	Method
AGGCGCCTGACGGCGCCAGTCGCGACGCGGAGCGGCGCTCCAACAGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP014226_2

>merge|NZ_CP014226|2|2166087-2166210|CRISPRCasFinder
AGGCGCCTGACGGCGCCAGTCGCGACGCGGAGCGGCGCTCCAACAGCTGTTCTTTCATGCCACGGCGGCCTCCGCCAAGGCGCCTGACGGCGCCAGTCGCGACGCGGAGCGGCGCTCCAACAGC

>NZ_CP014226|2|2|2166087-2166210|CRISPRCasFinder
AGGCGCCTGACGGCGCCAGTCGCGACGCGGAGCGGCGCTCCAACAGC	TGTTCTTTCATGCCACGGCGGCCTCCGCCA
AGGCGCCTGACGGCGCCAGTCGCGACGCGGAGCGGCGCTCCAACAGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP014226.1\|WP_066448430.1\|2164129_2165833_+\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|236236
NZ_CP014226.1\|WP_066448448.1\|2171872_2172727_-\|formyltetrahydrofolate-deformylase	unknown	unknown	gnl\|CDD\|235676
NZ_CP014226.1\|WP_066448409.1\|2155205_2156081_+\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|223769
NZ_CP014226.1\|WP_066448435.1\|2166869_2167883_-\|beta-N-acetylhexosaminidase	unknown	unknown	gnl\|CDD\|235417
NZ_CP014226.1\|WP_066448452.1\|2174684_2174978_-\|H-NS-histone-family-protein	unknown	unknown	gnl\|CDD\|225468
NZ_CP014226.1\|WP_066448412.1\|2156993_2157782_-\|metal-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224046
NZ_CP014226.1\|WP_066448445.1\|2170036_2171092_+\|DNA-polymerase-IV	unknown	unknown	gnl\|CDD\|235035
NZ_CP014226.1\|WP_083517539.1\|2163572_2164013_+\|MerR-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133403
NZ_CP014226.1\|WP_066448439.1\|2168491_2169157_-\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380065
NZ_CP014226.1\|WP_066448446.1\|2171179_2171851_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225775
NZ_CP014226.1\|WP_083517538.1\|2159304_2159832_-\|C40-family-peptidase	unknown	unknown	gnl\|CDD\|366353
NZ_CP014226.1\|WP_066448425.1\|2160037_2160571_+\|lactoylglutathione-lyase	unknown	unknown	gnl\|CDD\|319900
NZ_CP014226.1\|WP_066448442.1\|2169351_2169996_+\|transcriptional-repressor-LexA	unknown	unknown	gnl\|CDD\|234688
NZ_CP014226.1\|WP_066448437.1\|2167971_2168490_-\|L,D-transpeptidase	unknown	unknown	gnl\|CDD\|341130
NZ_CP014226.1\|WP_066448432.1\|2166237_2166816_-\|hypoxanthine-guanine-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|181675
NZ_CP014226.1\|WP_066448419.1\|2158525_2159140_-\|thiamine-phosphate-synthase	unknown	unknown	gnl\|CDD\|238317
NZ_CP014226.1\|WP_083517717.1\|2156077_2157007_-\|metal-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224033
NZ_CP014226.1\|WP_066452314.1\|2157995_2158478_+\|manganese-binding-transcriptional-regulator-MntR	unknown	unknown	gnl\|CDD\|182927
NZ_CP014226.1\|WP_066448428.1\|2160638_2161376_-\|dioxygenase	unknown	unknown	gnl\|CDD\|153375
NZ_CP014226.1\|WP_066448450.1\|2172975_2174568_+\|ribonuclease-J	unknown	unknown	gnl\|CDD\|223668

Protein	Function_ID	Function_description	E-value
NZ_CP014226.1\|WP_066448430.1\|2164129_2165833_+\|AMP-binding-protein	gnl\|CDD\|236236	PRK08315, PRK08315, AMP-binding domain protein; Validated.	0
NZ_CP014226.1\|WP_066448448.1\|2171872_2172727_-\|formyltetrahydrofolate-deformylase	gnl\|CDD\|235676	PRK06027, purU, formyltetrahydrofolate deformylase; Reviewed.	0
NZ_CP014226.1\|WP_066448409.1\|2155205_2156081_+\|DMT-family-transporter	gnl\|CDD\|223769	COG0697, RhaT, Permeases of the drug/metabolite transporter (DMT) superfamily [Carbohydrate transport and metabolism / Amino acid transport and metabolism / General function prediction only].	2.56406e-12
NZ_CP014226.1\|WP_066448435.1\|2166869_2167883_-\|beta-N-acetylhexosaminidase	gnl\|CDD\|235417	PRK05337, PRK05337, beta-hexosaminidase; Provisional.	6.30422e-170
NZ_CP014226.1\|WP_066448452.1\|2174684_2174978_-\|H-NS-histone-family-protein	gnl\|CDD\|225468	COG2916, Hns, DNA-binding protein H-NS [General function prediction only].	9.88454e-05
NZ_CP014226.1\|WP_066448412.1\|2156993_2157782_-\|metal-ABC-transporter-ATP-binding-protein	gnl\|CDD\|224046	COG1121, ZnuC, ABC-type Mn/Zn transport systems, ATPase component [Inorganic ion transport and metabolism].	2.55056e-91
NZ_CP014226.1\|WP_066448445.1\|2170036_2171092_+\|DNA-polymerase-IV	gnl\|CDD\|235035	PRK02406, PRK02406, DNA polymerase IV; Validated.	0
NZ_CP014226.1\|WP_083517539.1\|2163572_2164013_+\|MerR-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|133403	cd04776, HTH_GnyR, Helix-Turn-Helix DNA binding domain of the regulatory protein GnyR. Putative helix-turn-helix (HTH) regulatory protein, GnyR, and other related proteins. GnyR belongs to the gnyRDBHAL cluster, which is involved in acyclic isoprenoid degradation in Pseudomonas aeruginosa. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. A typical MerR regulator is comprised of distinct domains that harbor the regulatory (effector-binding) site and the active (DNA-binding) site. Their conserved N-terminal domains contain predicted winged HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.	3.61062e-46
NZ_CP014226.1\|WP_066448439.1\|2168491_2169157_-\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|380065	pfam17939, TetR_C_30, Tetracyclin repressor-like, C-terminal domain. TetR family regulators are involved in the transcriptional control of multidrug efflux pumps, pathways for the biosynthesis of antibiotics, response to osmotic stress and toxic chemicals, control of catabolic pathways, differentiation processes, and pathogenicity. The TetR proteins identified in overm ultiple genera of bacteria and archaea share a common helix-turn-helix (HTH) structure in their DNA-binding domain. However, TetR proteins can work in different ways: they can bind a target operator directly to exert their effect (e.g. TetR binds Tet(A) gene to repress it in the absence of tetracycline), or they can be involved in complex regulatory cascades in which the TetR protein can either be modulated by another regulator or TetR can trigger the cellular response. TetR regulates the expression of the membrane-associated tetracycline resistance protein, TetA, which exports the tetracycline antibiotic out of the cell before it can attach to the ribosomes and inhibit protein synthesis. TetR blocks transcription from the genes encoding both TetA and TetR in the absence of antibiotic. The C-terminal domain is multi-helical and is interlocked in the homodimer with the helix-turn-helix (HTH) DNA-binding domain. This entry represents the C-terminal domain present in the Pseudomonas aeruginosa PsrA which regulates the fadBA5 beta-oxidation operon. Functional analysis of PsrA indicated its importance in regulating b-oxidative enzymes. It has also been suggested that PsrA, a member of the TetR family of repressors, could affect global gene expression including activation of rpoS.	3.23453e-24
NZ_CP014226.1\|WP_066448446.1\|2171179_2171851_-\|hypothetical-protein	gnl\|CDD\|225775	COG3235, COG3235, Predicted membrane protein [Function unknown].	1.27098e-28
NZ_CP014226.1\|WP_083517538.1\|2159304_2159832_-\|C40-family-peptidase	gnl\|CDD\|366353	pfam00877, NLPC_P60, NlpC/P60 family. The function of this domain is unknown. It is found in several lipoproteins.	8.11773e-34
NZ_CP014226.1\|WP_066448425.1\|2160037_2160571_+\|lactoylglutathione-lyase	gnl\|CDD\|319900	cd07233, GlxI_Zn, Glyoxalase I that uses Zn(++) as cofactor. This family includes eukaryotic glyoxalase I that prefers the divalent cation zinc as cofactor. Glyoxalase I (also known as lactoylglutathione lyase; EC 4.4.1.5) is part of the glyoxalase system, a two-step system for detoxifying methylglyoxal, a side product of glycolysis. This system is responsible for the conversion of reactive, acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids and involves 2 enzymes, glyoxalase I and II. Glyoxalase I catalyses an intramolecular redox reaction of the hemithioacetal (formed from methylglyoxal and glutathione) to form the thioester, S-D-lactoylglutathione. This reaction involves the transfer of two hydrogen atoms from C1 to C2 of the methylglyoxal, and proceeds via an ene-diol intermediate. Glyoxalase I has a requirement for bound metal ions for catalysis. Eukaryotic glyoxalase I prefers the divalent cation zinc as cofactor, whereas Escherichia coil and other prokaryotic glyoxalase I uses nickel. However, eukaryotic Trypanosomatid parasites also use nickel as a cofactor, which could possibly be explained by acquiring their GLOI gene by horizontal gene transfer. Human glyoxalase I is a two-domain enzyme and it has the structure of a domain-swapped dimer with two active sites located at the dimer interface. In yeast, in various plants, insects and Plasmodia, glyoxalase I is four-domain, possibly the result of a further gene duplication and an additional gene fusing event.	3.71514e-70
NZ_CP014226.1\|WP_066448442.1\|2169351_2169996_+\|transcriptional-repressor-LexA	gnl\|CDD\|234688	PRK00215, PRK00215, transcriptional repressor LexA.	2.43065e-101
NZ_CP014226.1\|WP_066448437.1\|2167971_2168490_-\|L,D-transpeptidase	gnl\|CDD\|341130	cd16913, YkuD_like, L,D-transpeptidases/carboxypeptidases similar to Bacillus YkuD. Members of the YkuD-like family of proteins are found in a range of bacteria. The best studied member Bacillus YkuD has been shown to act as an L,D-transpeptidase that gives rise to an alternative pathway for peptidoglycan cross-linking. Another member Helicobacter pylori Csd6 functions as an L,D-carboxypeptidase and regulates helical cell shape and motility. The conserved region contains a conserved histidine and cysteine, with the cysteine thought to be an active site residue.	2.16132e-18
NZ_CP014226.1\|WP_066448432.1\|2166237_2166816_-\|hypoxanthine-guanine-phosphoribosyltransferase	gnl\|CDD\|181675	PRK09162, PRK09162, hypoxanthine-guanine phosphoribosyltransferase; Provisional.	1.25925e-113
NZ_CP014226.1\|WP_066448419.1\|2158525_2159140_-\|thiamine-phosphate-synthase	gnl\|CDD\|238317	cd00564, TMP_TenI, Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.	6.2959e-72
NZ_CP014226.1\|WP_083517717.1\|2156077_2157007_-\|metal-ABC-transporter-permease	gnl\|CDD\|224033	COG1108, ZnuB, ABC-type Mn2+/Zn2+ transport systems, permease components [Inorganic ion transport and metabolism].	4.86976e-72
NZ_CP014226.1\|WP_066452314.1\|2157995_2158478_+\|manganese-binding-transcriptional-regulator-MntR	gnl\|CDD\|182927	PRK11050, PRK11050, manganese-binding transcriptional regulator MntR.	5.98978e-66
NZ_CP014226.1\|WP_066448428.1\|2160638_2161376_-\|dioxygenase	gnl\|CDD\|153375	cd07363, 45_DOPA_Dioxygenase, The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine. This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.	3.17216e-114
NZ_CP014226.1\|WP_066448450.1\|2172975_2174568_+\|ribonuclease-J	gnl\|CDD\|223668	COG0595, COG0595, mRNA degradation ribonucleases J1/J2 (metallo-beta-lactamase superfamily) [Translation, ribosomal structure and biogenesis; Replication, recombination and repair].	4.26062e-123

