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_CP043808	Serinicoccus marinus DSM 15273 chromosome, complete genome	9 crisprs	cas3,DEDDh,DinG,PD-DExK,WYL,cas4,csa3	1	1	3	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP043808_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043808_1

236353-236455

Orphan

Consensus_repeat	Method
CGGAGGCATACCCGAGCGCCGGCGAGCCGACCCATGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043808_1

>merge|NZ_CP043808|1|236353-236455|CRISPRCasFinder
CGGAGGCATACCCGAGCGCCGGCGAGCCGACCCATGAGGCCGGTGGTCACGTCGCGGAGGCGCAGGCGGAGGCATACCCGAACGCCGGCGAGCCGACCCATGA

>NZ_CP043808|1|1|236353-236455|CRISPRCasFinder
CGGAGGCATACCCGAGCGCCGGCGAGCCGACCCATGA	GGCCGGTGGTCACGTCGCGGAGGCGCAGG
CGGAGGCATACCCGAACGCCGGCGAGCCGACCCATGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043808.1\|WP_022923263.1\|220164_221181_-\|UDP-glucose-4-epimerase-GalE	unknown	unknown	gnl\|CDD\|187558
NZ_CP043808.1\|WP_028130715.1\|222003_222486_+\|nucleoside-deaminase	unknown	unknown	gnl\|CDD\|238612
NZ_CP043808.1\|WP_022923252.1\|234484_235732_-\|3-hydroxyacyl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|236211
NZ_CP043808.1\|WP_149814472.1\|223423_223717_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_022923247.1\|239203_240148_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_022923258.1\|223922_224642_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213222
NZ_CP043808.1\|WP_022923260.1\|222482_223250_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|237189
NZ_CP043808.1\|WP_022923256.1\|225819_228612_-\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|225669
NZ_CP043808.1\|WP_022923262.1\|221230_221833_-\|RDD-family-protein	unknown	unknown	gnl\|CDD\|377640
NZ_CP043808.1\|WP_022923246.1\|240247_241948_+\|phenylacetic-acid-degradation-protein-PaaN	unknown	unknown	gnl\|CDD\|143445
NZ_CP043808.1\|WP_052327709.1\|242367_242826_+\|NUDIX-hydrolase	unknown	unknown	gnl\|CDD\|239217
NZ_CP043808.1\|WP_022923243.1\|243897_244623_-\|purine-nucleoside-phosphorylase	unknown	unknown	gnl\|CDD\|180275
NZ_CP043808.1\|WP_022923250.1\|236580_237378_+\|MerR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133382
NZ_CP043808.1\|WP_022923248.1\|238283_239042_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|377658
NZ_CP043808.1\|WP_022923244.1\|242844_243867_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_CP043808.1\|WP_149814476.1\|246779_247445_-\|glycosyltransferase-family-1-protein	unknown	unknown	gnl\|CDD\|340817
NZ_CP043808.1\|WP_022923255.1\|228608_232250_-\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|274576
NZ_CP043808.1\|WP_168714892.1\|237780_238263_+\|AraC-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|378964
NZ_CP043808.1\|WP_033418355.1\|234038_234455_-\|hotdog-fold-thioesterase	unknown	unknown	gnl\|CDD\|131339
NZ_CP043808.1\|WP_149814475.1\|246138_246786_-\|glycosyltransferase-family-1-protein	unknown	unknown	gnl\|CDD\|340817

Protein	Function_ID	Function_description	E-value
NZ_CP043808.1\|WP_022923263.1\|220164_221181_-\|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_CP043808.1\|WP_028130715.1\|222003_222486_+\|nucleoside-deaminase	gnl\|CDD\|238612	cd01285, nucleoside_deaminase, Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.	1.2688e-31
NZ_CP043808.1\|WP_022923252.1\|234484_235732_-\|3-hydroxyacyl-CoA-dehydrogenase	gnl\|CDD\|236211	PRK08268, PRK08268, 3-hydroxy-acyl-CoA dehydrogenase; Validated.	8.03234e-136
NZ_CP043808.1\|WP_022923258.1\|223922_224642_-\|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.	8.92618e-98
NZ_CP043808.1\|WP_022923260.1\|222482_223250_+\|SDR-family-oxidoreductase	gnl\|CDD\|237189	PRK12748, PRK12748, 3-ketoacyl-(acyl-carrier-protein) reductase; Provisional.	2.7473e-65
NZ_CP043808.1\|WP_022923256.1\|225819_228612_-\|FtsX-like-permease-family-protein	gnl\|CDD\|225669	COG3127, COG3127, Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, permease component [Secondary metabolites biosynthesis, transport, and catabolism].	1.63424e-09
NZ_CP043808.1\|WP_022923262.1\|221230_221833_-\|RDD-family-protein	gnl\|CDD\|377640	pfam06271, RDD, RDD family. This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. This region contains two predicted transmembrane regions. The arginine occurs at the N-terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this region is unknown. However this region may be involved in transport of an as yet unknown set of ligands (Bateman A pers. obs.).	2.97221e-19
NZ_CP043808.1\|WP_033418355.1\|234038_234455_-\|hotdog-fold-thioesterase	gnl\|CDD\|131339	TIGR02286, Acyl-coenzyme_A_thioesterase_PaaI, phenylacetic acid degradation protein PaaD. This member of the domain family TIGR00369 (which is, in turn, a member of the pfam03061 thioesterase superfamily) is nearly always found adjacent to other genes of the phenylacetic acid degradation pathway. Its function is currently unknown, but a role as a thioesterase is not inconsistent with the proposed overall pathway. Sequences scoring between trusted and noise include those from archaea and other species not known to catabolize phenylacetic acid and which are not adjacent to other genes potentially involved with such a pathway.	1.44076e-30
NZ_CP043808.1\|WP_022923246.1\|240247_241948_+\|phenylacetic-acid-degradation-protein-PaaN	gnl\|CDD\|143445	cd07127, ALDH_PAD-PaaZ, Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like. Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.	0
NZ_CP043808.1\|WP_052327709.1\|242367_242826_+\|NUDIX-hydrolase	gnl\|CDD\|239217	cd02883, Nudix_Hydrolase, Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of nudix hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.	6.24232e-16
NZ_CP043808.1\|WP_022923243.1\|243897_244623_-\|purine-nucleoside-phosphorylase	gnl\|CDD\|180275	PRK05819, deoD, DeoD-type purine-nucleoside phosphorylase.	3.2087e-144
NZ_CP043808.1\|WP_022923250.1\|236580_237378_+\|MerR-family-transcriptional-regulator	gnl\|CDD\|133382	cd01107, HTH_BmrR, Helix-Turn-Helix DNA binding domain of the BmrR transcription regulator. Helix-turn-helix (HTH) multidrug-efflux transporter transcription regulator, BmrR and YdfL of Bacillus subtilis, and related proteins; N-terminal domain. Bmr is a membrane protein which causes the efflux of a variety of toxic substances and antibiotics. BmrR is comprised of two distinct domains that harbor a regulatory (effector-binding) site and an active (DNA-binding) site. The conserved N-terminal domain contains a winged HTH motif that mediates DNA binding, while the C-terminal domain binds coactivating, toxic compounds. BmrR shares 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.	5.51215e-37
NZ_CP043808.1\|WP_022923248.1\|238283_239042_+\|hypothetical-protein	gnl\|CDD\|377658	pfam06441, EHN, Epoxide hydrolase N-terminus. This family represents the N-terminal region of the eukaryotic epoxide hydrolase protein. Epoxide hydrolases (EC:3.3.2.3) comprise a group of functionally related enzymes that catalyze the addition of water to oxirane compounds (epoxides), thereby usually generating vicinal trans-diols. EHs have been found in all types of living organisms, including mammals, invertebrates, plants, fungi and bacteria. In animals, the major interest in EH is directed towards their detoxification capacity for epoxides since they are important safeguards against the cytotoxic and genotoxic potential of oxirane derivatives that are often reactive electrophiles because of the high tension of the three-membered ring system and the strong polarization of the C--O bonds. This is of significant relevance because epoxides are frequent intermediary metabolites which arise during the biotransformation of foreign compounds. This family is often found in conjunction with pfam00561.	1.8129e-18
NZ_CP043808.1\|WP_022923244.1\|242844_243867_+\|alpha/beta-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	2.36098e-25
NZ_CP043808.1\|WP_149814476.1\|246779_247445_-\|glycosyltransferase-family-1-protein	gnl\|CDD\|340817	cd03784, GT1_Gtf-like, UDP-glycosyltransferases and similar proteins. This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.	1.04843e-10
NZ_CP043808.1\|WP_022923255.1\|228608_232250_-\|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.	8.48334e-06
NZ_CP043808.1\|WP_168714892.1\|237780_238263_+\|AraC-family-transcriptional-regulator	gnl\|CDD\|378964	pfam12833, HTH_18, Helix-turn-helix domain.	2.54628e-11
NZ_CP043808.1\|WP_149814475.1\|246138_246786_-\|glycosyltransferase-family-1-protein	gnl\|CDD\|340817	cd03784, GT1_Gtf-like, UDP-glycosyltransferases and similar proteins. This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.	6.20813e-29