>NZ_CP014226.1|WP_066448430.1|2164129_2165833_+|AMP-binding-protein
MTRQHSQIRVQNSYVSGISDTPLKGQTIGDCFDETVARFPDGDALLSLHQGLRYTWTELQQAVDEAARALLALGLAKGDRVGIWSPNCAEWTITQFATAKIGAVLVNINPSYRTHELEYALKQSGASTLVLQGKFKSSDYVATLAELAPEIRDAAPDTFSCASLPELKRVVCLDADLALPGMLTWQGMLGHADQVSAERLAEVQGTLQFDDPINIQYTSGTTGAPKGATLSHHNILNNGFFVARTMGFTEKDRLVIPVPLYHCFGMVMGNLGCVTHGATMIYPGDGFDPEATLKAVSEEKATALYGVPTMFIAELEHANFAQYDLSTLRTGIMAGSICPIEVMRQVIDKMNMEDVTICYGMTETSPVSFQTQTDAPLDKRVTTVGTIHPHLEVKLVSPETGAVVPRGETGELCTRGYSVMLGYWENEEATDKSIDAAGWMHTGDLATMDEEGYVAIVGRIKDMIIRGGENIYPREIEDFLYTHPAISDVQVIGVPDEKYGEEVMAWVKLSEGQQLTGDELKEFCKGKIAHYKVPRYVKFVDEFPMTVTGKIQKFKMREEATHELGLA
>NZ_CP014226.1|WP_083517539.1|2163572_2164013_+|MerR-family-DNA-binding-transcriptional-regulator
MSTAEPEATTVINGSLPQQRRTYSIGELARMFEVTPRTIRFYEQEGLLAPERRGQTRIYHEKDRVRLKLTLRGKRLGFSLAEIREVIEMYDAMPDGNARQLKRLLEILSDKRTNMERQLEDIRLMQRELDDVEMRARDVLKRLDQQ
>NZ_CP014226.1|WP_066448428.1|2160638_2161376_-|dioxygenase
MQPSLFISHGSPMLALTKTPAHDFLRELGQALRPKAVVVVSAHWESDRLLVSTSAHPETIHDFGGFPRALYECQYPAPGEPELARRLARELNAVPTERGLDHGAWVPLSLMLPEANVPVVSLSLPVQWSNAELVALGGKLAALREENILVIGSGSLTHNLMELQAQGSEMPAWVGEFADWVHKRLDADDRTALLDWEQARYARENHPTSEHFQPLLVAMGAGGQAERLHHSVEHGVLAMDVYAFA
>NZ_CP014226.1|WP_066448425.1|2160037_2160571_+|lactoylglutathione-lyase
MNFKGEQHPGVKMPTGDTLGFRLNHTMLRVKDPELALAFYTRVFGMSVLRRLDFEELGFSLYFLARLEEEEQVPEEKGERTVWTFSQKGLLELTHNWGTEDQADFAYHDGNAEPQGFGHICFSVPNLDAAEAWFDANDVEFIKRADQGKMKDVVFVKDTDGYWIEVVQADRLAALGD
>NZ_CP014226.1|WP_083517538.1|2159304_2159832_-|C40-family-peptidase
MARVAWFEPVALPGRSRPLHGQGRLVLLLIALMLLAGCASRDMATQDPRAGEGLSIERALILATAEGALGTPYRFGGNSPEGLDCSGLVELSYRAAGIPVPRTADDQYRTLPEARQARPGDLLFFGDRRKATHVGIYRGNGQMIHAPGRGRQVVSVPLDVDYWQDRFLGAASPAP
>NZ_CP014226.1|WP_066448419.1|2158525_2159140_-|thiamine-phosphate-synthase
MRLDLTLYLVTDPRLCARHGLVETVVAAVRGGVTLVQLRDKQASDEELIDQARRLKAALAGSGVPLIINDRLDVALASEADGLHLGQDDGEVAAARQALGEHAILGLSVQNLDQMSRLDPEPLDYLGLGPVFATATKPNHARPLGFDGLATLVAASPLPAVAIGGLQAEHVGRVRTAGAKGPAGGAAICGQPDPEAAAQAFFNV
>NZ_CP014226.1|WP_066452314.1|2157995_2158478_+|manganese-binding-transcriptional-regulator-MntR
MTDSPKKVTPDRLCKADALPPSDQHAKQYAAVRNAHETELLEDYVELIADLLQHHGEARSTDIAARMGVSQATVSKTVARLKSLGLVSSKPYRSLFLTEKGEAMAAMSHQRHAIVLRFLRALGVSDHTARIDAEGMEHHVSQETLDIMQRFTREKERGSS
>NZ_CP014226.1|WP_066448412.1|2156993_2157782_-|metal-ABC-transporter-ATP-binding-protein
MTDPAPALQASRLYAAYHQQPVLEDISLSLPQGQWTAIVGPNGAGKSSLLNLVIGSLAPLRGELRILGNSPAAQRRAGNIAYMAQQENMEWDFPISVRETVLTGRYGMMRHDPLWRRLLPRYWANPSHRQAVEAALEAVDMADHAARPIGELSGGQKKRVMLARALAQQAKILLLDEPLAGVDPPSEALILETLERERAAGRTVIMVTHDMQGARRHADNVMLINRTLIGMGPPEEMLSDAMLARLAVGTPSTEHGRVPVAA
>NZ_CP014226.1|WP_083517717.1|2156077_2157007_-|metal-ABC-transporter-permease
MLPLEAFAISVIDALIVLLMMAVNLLPESLAAPFEYRFMQRALLTSVLVGAICGLLSCYVVLKRWSLLGDAISHAVLPGVAIAYLLGWPFFIGAFVTGALTSLGIGALERHTRIKADAAMGLMFTAAFALGIVIISKIATSTHLMHILFGNVLGVQTSALMLTLAASLVAVLAIWLAYRPLLLYTFDPQQAQALGFNTSIIHYGLILLLTLTIVASLETVGIILVVAMLITPGATAHLLTDRFPTMLALSVGVGVTSAVVGLMLSVALDVASGGAIVLVASGLFLIALLAAPKHGLVGRHWRRWRLNRA
>NZ_CP014226.1|WP_066448409.1|2155205_2156081_+|DMT-family-transporter
MTPSLKGILCMCMGVLCLAIGDAIAKWLGEVHSPLQIIFFRTLVSLPLIAVLAHFGGGLTKLRTQRPGVHLVRGLIYTGTMFFFVLGLTLLPLAEATAIAFVAPLFVTLLSVPLLGEKIDPPVLAASLLGFVGVLVVVRPGGDAFHPGALALLAAAVFYALMMITARRYGAREHLWAMVFYMTLVPLLLTAVALPWVWQTPHPWHWLGFLGAGIIGVGATAFITLAFRFAPAAIAAPFDYTAMLWAVILGWWFWGEMPDVWVFVGSTLIIGSGLAIAYHDRRTTLKRRPTA
>NZ_CP014226.1|WP_066448432.1|2166237_2166816_-|hypoxanthine-guanine-phosphoribosyltransferase
MPKLDPDFHQSLATMRDVMESADCLITQEEVEAALDHMAEQITSDLGDKLPVFYCVMNGGLITTGHLLTRLGFPLEVDYLHATRYRGGIRGGDLFWRVSPEVPMADRHVVIVDDILDEGTTLAAILDYCHKAGAKSISTAVLVDKRHDRKAVPDLRADYCGLEVVDRYVFGFGMDYKGYWRNAPGIFAPKGL
>NZ_CP014226.1|WP_066448435.1|2166869_2167883_-|beta-N-acetylhexosaminidase
MTQTLGPVMLDLEGTQLSDDERRLLLRPEVGGVILFSRNIEDARQVRSLCNTIRQLRPELLLTVDQEGGRVQRLRQGVTRIPSMGRIGRDYVAAPEVTLRLCLDTGWLLGMEMAACGLDLSFAPVLDVDGGISSVIGDRSFSSDPLAVSAMAEAFVAGLHEAGMAAVGKHFPGHGGVAADSHLELPVDDRPIDVIRGHDLVPFADLACRLDGVMPAHVIYSAFDARPAGFSNSWLGLLRESLGFKGTIFSDDLGMAGAGYAGGPYERAQAALDAGCDMVLVCNDRAAALEVLDACQGRTIRPATRLRYGRARPEPEALEALGRWRRVHARLEAMAQD
>NZ_CP014226.1|WP_066448437.1|2167971_2168490_-|L,D-transpeptidase
MRTPRLTELPPATGTWLEVDVANQCLVHWQGSRPQAEWAVSTALAGTGQQEGSGCTPLGWHYVRAAIGDGLPTGTVFRGRRPTGERFSPALAEAHPHRDWILTRIIWLCGLERGFNRGGEVDSQRRYIYFHGTPPDQPMGVPRSHGCIRLSASSLLHLFSLAPPGTPVWLHD
>NZ_CP014226.1|WP_066448439.1|2168491_2169157_-|TetR/AcrR-family-transcriptional-regulator
MAQTDTVTRILDTAEVLFAERGFAETSLRTITSKARVNLAAVNYHFGSKKSLIQAVFARYLDPFTVRFHHALDELEAQHAGGVIPLEVLLETMARTVLEVPGERHSLKVFMKLLGLAYSQAQGHLRRYIQDEYGSVFSRFTDLVRLATPDLPDSERFWRLHFVLGTVIFTLSGLDALRDIAEKDYQEHVSVRDLIRRLRPVVVAAMNAPLPPPPMPKAEAS
>NZ_CP014226.1|WP_066448442.1|2169351_2169996_+|transcriptional-repressor-LexA
MSRPLTSRQQNVYDFIVKTMNEFGYPPTRAEIARALGFRSPNAAEEHLRALERKGVIRVIRGTSRGIRLPAQDAEPVGGEPAVEGLPIIGEVAAGSPILAAEHIDRYCPLPPEFFTPRADYLLKVRGLSMKDAGILEGDLLAVHRTDRVRDGQIVVARLEDEVTVKRFHRNGHQVILEAENADFAPIEVDLRHQPLEIEGVGVGVIRGGSGQAL
>NZ_CP014226.1|WP_066448445.1|2170036_2171092_+|DNA-polymerase-IV
MDSVRKILHADCDCFYAAVEMRDNPALREIPLAIGGSAEGRGVIATCNYPARRYGIHSAMPTARALRLCPQLTLLHGDFDRYREASRQIQAIFHELTPLVEPLSLDEAFLDVTAVTRFSGSATWMARWLKEECQRRVGITVSVGAAPSKFLAKIASDWEKPDGLTVITPDRVATFIKTLPVTKLNGVGPATARRLKSLDIDTCDDLQRLPQDRLIHEFGKFGHRLFELARGIDTRPVRVERERKSVSVETTFATDLPGLPDCHRELAALCDRLESRLARHGHPPLAGLFVKVRFDDFSLTTIEGRGSTLCNQTFNALLAQAWARKKRPVRLLGVGARLVPEDARRQLTLPL
>NZ_CP014226.1|WP_066448446.1|2171179_2171851_-|hypothetical-protein
MSFSEPMLAPWLLIACGVLSLGVVGLALAQRPWETLIADRALQHRWLAATVAVVLLWQLRAQAVDWLTLHLMFTALLTLIFKAPLALITNLLANLALVLLGKAAWPLLGVNVLITGVIPVGITVLVWRLVDRRLPDNLMVFLFLCGFFGAALATLGTGLTGLGLVMLGATDPEAIYLAQEYALFLPLLMPSEAFLTGMLLSILMVYHPGWVATFNDHRYIDTK
>NZ_CP014226.1|WP_066448448.1|2171872_2172727_-|formyltetrahydrofolate-deformylase
MSHYYRLVVSCPDRRGIVARVSGFISGHGGSITEASQHSDLASGRFFMRYEILSDSIDMTGDELRKAFEPVAREFEMEWALRDTRRRQRVVVMVSRESHCLVDLLYRWTAGEMEGDIVGVISNHPDMRGMVEWHGLPYFHVPVDAADKAAAFAEIEAQVEALDADTVVLARYMQILPPGLCRRYAGRVINIHHSFLPSFVGARPYHQAHDRGVKLIGATCHYVTEELDAGPIIEQDIHRVSHCHTPGDLVRFGRDVEKAVLARGLRWHLEDRVLIHGNKTVVFA
>NZ_CP014226.1|WP_066448450.1|2172975_2174568_+|ribonuclease-J
MNLGLYGHDGEWIAVDCGMMIRQDLPDSPLQVPSLDTAVALGIAPSALIITHGHEDHIGAAAWLWPKWQCPVHATPLAAGLLRAKFTERGLATDAIQVIDPGEALETGPFTLRYLPLTHSIPESCALLIAVGGYRVLHTGDWKLDPEPLIGPPVKGSLFRALAPVDLVVGDSTNATLPGHSRSEGEVARALEHRLSQCTGRVVVSCFASNLARVLAIALAAERCGRRVSLMGRAMERMVGVARGLGYLDDMPPLVPASDLGYLPPDEVLVIATGSQGEPRAALSRLANGRHHSLELSPGDTVIFSAKAIPGNEPQIERLKHGLRRLDVAIWDEFNHPELHASGHPAQEELRIFYGWIKPKHLLPVHGEPQHQRAHRALADTLGIQAPVSPVNGDLIRLDVDGLTLEARHPQRPCIVSQNAVTPLPGLAAERGSSRHGILHLALPIASTGPGWTRIGRLMLDAHRVSALDEDALADWLDERLEELHAESLAELRVALQPMLTAWLADHLRQLPDIHLQLLAVEAPAFGDKD
>NZ_CP014226.1|WP_066448452.1|2174684_2174978_-|H-NS-histone-family-protein
MSSETLERIARNKNVARAAARQLSMEQLNKLSDVIGEVIEQKKEEDKLREKEEADKERKLAEIREAMSDAGLSVEDLVGEPPRRRRGRPPKKNAGGS

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Crispr_ID: NZ_CP014226_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP014226_3

3527549-3527642

Orphan

Consensus_repeat	Method
GAGGAGGCGCTGCAGCACCGCTCGGGGCTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP014226_3

>merge|NZ_CP014226|3|3527549-3527642|CRISPRCasFinder
GAGGAGGCGCTGCAGCACCGCTCGGGGCTGGCATCCATGGCGAGGGACGCCGGGGTCGGTCGTAGAGGAGGCGCTGCAGCACCGCTCGGGGCTG

>NZ_CP014226|3|3|3527549-3527642|CRISPRCasFinder
GAGGAGGCGCTGCAGCACCGCTCGGGGCTG	GCATCCATGGCGAGGGACGCCGGGGTCGGTCGTA
GAGGAGGCGCTGCAGCACCGCTCGGGGCTG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP014226.1\|WP_083517640.1\|3536520_3536694_-\|DUF2970-domain-containing-protein	unknown	unknown	gnl\|CDD\|378581
NZ_CP014226.1\|WP_066451713.1\|3531718_3531916_+\|DUF2909-domain-containing-protein	unknown	unknown	gnl\|CDD\|378564
NZ_CP014226.1\|WP_066451696.1\|3522052_3522661_-\|FMN-dependent-NADH-azoreductase	unknown	unknown	gnl\|CDD\|234675
NZ_CP014226.1\|WP_066451722.1\|3535208_3536327_-\|cytochrome-c-oxidase-subunit-II	unknown	unknown	gnl\|CDD\|224537
NZ_CP014226.1\|WP_066451695.1\|3520840_3521908_+\|metal-dependent-hydrolase	unknown	unknown	gnl\|CDD\|377294
NZ_CP014226.1\|WP_066451717.1\|3532868_3533462_-\|cytochrome-c-oxidase-assembly-protein	unknown	unknown	gnl\|CDD\|235341
NZ_CP014226.1\|WP_066452414.1\|3518156_3519134_-\|kinase	unknown	unknown	gnl\|CDD\|226699
NZ_CP014226.1\|WP_066451710.1\|3529141_3530206_-\|heme-A-synthase	unknown	unknown	gnl\|CDD\|367131
NZ_CP014226.1\|WP_066452415.1\|3530280_3530787_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP014226.1\|WP_066451700.1\|3522846_3523425_-\|superoxide-dismutase	unknown	unknown	gnl\|CDD\|182534
NZ_CP014226.1\|WP_066451720.1\|3533497_3535135_-\|cytochrome-c-oxidase-subunit-I	unknown	unknown	gnl\|CDD\|238833
NZ_CP014226.1\|WP_066451706.1\|3524885_3525503_-\|YitT-family-protein	unknown	unknown	gnl\|CDD\|224203
NZ_CP014226.1\|WP_066451692.1\|3520249_3520786_+\|DNA-3-methyladenine-glycosylase-I	unknown	unknown	gnl\|CDD\|225374
NZ_CP014226.1\|WP_066451715.1\|3532014_3532872_-\|cytochrome-c-oxidase-subunit-3	unknown	unknown	gnl\|CDD\|238834
NZ_CP014226.1\|WP_066451702.1\|3523535_3524195_+\|transcriptional-regulator	unknown	unknown	gnl\|CDD\|225222
NZ_CP014226.1\|WP_083517637.1\|3519735_3520158_-\|metal-binding-protein	unknown	unknown	gnl\|CDD\|225564
NZ_CP014226.1\|WP_066451708.1\|3525611_3527417_-\|single-stranded-DNA-exonuclease	unknown	unknown	gnl\|CDD\|273193
NZ_CP014226.1\|WP_066451704.1\|3524469_3524889_+\|glyoxalase	unknown	unknown	gnl\|CDD\|319942
NZ_CP014226.1\|WP_083517639.1\|3530910_3531720_-\|SURF1-family-protein	unknown	unknown	gnl\|CDD\|119401
NZ_CP014226.1\|WP_083517638.1\|3528363_3529149_-\|UbiA-family-prenyltransferase	unknown	unknown	gnl\|CDD\|235293