>NZ_CP043808.1|WP_022923252.1|234484_235732_-|3-hydroxyacyl-CoA-dehydrogenase
MPESPTPPHALLSPPDQTAVAVIGAGAMGAGIAQVAAQAGHPVILVDAQPEAAERAVAGLRATFDKLVAKGKVTREDADATLGRVTPHTTADMRTIPAVVLVIEAVVEHLDVKRAIFRQLESAQPSTTVLATNTSSLSIDDIVGEAGFGHDAALHGGTSPAMAHPERVLGLHFFNPPPLMRLVEVITGADSGADVLDAASELVRRWGKMPVRCTSTPGFIVNRVARPFYGEAQRMVAEGLVDPATVDLALRGAGFRMGPFELTDLIGQDVNLAVGESVWRQTGEDPRYAPTDWQRDLVREGRLGRKTGRGVFEYADGRPVDAEPDAALAEQLVGGPVQTDPVARTLAMLVNEGVDLVHRGEASAEDVDTAMTLGTNYPHGPFAWLEQIGADTVRRQLAELDELYPGGRYRPSEAL
>NZ_CP043808.1|WP_033418355.1|234038_234455_-|hotdog-fold-thioesterase
MWDQDRASAALGIELVDVEVETTEGGRRLGRARTRMRIVDTMVNGHDIAHGGYVFTLADSTFALACNATGRTTVAASCDITYLLPSRLDDELIATATERVTYGRSGITDVTVCRATDNAVVAEFRGHSRAVRPASGER
>NZ_CP043808.1|WP_022923255.1|228608_232250_-|FtsX-like-permease-family-protein
MRWASFATARARASSGLLLTLLALVVVTTAIIAGTVGYSAAAASTAARAALTQGEPTETGVQVQTRLAEDPQRQDELARSTIADAFAPAPVSIGRLVVSEPRPTQHDGSSLEGELVVTGGPELAPGDAPTDLVTVVDGTWPADGAGDETPDTPAAGALHVGAAQAWGLEVGDVLVVADRAVEITATWQPVDAQDAFWFSDELVRTGVADEESTLGPVVVDEELARQVGAPFVRWPVQPDADAVTPDDLRVLATGAETLRAELREVEGLTVRGVQVEGDLAPTAGQAATNLATARALGVVPLSVLVLVTGLAVVQLARLLATTREPQAQLLVARGATRGQLLLSTLAESLAVTVLGAVAGTLLARLVLLLVPGSEGATTRVVLAGALTLLGVALALTAIAWLQARRLAGGQVVADRSGRARAATALATLVLVLGAAGLSWWQLRRAGSPLTRGPDGELGTDLVAGAAPALLLAAAAVVAVALLGPLSRAVELLTRRTRTTAAHLSSAQVSRRLQVYAVPVVLTVLAVGSTTLAALYSGTSAQLRDDLAAVGEGAPLRADLVRPPATVEPGVVPAPPPDLAELPEIGAAALVWSEPDARVGDVPVPLTLAQTGADGGLADVANMPQGIPGGLVPTGLDAVLDADGDAPTQQAITVPDGATEVTIDVQAERGVDRWELARLDGIAETEREIADELAEVAAESPEDEPAPEGEQPPTGASEELIVERLDSEVASASAPLEIVLTVLVEDVRTGLTSTVTAGTIELAGPRLSYDPATLGDFAAEPTSTATSLGLALPEGRQHRLRAVTVELPDTLPPEVPLDFLYSISSTTLDLDLSMRTGDVDLLEDTGGWASTDALTAEQAAPLVAEAADVEEATFETTVQVEEGYVGDEGPFVQTRTDSNEPFVPTWLDTSISPWHLEVPDTRIGGTELVVAPGAAPLDLTGSPPGAPPGSGTEDDTSASATVPVALTRQAAAAADLAAGDPMTLSLVGTTVPARVAAVVTALPGQQGETAALADSRVASLVLAEQRRSLTWPTQVWATPAAGTQEAVDSLTARDDLRAVTGPGTVSVTDATIAARLVFWVASAGAVLLALTGIAAVGATLLSSRRAEVAVLRALGMPPAAQSRSRAMELVGVVAAAIAVGLLAGWLVGQAVVPELASSTTQPGRLRLPAALRLEAAPWAAVLGVAAVGSGLLALLLGSRVRAQALDRTYREEIR
>NZ_CP043808.1|WP_022923256.1|225819_228612_-|FtsX-like-permease-family-protein
MRPRHGIPRRTGAVGLARRQFAADPWVSLGLALLVGTVGLLLTAVPRGLVDIQSRQLVQEIGGLSAAQRDLRGDWQRTVVLGSTEDLTGDPAADGWAPLVEGAERIRAGQPEPLRSTLGPAQFLVRLTEDVGYAPPVESGYYAASLSLAVDPDLTEHVELVNGDWPELVVDTPDLGIPGPQTEQEGAPAEEPDDPEPVPVLLLDDAADELLLEVGEEVQGLVVAGTYTPTNPDDPRWQHVDNGATMGTLYDPNRGESAYATAFLAPDNRGSIGSPASTRMRMWFPVLPEAITGSTGQVETLQAQVNGFLAEQHVVATADQMLDTQAAQVPLFTTDLTEALGRIVSQQRATASLLAVVAAGPLGVALAVAALGARLVVHRRRQALAMTLARGASPAQLRRVIAGEGLLLGVPAAALGHLVASVLVPGPTPWWQWVVTAAVALVPPVALAASVDDASLQQRRSDLSPRSANRWRWVVELAVVALAGVATWRLLDRGARGDDAAATGIDLLAAGTPVLIALAACVLTLRLYPLPLRALAASLRRRPALTPFLGASRALRDPAGGLVPALAVVLGTAIALVSAVLLSTVTRGAEVAAWEANGAAVRLNGPLLSEELRAEIQQIEGVAAVGGIGDTGATRDLVVDGEREAIRVWVAEPEVEEVYARSAPVPGLPPDFWRDEGIPAVVTLLGADDMVPEGATDVQVSQLGDAEVVGHRDQVPGVLVTGSGVLVDGERWEEAGGSMPDVRSTLVAVSDDASPTEVADAVTDLVGTGGVVTTVTTRLEAFEEAPVTTGLRQLFVGATVVSGLLTVLAVVVVQLMGSTARTALLATLRTLGLGTRQTRALTAWELAPLLVTSLLVGTLLGLGVPWVLLRGLDLTGLTGGSAQPALVLDLPLLGAVLGAVVLTVLIAVTVSAWIAGRTNLAQALRVGEDR
>NZ_CP043808.1|WP_022923258.1|223922_224642_-|ABC-transporter-ATP-binding-protein
MSERTAYQEQVGGSAAAVVLSGRDLHRTFGTGATQVHALAGVDLEVPAGQLTVVRGPSGSGKTTLLNLLGGLDRPTEGEVMLDDGRVLSELPEKDVLAVRRERIGYVFQSFGLVPVLSAAENVEVPLRLQRTPVGERTRRVEEALELVGLARHSRQRPYELSGGQQQRVGIARALVSDPDILIADEPTGQLDSETGAMIMDLLVRLTHERHIASVVSTHDPSLMGRADQVVELHDGRRV
>NZ_CP043808.1|WP_149814472.1|223423_223717_-|hypothetical-protein
MQGQEHPLDQPQGEGLLGRPLGGSTGRTSSSRILLVGVAALVVVGLLVGFLTDWSLSAIGLAVGASVGLVLVAVLMRRPPPTRLETREKNKTQRNRW
>NZ_CP043808.1|WP_022923260.1|222482_223250_+|SDR-family-oxidoreductase
MSRGTVLLTGVGRRRGIAAGIALALAEDDWDLTLCHWPGYDDRVGLDHGPDDAEAVATRCRELGAQVEVIAADLADPEVPERLVREANRRGDLTALVLSHAESVDSAIRTTTVESWDRHFAVNARASWLLIKALAEQLSPPVVERGAARVVALTSDHTAYNLPYGASKGALDRLVVAAAHELADLGVRANVVNPGPIDTGWMTEEIREAGIAQTPLGRLGTPQDTADLVRFLFSEQGGWITGQLLHSNGGFRTAD
>NZ_CP043808.1|WP_028130715.1|222003_222486_+|nucleoside-deaminase
MDDTDRIHLTRAVELAQAALEAGDDPFGSVLVSPQGEVLLEDHNHVGGGDHTQHPELAIARWAAQHLSPPDRAESTVYTSGEHCPMCAAAHGWVGLGRIVYASSTAQLTAWSAELGREPGPVAPLPIQELVPGAVVDGPDPELAEQVRALHARSAGGGPR
>NZ_CP043808.1|WP_022923262.1|221230_221833_-|RDD-family-protein
MSWAPPPPDRERDHLTGPTDAAPWDVPPIPAWSPTSAYGQPEDTPPTRPAPPPQLRYADWGERVAATLLDWCLLFGVLVVLGVVGGIVEPLEDLAGFAWLASLGYLAWLNGSKGQSPGKALLGLKVVREADGSPLGGFVGLVRGGLLGLLSLFTVGIFFLISVLWPFRDPKQRAVHDIAVSAVVVSGYPKAPVSPRLLKP
>NZ_CP043808.1|WP_022923263.1|220164_221181_-|UDP-glucose-4-epimerase-GalE
MRVLVTGGAGYIGSHTVIALARAGHEVVVVDDFSNSKPSVTPRLEELAGIPVPVHAFDLADGDKLDSLLGQESFDAVIHFAAFKAVGESVEKPIDYYRNNIGATLRLVEAMVTRDVPYLVFSSSATVYGEDAPVPMTEGLPTSATNPYGWTKVMNEQILRDVTHAYPQLKVALLRYFNPVGAHPSGRIGEDPSDIPNNLMPFIAQVAVGRRERLSVFGDDYDTVDGTGVRDYIHVEDLAEGHVAALEWISTHDRPLSVWNLGTGRGTSVLELVSAFERANGREIPYDVVARRPGDIASSYADPSLAESELGWRATRSVEDMCADTWRWQQANPQGYPD
>NZ_CP043808.1|WP_022923250.1|236580_237378_+|MerR-family-transcriptional-regulator
MLSIGEFARLAGVSVRMLRHYDQLGLLRPDRVDSHSGYRSYAAAQLARANQLIGLKDLGFTLEQVGVLLDGELAEGEVVALMRARRDALRAQIATDEHRLASIEARLRSIAKENPMSEFVETSLPTLTLVQRSVRIEEMSQVEEAMSGMFQQVNDLLRDTPRAGPGVATYTPQGEGMIAAAAEQIGDAPAPDGLERATVEAQPRALTVRYTGEDLSGIQRAWQGLVAEVEARGLTPHGTCREVYDVTPFDGDGAGWSVDLQQPVN
>NZ_CP043808.1|WP_168714892.1|237780_238263_+|AraC-family-transcriptional-regulator
MRDLPCDGAFVEIGGVRLPVPGYADTRALEEMVTLLHRQGVLVTDEAIAAALAGDAPAYSDRQLRRRSSAAAGMGPKQLQQLARVRAAYRLLHAGRTLAEAAVEAGYSDQAHMTRGMRAVAGTSPARILAADLDSFGSRPGEDGRIVSIARNPAGGRVEA
>NZ_CP043808.1|WP_022923248.1|238283_239042_+|hypothetical-protein
MTDTTHTTPRDAEGAAPTITQEVLDDLAQRLARTRWSTSPAPVRGMSTARLQELVRCWQEADWRSTEAWLADHGSALTTTADGRALHYLHVPGAGGAAGGLPIALLHGWPDSPLFYRRMLPLLVGAGHPVVVPSAILWLTGRSRSSIRLYSEPEVNWHADAWEEPAGDGAGSAEQSAWSGSAGGEAWKPAKVDVPTAFALFGGDLMMPPRELCERFFAVERFTLYPEGGHWPALEEPEQVVRDLLAFADGRS
>NZ_CP043808.1|WP_022923247.1|239203_240148_+|hypothetical-protein
MARAPSAAARRRAWRHEVARLLADRHSGVVRRADLIAEGLTDEDIRAEVDRGVWHRAGCHTLCIAGTEPRGEGLLWWALWESGPRAVLDGATSLVVSGLKHWEASPIDVSVPRNATVRSLPGVRHHVLRDLGPAIPVGLRRTKTDVALLRAAQWERTDRAAATLVAMTVQQRLVSTSALMDRWGGTRRCARRQLLGAVIRDVCDGSHSINELDVVAACRAHGIPAPSRQSTRTVGAGRVYLDLFWDDYGVHGEIQGAHHQWGLHGVDDAVRGNALAIDQRDLVSLQIPVLGWRLDPAVFLDQIASALRRGGWAG
>NZ_CP043808.1|WP_022923246.1|240247_241948_+|phenylacetic-acid-degradation-protein-PaaN
MATTATTHPLLDTHRETLEAATQALRERSYYSRYPESPSPRVYGEGSSERGQLAHQETLNKDFDGLAEQPTTGRSVGSEKSPYGPTLGVRYPELDVEAAMTAAQEAMPAWRDAGAEVRAAVLTEAIERINARSHEMAHAVMHTSGQPFVMSFQAGGPHAQDRALEAVVVALEEQRRVPGSVTWEKPAKGDPIRMQKDYRVVPRGVALVIGCNTFPTWNAYPGIFASLATGNPVVIKPHPRAVLPLALTTQIARETLAEAGFDPALVQLAAEDDGGTLAKDLALHDAVKIIDYTGGPGFGHWLETEAAGAGKLVYTEKAGLNTVVVDSTDDLKGMLGNLAFSFSLYSGQMCTAPQNVYVPPTVRTDEGDLSAGEFADKLGQAISRFTADDAKAVEILGATVNDDVRGRATDIPALADRLGGDVVLDSRAVAHPAYPDAVVRTPALVGVDATNDQAYTQECFGPVAFVVRTEDTADSLRRFSRTVAEHGGMTAAVYATDEEVLDDAREAAADAGVALSENLTGQIFVNQTAAFSDFHGTGANPAANAAYADAAFVANRFRVITSRRHV
>NZ_CP043808.1|WP_052327709.1|242367_242826_+|NUDIX-hydrolase
MLDATLPRKRLIAQGLLRDDAGRVLLCELTYKQDWDLPGGVVDPDESPRATLAREIREELGLELPVGDLLAVNWLPRYKQWTDALLLVFDLGVRPGVTDEAVLQRTELRALHWVEPRHLEGRVAPYVARHLASIGSGEAAGLVLEDGIPTQE
>NZ_CP043808.1|WP_022923244.1|242844_243867_+|alpha/beta-hydrolase
MRLRDVQTARTTTAVREAGDPGSPTVVLIHGNVSSSAFFDVLIEELAADFHVLAPDFRGYGDSARATIDATRGMADLSDDVAAVLDTLGVEGAVDVLGWSAGGNVALQLAMDHPGRVRRLVLEAPGSPFGFGGSTGEDGRPVADDFAGSGGGTANPQFCAALAAGDRGEEPTSPRTTLRSFYVAPGFTFAPEAEEAYLDAMLKTTVGDDVYPGDTATSDNWPGVAPGTTGMNNALSPKYLDQSGFADLDPAPPVLWIRGDADQIVSDTSMFDLAQLGKLGAVPGYPGEEVCPTQPMVSQMRAVLQAAGEFTEVVYEGCGHSPHLEQPERFVDEVRAFLQA
>NZ_CP043808.1|WP_022923243.1|243897_244623_-|purine-nucleoside-phosphorylase
MSTHIAAEPGQIAPRVLLPGDPLRARWIAENFLEDAVCYTEVRGMLGFTGTYRGEQVSVQGTGMGQPSASIYVNELIREYAVQQLVRVGSCGALTEGLKVRDVVLAQAAATDSSMNSLRFSGYHYPATADFALLRAAVEAAEAADAPHLVGTVFSSDSFYHSRPELTQKVVEYGVVAVEMEAAEIYTLAAQHGRQALAICTVSDHIVTGEETSAQEREQTFGDMITIALDAALATPLPTAS
>NZ_CP043808.1|WP_149814475.1|246138_246786_-|glycosyltransferase-family-1-protein
MLTGYPFRDSPPGTTLDAGLERFLAAGPPPVYAGFGSQSLRQTQEALRHTIEGALAAGHRVVALRGTGLEERYDERVTFVDGAPHDLLFPRMSAIAHHGGAGTTAEATRSGVPQVVVPFALDQPFFARRAHEIGVAAPPVPVGRTSVDTLRGAFRAVGDSGTRRQAALIGARVRAERGPQAAADRIEATLLRPRRAQRRAGPPSAAPAARIGVLG
>NZ_CP043808.1|WP_149814476.1|246779_247445_-|glycosyltransferase-family-1-protein
MRIAMLAGGSRGDYQPVLAVARELQARGHDVGVTASSDFAPTLRDAGLAVEEIRVDAMRIYREGTVAERMAGASIGRQVGALRHQAEAMAPELARALVDLWPRYDAVVSTALTFPWAGQLSAHDPRPQVLMLFVPALPSVWGDASMFATRAGRSPRNLLDGLRALGPGMAMGSPVADALADHGVPRGRGLRAARHTLTVPALIAHSPLSSRRAGSAAAGSC

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Crispr_ID: NZ_CP043808_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043808_2

1088737-1088867

Orphan

Consensus_repeat	Method
CCCGTTCCTTTCTGGCCGCTTCCTGCTCGCGCCCGGTGCGGGCGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043808_2

>merge|NZ_CP043808|2|1088737-1088867|CRISPRCasFinder
CCCGTTCCTTTCTGGCCGCTTCCTGCTCGCGCCCGGTGCGGGCGGGCACGACGTGCCGGTGGGACCGTGCGCTCGTGCGTCAGCGCCCCGTTCCTTTCTGGCCGCTTCCTGCTCGCGCCCGGTGCGGGCGG

>NZ_CP043808|2|2|1088737-1088867|CRISPRCasFinder
CCCGTTCCTTTCTGGCCGCTTCCTGCTCGCGCCCGGTGCGGGCGG	GCACGACGTGCCGGTGGGACCGTGCGCTCGTGCGTCAGCGC
CCCGTTCCTTTCTGGCCGCTTCCTGCTCGCGCCCGGTGCGGGCGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043808.1\|WP_022924802.1\|1088900_1089683_-\|DUF4191-domain-containing-protein	unknown	unknown	gnl\|CDD\|379389
NZ_CP043808.1\|WP_022924812.1\|1079296_1082776_+\|TM0106-family-RecB-like-putative-nuclease	unknown	unknown	gnl\|CDD\|225160
NZ_CP043808.1\|WP_022924814.1\|1078038_1078446_+\|HIT-family-protein	unknown	unknown	gnl\|CDD\|223611
NZ_CP043808.1\|WP_022924810.1\|1083394_1084333_+\|prenyltransferase	unknown	unknown	gnl\|CDD\|260125
NZ_CP043808.1\|WP_157609199.1\|1085729_1085879_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_084485137.1\|1085902_1086178_-\|NYN-domain-containing-protein	unknown	unknown	gnl\|CDD\|224349
NZ_CP043808.1\|WP_052327805.1\|1091837_1092869_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213235
NZ_CP043808.1\|WP_022924800.1\|1090854_1091838_-\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|372253
NZ_CP043808.1\|WP_084485136.1\|1086795_1087242_+\|tyrosine-type-recombinase/integrase	unknown	unknown	gnl\|CDD\|271189
NZ_CP043808.1\|WP_022924813.1\|1078456_1079176_-\|potassium-channel-family-protein	unknown	unknown	gnl\|CDD\|369572
NZ_CP043808.1\|WP_022924794.1\|1098618_1098795_+\|DUF5302-family-protein	unknown	unknown	gnl\|CDD\|379949
NZ_CP043808.1\|WP_022924797.1\|1093780_1095439_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_CP043808.1\|WP_022924796.1\|1095441_1096410_-\|TIGR01777-family-protein	unknown	unknown	gnl\|CDD\|273800
NZ_CP043808.1\|WP_022924811.1\|1082772_1083402_+\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|225136
NZ_CP043808.1\|WP_022924798.1\|1093028_1093694_-\|lipoyl(octanoyl)-transferase-LipB	unknown	unknown	gnl\|CDD\|184638
NZ_CP043808.1\|WP_149814588.1\|1087163_1088588_-\|type-I-glutamate--ammonia-ligase	unknown	unknown	gnl\|CDD\|273198
NZ_CP043808.1\|WP_028130985.1\|1100520_1101633_+\|glycine-cleavage-system-aminomethyltransferase-GcvT	unknown	unknown	gnl\|CDD\|234742
NZ_CP043808.1\|WP_022924815.1\|1076693_1078028_+\|aspartate-aminotransferase-family-protein	unknown	unknown	gnl\|CDD\|223239
NZ_CP043808.1\|WP_022924795.1\|1096420_1098430_-\|2-oxoglutarate-dehydrogenase,-E2-component,-dihydrolipoamide-succinyltransferase	unknown	unknown	gnl\|CDD\|200219
NZ_CP043808.1\|WP_028130986.1\|1098867_1100388_-\|leucyl-aminopeptidase	unknown	unknown	gnl\|CDD\|234863

Protein	Function_ID	Function_description	E-value
NZ_CP043808.1\|WP_022924802.1\|1088900_1089683_-\|DUF4191-domain-containing-protein	gnl\|CDD\|379389	pfam13829, DUF4191, Domain of unknown function (DUF4191).	2.72451e-80
NZ_CP043808.1\|WP_022924812.1\|1079296_1082776_+\|TM0106-family-RecB-like-putative-nuclease	gnl\|CDD\|225160	COG2251, COG2251, Predicted nuclease (RecB family) [General function prediction only].	5.91513e-52
NZ_CP043808.1\|WP_022924814.1\|1078038_1078446_+\|HIT-family-protein	gnl\|CDD\|223611	COG0537, Hit, Diadenosine tetraphosphate (Ap4A) hydrolase and other HIT family hydrolases [Nucleotide transport and metabolism / Carbohydrate transport and metabolism / General function prediction only].	1.28488e-39
NZ_CP043808.1\|WP_022924811.1\|1082772_1083402_+\|methyltransferase-domain-containing-protein	gnl\|CDD\|225136	COG2226, UbiE, Methylase involved in ubiquinone/menaquinone biosynthesis [Coenzyme metabolism].	8.30806e-20
NZ_CP043808.1\|WP_022924800.1\|1090854_1091838_-\|ABC-transporter-permease-subunit	gnl\|CDD\|372253	pfam12679, ABC2_membrane_2, ABC-2 family transporter protein. This family is related to the ABC-2 membrane transporter family.	6.32838e-05
NZ_CP043808.1\|WP_084485137.1\|1085902_1086178_-\|NYN-domain-containing-protein	gnl\|CDD\|224349	COG1432, COG1432, Uncharacterized conserved protein [Function unknown].	0.00864746
NZ_CP043808.1\|WP_052327805.1\|1091837_1092869_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213235	cd03268, ABC_BcrA_bacitracin_resist, ATP-binding cassette domain of the bacitracin-resistance transporter. The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.	6.50869e-88
NZ_CP043808.1\|WP_084485136.1\|1086795_1087242_+\|tyrosine-type-recombinase/integrase	gnl\|CDD\|271189	cd01189, INT_ICEBs1_C_like, C-terminal catalytic domain of integrases from bacterial phages and conjugate transposons. This family of tyrosine based site-specific integrases is has origins in bacterial phages and conjugate transposons. One member is the integrase from Bacillus subtilis conjugative transposon ICEBs1. ICEBs1 can be excised and transfered to various recipients in response to DNA damage or high concentrations of potential mating partners. The family belongs to the superfamily of DNA breaking-rejoining enzymes, which share the same fold in their catalytic domain and the overall reaction mechanism. The catalytic domain contains six conserved active site residues. Their overall reaction mechanism involves cleavage of a single strand of a DNA duplex by nucleophilic attack of a conserved tyrosine to give a 3' phosphotyrosyl protein-DNA adduct. In the second rejoining step, a terminal 5' hydroxyl attacks the covalent adduct to release the enzyme and generate duplex DNA.	2.95362e-12
NZ_CP043808.1\|WP_022924813.1\|1078456_1079176_-\|potassium-channel-family-protein	gnl\|CDD\|369572	pfam07885, Ion_trans_2, Ion channel. This family includes the two membrane helix type ion channels found in bacteria.	1.14894e-14
NZ_CP043808.1\|WP_022924794.1\|1098618_1098795_+\|DUF5302-family-protein	gnl\|CDD\|379949	pfam17227, DUF5302, Family of unknown function (DUF5302). Family of unknown function found in Actinobacteria with highly conserved motif of FRRKSG found at the C-terminus.	3.35497e-08
NZ_CP043808.1\|WP_022924797.1\|1093780_1095439_+\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.19903e-51
NZ_CP043808.1\|WP_022924796.1\|1095441_1096410_-\|TIGR01777-family-protein	gnl\|CDD\|273800	TIGR01777, Hypothetical_UPF0105_protein_Rv2216/MT2273/Mb2239., TIGR01777 family protein. This model represents a clade of proteins of unknown function including the E. coli yfcH protein. [Hypothetical proteins, Conserved].	1.47638e-115
NZ_CP043808.1\|WP_022924810.1\|1083394_1084333_+\|prenyltransferase	gnl\|CDD\|260125	cd13962, PT_UbiA_UBIAD1, 1,4-Dihydroxy-2-naphthoate octaprenyltransferase. Human UBIAD1 is an enzyme involved in the synthesis of MK-4. Menaquinones (MKs, also called bacterial forms) are one of the two forms of natural vitamin K, the other being the plant form, phylloquinone (PK). All forms of vitamin K have a 2-methyl-1,4-naphthoquinone (menadione; K3) ring structure in common. At the 3-position of the ring, PK has a phytyl side chain while MKs have several repeating prenyl units. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.	2.42584e-26
NZ_CP043808.1\|WP_022924798.1\|1093028_1093694_-\|lipoyl(octanoyl)-transferase-LipB	gnl\|CDD\|184638	PRK14345, PRK14345, lipoyl(octanoyl) transferase LipB.	5.19778e-121
NZ_CP043808.1\|WP_149814588.1\|1087163_1088588_-\|type-I-glutamate--ammonia-ligase	gnl\|CDD\|273198	TIGR00653, Glutamine_synthetase, glutamine synthetase, type I. Alternate name: glutamate--ammonia ligase. This model represents the dodecameric form, which can be subdivided into 1-alpha and 1-beta forms. The phylogeny of the 1-alpha and 1-beta forms appears polyphyletic. E. coli, Synechocystis PCC6803, Aquifex aeolicus, and the crenarcheon Sulfolobus acidocaldarius have form 1-beta, while Bacillus subtilis, Thermotoga maritima, and various euryarchaea has form 1-alpha. The 1-beta dodecamer from the crenarcheon Sulfolobus acidocaldarius differs from that in E. coli in that it is not regulated by adenylylation. [Amino acid biosynthesis, Glutamate family].	0
NZ_CP043808.1\|WP_028130985.1\|1100520_1101633_+\|glycine-cleavage-system-aminomethyltransferase-GcvT	gnl\|CDD\|234742	PRK00389, gcvT, glycine cleavage system aminomethyltransferase GcvT.	7.0739e-179
NZ_CP043808.1\|WP_022924815.1\|1076693_1078028_+\|aspartate-aminotransferase-family-protein	gnl\|CDD\|223239	COG0161, BioA, Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Coenzyme metabolism].	4.36058e-144
NZ_CP043808.1\|WP_022924795.1\|1096420_1098430_-\|2-oxoglutarate-dehydrogenase,-E2-component,-dihydrolipoamide-succinyltransferase	gnl\|CDD\|200219	TIGR02927, putative_dihydrolipoamide_acyltransferase, 2-oxoglutarate dehydrogenase, E2 component, dihydrolipoamide succinyltransferase. This model represents an Actinobacterial clade of E2 enzyme, a component of the 2-oxoglutarate dehydrogenase complex involved in the TCA cycle. These proteins have multiple domains including the catalytic domain (pfam00198), one or two biotin domains (pfam00364) and an E3-component binding domain (pfam02817).	0
NZ_CP043808.1\|WP_028130986.1\|1098867_1100388_-\|leucyl-aminopeptidase	gnl\|CDD\|234863	PRK00913, PRK00913, multifunctional aminopeptidase A; Provisional.	0