Protein	Function_ID	Function_description	E-value
NZ_CP014226.1\|WP_083517640.1\|3536520_3536694_-\|DUF2970-domain-containing-protein	gnl\|CDD\|378581	pfam11174, DUF2970, Protein of unknown function (DUF2970). This short family is conserved in Proteobacteria. The function is not known.	9.15257e-14
NZ_CP014226.1\|WP_066451696.1\|3522052_3522661_-\|FMN-dependent-NADH-azoreductase	gnl\|CDD\|234675	PRK00170, PRK00170, azoreductase; Reviewed.	3.76639e-78
NZ_CP014226.1\|WP_066451722.1\|3535208_3536327_-\|cytochrome-c-oxidase-subunit-II	gnl\|CDD\|224537	COG1622, CyoA, Heme/copper-type cytochrome/quinol oxidases, subunit 2 [Energy production and conversion].	7.63284e-71
NZ_CP014226.1\|WP_066451695.1\|3520840_3521908_+\|metal-dependent-hydrolase	gnl\|CDD\|377294	pfam04307, YdjM, LexA-binding, inner membrane-associated putative hydrolase. YdjM is a family of putative LexA-binding proteins. Members are predicted to be membrane-bound metal-dependent hydrolases that may be acting as phospholipases. It is a member of the SOS network, that rescues cells from UV and other DNA-damage. Expression of YdjM is regulated by LexA.	1.56259e-34
NZ_CP014226.1\|WP_066451717.1\|3532868_3533462_-\|cytochrome-c-oxidase-assembly-protein	gnl\|CDD\|235341	PRK05089, PRK05089, cytochrome C oxidase assembly protein; Provisional.	5.57637e-78
NZ_CP014226.1\|WP_066452414.1\|3518156_3519134_-\|kinase	gnl\|CDD\|226699	COG4248, COG4248, Uncharacterized protein with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only].	7.97203e-29
NZ_CP014226.1\|WP_066451710.1\|3529141_3530206_-\|heme-A-synthase	gnl\|CDD\|367131	pfam02628, COX15-CtaA, Cytochrome oxidase assembly protein. This is a family of integral membrane proteins. CtaA is required for cytochrome aa3 oxidase assembly in Bacillus subtilis. COX15 is required for cytochrome c oxidase assembly in yeast.	9.62202e-64
NZ_CP014226.1\|WP_066451713.1\|3531718_3531916_+\|DUF2909-domain-containing-protein	gnl\|CDD\|378564	pfam11137, DUF2909, Protein of unknown function (DUF2909). This is a family of proteins conserved in Proteobacteria of unknown function.	5.44281e-08
NZ_CP014226.1\|WP_066451700.1\|3522846_3523425_-\|superoxide-dismutase	gnl\|CDD\|182534	PRK10543, PRK10543, superoxide dismutase [Fe].	5.625e-110
NZ_CP014226.1\|WP_066451720.1\|3533497_3535135_-\|cytochrome-c-oxidase-subunit-I	gnl\|CDD\|238833	cd01663, Cyt_c_Oxidase_I, Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.	0
NZ_CP014226.1\|WP_066451706.1\|3524885_3525503_-\|YitT-family-protein	gnl\|CDD\|224203	COG1284, COG1284, Uncharacterized conserved protein [Function unknown].	2.95499e-40
NZ_CP014226.1\|WP_066451692.1\|3520249_3520786_+\|DNA-3-methyladenine-glycosylase-I	gnl\|CDD\|225374	COG2818, Tag, 3-methyladenine DNA glycosylase [DNA replication, recombination, and repair].	1.72784e-61
NZ_CP014226.1\|WP_066451715.1\|3532014_3532872_-\|cytochrome-c-oxidase-subunit-3	gnl\|CDD\|238834	cd01665, Cyt_c_Oxidase_III, Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme.	2.84971e-88
NZ_CP014226.1\|WP_066451702.1\|3523535_3524195_+\|transcriptional-regulator	gnl\|CDD\|225222	COG2345, COG2345, Predicted transcriptional regulator [Transcription].	4.04037e-56
NZ_CP014226.1\|WP_083517637.1\|3519735_3520158_-\|metal-binding-protein	gnl\|CDD\|225564	COG3019, COG3019, Predicted metal-binding protein [General function prediction only].	1.83351e-39
NZ_CP014226.1\|WP_066451708.1\|3525611_3527417_-\|single-stranded-DNA-exonuclease	gnl\|CDD\|273193	TIGR00644, recJ, single-stranded-DNA-specific exonuclease RecJ. All proteins in this family are 5'-3' single-strand DNA exonucleases. These proteins are used in some aspects of mismatch repair, recombination, and recombinational repair. [DNA metabolism, DNA replication, recombination, and repair].	5.64818e-124
NZ_CP014226.1\|WP_066451704.1\|3524469_3524889_+\|glyoxalase	gnl\|CDD\|319942	cd08354, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	5.46042e-50
NZ_CP014226.1\|WP_083517639.1\|3530910_3531720_-\|SURF1-family-protein	gnl\|CDD\|119401	cd06662, SURF1, SURF1 superfamily. Surf1/Shy1 has been implicated in the posttranslational steps of the biogenesis of the mitochondrially-encoded Cox1 subunit of cytochrome c oxidase (complex IV). Cytochrome c oxidase (complex IV), the terminal electron-transferring complex of the respiratory chain, is an assemblage of nuclear and mitochondrially-encoded subunits. Its assembly is mediated by nuclear encoded assembly factors, one of which is Surf1/Shy1. Mutations in human Surf1 are a major cause of Leigh syndrome, a severe neurodegenerative disorder.	1.48681e-42
NZ_CP014226.1\|WP_083517638.1\|3528363_3529149_-\|UbiA-family-prenyltransferase	gnl\|CDD\|235293	PRK04375, PRK04375, protoheme IX farnesyltransferase; Provisional.	1.34109e-83