>NZ_CP043808.1|WP_149814588.1|1087163_1088588_-|type-I-glutamate--ammonia-ligase
MFSNADEVLAYIKDEDVKFIDVRFCDLPGVMQHFNVPAGSFDQDAFDTGQMFDGSSIRGFKSIHESDMKLIPDPQTAYVDQFRAEKTLIMNFSIVDPFTDEPYERDPRQIARKAEEHLASTGIADTAFFGAEAEFYVFDDVRFATGPSGGYYHIDSIEAAWNTGRSEDGGNRGYKPRFKGGYFPVPPVDHFADIRDRMVLDLATVGLDVERAHHEVGTAGQQEINYKFNTLLHSGDDMMKFKYVIKNSAWAAGKTATFMPKPLFGDNGSGMHTHQSLWKDGEPLFYDENGYGGLSDIARWYIGGLLQHGPALLAFTNPSLNSYHRLVPGFEAPINLVYSARNRSACVRIPITGSSAKAKRVEYRVPDPSANPYLAFSAQLMAGLDGIKNRIEPPEPVDKDLYELPPEDLADIAQLPTSLPEVLDALEDDHAFLTEGEVFTEDLLGAWVDYKRANEITPMRLRPHPHEFELYFDI
>NZ_CP043808.1|WP_084485136.1|1086795_1087242_+|tyrosine-type-recombinase/integrase
MALLDQLGQPVGPWQVERAVLAAREQVDGLPEGFRFHDLRHYFASMLIASGLDVKVVQTRLRHASARTTARRLRPPHARLGRHLTGSRLGRARAACGFRLARTLSWKHRGPDQRLCWSGPLSDQMSKYSSNSCGCGRRRIGVISLARL
>NZ_CP043808.1|WP_084485137.1|1085902_1086178_-|NYN-domain-containing-protein
MVALACVREAQREDVDVVVLASRDTDLVPVLDELCAMRADDPSSARVETVAWHNPGGRSFGSLRPTGPRRIWNTNLGPACFEASLDRDDYS
>NZ_CP043808.1|WP_157609199.1|1085729_1085879_-|hypothetical-protein
MTESRDTWTTRDYPVLVDLTEHLDVGGLPVQPHEVKRDELDTEAVTRCG
>NZ_CP043808.1|WP_022924810.1|1083394_1084333_+|prenyltransferase
MGEGRRRRPWGGRGAAAFRLSRPDQVLLVLVVAAVGWLAGSRGASTEQGSTLAGAGGAPCGAGLAPLGVLTAAAGVLAVAVSVHAVNEFADAATDARTVRTRFSGGSGALADHGLPAVFALRVALAAGGAAVVVVGVGLVTGWVSGLVAVLLLVGLVGGWTYSVGPWPWSRHGWGEVVNAVLGGLLLPATGAVVAGAPLGWSVRVFVPFALLTFVNLLETQWPDREADWSVGKHTLASRPSAPVLRRAGAVAILAAYLVSVVVHPWPVAAAGLLVAPLSVYAVARLGHGPPGPSVAAMVLFLLLHGAAWVLA
>NZ_CP043808.1|WP_022924811.1|1082772_1083402_+|methyltransferase-domain-containing-protein
MSVGRYGPLTARAYDLLSGEPVYVVGRRLAIPALGLRPGERVLDVGCGTGLNLSALMHDVGPTGLVVGLDRSAAMLGRAGRRRTRSHDGRLRLVEGDMTDPRALVEAAAGRAFDAVLFTYSLSLAPDPGPAWRAVRDVLRSGARVGVVDMARPTGNAAWASPLAQAACWLGGADIDAHPWTVVEPDLSGTRSWSRWGGHVRVCVGTWGG
>NZ_CP043808.1|WP_022924812.1|1079296_1082776_+|TM0106-family-RecB-like-putative-nuclease
MFALDGHRLVWSPSDLGAALDCEFSFLRGLDAQLGWAEPPATAPDPMGEHLAALGQRHEDELLAAYRQQGEVLELARPQWPPTLVGLRESAQATVRALQGPARTLSQACVFDGEMLGFADVVERVEDGWRVCDAKLARSASARALVQLGAYAEQLRGLGVPTSATVSLLLGSGERLDVATADVAGVFREVRARFRRLVRGHVAAGEPTSWEQGRYAACGRCEECRRAVEEHQDLLLVAGVHGVQREQLRATGLRTVADLARATERPPDMPAETFERLRAQAALQAGTPPGEAAYALLGTAATTLALLPAPSEGDLFFDFEGDPHHHEGDRSRTGLQYLWGTTDTAGSYTAVWAHSFAEERAAFVAFVDDLGARRLRWPDLHVYHYAPYETSALKAMAMRYQVREEELDVLLRAEVFVDLYAVVRGSVMTSAPSYSIKALEPLYMGAELRSEDGVVSGDASILAYHEFRLWAQEDPERAMERLDALADYNAYDCRSTLGLRDWLLERAQEAGVRHLVVPRALDDEPREAAQEQDALMAALTARSGPDTRSRRSTAEQAYAMLATALGYHAREAKQFWWGHYDRLGHPLGSWARSRDVFAVESAEVVADWEHPGGRARSLQRTVRLTGDWGRGSTVRDRGQLVYPTPAPTGSRGPEGAPFAAADPSAVAPDPHDARVLVVSERRKEAETFADLPVALVPAAPPDARQLAEAIARVAQESARAPDLPAAPALDLLARRPPRLLGREALPHSGDVVEDVVSALLALDRSYLAIQGPPGTGKTYTGSLVIRRLVEEHGWRVGVVAQSHAVVENVLGGVVDAGLDPELVGKSKNETPHRPWVDVTDNVGGRAAFLEDHRETGCVLGGTAWTFSHPDLVQPGGLDLLVVDEAGQFALAPTIAVGAAAARLLLLGDPQQLPQVSQGTHAEPVDESALGWLMHGEPTLDPAHGYFLEQTYRMHPAVTATVSELAYAGQLGSAAPAAARSLDGVEPGLEVVRVAHAGNRTESPEEAAEVVRQVRAYLGATWEDPADPATPRPLGPADVLVVAPYNAQVVLIRGALEEAGLDGVRVGTVDKFQGQEAVVAILSMTASSAADVPRGMGFLLSRNRLNVAISRARWRAVLIRSEALTAHLPSSADALLQLGAFVALCDAGASRADGDGGRAG
>NZ_CP043808.1|WP_022924813.1|1078456_1079176_-|potassium-channel-family-protein
MNRLERWESRTQIPLMIAALVFLVAFAVPIVDPGLPTGLRGTLMTVQDVVWVIFLVDYVYRLVVAPKKWEFVRRHPIDLAAVALPALRPLRLVAALSFVHQVAGEKLRGHVAMYVGVATILVVTISSLAVLNVERGEPGASIETWQDALWWSFVTVTTVGYGDYSPVTVEGRLFAVGLMLCGIALLGIVTASLASWLIERIAEPDPARQPATAADVTALTEQVRELRAEVAALRGEEGP
>NZ_CP043808.1|WP_022924814.1|1078038_1078446_+|HIT-family-protein
MSCLFCRIIAGEEPAHVVLDREHVVGFLDVRPLFKGHVLLVPREHVDTLTELPDALVEPFFATVREVAAVVRDELGAQGTFVAMNNTVSQSVPHLHAHVVPRTKGDGLRGFFWPRVRYADGEAARYAKELRAALS
>NZ_CP043808.1|WP_022924815.1|1076693_1078028_+|aspartate-aminotransferase-family-protein
MASAHVFSRGGAERVRVDHGRGAELVDVEGRRYLDAAGGAVVVGIGHGVTEVVEVAAAQASRVAYVHGSAFSSEVLEEYADALGPLLPLENPRIYPVSGGSEAVESALKMARAYHLARGEDRDVVIGRHGSYHGNTRGALSVSGRQGLRQPYLPWLTGVAHTSTPYEYRCPFPEAHPDGCARRHAEALEAEIQGLGPARVAAFVAEPISGAGLGACVPPDDYWPAIAEVCARHGVLVVADEVMTGFGRTGAWFGGDHFGLRPDLLVAGKGTASGYWPLGLAVASGAVHDTLREGGFVHGFTYSHHVVGAATGLAVLRVLQREGLVEASARQGERLHAALRRELADVRVVGDVRGRGLLQAVELVADPATREPFERSERVTERVLEACREQGVLVYPGTGCADGRRGDLLLLGPPLVVTDDEVDRIAAGVAQGLRDVLGGVGAGG
>NZ_CP043808.1|WP_022924802.1|1088900_1089683_-|DUF4191-domain-containing-protein
MSSATTEPEPKKRRFGRNRKPKDPNKPGRLAQVRQVFSMTRKADPSAVWWMVLAALAVLVVALLVGLWLDQVVYLMIIGVPLALLAAVVILGRRAERAAFTQIEGQPGASAAVLQQLRRGWYYDQEPVAAEAGGQVRGMRDLNNAAMVFRAVGRPGVVLISEGPRGSAQRLVKAEERKVARVVGGEVPVHTITVGNGEGQTPLRSVVKTIKRFDKALTNDEALVVQQRMKALGNRNKPAVPAGMDPTRPPRASRRALRGR
>NZ_CP043808.1|WP_022924800.1|1090854_1091838_-|ABC-transporter-permease-subunit
MRLTVVEVRRLLWRRIPALAVLAAVIISVIALIGVHGQARQIAQARAGADVALEQAIADWEENGEQYLQECLQGQEDERRAAGDASVDWGCDQMEAPSAEQWYGELPPVGEQYTELLAIAVYPLLLLALAVGSTGVAAEFGHRTMGSFLTFVPRRAPVFGAKVLAGALLSVPVVAVCLVALVLGVPAVYRLTGNDPSILADGVLPSFWMSVRILGLGLAAGALGAAAAFVLRHSALVIGLLVGYLMVVEGLLSSLLPGISRFSVGRNVEAVVRDGVEWITYTNCREVEGCREVTQQLSLGQGVLTLSVVLVVVLGLGLLRFLRSDID
>NZ_CP043808.1|WP_052327805.1|1091837_1092869_-|ATP-binding-cassette-domain-containing-protein
MSVPHVALTDEGPAVTTRGLRKTYRTVRGRRVAVHGLDMDVPAGGVHGFLGPNGSGKTTTIRMLLGLVRPDRGDVQIFGTPVPRQLPQVVDRVGAIVESPKFFPTFTGARNLALLAQAIGTPQSRVGEVLDEVGLGSRGRDTFTSYSLGMKQRLAIAATLLKSPDLLIFDEPTNGLDPAGIHEIRRTMRRLADEGRTVLVSSHILSEVEQIADTVTIIGRGRVLAQGSVAGLIGGGGESVEVGVRHPGAAARLLRDAGFTVDWRALPQGEDAAEALARADGSQESGLLTVTGAQPAEITRLLAGQGLWVERLVPSRRGLEQIFLELTGDDALASTRDERGGAA
>NZ_CP043808.1|WP_022924798.1|1093028_1093694_-|lipoyl(octanoyl)-transferase-LipB
MRVEHLGLAPNLVDYDQAWEHQREVHAAVVAGSLPGTVLLLEHAAVYTAGKRTEAHERPLDGTPVVDVDRGGKITWHGPGQLVGYPIVRLPSPVDVVAHVRRLEDVMIGVCRELGVETTRVEGRSGVWLPADGTRPERKIGAIGIRVSQDVTMHGFALNCDCDLGWADAIIPCGIADAGVTSLTAELGRHVPVAEVLPLVEDHLARVLDPVTPGQPTVPTR
>NZ_CP043808.1|WP_022924797.1|1093780_1095439_+|serine/threonine-protein-kinase
MNLPTVPGYDVLGRLGRGASAEVWRGRRRADGLPVALKLVRPKGGAADVPAVLAEAGLMAGLRHEHVLRLYDVLPLGSPEDPTVALVTQLAAGGSLAQVLQSRRLLSPGELVTVLHPVSSALAELHRLGVVHGDVSPGNVVFRSDGMPLLGDLGTARVTGEDGLRGWGTRGPDGMVAPEVVEGFAATSESDVYQVGALAWLALVGDVPGPGFDRPPLAEVAPLLAPDLVDLVRRCMAPQPEDRPGAEELPALLLAVADPEPVEVAPDVDAAVGVTERLRQVALTDAAQAQPPRGGRWRRLLARGVGRPRPEPARVPDPTSPRVAASRRRGAHRESGAPAGARRRRPGLVLAAVLVLLVGVLGVVVVLRPTASVSHGDGPPSVGPAAADVPAVTAPAPPVRAVPPAGGKPDTATPSAGPDRRDGIWDEARASEVVQGLLDGRAAAWEEVDPGRLEEVVAPGSPAARAELSQLSEADRAGVSYPQVDFTVSRARTASVQDGRVEVDLTVRRAQLTVRRDGEVVHTAGAREDEVRVVLSRHGGRWLLQEWGPPAR
>NZ_CP043808.1|WP_022924796.1|1095441_1096410_-|TIGR01777-family-protein
MTDPASSSTRVVAITGASGLIGSALSEAVRERGDEVVHLVRRDTRPSDQLPEGVREATWDPGSRLDPEVLAGVHGVVHLAGAGIADKRWTDERKKVLVSSRLDGTSTIADALAALANREGGASGTPRLVSGSAVGYYGDRGDEVLTEESRPGEGFLSQLCQDWEAATAPAEQAGVPVAHVRTGIVLAPGGGALGRLLPLVRLGLGGPLAGGDSWWPWITLHDHVRALLFLLDRPEITGPVNLGGPEPATQQQVTQALASQLHRPAVLPVPGFALRLVLGEMSQEILSSTRVLPEVLTGAGFTFDHADLQAAAAWVVQQDQAA
>NZ_CP043808.1|WP_022924795.1|1096420_1098430_-|2-oxoglutarate-dehydrogenase,-E2-component,-dihydrolipoamide-succinyltransferase
MSERVSMPALGESVTEGTVTRWLKSVGDSVEVDEPLLEVSTDKVDTEIPSPVAGTLQEILAEEDETVEVGADLCVVGDGDGGDSSDSGGSDAQADEEESQQEDSGDADESDEQEQESGDSGESQDASDSKDESSEDTGSGDSGGSSGGGGGSEGETVTMPALGESVTEGTVTRWLKSEGDSVEVDEPLLEVSTDKVDTEIPSPVAGVLTSILAGEDETVEVGGELAVIGGESSGGGSDEGSSQDEEKSEEPAEVDKEEKAEGESEEKPAEDEKKEEKAEEDSSEDLGGEQEKQEKAAQEASESSGTSDADDSGQAVGVGTTSAEAGSTSHKDADGDGTRDVEQRQQSTASTPQGQDVSAYVTPLVRKLAAQHDVDLGSLTGTGVGGRIRKQDVLDAAQAKKEQPAEAPAAQEEKAATPETSAPSGGGSPSPESEAKRGTTEKMSRLRKVIATRMVESLQTSAQLTTVIEVDVTKISRLRKRAKDEFLKREGTKLSFMPFFAMAAIEALKEHPIVNASVEDDSIVYHAAEHLGVAVDTPRGLLVPVIKDAGDLNIAGLARKIADLAERTRDNKVTPDELSGGTFTLTNTGSRGALFDTPIINQPNVGILGTGAVVKRPVVIVDEDGMETIAIRDMVYLAISYDHRVVDGADAARFLATMKERLEDGKFEV
>NZ_CP043808.1|WP_022924794.1|1098618_1098795_+|DUF5302-family-protein
MSDDPVTDDVKAKFREALAKKQAHGGTDVSDHSEHGKVAQERDAKTSGAQQMFRRKSG
>NZ_CP043808.1|WP_028130986.1|1098867_1100388_-|leucyl-aminopeptidase
MSGCMPVTFTTDDLATAQVDALVLGATKRDGALALLEGHGLDEDVVRSVSDALSALGAEGSTDEVSLLAGVDGVEAGLVLVVGVGGSGPAPRTEQLRRAAGVAARSLTGRGSAVFALGQEGRDQALAVAEGAALGAYSYVEQHGVGKAGSAKAPLASASVRGLDGEEAQAAQAEVSAMVDAVSYARDLVNTPPNLLYPETFAADVVSRAQEAGVEVEVWDPEQLAAEGCGGIIGVGQGSARGPRLVTLRYTPEGADRHLALVGKGITFDSGGLCLKPGASMVTMKMDMGGAAACAAATLAIAELGLPVQVTAYLCLAENMTGDLAQRPGDVVTMRGGRTVEIINTDAEGRLVMADGLALATEQQPDAIVDVATLTGACIVALGERTIGVMGNDDELRDSLVRLGTDAGDTAWALPMPEEIRPTLDTPVADLKHTGERSAGAMVAATFLQEFVGTRGEGAQASPIPWAHLDIAGPAYNEKSAWGYYPKGGTGAGVRSLVALARSFAG
>NZ_CP043808.1|WP_028130985.1|1100520_1101633_+|glycine-cleavage-system-aminomethyltransferase-GcvT
MSDSATMTSPLHDRHLALGAKMADFGGWSMPIEYPGGGVVAEHTAVRERVGLFDVSHLGNALVTGPGAKDFLNSCLTNDLDRIEPGRAQYTMCCSSDGGVVDDMIAYLRSEDEVFLIPNAANTARVVELLQEAEQRPEDVSVENQHHDYAILALQGPRVDEVMDELGLPTGHDYMSFVEAQWQGVPVTVCRTGYTGERGYELVCASADAPALWDALTAAMEPLGGLPCGLGARDTLRTEMGYALHGHELSDQITPVMGRTGWAVGWGKEAFWGREVLTAQREAKECRLGGGLVVTGRGIPRAGCRVLDSSGREVGEVTSGTFSPTRKQGIALALLDRGTEQGTELVVEVRGREVPVEVSKPPFVEGGAAG