>NZ_CP014226.1|WP_066451708.1|3525611_3527417_-|single-stranded-DNA-exonuclease
MDVIAPPDLHARLRPRLLPRPRNQALYARAQAEGLTELQARVLAGRLAGYEGELAPLTQPSLRYLEHPERLADGRRAAERIAQAVVEGEHIGILTDYDVDGITSHVVIRRTLVELFGVPEARLHSLIGHRIHDGYGISLPLVERTLSLKPRPSLVITADCGSSDEPRIARLRAAGIDVVVSDHHALPVEGPPASAHAVVNPTRDDCDYPDATIAGCMVAWLVMSLARQVLIEWGALPSATPKLSPWLSYVALGTVADCVSLGASPANRAVVSHGLTLINRMEAACWRAMAARLGEDSTPFTAETLAFQMGPRINARSRLDDPYAALHFMLAADDGTATRHLETLDQDNQSRKAIEADMTEQARLLAVPQLDANHPAIVVFLEGGHAGGQGIVASRLVQAYGRPALVMTPAAAPGMLTGSGRSIEALHLRDALQRTFELAPEALPRFGGHRGAAGVGVPADRFDAFRTAFLQAVGEQLGGIELFPHVLTDGELLPAQFDLSTLDELERLGPYGREFDAPLFEGAFLVEALRPVGADGSHLMMTLSAGAVSLRAIWFRALTPGELPAFGLGDRLRCAYRLSRNRWKGRESLQLMVDYAEPLDG
>NZ_CP014226.1|WP_066451706.1|3524885_3525503_-|YitT-family-protein
MDPQDLSADPHRPYEDVMAMLVGTLFVALGVTFYTQALLLTGSTAGMAFLLQYATGWRFGVWFFLINLPFYYLAVKRMGWSFTLRTFVAIGLVSLFSELTGKWITIESLNPLYATLMGGSLIGIGMLVLFRHRTSLGGINILALYLQARYGLRAGYVQLGIDGLIMLAALLVLPADRVGLSVLGAVALNLIIALNHKPGRYMGVS
>NZ_CP014226.1|WP_066451704.1|3524469_3524889_+|glyoxalase
MPRLNGVLETALYVDDMDRARVFFEGVMGLEPFNADHRFTAYDAGRGSVLLLFLQGETLETVKLPNDMGTIPPHDGKGRVHLAFAISAASLPEWEAQLDDHGVAIEGRTHWPKGGESLYFRDPDGHLIELATPGVWPNY
>NZ_CP014226.1|WP_066451702.1|3523535_3524195_+|transcriptional-regulator
MSSDPNEKPADTAAERLLHLLKSRGPHSAAELGEMLGTTGENARQQLSKLARRGLVAQRSRPGGVGRPVVEWRLTEAGHGHFPDTHAELASRLIISVRDTLGEAALGRLVEARGAETLAHYRLELADAGTLASRVARLAEIRSREGYMAEWQEGADGSLLLVENHCPICSAARTCPAFCHSELQVFRAVLGPDVSVERVEHVLEGARRCAYRIIKQVGS
>NZ_CP014226.1|WP_066451700.1|3522846_3523425_-|superoxide-dismutase
MAFELPALPYEKNALEPHISAETLEYHYGKHHQAYVTKLNELVEGTDNASKSLEEIIKSASGGLFNQAAQVWNHTFYWHCLSPNGGGEPSGALAEAINAKFGSFDKFKETFNSNAVANFGSGWTWLVKTDDGGVDIVNTSNADTPIAHGQTPVLTIDVWEHAYYIDYRNARPKYLDSVWNLINWDFVAQNFS
>NZ_CP014226.1|WP_066451696.1|3522052_3522661_-|FMN-dependent-NADH-azoreductase
MTTRALVVTSSILGTQGQSMALAEHFTTRSNERDALEVTRRDLVADELPHLGVAELFSWQVPAVERTPEQRALAELSDGLIDELKAHDVLVLAVPLYNMGIPSQLKAWFDRVLRAGETFRYTDKGPQGLVEGKRAVILAARGGQYAGTEMDSQTPHLKGMLGLIGITDVTVVFAEGLAMGERHRDASLKEARQAIDGLVAAL
>NZ_CP014226.1|WP_066451695.1|3520840_3521908_+|metal-dependent-hydrolase
MDTLTQAALGAAVGGAVLGRRLGRKAIVIGAVLGTLPDLDVFLDYGDAVANYTQHRGFTHSLFVLTGLGTLLALTADRFAPARDIALRHWWAFFVLCLVTHPLLDALTTYGTQLWWPMDVRPSAWPVVFIIDPLYTLPLLAGIGVALVTGNGRRGPAWGLALSSAYLLFAMGAKILVEQRLEPVLAEQGLQEAPRLIQPTPFNTLLWRVTIIDGAQHHETLLSVFDGNREPTFETFDRGGELEPTALAFERGERLHWFAGPFLRYEIRDLEGEETLVATDLRLGFPGFHAFSFTLAVREDGDWRPAVPTEQLSFDARADLDALGQLGSRIFSPEPPLCTSEFVADRWVVDTPASC
>NZ_CP014226.1|WP_066451692.1|3520249_3520786_+|DNA-3-methyladenine-glycosylase-I
MSHYCDLAPGHPFHGPYHDTEYGFPVDDDRALFERLVLEINQAGLSWLTVLKKRAAFRLAFEDFHIDRIANYAEEDRQRLLSDAGIIRNRLKVDAVIHNAGVVQSLRSEHGSFKAWLDHHHPLPHADWVKLFRKTFRFTGPEIVGEFLMSTGYLNGAHRDDCPVQARILTAGPAWQST
>NZ_CP014226.1|WP_083517637.1|3519735_3520158_-|metal-binding-protein
MKTLTVNRKTRKAAALSLLAGGVLALYLVLAPGASTQAGSVVEMYQDPNCGCCTDWADHLREEGFEVRQHKTRDMRSVKMEHGVTPELSSCHTALIDGYVIEGHVPAADIKRLLEERPEVVGLXRYRGIRTREALSSERA
>NZ_CP014226.1|WP_066452414.1|3518156_3519134_-|kinase
MRARVVTDSLGKTRRLGKRLERGGEGEIFALQERPDVIVKWYYPEVLDKRGDELHRKVEAMRELRDAHMTRDVCWPLIRVFDDKHRWIGFAMYRARGVRMGFLAHALLYQRYFPGLDRRQIVDYLIRFVEIVQQLHRAGVCIGDYNLNNIFCVPSTQEVTLIDCDSYQLRMGGTFYPCPVGSPDMTPKEHQGVAFRDIVRTPRSEAFSLAIVLFKCLMLGRHPYDIVGGDDPVRNLRRGNFAYGHGQRDVPQGAWYDLWRELPEPIRDMFVTTFTAGASAPSRRATLPQWHAALTTYRQQLEAGECPRELARPSAKPDSQVLHAR
>NZ_CP014226.1|WP_083517638.1|3528363_3529149_-|UbiA-family-prenyltransferase
MSNAVIKRTGLKRTLGAPFNTEDAADWTGQDLLTLCKPRVVVVMLACALVGMALATPALPPLSTVIFGLAGIGFAAGGAAAFNHVVDRRLDAMMLRTSRRPLASQRMPTWLALAWASLLSVSGILLLLWQVNALTAWLTLGSLIGYALIYTAFLKRATPQNIVIGGVAGAAPPLLGWTAVTGQLGPEPLLLLLIVFAWTPPHFWALGHLEERWVDRRDRQNAVTRLGQSQAGQMQCRHHAGEPELPFGLDRPAILPGAPLA
>NZ_CP014226.1|WP_066451710.1|3529141_3530206_-|heme-A-synthase
MQDISTRGHQGSSRLGLLLSLSLVGVFFTSAVILVGVWTRLVDAGLGCPDWPGCYGRLVVPDAERAMAHSPDAPLEVFKAWVEMIHRYVASALGLLVIALLVAGAGLRKRQGYPWGVSVALLVVILLQGAFGAFTVTLKLWPQVVTMHLLGGLAVLLLFLWLHLRLRRYAAGDTGERPRRRLTPLWGLALLLLLLQLALGGWVSSNYAGIACQGFPTCNGQWWPEMDWSEGFHLTQTVGPNYLHGQLHADARVAIHQGHRIGALLLGLVLLALAVRYWHESRLRPWLGGVVGIYVLQLGLGIANVLLWLPLWLALLHTAGAVALVLCLALAVWHWREAVEDETTIRKDKEWAHV
>NZ_CP014226.1|WP_066452415.1|3530280_3530787_-|hypothetical-protein
MALIAIFAIPVATAWIMVEWRIGIPEQRTAHGELAPAVPALANWPLVEPLEALEPGDWILAFDCSTQCEALADQWWRLHRALGREAPRVSRLRIGGDGPALPGESVAQWTHTPEWHSPGRVWLVDPRGEAVLTYAREVELRGVMDDISHLLRMNPEKRAAPELEVGNR
>NZ_CP014226.1|WP_083517639.1|3530910_3531720_-|SURF1-family-protein
MSYSIKGQGAGGKGMPTMRLPGWRLGLWCVLWSLLVALGLALGLWQWERADDKRDYLANLDAAPTLEAPLTAPPDGTRLTLRGEYQADDTLFLDNRTLNGQVGVAALTPLRTEDGRLWLVQRGFMATGPVRETPEVDTPQGQVTLKGRWQEVGDSGPLYGPNREGLRLQQMDLAAWSQSPGFAHDGWLHLEEGGGLLEPWWEPSVMPPERHVGYAVQWWGLALAALVMMIVGGRRLARDRRARFASDDCPPQGLEPLPKQPPTEPPKEG
>NZ_CP014226.1|WP_066451713.1|3531718_3531916_+|DUF2909-domain-containing-protein
MLLKILIAVVFLAMVTSLAAGVGFLLRDDSQSRRLLVSLKIRVGLAALLLALLFYGFYFGDLGTA
>NZ_CP014226.1|WP_066451715.1|3532014_3532872_-|cytochrome-c-oxidase-subunit-3
MSGSYYVPATSKWPVLGSLALGMMMVGTGMVLVHGRGTLIMLLGLAGVVAVMALWFRDVVVESRSGLYDAQMDRSFRWGMGWFIFSEVMFFAAFFGALFYVRMFAIPWLGGEGTKGPTALLWPEFTAHWPLLSPPDPSISGPAQVFSPWHLPLVNTLILISSSITLTVAHEALKEGHRKICRNWLAGTVLLGLTFIVIQGVEYYEAYAHYGITLEAGIYGATFFILTGFHGVHVIVGTLILIVMLVRVMKRHFSPEEHFGFEASCWYWHFVDVVWVGLFLFVYVF
>NZ_CP014226.1|WP_066451717.1|3532868_3533462_-|cytochrome-c-oxidase-assembly-protein
MSRNETDTQEVRVRRTVWRSVAALVGMFAFAFALVPLYDVFCRVTGINGKVDTNAQALVHDDVDDSRMVTVQFITRNGSGLPWRMEVETRQVRIHPGQTSEVNFSFNNQSSGESWGRAVPSVSPSTATRHVRKASCFCFEEQRLEAGERLELPLVFQLDRDLPPEINTVTLVYTLYPVEGKKAPLQAAAKTIEGDEA
>NZ_CP014226.1|WP_066451720.1|3533497_3535135_-|cytochrome-c-oxidase-subunit-I
MAPKVPPQPTLEQSSTAAEAGHGHAHAAPPKGLMRWLLTTNHKEIGSLYLIFSLVMFFIGGIFALVVRLELFQPGMQFVNPEFFNQMTTMHGLIMVFAAVMPAFTGLANWMIPLQIGAPDMALPRLNNFSFWLLPVAFGLLLSTLFMPGGGPNFGWTFYAPLSTTYAPPSTTFFILALHIAGISSILGAINIVATILNMRAPGMRMMDMPLFVWTWLITGFLLIAVMPVLAGVITMMLMDINFGTSFFNAAGGGDPVLFQHLFWFFGHPEVYIMILPAFGIVSAIIPAFARKRLFGYASMVYATAAIALLSFMVWGHHMFVVGMPLAGQLFFMYATMLIAVPTGVKVFNWIATLFQGSISFEPPMLFALAFVVLFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFAIMAGVYFWLPKWTGHYPNERLSQWHFWLSVIGVNLTFFPMHFSGLAGMPRRIPDYALQFADFNMVSSIGAFMFGFSQLLFVAVVIMCVRGGKKAPAAAWGDYADDLEWSVPSPAPLHTFETPPNYQRPAH
>NZ_CP014226.1|WP_066451722.1|3535208_3536327_-|cytochrome-c-oxidase-subunit-II
MRTLLVWLAGGLSLVGSSQAALASGWNMPVGVTDLSREIYNLHMAIFWICVVIGVVVFGVMFYSLIRYRHSKGAKAANFHENTTVEVIWTAVPLLILVGMAIPATATLQKIYDPSDAELDVMVTGQQWRWRYEYLGEDVAFNSNLATPRTQIRGDEVRGENYLLEVDEPLVLPINRKVRFLFTSDDVIHAWWVPDFAVKQDTIPGFISENWVRINEPGIYRGQCAELCGVDHAFMPIVVHAMEEDDFETWLAERKEMAAEEALGVDRDWEMDELMERGEAVYGSICASCHQVEGQGSPPAFPALAGNEQMLDDIDWHKDVIINGVSGTAMPSFRTTLNPVELAAVITYTRNAWGNDTGDAVQPAEIAERLER
>NZ_CP014226.1|WP_083517640.1|3536520_3536694_-|DUF2970-domain-containing-protein
MWKVVKSVLAAFLGVQKEQQRREDFEKGNPMAFILVGIIMALLFVGVIAVVAIWAAG

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Crispr_ID: NZ_CP014226_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP014226_4

3549533-3549616

Orphan

Consensus_repeat	Method
CTCCTCCGAGGCGCCTACCGGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP014226_4

>merge|NZ_CP014226|4|3549533-3549616|CRISPRCasFinder
CTCCTCCGAGGCGCCTACCGGCGGCGTTGCCGACGTTCGCGGCCATCACTTGCGTTTCAACCTCCTCCGTGGCGCCTACCGGCG

>NZ_CP014226|4|4|3549533-3549616|CRISPRCasFinder
CTCCTCCGAGGCGCCTACCGGCG	GCGTTGCCGACGTTCGCGGCCATCACTTGCGTTTCAAC
CTCCTCCGTGGCGCCTACCGGCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP014226.1\|WP_066451750.1\|3552888_3553617_-\|C-type-lysozyme,-inhibitor	unknown	unknown	gnl\|CDD\|226176
NZ_CP014226.1\|WP_066451747.1\|3549850_3550861_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372012
NZ_CP014226.1\|WP_066451752.1\|3553727_3556028_-\|5-methyltetrahydropteroyltriglutamate---homocysteine-S-methyltransferase	unknown	unknown	gnl\|CDD\|235367
NZ_CP014226.1\|WP_066451738.1\|3547530_3548247_+\|nucleotidyl-transferase-AbiEii/AbiGii-toxin-family-protein	unknown	unknown	gnl\|CDD\|378065
NZ_CP014226.1\|WP_144439741.1\|3540607_3542560_-\|HAMP-domain-containing-protein	unknown	unknown	gnl\|CDD\|185001
NZ_CP014226.1\|WP_144439691.1\|3551145_3552480_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224511
NZ_CP014226.1\|WP_066451737.1\|3547321_3547534_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP014226.1\|WP_158509955.1\|3543652_3543796_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP014226.1\|WP_066451733.1\|3543068_3543368_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP014226.1\|WP_083517643.1\|3559719_3562614_+\|ribonucleoside-diphosphate-reductase-subunit-alpha	unknown	unknown	gnl\|CDD\|235966
NZ_CP014226.1\|WP_066451739.1\|3548418_3548631_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|140300
NZ_CP014226.1\|WP_066451735.1\|3545514_3546309_-\|glycosyl-transferase	unknown	unknown	gnl\|CDD\|226297
NZ_CP014226.1\|WP_066451743.1\|3549174_3549501_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|213767
NZ_CP014226.1\|WP_066451762.1\|3562687_3563938_+\|ribonucleotide-diphosphate-reductase-subunit-beta	unknown	unknown	gnl\|CDD\|235968
NZ_CP014226.1\|WP_066452416.1\|3543971_3544418_+\|CAP-domain-containing-protein	unknown	unknown	gnl\|CDD\|349398
NZ_CP014226.1\|WP_066451757.1\|3558668_3559382_-\|response-regulator	unknown	unknown	gnl\|CDD\|236738
NZ_CP014226.1\|WP_066451756.1\|3557030_3558665_-\|HAMP-domain-containing-protein	unknown	unknown	gnl\|CDD\|236724
NZ_CP014226.1\|WP_066451764.1\|3564216_3564525_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP014226.1\|WP_066452417.1\|3546479_3547007_+\|DUF1269-domain-containing-protein	unknown	unknown	gnl\|CDD\|274763
NZ_CP014226.1\|WP_066451753.1\|3556129_3557044_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176132

Protein	Function_ID	Function_description	E-value
NZ_CP014226.1\|WP_066451750.1\|3552888_3553617_-\|C-type-lysozyme,-inhibitor	gnl\|CDD\|226176	COG3650, COG3650, Predicted membrane protein [Function unknown].	1.50964e-08
NZ_CP014226.1\|WP_066451747.1\|3549850_3550861_+\|hypothetical-protein	gnl\|CDD\|372012	pfam12281, NTP_transf_8, Nucleotidyltransferase. This is a family of bacterial proteins that have a nucleotidyltransferase fold. The fold-prediction is backed up by conservation of three highly characteristic sequence motifs found in all other nucleotidyl transferases: i) pDhDhhh(h/p), where p is a polar residue and h is a hydrophobic residue; ii) upstream of the first, a GG/S; iii) a conserved D/E in a hydrophobic surround. In the classification of nucleotidyltransferases proposed in this is a group XVIII NTP-transferase. Many of these sequences were classified in the COG database as COG5397. The exact function is not known.	1.34595e-39
NZ_CP014226.1\|WP_066451738.1\|3547530_3548247_+\|nucleotidyl-transferase-AbiEii/AbiGii-toxin-family-protein	gnl\|CDD\|378065	pfam08843, AbiEii, Nucleotidyl transferase AbiEii toxin, Type IV TA system. This family was recently identified as belonging to the nucleotidyltransferase superfamily. AbiEii is the cognate toxin of the type IV toxin-antitoxin 'innate immunity' bacterial abortive infection (Abi) system that protects bacteria from the spread of a phage infection. The Abi system is activated upon infection with phage to abort the cell thus preventing the spread of phage through viral replication. There are some 20 or more Abis, and they are predominantly plasmid-encoded lactococcal systems. TA, toxin-antitoxin, systems on plasmids function by killing cells that lose the plasmid upon division. AbiE phage resistance systems function as novel Type IV TAs and are widespread in bacteria and archaea. The cognate antitoxin is pfam13338.	2.95007e-09
NZ_CP014226.1\|WP_144439741.1\|3540607_3542560_-\|HAMP-domain-containing-protein	gnl\|CDD\|185001	PRK15041, PRK15041, methyl-accepting chemotaxis protein.	5.12398e-72
NZ_CP014226.1\|WP_144439691.1\|3551145_3552480_+\|hypothetical-protein	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	0.00106555
NZ_CP014226.1\|WP_066451752.1\|3553727_3556028_-\|5-methyltetrahydropteroyltriglutamate---homocysteine-S-methyltransferase	gnl\|CDD\|235367	PRK05222, PRK05222, 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional.	0
NZ_CP014226.1\|WP_083517643.1\|3559719_3562614_+\|ribonucleoside-diphosphate-reductase-subunit-alpha	gnl\|CDD\|235966	PRK07207, PRK07207, ribonucleoside-diphosphate reductase subunit alpha.	0
NZ_CP014226.1\|WP_066451739.1\|3548418_3548631_+\|hypothetical-protein	gnl\|CDD\|140300	PTZ00274, PTZ00274, cytochrome b5 reductase; Provisional.	0.00482566
NZ_CP014226.1\|WP_066451735.1\|3545514_3546309_-\|glycosyl-transferase	gnl\|CDD\|226297	COG3774, OCH1, Mannosyltransferase OCH1 and related enzymes [Cell envelope biogenesis, outer membrane].	2.19931e-46
NZ_CP014226.1\|WP_066451743.1\|3549174_3549501_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|213767	TIGR03070, couple_hipB, transcriptional regulator, y4mF family. Members of this family belong to a clade of helix-turn-helix DNA-binding proteins, among the larger family pfam01381 (HTH_3; Helix-turn-helix). Members are similar in sequence to the HipB protein of E. coli. Genes for members of the seed alignment for this protein family were found to be closely linked to genes encoding proteins related to HipA. The HibBA operon appears to have some features in common with toxin-antitoxin post-segregational killing systems. [Regulatory functions, DNA interactions].	1.60702e-08
NZ_CP014226.1\|WP_066451762.1\|3562687_3563938_+\|ribonucleotide-diphosphate-reductase-subunit-beta	gnl\|CDD\|235968	PRK07209, PRK07209, ribonucleotide-diphosphate reductase subunit beta; Validated.	0
NZ_CP014226.1\|WP_066452416.1\|3543971_3544418_+\|CAP-domain-containing-protein	gnl\|CDD\|349398	cd05379, CAP_bacterial, Bacterial CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins. Little is known about bacterial and archaeal members of the CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Studies of eukaryotic proteins show that CAP domains have several functions, including the binding of cholesterol, lipids and heparan sulfate. This group includes Borrelia burgdorferi outer surface protein BB0689, which does not bind to cholesterol, lipids, or heparan sulfate, and whose function is unknown.	4.41399e-38
NZ_CP014226.1\|WP_066451757.1\|3558668_3559382_-\|response-regulator	gnl\|CDD\|236738	PRK10701, PRK10701, DNA-binding transcriptional regulator RstA; Provisional.	4.34643e-87
NZ_CP014226.1\|WP_066451756.1\|3557030_3558665_-\|HAMP-domain-containing-protein	gnl\|CDD\|236724	PRK10604, PRK10604, sensor protein RstB; Provisional.	1.40005e-74
NZ_CP014226.1\|WP_066452417.1\|3546479_3547007_+\|DUF1269-domain-containing-protein	gnl\|CDD\|274763	TIGR03750, hypothetical_protein, conjugative transfer region protein, TIGR03750 family. Members of this protein family are found occasionally on plasmids. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition. [Mobile and extrachromosomal element functions, Plasmid functions].	0.00523115
NZ_CP014226.1\|WP_066451753.1\|3556129_3557044_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176132	cd08441, PBP2_MetR, The C-terminal substrate binding domain of LysR-type transcriptional regulator metR, which regulates the expression of methionine biosynthetic genes, contains type 2 periplasmic binding fold. MetR, a member of the LysR family, is a positive regulator for the metA, metE, metF, and metH genes. The sulfur-containing amino acid methionine is the universal initiator of protein synthesis in all known organisms and its derivative S-adenosylmethionine (SAM) and autoinducer-2 (AI-2) are involved in various cellular processes. SAM plays a central role as methyl donor in methylation reactions, which are essential for the biosynthesis of phospholipids, proteins, DNA and RNA. The interspecies signaling molecule AI-2 is involved in cell-cell communication process (quorum sensing) and gene regulation in bacteria. Although methionine biosynthetic enzymes and metabolic pathways are well conserved in bacteria, the regulation of methionine biosynthesis involves various regulatory mechanisms. In Escherichia coli and Salmonella enterica serovar Typhimurium, MetJ and MetR regulate the expression of methionine biosynthetic genes. The MetJ repressor negatively regulates the E. coli met genes, except for metH. Several of these genes are also under the positive control of MetR with homocysteine as a co-inducer. In Bacillus subtilis, the met genes are controlled by S-box termination-antitermination system. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	9.34109e-120