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Crispr_ID: NZ_CP043808_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043808_3

1599640-1599725

Orphan

Consensus_repeat	Method
TGACCGTGGAAGTCCTGCCGGGGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043808_3

>merge|NZ_CP043808|3|1599640-1599725|CRISPRCasFinder
TGACCGTGGAAGTCCTGCCGGGGCAAGATTTCCCCGGTCGGCGGGCATACCGGCAGTGGTGCTGACCGTGGAAGTCCTGCCGGGGC

>NZ_CP043808|3|3|1599640-1599725|CRISPRCasFinder
TGACCGTGGAAGTCCTGCCGGGGC	AAGATTTCCCCGGTCGGCGGGCATACCGGCAGTGGTGC
TGACCGTGGAAGTCCTGCCGGGGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043808.1\|WP_161600222.1\|1593559_1593739_-\|cell-wall-binding-repeat-containing-protein	unknown	unknown	gnl\|CDD\|367829
NZ_CP043808.1\|WP_157609176.1\|1587376_1588453_-\|DUF2332-family-protein	unknown	unknown	gnl\|CDD\|378386
NZ_CP043808.1\|WP_022923878.1\|1609556_1610267_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293792
NZ_CP043808.1\|WP_149814671.1\|1593683_1595909_-\|SpoIID/LytB-domain-containing-protein	unknown	unknown	gnl\|CDD\|274252
NZ_CP043808.1\|WP_052327747.1\|1606507_1607839_-\|M18-family-aminopeptidase	unknown	unknown	gnl\|CDD\|235073
NZ_CP043808.1\|WP_161600221.1\|1588449_1590090_-\|DUF222-domain-containing-protein	unknown	unknown	gnl\|CDD\|367155
NZ_CP043808.1\|WP_022923868.1\|1597167_1597854_+\|crossover-junction-endodeoxyribonuclease-RuvC	unknown	unknown	gnl\|CDD\|234587
NZ_CP043808.1\|WP_052327726.1\|1610248_1610938_-\|GTP-pyrophosphokinase-family-protein	unknown	unknown	gnl\|CDD\|225232
NZ_CP043808.1\|WP_149814667.1\|1585931_1586417_-\|nitroreductase-family-deazaflavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|281995
NZ_CP043808.1\|WP_022923872.1\|1600309_1602301_+\|protein-translocase-subunit-SecD	unknown	unknown	gnl\|CDD\|235615
NZ_CP043808.1\|WP_022923881.1\|1612473_1613157_-\|peptidylprolyl-isomerase	unknown	unknown	gnl\|CDD\|223725
NZ_CP043808.1\|WP_022923860.1\|1586823_1587375_+\|HIT-domain-containing-protein	unknown	unknown	gnl\|CDD\|238606
NZ_CP043808.1\|WP_022923880.1\|1611011_1612412_+\|histidine--tRNA-ligase	unknown	unknown	gnl\|CDD\|223202
NZ_CP043808.1\|WP_022923874.1\|1603533_1604070_+\|adenine-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|235028
NZ_CP043808.1\|WP_022923875.1\|1604158_1606498_+\|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|223394
NZ_CP043808.1\|WP_149814669.1\|1591452_1592667_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_033418536.1\|1607835_1609077_-\|DUF349-domain-containing-protein	unknown	unknown	gnl\|CDD\|377186
NZ_CP043808.1\|WP_022923869.1\|1597850_1598459_+\|Holliday-junction-branch-migration-protein-RuvA	unknown	unknown	gnl\|CDD\|234645
NZ_CP043808.1\|WP_022923871.1\|1599926_1600313_+\|preprotein-translocase-subunit-YajC	unknown	unknown	gnl\|CDD\|376903
NZ_CP043808.1\|WP_022923858.1\|1585421_1585907_+\|GNAT-family-N-acetyltransferase	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP043808.1\|WP_161600222.1\|1593559_1593739_-\|cell-wall-binding-repeat-containing-protein	gnl\|CDD\|367829	pfam04122, CW_binding_2, Putative cell wall binding repeat 2. This repeat is found in multiple tandem copies in proteins including amidase enhancers and adhesins.	0.00968211
NZ_CP043808.1\|WP_157609176.1\|1587376_1588453_-\|DUF2332-family-protein	gnl\|CDD\|378386	pfam10094, DUF2332, Uncharacterized protein conserved in bacteria (DUF2332). Members of this family of hypothetical bacterial proteins have no known function.	3.36078e-105
NZ_CP043808.1\|WP_022923878.1\|1609556_1610267_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293792	cd06262, metallo-hydrolase-like_MBL-fold, mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, 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 which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.	4.30073e-51
NZ_CP043808.1\|WP_149814671.1\|1593683_1595909_-\|SpoIID/LytB-domain-containing-protein	gnl\|CDD\|274252	TIGR02669, stage_II_sporulation_protein_D, SpoIID/LytB domain. This model describes a domain found typically in two or three proteins per genome in Cyanobacteria and Firmicutes, and sporadically in other genomes. One member is SpoIID of Bacillus subtilis. Another in B. subtilis is the C-terminal half of LytB, encoded immediately upstream of an amidase, the autolysin LytC, to which its N-terminus is homologous. Gene neighborhoods are not well conserved for members of this family, as many, such as SpoIID, are monocistronic. One early modelling-based study suggests a DNA-binding role for SpoIID, but the function of this domain is unknown. [Unknown function, General].	1.00017e-31
NZ_CP043808.1\|WP_052327747.1\|1606507_1607839_-\|M18-family-aminopeptidase	gnl\|CDD\|235073	PRK02813, PRK02813, putative aminopeptidase 2; Provisional.	0
NZ_CP043808.1\|WP_161600221.1\|1588449_1590090_-\|DUF222-domain-containing-protein	gnl\|CDD\|367155	pfam02720, DUF222, Domain of unknown function (DUF222). This family is often found associated to the N-terminus of the HNH endonuclease domain pfam01844. The function of this domain is uncertain. This family has been called the 13E12 repeat family.	7.89597e-12
NZ_CP043808.1\|WP_022923868.1\|1597167_1597854_+\|crossover-junction-endodeoxyribonuclease-RuvC	gnl\|CDD\|234587	PRK00039, ruvC, Holliday junction resolvase; Reviewed.	1.79123e-72
NZ_CP043808.1\|WP_052327726.1\|1610248_1610938_-\|GTP-pyrophosphokinase-family-protein	gnl\|CDD\|225232	COG2357, COG2357, PpGpp synthetase catalytic domain [General function prediction only].	3.32286e-82
NZ_CP043808.1\|WP_022923872.1\|1600309_1602301_+\|protein-translocase-subunit-SecD	gnl\|CDD\|235615	PRK05812, secD, preprotein translocase subunit SecD; Reviewed.	1.68482e-108
NZ_CP043808.1\|WP_149814667.1\|1585931_1586417_-\|nitroreductase-family-deazaflavin-dependent-oxidoreductase	gnl\|CDD\|281995	pfam04075, F420H2_quin_red, F420H(2)-dependent quinone reductase. This family of proteins is found in the genera Mycobacterium and Streptomyces. Member protein Rv3547 has been characterized as a deazaflavin-dependent nitroreductase. Rv1558 is an F420H(2)-dependent quinone reductase involved in oxidative stress protection.	5.94151e-37
NZ_CP043808.1\|WP_022923860.1\|1586823_1587375_+\|HIT-domain-containing-protein	gnl\|CDD\|238606	cd01275, FHIT, FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH/Qxx (x, is a hydrophobic amino acid), On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified into three branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases. Fhit plays a very important role in the development of tumours. Infact, Fhit deletions are among the earliest and most frequent genetic alterations in the development of tumours.	6.4945e-58
NZ_CP043808.1\|WP_022923880.1\|1611011_1612412_+\|histidine--tRNA-ligase	gnl\|CDD\|223202	COG0124, HisS, Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis].	2.38542e-141
NZ_CP043808.1\|WP_022923874.1\|1603533_1604070_+\|adenine-phosphoribosyltransferase	gnl\|CDD\|235028	PRK02304, PRK02304, adenine phosphoribosyltransferase; Provisional.	4.68779e-77
NZ_CP043808.1\|WP_022923875.1\|1604158_1606498_+\|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase	gnl\|CDD\|223394	COG0317, SpoT, Guanosine polyphosphate pyrophosphohydrolases/synthetases [Signal transduction mechanisms / Transcription].	0
NZ_CP043808.1\|WP_022923881.1\|1612473_1613157_-\|peptidylprolyl-isomerase	gnl\|CDD\|223725	COG0652, PpiB, Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones].	6.14144e-46
NZ_CP043808.1\|WP_033418536.1\|1607835_1609077_-\|DUF349-domain-containing-protein	gnl\|CDD\|377186	pfam03993, DUF349, Domain of Unknown Function (DUF349). This domain is found singly or as up to five tandem repeats in a small set of bacterial proteins. There are two or three alpha-helices, and possibly a beta-strand.	5.77544e-16
NZ_CP043808.1\|WP_022923869.1\|1597850_1598459_+\|Holliday-junction-branch-migration-protein-RuvA	gnl\|CDD\|234645	PRK00116, ruvA, Holliday junction branch migration protein RuvA.	5.81744e-70
NZ_CP043808.1\|WP_022923871.1\|1599926_1600313_+\|preprotein-translocase-subunit-YajC	gnl\|CDD\|376903	pfam02699, YajC, Preprotein translocase subunit. See.	1.19532e-18

>NZ_CP043808.1|WP_022923869.1|1597850_1598459_+|Holliday-junction-branch-migration-protein-RuvA
MIASVRGTVRHVGLDHLVVEVGGVGLLVHTTPETAAGASSGQEVSLETTLVVREESLTVYGFDGPDAKAIFERVQTVSGVGPRLALAMLSVHSPDDVRAAIAQGDLVALTKVPGIGKKSAERLVLELKDKILAVGVDPGLPQRAAGTVASADDAVQSQVREALQGLGWTAKQADGALATVTKDEAPADVAALLRAALRELGR
>NZ_CP043808.1|WP_022923868.1|1597167_1597854_+|crossover-junction-endodeoxyribonuclease-RuvC
MRVLGVDPGLTRCGLGVVEGLPGRQLRLVEVGVVRTPPSEDPAERLLTLQTELDEWFARTRPEAVAVERVFASTRNSSIMGVAQASALPLLAAARLGLPVVLHTPSEVKAAVTGNGRADKGQVTRMVTRILTLEQAPRPADAADALALAICHLWRGGSQARLEGEAGGSDRLKDAERAAARARPNRLAQLHDEHRTAARSAAARASARAGGRVTSTVTTATSSRRNPR
>NZ_CP043808.1|WP_149814671.1|1593683_1595909_-|SpoIID/LytB-domain-containing-protein
MRRPSVAGLALALVVSLTGAPASASPAAPEPDLADPASGSSLPWAQQAQAAPEPESAEDLGETTVVTTDDVLPAPVPGSEVYPVPADGSYDITGGGYGHRIGMSQWGAHGAGLEGLSHEEIVDFYYPGTRLETWSAQDISVGITIDGDGVTRVAHRSGLRVSAAPGSRTYALPSGRSQWRVRATTSSATSCVLEGYDGSTWSSWWPSGMSRRCPVTFSSAQEGTVDLYLPGGSRRVYRGALTATHHGSSALATVNHLPEQHYLRSVVAAEMGPSFHPEALRAQSVAARTYARRSASTSYYDICDSTACQAYRGRGVRRGDGSLLSYEYSANNAAVDDTAGEVLTFAFPQGRRLATTMYSASTGGQTIAAGNGHDYLRAQKDPYDATPANPRHRWSASLPRTALQQRYGIHRVERVQVLTRDGVGAWGGRILTARVEGFTSGGAYTYAHATGTGLMLSRYWPTWSEGLSSDYFTFAGAAPTPTKPVRLSGTDRYGTAARVAEQWSPGVGVVYVVSGQDYPDALAASARAGVYDAPLLLTRHDRLPGATTRALERLRPDRLVVLGGTDAVSGGVLRDLRGYARTGRVDRVAGTDRYGTAAALAGYYPSRVDRVLLASGRDFPDALAGAAVANGQQAPLLLTRPEGLPSTTIRARCGACSRARSSCSAATAPSPTPSCGRPGNMPPAASCAGPGTTATAPRPGSRRPSRAARPGLRGARHRLPGRARGCRAGGPSRRTARADPG
>NZ_CP043808.1|WP_161600222.1|1593559_1593739_-|cell-wall-binding-repeat-containing-protein
MAAALAGRHDAPLVLTPGDRVAAGADQALSHLRPRSMYVLGGTGGITRPTMDRLARYLR
>NZ_CP043808.1|WP_149814669.1|1591452_1592667_-|hypothetical-protein
MAALLLVLPLLLSGPTPSPSGGAAPSTLPDPFPAYAHLPATVERSPAGPALMGFTHGYGVEFMDYPQAIAVGADGGTYRRLDTADDASVRSDQGDPGPMLLSPDGRSVAVGGRGNDGYLATVSLEDGSVRTWPLPDGRSTTPLAWSGDGRSVFVGLVEDDTHRYSYLDGAPPRVVYDVRRADLDAPEGTEPVRLPEVAATTGIAPLPQDGGLLVSTGDGAELRSADGMQVVATGLDLGLDLGPTAVSPDGRRVVTGGAGSVQVSTLDGGAVTSTDPLDLSVTTDRPAGAGRMAEPLGWLAADRILVSTYDTETAALRLHLWSVDVDSGAAQELLVAEPGWTGAAVGEISVAADLLDGAEVGDPGMVDRGRVLMLLRGALLVALVALVLRAVRQAGAARQAYRDA
>NZ_CP043808.1|WP_161600221.1|1588449_1590090_-|DUF222-domain-containing-protein
MTDCRDALMTLGADDLRALDDDARLALLRQLEELTRSAAAVSARLQVDFRDSQMEQQQAAGVPRSRRGKVVADELAHARMTSPYWGSRELSSARALVEEMPQTLAALTGGHIGALQARADTEATTCLSVEDRAEVDRRLAPRLPGSSTQEITGAARSLVYEIDPAAYVARARRAAQDRGVSVHPAPDVMARLSAHLPAHQAVACYAALRTHATAARASGDPRGLNQLMADELHQRLTGRAVVDGIDIEVGLVITDQALFGGASDAAELEGYGPVPAEVARQLLRPEDAVGDGNGGGRGSGDRGDGVDGRGSGDRGDGVDGRSSSRSRGDRGGDGRDCGSSSRRDGGSGPGSSSQELCPESGWCTDASCDLLHGPPITPPAHPGFPAPPAPSPPSRPVPPHATDSPAHESPDASRPAPSCEPDRDPEPTAERREAVVWLRRLWVDPVSHVLVEQDSRRRRFTGELRRFVISRDRTCRNRWCGAPIRDVDHVVRHSDGGATTADNGRGLCHRCNLARERHRHRPAHDHRSAPPLLPSLGDSSARPRAG
>NZ_CP043808.1|WP_157609176.1|1587376_1588453_-|DUF2332-family-protein
MRAPVSQELDQIRRPFREWARTMQRQAPFYTRIARHVLDRDDVLSLLFACPVPEQRTPVLLFAAVHDLLLQHPDLPLAQWYPSIAPDPRDDDPGRAFVETVVAHRTHLERTVATRSTQTNEVGRCALFLPVLARLADEVGPLALLDIGASAGLVLNFDRYSYDYDGRVVHPVDGPSAVRVSCRTDGTVPVPRAMPPIVDRLGLDQHPVDVANPLAARWLRACVWPDQLERLDRLDGAIAIAQHQPVEVRRGDAVDDLASAVDDLDGHPVVMNSWVLNYLTARRRSDYVEALDQIGADRGLSWVFAESPHVTPDLPHPNADHPESTHLNLVRWRDGVRAVEFLAECHPHGVSATWRHDG
>NZ_CP043808.1|WP_022923860.1|1586823_1587375_+|HIT-domain-containing-protein
MTSVPEPEDAITFAGSQDGFERLWTPHRMAYVRGERPSPDAGSGCPFCAAPGQEDAESLVVHRGEHCYVVLNLFPYNPGHLLICPYRHVSLYVDMTPEETAEFTELTRQAIHAITAASNPAGYNIGMNQGEVAGAGVAAHLHQHVVPRWMGDANFLPIVAQTKAVPQLLQDVREQLAGHWPAS
>NZ_CP043808.1|WP_149814667.1|1585931_1586417_-|nitroreductase-family-deazaflavin-dependent-oxidoreductase
MDDSSARHDLDAAAIGDPAAYLPEKSDWVATQLRDIDAAGDTAAATIQDRPVVVITMRGARSGMLRRVPLMRVEHEGSYLAVASKGGAPEHPAWYYNVAKNPDVLVQDGASQQALRGARARRGRERDAWWERAVQTFPSYADYQEKTDRLIPVFVLEPLGG
>NZ_CP043808.1|WP_022923858.1|1585421_1585907_+|GNAT-family-N-acetyltransferase
MPTLGEAAQGVRVRALADDEALLLGALHKQALVRAGTDPDAGEPMHVRAFASAWHRRADDLPAWVAEHDGEHVGVAVVRRTMLPHLAGAPRLLVLSALGPADTVGEEAVCLALVRQVISWARERGDERVEVAGDVALPAPVLDAVRAVVRQATSVSLPTQP
>NZ_CP043808.1|WP_022923871.1|1599926_1600313_+|preprotein-translocase-subunit-YajC
MTLATGSAAGAGGSGLTLLILALPIIFLLFLMFNQRRRARSVNEAQSQLQPGQEVMTTSGMFGVIRAVEDEVIHLEAGGVVLRFQRRAILPMSMVGSLGGRPGPAATDQGDGGTADGDTPTDTDGPTR
>NZ_CP043808.1|WP_022923872.1|1600309_1602301_+|protein-translocase-subunit-SecD