>NZ_CP014226.1|WP_066451743.1|3549174_3549501_+|helix-turn-helix-domain-containing-protein
MKRHSLSPDEREEKLIEATRRLVAGEISEGDLLRLLRRDVLGLTQNDYARLVGISRRTLSDMEGDKGNVTLEVMNRAFRPLGLKVCLMPRQPALLEKVMEKEPDNTKE
>NZ_CP014226.1|WP_066451739.1|3548418_3548631_+|hypothetical-protein
MLPRLAVIPTAAASAKAPAGASRDAEQRSNSNPLHQRNHAAVGGSFSSRLEAEGLPAVLPMVATTANVSD
>NZ_CP014226.1|WP_066451738.1|3547530_3548247_+|nucleotidyl-transferase-AbiEii/AbiGii-toxin-family-protein
MMYRRAHHRAIGQLLTHFDGDFLSANNILFGGGTRIALELHEFRESVDIDLFCIGRSAYRAARSAITPHSFGPLLLPGHTLALLNDREIRADRDAIRALLEGPGHPIKLEIIHFDNEAIKPDPRSQLFPIPFVGKEGCFATKLTANADRYMNHSKDILDLCMMRREWGEIPEAAWKIACEDYGEGVILRGLRGALSRVVANQHVVLEHATTSLQIEQALAQELISTEAPEWLSKLGLH
>NZ_CP014226.1|WP_066451737.1|3547321_3547534_+|hypothetical-protein
METTLINRHRYPELDLILWDRAETFVEPDVAFRLYEERWRFVDQDRLEQEEQELILQLKKAYGHGHMLVA
>NZ_CP014226.1|WP_066452417.1|3546479_3547007_+|DUF1269-domain-containing-protein
MMQRLYFLIPDKETTSVVVDELHSMGLTKDELHVMGKDWRPLEKEGVPVATLIQTSDVVNASKRGAIAGAVLGLILGLIAHYIILDTNIVWITLGMIVFGALFGVFASTLVGVSVRDVKVGKYDKAIKRGSMLLIIDVPEAREEEFRNTIKRHHPEVIIDKISTKDQKQNVPEGH
>NZ_CP014226.1|WP_066451735.1|3545514_3546309_-|glycosyl-transferase
MKNIGVLAFARFLKLLANTTKVAAYGFHYLFPDKRFIIPERAPPLWRSRRSSRIPRTLWQTNFTNRATLPVYLNYLCNRLLAPCYEYRFLITEDRASFIEANFSPEIFAAYSRLQVGAAQADYWRVLVLHKRGGVYLDIDAHVVWPLDRIVKPAFDELFIATKRGEISNYFIASAPNNPHLQRVAEAIRENIEDDSEKNIFELTGPGVFNKVLSRDAVRTRLYRYTCNQGNFTNEHFQYIDKPEGKWTRQQQQIDVVRKLEPGE
>NZ_CP014226.1|WP_066452416.1|3543971_3544418_+|CAP-domain-containing-protein
MLHAGECEPDARQQAMLERVNEARSEDRQCGDDAYKATQSLAWSCRLEEAAEAHSQDMAKNEFFGHTDAEDVGVNERVNDTGYDWMAVGENIAAGQADVAEVIEGWLSSPGHCANIMSDQFTEMGAAVVEAEDSEYSPFWTQVFARPR
>NZ_CP014226.1|WP_158509955.1|3543652_3543796_+|hypothetical-protein
MKRILEHAAAWLLRVMESHETRQPQTQHAWCCYRADRNYPPGDNRRH
>NZ_CP014226.1|WP_066451733.1|3543068_3543368_+|hypothetical-protein
MKRINYSQQGIEIELVLTRDPFNCEWLAVARWEASPGAIASLHSMPAIRATASEADAWDTAKEWANRLVMEEWLNSTDLAAVTPTGTHTGYVMRCTHLP
>NZ_CP014226.1|WP_144439741.1|3540607_3542560_-|HAMP-domain-containing-protein
MSGKFILVLALPVLAMLWFAGIGILERQQLATNMTELSELAELSADAGNLVHELQRERGMSVGYIGSGGNSFGNRLSAQHPHTDLAIQALQNTLSEMDIASIDEAFAQRASVMESQLATVADMRRQVLDLSANSDRATTFYTEFNEALITMIGRIAHLAEDDDITLQLGAYVSLLKAKDLAGIERAMLTNAFSINVMAGSTYQRMMTLFGRQEAYQDSFHSMANAEQRELLDSLLSGPEMERLAEMRQVAIDRGVQGFFGIDSEAWFDQQTLKLDRMKEVEDAVSANVLNEASVLRNDARRDLTGFLLMAAIAGFAALVLSLLVVRSLLRPLHHNLQDIQERGGDLTRRLDVPGSDELSRLYAAFNKASDEMEALVGNIQNNALSVEVASGEISQGNQDLAQRTEEQSASLVETATSMEQITATVRNTADNARQAETMTGEVSQETSDATGVAERASQAMQQIYTANQEVTSIVAAIDSIAFQTNLLALNASVEAARAGEHGRGFAVVAQEVRKLAGRSAEEAEQIRRLVDNNVARISEGESLVNETTTALETIAVKVTQVADLVRDMSAATGEQSAGIEQINQAVSQLEEVTQQNAALVEQVAAASRSLDDQAGDMAKLMRRFKVTTMGGAILHRRQHQLTSVDEPAFG
>NZ_CP014226.1|WP_066451747.1|3549850_3550861_+|hypothetical-protein
MSYQRLQPEQSRVAVNAIQLFEALEQHRGQARQVKGSMHWKRIHGREYLYRAYTGGKNHSLGPRSAETEAIREAFDTRKAEHQAREQSLKEQLQLHAAYIRANRLNRFPVAGARVIRALQRRNLPFRIIGTNALYAYEARAGVRIEPEHLATADMDVLMDARQGLRIVTALEGETLLSVIRSSDRSFEPLTDTPYEFRAANAQGYMIDLITQAAEVMAMNDFEHHLEAGDLKPVGIDSLKWAIASPRFEAVVFDERGMPLRLSTVDPRAFVLHKHYVSQRSDREPIKRHRDEAQAQLIATLLGNELRELSTTLAVERAFPHLVRQQASTRFDDFDV
>NZ_CP014226.1|WP_144439691.1|3551145_3552480_+|hypothetical-protein
MASNHNAPTHPASADSASLDTLIGGCIEGDITAFEHLASACLPGLLGVSAGFLEQPEHHEAVCRDTLVLAWRNLSEPGSNTAPSVWLYGIFASRLYNQLLALHGSQQAMRRRVDALEAEHSTTVDSPTGPRPALLSGTRLLALSHQVPSVAPSPLLLAELNERISAEIAQRNAPLTPTGERVYPPLYDPALRYRMFRSRAAFQIKEGFKRRLGRPFEDQWFERWLNKKAGSALLESQGLPRRSIEAHLGGRLDLEIDPNALSRGMDFPASFPNRTQRRKISNQFIWPGDWDLKTPALADTQRQKFIRDLWSHRLDLTASDSYNRLLNRVELGGALRMHHHGILLDSESRIHAYLERYLLFMEDMSCFGYKANLGKDTLGIAIDRHGGMVKVNKGLHRLAMAQILGIQRVTVRVRAVHQLWWEQHKGSEQGKRALENVTAALPHR
>NZ_CP014226.1|WP_066451750.1|3552888_3553617_-|C-type-lysozyme,-inhibitor
MTLFGLSSFRPALLAAASLLLVGCAATPVDGPRPGTGQVASTAPLLPSMLFPGGAERFEAWRCTPQQDLVTAFGERELRLWSAHGAYRLAPAVVASGARYQQGDLSFWNKGGDAVVESANGRLDCSADMARSPLTREQRPGVMFHGRGNEPGWHVNLAHDTPELTLTLDYGARELTLPYRVTAMDNAQGRVSLASGLTDQPFELWLEARACFDDMSGEPFPARVTLTIDGETLRGCGQGIAP
>NZ_CP014226.1|WP_066451752.1|3553727_3556028_-|5-methyltetrahydropteroyltriglutamate---homocysteine-S-methyltransferase
MTLAHISGYPRIGGGRELKHAVEAYWRGESDREALESTGRELRRSHWQVQREAGLDLVTVGDFAFYDHVLNVSTLLGAVPPRFAAEEEVVAGDVDLDTTFRMARGRAPSGEPAAACEMTKYFDTNYHYLVPELHAGQRFQLASSRLFDEVAEARDAGHPVKVVLTGPLTWLWLAKEKGDEAFDRLSLLDALLPVYGEILARLADQGVTWVQLDEPALVQDLPREWKQAFESAYNTLRNAPVKLMVASYFGGLGDNLQLAVSLPVDGLHIDVVRDPGQLTTVIDNLPGYKVLSVGAIDGRNIWRADLAVLRERLASARMRLGERLWVAPSCSLLHVPVDLDAEPDLDEELRSWFAFARQKLDETVTLSRLLGNRATAEDRARLEAATAALDARRESPRIHKPAVAERLAAIAEGDTRRAGAYPERARQQRRALDLPLFPTTTIGSFPQTAEIRAARRAFKAGELGRDEYEARMRDEIADAVVRQERLGIDMLVHGEAERNDMVEYFGEQLEGYVFTRFGWVQSYGSRCVKPPVIVGDVARPAAMTVRWSEYAQTLTDRPMKGMLTGPVTMLQWSFVRDDQPRSTTCRQIALALRDEVADLEAAGIPAIQIDEPALREGLPLRRGEWPAYLDWAVACFRLTAAVARDATQIHTHMCYSEFNDIIAAIAALDADVITIETSRSDMELLDVFQDFAYPNEIGPGVYDIHSPNIPQVDWMVQLMEKAAERIPAERLWVNPDCGLKTRGWAEVEPALAHMVEAARELRRRHG
>NZ_CP014226.1|WP_066451753.1|3556129_3557044_+|LysR-family-transcriptional-regulator
MLELRHLRTLIALRDAGSLVEAAERVHLTQSALSHQIKDLEERLGSQLFVRKSRPVEFTRAGQRLLALAEQVLPLVRMAERDLARLVGHEPGRLHMAIECHSCFQWLMPTIDHFRDHWPEVEIDIPGGHHFDPLPALAREQLDLVITADPQTLPGVYYEPLFRYQGLLAVARQHPLADRSFVVPQDLAEETLITYPVEHSRLDVFTQFLNPAGVRPRELRTAELTIMMMQLVASGRGVCALPNWALTEYLERDYVKAVALGEEGMWSTLYAAIREESRDQPWMEDFLRTARETSFAVLEGIRPA
>NZ_CP014226.1|WP_066451756.1|3557030_3558665_-|HAMP-domain-containing-protein
MQRFLADGTFLRVYLALAMALLLTFGLALMGLALVDRVRIEQYREQLAEAPLQLLTRKVAALPANERGDWLTQQSDRLDMRLSLRSPDDAGLGWFERRRLERGSVLVKPEEGANWRLYRRIAGEYRVLEARLSGLNERQLRGLAQMLGDWLAEEEGEARQRRLANVTTPALPIHLSDLAPEGLDSHQLSRLREGELVIRLLPGHWALTVYLAVPVQDGGRQWLSIGPVSALEPTPISLLLLVLVIMLAVLAAIIYLIVRGVEARLARLELAAGRIASGRLDTRVKVDGGGFIGRVGMAFNAMAAQVQSLLRSQQEMIRAVSHELRTPVARIRFAVQMVEDMTDDPAVHRQLQGIDGDIEELDQLIDEILTYARLDSGIVNGAELQRTVVDCRAMAQRVLETLAPLHAHLRLELAPGPEVETLADSRYLQRALQNLVANACRHARSHVLVRLTVEARLVRLDIEDDGPGVPESERQVIFKPFARLDDSRTRRSGGYGLGLSIVQKIMVWHGGSVVVDDSQELGGARFSLLLPKPKEIERLSVKPA
>NZ_CP014226.1|WP_066451757.1|3558668_3559382_-|response-regulator
MEHNLESSDMEHVLIIEDDVRLAELTRDYLEANGFQVTVEAEGSRGVEQIQALQPDLVILDLMLPGEDGLSICRRARPDYSGPILMLTARTDDMDQVLGLEMGADDYVPKPVQPRVLLARMRALLRRADNTEQGGDIRLSFGNLDIDSATREAWLEGDRIDLTSAEFDLLWLLASNAGRVLTREEIFSDLRGIKYDGQDRSIDVRVSRIRPKIGDDPNHPHRIKTVRSKGYLFVKDA
>NZ_CP014226.1|WP_083517643.1|3559719_3562614_+|ribonucleoside-diphosphate-reductase-subunit-alpha
MEQLQTPDAASLSITAPQTLRVIKRNGDVAVFDVSKIAVAMSKAFIAVEGDNAATSSRVRDFVAEASRTIAETFQRRMPDGGTVHIEDIQDQVELALMRAGEQKVARAYVLYREAHARARAAAGDDIEKPHPTLNVTALDGSRRPLDLGRIETLVFDACAELANVDPNRIVEEALKNLYDGVTVDGVSQALMMTARTLVEKDPNYTYVTARLLQDNLRREALSFLGVAEEATFGEMAELYKPAFHAYVARGIEFEQLDPRLAEFDLERLGDALDHTRDNAFTYLGLQTLYDRYFIHKDDVRYELPQVMFMRVAMGLSLNEDDREGRAIEFYELLSSFDYMASTPTLFNAGTLRSQLSSCYLTTVPDNLDGIYSAIRDNALLSKWAGGLGNDWTPVRALGSYIKGTNGKSQGVVPFLKVVNDTAVAVNQGGKRKGAVCAYLETWHLDVEEFLDLRKNTGDDRRRAHDMNTANWVPDLFMKRVFDDKEWTLFSPSNCPDLHDLYGAAFEKRYEEYEAMTYSGQLKLYKRVRAKDLWRKMLSMLFETGHPWITFKDPCNLRSPQQHAGVVHSSNLCTEITLNTSVDEIAVCNLGSINLAQHVTDGQLDNEKLGKTVRTAVRMLDNVIDINYYAVPQARNSNFKHRPVGLGIMGFQDALYALGIAYASDGAIEFADRSMELVSYHAIEASSDLAAERGRYESFDGSLWSQGVLPIDSIEKLRVERGEQYIEVDTSSTQDWGRIRNKVVKQGMRNSNVMAIAPTATISNICGVTQSIEPTYQNLYVKSNLSGEFTVVNAFMVNDLKERGLWDEVMINDLKYYDGSVQPIDRVPDDLKAKYASAFEVEPKWLVEAASRRQKWIDQAQSLNLYIKGVSGKKLDVTYRMAWFRGLKTTYYLRALGATSVEKSTVERGTLNAVSNGGAPKPTPAAPAASEPRGIEDFLSGKAGSGSRAPSASEIDDLGCEACQ
>NZ_CP014226.1|WP_066451762.1|3562687_3563938_+|ribonucleotide-diphosphate-reductase-subunit-beta
MLNWDEFNEDETAVADKPAPATPAPAAKAQPSAPADAGEIQEASGNYVIAEADRIERARKSLEELDVAAGLEELEMGAARIEVSDKQMINARADLNQLVPFKYEWAWQKYLDGSANHWMPQEVNMNADIALWKSQEGLTADERRIVERSLGYFSTADSLVANNLVLALYRLITNPECRQYLLRQAFEEAIHTHAYQYCVESLGMDEGAVFNMYREVPSVAAKSAWSLKHTQSLARSDFNTGTPETDQELLRNLVAFYCVTEGIFFYCGFSQILSMGRRNKMTGVAEQFQYILRDESMHLNFGVDMINQIKIENPHLWTPEFQDEVTQMILEGTELEIAYARDTMPRGVLGMNAAIMEEYLRFICNRRLAQIGLKEQYPGAQNPFPWMSEIIDLRKEKNFFETRVTEYQVGGALSWD
>NZ_CP014226.1|WP_066451764.1|3564216_3564525_+|hypothetical-protein
MHPTRSVEARRDPQAWQTALDRALAAHESEDALAHYPHVAFAFPSSSPNPYSGDYPLLNYREPKEWAPTRGWRGRPAPDRAPAGEKYSPPVRFTRGKAWSSH