MTTSTPAPRRDEDLPGAGEASGRRQRRSGGGRRSGGQRSARIRGPLRTLLSLLVITVLLFGGIGAARLWAEPAASLTPQLGLDLAGGRQIVMEPLTEDGTNVSAEQLDQAIDIIRRRVDGGGVTEAEVTRQGQNVSVAIPGNPTPDQVEALSRSSQLRFRPVLVAQFTAPEMEMPEQRTLPLPPSLIEEQLEEFEQQQQDAQEDSETQDSVEEGTSDEAEQTEENRGGTRLPSSGSDDAPATEAPGVPAEDGSDSTAPPVQEGELPAASDPSSLAQITPELQEEFSALDCAAEGVATQVAAAPTDQPTVACTVEGDEKFILGPVELTGSSVTDATAGPETVQGGAVTGRWQVVLTFDGEGGQTFAEITSRLYGYPQGEAQNRFATVLDGQVITAPTVNGVISGGTATISGDFTPEESQSLANQLKFGALPLSFEVQTSEQISPTLGGEQLRYGVIAGIIGLLLVFAYMLVQYHALGLVAIGSLVVAALLAYGSVTLLGWANNFRLTMAGVTGLIVAIGITADSFIVYFERIRDEVRAGRPLRYAVDTGWERARRTLIISDVVNLIAATVLYLLSESGVKAFAFALGLTTIIDLVVVFMFTHPLVSILANTRFFGEGKKWSGMEPERLGAKRSAYLGRGRVREPEVITPGRRRHTREELEGGVV
>NZ_CP043808.1|WP_022923874.1|1603533_1604070_+|adenine-phosphoribosyltransferase
MADPDPRLAADVLAGMRDIPDFPEEGVVFKDFTPVLLDRGLRDRIVEDTVERRRGQVDVVAGIEARGFILGAMIAHELGVGFVPVRKGGKLPAAVHSQSYTLEYGTATLEIHQDAVSHHERVLVVDDVLATGGTLAATCELIERCGASVAAIELVLEIEELAGRDKLTGYDLHCLTSV
>NZ_CP043808.1|WP_022923875.1|1604158_1606498_+|bifunctional-(p)ppGpp-synthetase/guanosine-3',5'-bis(diphosphate)-3'-pyrophosphohydrolase
MNEPAASTPPARVGGGLRPRWARLGGTRASTNPALEPLLRSVRATHPKADLALIERAYAVADEMHKGQQRKSGDAYITHPLAVATILAELGMTPSTIAAALLHDTVEDTPYSLAQLRKDFGDEIAMMVDGVTKLDKVTYGDAAQAETVRKMVVAMARDIRVLVIKLADRLHNARTWRYVSAESAARKAGETLEIYAPLAHRLGMNTIKWELEDLSFAQLYPKVYDEIVRMVADRAPAREEMLSRIRGEIGDELHGAKIRATVTGRPKHYYSVYQKMIVRGHDFDKIYDLVGVRVLVESIQDCYAVLGALHNRWNPVPGRFKDYIAMPKFNMYQSLHTTVIGPSGKPVEIQIRTYQMHRRAEYGVAAHWKYKEQSPDGTKAVAGPDGAPGALEGMQWLRQLIDWQQETSDPGEFLDSLRFEMGAAEVYVFTPDGDVMALPAGATPVDFAYAVHTEVGHRCVGGRVNGKLAPLDSELGNGDVCEIITSKAQDAGPSRDWLTFVKSPRARNKIRQWFTRERREEMVDSGKDEIAKVLRKQNAPLQRLMRHDTLTAVAQGLNYKDIDGLFAAVGEGHVSAQHVVKQLLATLGGEDGTEEDLAEAVRPRRGRIAQADPGVTVVGADDVWVKIARCCTPVPGDPILGFVTHGKGVSVHRTDCTNAAELQSKSPERIIRVAWAPTASSLFLVNMQVEALDRSALLSDITRVLSEQHVNILSASVQTNRDRVALSKFTFEMADPSHLESVLRAVRRIPAVLDAYRVTGTTSTDPHRREASEPSPSAS
>NZ_CP043808.1|WP_052327747.1|1606507_1607839_-|M18-family-aminopeptidase
MSSLTRLATQVSEVAEGLCAYLDASPSPFHAVHAAQQLLTDAGFTELDETSPTPSSPGHYVVRRGGSLISWSTAHLPADRPAHTAYRVVGAHTDSPNLRIKPQPDWTRAGWQMLGVEVYGGALTHSWLDRDLGLSGRVAVRDATAPHGISQLLWRCDDPLLRVSQLAIHLDRTVRSEGLKLNDQDHLAPHWSTGTEASTFRDWLAGQVDVAPEDLLGFDAMTHDLTPARRIGGEGELVASARLDNLATSYAAVRALLQAVAAPGEAASVPVVVLFDHEEVGSTSERGAQSTFLPSWLERIVLAAGGTREDYWRALAGSVIASGDMAHATHPNYAERHEPGHPILMNGGPVLKVNTNLRYATDSVGAAAFTLACEQAGVPMQTFVTRSDLPCGSTVGPMTSALTGATTVDFGAPVLSMHSTREVCGTLDQAGYAAALAAFLSPA
>NZ_CP043808.1|WP_033418536.1|1607835_1609077_-|DUF349-domain-containing-protein
MKHGRVAEDGTVYVVAADGTEREVGSYPGASPEEALAYFARKYDEMLASADLLKARLAGTDVSAHDARQSLAHLKEQIGEAHVVGDLAALSAVVKHLEEEVKVRSRTEQEERLQAKAQAAQEREKLVVEAEQLAATEPAKVQWKQSSGRVRELLEEWKAHQRSGPRLDKEVENALWQRFSHARSDFDKMRKTWFAHLDEEHASAKATKERLVREAEALSTSKDWGATAGAFKRLMQDWKRAGRASRADDDALWARFKAAQDSFFDAKDEVVAAEEAEFTENLKVKEGLLEEAEALTVDEAHLDQTKAELRKIQDRWDAAGKVPRADSKRVENRLRAVEQKVRDVEDSQWQRTDPELNARAQSMVDQLERAVQGLEADLAAAQAAGEDKKAQDLEAELATKKLWLTSARGGLGR
>NZ_CP043808.1|WP_022923878.1|1609556_1610267_+|MBL-fold-metallo-hydrolase
MFVRSIVADAFATNCYVMAPAEGEECLIVDPGIGVEDRVQDVLAEHRLRPAAVLLTHGHLDHVYAVTPVCQGTTAVSPYIHTDDRYRLTDPLATMSPELVAALEQQFGRRATWTEPERIVEFGAAGEDHTTLDLAGLRIEVAHAPGHTEGSVLFTAHDVPDGIPSDDLDRTVLSGDVLFAGSVGRTDLPGGDAAAMRRSLRDVVLPLADSSLVLPGHGPATTMARERGTNPYLTSL
>NZ_CP043808.1|WP_052327726.1|1610248_1610938_-|GTP-pyrophosphokinase-family-protein
MSTGAALPPSLELASRESITPAQLREVGAQLQRFLLEYEFGLREVETKIEILRDEFSHMHDYNPIEHVSSRVKSPDSLREKVLRRGLSTDLPTIRREITDIAGIRVTCSFVTDAYRIFDLLTQQDDITIRRVSDYIADPKPNGYKSLHAIIEIPVFLSTGRVEVPVEVQLRTIAMDFWASTEHKIHYKYDGNVPDSLLDELKTAADSAAELDARMHRLHRELHGQSEVR
>NZ_CP043808.1|WP_022923880.1|1611011_1612412_+|histidine--tRNA-ligase
MISPRTPSGVLELLPPEQIAFQRMLDSIRSGYERFGFLPVETPVFERSDVLLTKTGGETERQVYFAQSTGALEKARAQSPAEGTLPELALRFDLTVPLARYVAEHEHQLTFPFRRYQMQRVYRGERPQRGRFREFYQCDVDVIGSGELSVRHDAEAPAIINAIFTDLAIGDFTIQINNRRLLRGFYEDLGIADPQAQAAVLREVDKLDKRGPGYLRTTLTGDGFGLAEEVVEQILTFVQTRSTGHDDALARLDDVVAGSAGSEALAQGVAELREVLGLVRALGVPEANYCLNFSIARGLDYYTGTVYETTLDEHPELGSICSGGRYDDLAGQYTKSRLPGVGISIGLSRLFWQLREAGLIEVSAGESTVQVLVPQVDAELLDDQLALASQLRHGGINTEAVLDGGKLGKQLRYADRAGIRFVAILGQQEVADGTVTLKDLRRQDQFTVPRDEVVSALRVELAQPLV
>NZ_CP043808.1|WP_022923881.1|1612473_1613157_-|peptidylprolyl-isomerase
MRRALLPAVTALVLAGCGGEATYPGSSADEPQGGETPDVACTQPPTPPAEPRSYTQDDLPEPLSGERETLAATIETTCGDIELELYAGDAPQTVASFAFLAQEGYWEDSACHRLVTSGIFVLQCGDPTGTGQGSPGYAFGIENAPPDGLYPPGTLAMARTQDPDSNGGQFFIVYDDTQLPVGGGGYSIFGRVTAGLDIVETVAAEGNDSGGTAPAQPISLLSVSVDA

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Crispr_ID: NZ_CP043808_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043808_4

1635228-1635303

Orphan

Consensus_repeat	Method
GCCGATCGGGTCGGGCGTGTCGTCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043808_4

>merge|NZ_CP043808|4|1635228-1635303|CRISPRCasFinder
GCCGATCGGGTCGGGCGTGTCGTCGGCCCTAGCGTTCACCTGAACGCTGGTGCCGATCGGGTCGGGCGTGTCGTCG