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP014226_2	2.1\|2166134\|30\|NZ_CP014226\|CRISPRCasFinder	2166134-2166163	30	NZ_CP014226.1	1650276-1650305	2	0.933

1. spacer 2.1|2166134|30|NZ_CP014226|CRISPRCasFinder matches to position: 1650276-1650305, mismatch: 2, identity: 0.933

tgttctttcatgccacggcggcctccgcca	CRISPR spacer
tgttctttcatgccattgcggcctccgcca	Protospacer
***************. *************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP014226_2	2.1\|2166134\|30\|NZ_CP014226\|CRISPRCasFinder	2166134-2166163	30	NC_012811	Methylorubrum extorquens AM1 megaplasmid, complete sequence	371719-371748	6	0.8
NZ_CP014226_2	2.1\|2166134\|30\|NZ_CP014226\|CRISPRCasFinder	2166134-2166163	30	NZ_CP029452	Sinorhizobium fredii CCBAU 25509 plasmid pSF25509b, complete sequence	1995085-1995114	7	0.767
NZ_CP014226_2	2.1\|2166134\|30\|NZ_CP014226\|CRISPRCasFinder	2166134-2166163	30	NZ_CP006372	Aureimonas sp. AU20 plasmid pAU20e, complete sequence	41731-41760	8	0.733

1. spacer 2.1|2166134|30|NZ_CP014226|CRISPRCasFinder matches to NC_012811 (Methylorubrum extorquens AM1 megaplasmid, complete sequence) position: , mismatch: 6, identity: 0.8

tgttctttcatgccacggcggcctccgcca	CRISPR spacer
cgctccgtcaggccacggcggcctccgcct	Protospacer
.*.**. *** ******************

2. spacer 2.1|2166134|30|NZ_CP014226|CRISPRCasFinder matches to NZ_CP029452 (Sinorhizobium fredii CCBAU 25509 plasmid pSF25509b, complete sequence) position: , mismatch: 7, identity: 0.767

tgttctttcatgccacggcggcctccgcca	CRISPR spacer
gcgaccttcatgccacggccgccgccgcca	Protospacer
    *.************* *** ******

3. spacer 2.1|2166134|30|NZ_CP014226|CRISPRCasFinder matches to NZ_CP006372 (Aureimonas sp. AU20 plasmid pAU20e, complete sequence) position: , mismatch: 8, identity: 0.733

tgttctttcatgccacggcggcctccgcca	CRISPR spacer
tgttcgttcatgccacggcggagctggtcc	Protospacer
***** ***************  .. *.*

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site	Prophage annotation

Anti-CRISPR protein detection

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