>NZ_CP043808|4|4|1635228-1635303|CRISPRCasFinder
GCCGATCGGGTCGGGCGTGTCGTCG	GCCCTAGCGTTCACCTGAACGCTGGT
GCCGATCGGGTCGGGCGTGTCGTCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043808.1\|WP_022923905.1\|1634672_1634909_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_022923900.1\|1628990_1629716_+\|(d)CMP-kinase	unknown	unknown	gnl\|CDD\|234579
NZ_CP043808.1\|WP_022923904.1\|1633043_1634663_+\|BCCT-family-transporter	unknown	unknown	gnl\|CDD\|376718
NZ_CP043808.1\|WP_028130809.1\|1631213_1632683_+\|ribosome-biogenesis-GTPase-Der	unknown	unknown	gnl\|CDD\|179525
NZ_CP043808.1\|WP_149814674.1\|1646289_1646775_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_149814673.1\|1643029_1643242_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_022923912.1\|1641812_1643033_-\|M24-family-metallopeptidase	unknown	unknown	gnl\|CDD\|274380
NZ_CP043808.1\|WP_022923915.1\|1644299_1645733_+\|amidase	unknown	unknown	gnl\|CDD\|180437
NZ_CP043808.1\|WP_022923911.1\|1640598_1641816_-\|PLP-dependent-aminotransferase-family-protein	unknown	unknown	gnl\|CDD\|224089
NZ_CP043808.1\|WP_022923914.1\|1643307_1644303_+\|D-2-hydroxyacid-dehydrogenase	unknown	unknown	gnl\|CDD\|240625
NZ_CP043808.1\|WP_084485068.1\|1639402_1640545_-\|M20-family-metallopeptidase	unknown	unknown	gnl\|CDD\|349944
NZ_CP043808.1\|WP_022923896.1\|1625120_1626020_+\|segregation/condensation-protein-A	unknown	unknown	gnl\|CDD\|224273
NZ_CP043808.1\|WP_022923918.1\|1647459_1648377_+\|DUF881-domain-containing-protein	unknown	unknown	gnl\|CDD\|377575
NZ_CP043808.1\|WP_022923895.1\|1624224_1625109_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|379293
NZ_CP043808.1\|WP_022923919.1\|1648373_1648706_+\|small-basic-family-protein	unknown	unknown	gnl\|CDD\|377739
NZ_CP043808.1\|WP_022923897.1\|1626003_1626645_+\|SMC-Scp-complex-subunit-ScpB	unknown	unknown	gnl\|CDD\|377219
NZ_CP043808.1\|WP_022923899.1\|1627808_1628828_+\|LD-carboxypeptidase	unknown	unknown	gnl\|CDD\|132883
NZ_CP043808.1\|WP_022923901.1\|1629773_1630637_+\|sulfurtransferase	unknown	unknown	gnl\|CDD\|225450
NZ_CP043808.1\|WP_022923917.1\|1646827_1647463_+\|CDP-alcohol-phosphatidyltransferase-family-protein	unknown	unknown	gnl\|CDD\|223632
NZ_CP043808.1\|WP_028130808.1\|1626755_1627592_+\|rRNA-pseudouridine-synthase	unknown	unknown	gnl\|CDD\|224108

Protein	Function_ID	Function_description	E-value
NZ_CP043808.1\|WP_022923911.1\|1640598_1641816_-\|PLP-dependent-aminotransferase-family-protein	gnl\|CDD\|224089	COG1167, ARO8, Transcriptional regulators containing a DNA-binding HTH domain and an aminotransferase domain (MocR family) and their eukaryotic orthologs [Transcription / Amino acid transport and metabolism].	8.75634e-108
NZ_CP043808.1\|WP_022923900.1\|1628990_1629716_+\|(d)CMP-kinase	gnl\|CDD\|234579	PRK00023, cmk, (d)CMP kinase.	4.68879e-74
NZ_CP043808.1\|WP_022923904.1\|1633043_1634663_+\|BCCT-family-transporter	gnl\|CDD\|376718	pfam02028, BCCT, BCCT, betaine/carnitine/choline family transporter.	0
NZ_CP043808.1\|WP_028130809.1\|1631213_1632683_+\|ribosome-biogenesis-GTPase-Der	gnl\|CDD\|179525	PRK03003, PRK03003, GTP-binding protein Der; Reviewed.	0
NZ_CP043808.1\|WP_022923914.1\|1643307_1644303_+\|D-2-hydroxyacid-dehydrogenase	gnl\|CDD\|240625	cd05300, 2-Hacid_dh_1, Putative D-isomer specific 2-hydroxyacid dehydrogenase. 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, 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 subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.	1.8976e-133
NZ_CP043808.1\|WP_022923912.1\|1641812_1643033_-\|M24-family-metallopeptidase	gnl\|CDD\|274380	TIGR02993, ectoine_eutD, ectoine utilization protein EutD. Members of this family are putative peptidases or hydrolases similar to Xaa-Pro aminopeptidase (pfam00557). They belong to ectoine utilization operons, as found in Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. The exact function is unknown.	2.90569e-130
NZ_CP043808.1\|WP_022923915.1\|1644299_1645733_+\|amidase	gnl\|CDD\|180437	PRK06169, PRK06169, putative amidase; Provisional.	0
NZ_CP043808.1\|WP_084485068.1\|1639402_1640545_-\|M20-family-metallopeptidase	gnl\|CDD\|349944	cd08659, M20_ArgE_DapE-like, Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE)-like. Peptidase M20 acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase (ArgE/DapE) like family of enzymes catalyze analogous reactions and share a common activator, the metal ion (usually Co2+ or Zn2+). ArgE catalyzes a broad range of substrates, including N-acetylornithine, alpha-N-acetylmethionine and alpha-N-formylmethionine, while DapE catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelate (L,L-SDAP) to L,L-diaminopimelate and succinate. Proteins in this family are mostly bacterial and have been inferred by homology as being related to both ArgE and DapE. This family also includes N-acetyl-L-citrulline deacetylase (ACDase; acetylcitrulline deacetylase), a unique, novel enzyme found in Xanthomonas campestris, a plant pathogen, in which N-acetyl-L-ornithine is the substrate for transcarbamoylation reaction, and the product is N-acetyl-L-citrulline. Thus, in the arginine biosynthesis pathway, ACDase subsequently catalyzes the hydrolysis of N-acetyl-L-citrulline to acetate and L-citrulline.	9.93664e-107
NZ_CP043808.1\|WP_022923896.1\|1625120_1626020_+\|segregation/condensation-protein-A	gnl\|CDD\|224273	COG1354, scpA, Rec8/ScpA/Scc1-like protein (kleisin family) [Replication, recombination, and repair].	8.27743e-46
NZ_CP043808.1\|WP_022923918.1\|1647459_1648377_+\|DUF881-domain-containing-protein	gnl\|CDD\|377575	pfam05949, DUF881, Bacterial protein of unknown function (DUF881). This family consists of a series of hypothetical bacterial proteins. One of the family members YlxW from Bacillus subtilis is thought to be involved in cell division and sporulation.	4.6234e-36
NZ_CP043808.1\|WP_022923895.1\|1624224_1625109_+\|AAA-family-ATPase	gnl\|CDD\|379293	pfam13614, AAA_31, AAA domain. This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.	9.86625e-86
NZ_CP043808.1\|WP_022923919.1\|1648373_1648706_+\|small-basic-family-protein	gnl\|CDD\|377739	pfam06947, DUF1290, Protein of unknown function (DUF1290). This family consists of several bacterial small basic proteins of around 100 residues in length. The function of this family is unknown.	4.06841e-34
NZ_CP043808.1\|WP_022923897.1\|1626003_1626645_+\|SMC-Scp-complex-subunit-ScpB	gnl\|CDD\|377219	pfam04079, SMC_ScpB, Segregation and condensation complex subunit ScpB. This is a family of prokaryotic proteins that form one of the subunits, ScpB, of the segregation and condensation complex, condensin, that plays a key role in the maintenance of the chromosome. In prokaryotes the complex consists of three proteins, SMC, ScpA (kleisin) and ScpB. ScpB dimerizes and binds to ScpA. As originally predicted, ScpB is structurally a winged-helix at both its N- and C-terminal halves. IN Bacillus subtilis,one Smc dimer is bridged by a single ScpAB to generate asymmetric tripartite rings analogous to eukaryotic SMC complex ring-shaped assemblies.	6.78198e-68
NZ_CP043808.1\|WP_022923899.1\|1627808_1628828_+\|LD-carboxypeptidase	gnl\|CDD\|132883	cd07062, Peptidase_S66_mccF_like, Microcin C7 self-immunity protein determines resistance to exogenous microcin C7. Microcin C7 self-immunity protein (mccF): MccF, a homolog of the LD-carboxypeptidase family, mediates resistance against exogenously added microcin C7 (MccC7), a ribosomally-encoded peptide antibiotic that contains a phosphoramidate linkage to adenosine monophosphate at its C-terminus. The plasmid-encoded mccF gene is transcribed in the opposite direction to the other five genes (mccA-E) and is required for the full expression of immunity but not for production. The catalytic triad residues (Ser, His, Glu) of LD-carboxypeptidase are also conserved in MccF, strongly suggesting that MccF shares the hydrolytic activity with LD-carboxypeptidases. Substrates of MccF have not been deduced, but could likely be microcin C7 precursors. The possible role of MccF is to defend producer cells against exogenous microcin from re-entering after having been exported. It is suggested that MccF is involved in microcin degradation or sequestration in the periplasm.	4.17163e-94
NZ_CP043808.1\|WP_022923901.1\|1629773_1630637_+\|sulfurtransferase	gnl\|CDD\|225450	COG2897, SseA, Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism].	6.16303e-102
NZ_CP043808.1\|WP_022923917.1\|1646827_1647463_+\|CDP-alcohol-phosphatidyltransferase-family-protein	gnl\|CDD\|223632	COG0558, PgsA, Phosphatidylglycerophosphate synthase [Lipid metabolism].	2.77288e-24
NZ_CP043808.1\|WP_028130808.1\|1626755_1627592_+\|rRNA-pseudouridine-synthase	gnl\|CDD\|224108	COG1187, RsuA, 16S rRNA uridine-516 pseudouridylate synthase and related pseudouridylate synthases [Translation, ribosomal structure and biogenesis].	1.7528e-93

>NZ_CP043808.1|WP_022923905.1|1634672_1634909_-|hypothetical-protein
MWSDEQIYAWVVRDGTERAALVSPDAPTQEAQIWVVDSLTVTVAVLDSRPSGPSQELVSWDAEGEVTDVVPGPSRGDT
>NZ_CP043808.1|WP_022923904.1|1633043_1634663_+|BCCT-family-transporter
MDALARRLGLKTNPQIFFTSAGLMVVILILLLLFPGGIGEGFAAARSWVTTNLGWFFILGVTAWLIFLIWIAISKYGELRLGKGDEKPRYSRLSWFTMLFAGGIGTVLMFWGVAEPISHFSAPPFPGVEPYSAAAAEDAMNIALYHLGLHTWTIFTLPGLAFGFFIYRYDLPMRVSSVFYPFLKERIHGPIGKSIDVFAVLGTLFGLAVSLGLGTSQISAGLSELTGVGDGVVVKVVVIAVLTAVATVSVAVGLDKGIKRLSNLNIGMAVGMMLFVLFTGGATVFLLRELVESAGNYLAALPELSFWNDALANETTEDGWGWQAGWTVFYWAWTVTWAPFMGVFLARISRGRTVREFIGGVLVAPSLFTLVWFVIFGWSAMNIDGIGGDGGPISTAVGESVPLAMFTFFENFPWTPLLQGLVVVIVALFFATSADSAALVVDMLCSGEDEEGPVGQRVFWAVCLGALAALLIVLGGDEGLNALQQVITVIGLPIFILVFAMIPALFAGLRSEKLRVTRGDDDISPKEHIHRQSEETTDA
>NZ_CP043808.1|WP_028130809.1|1631213_1632683_+|ribosome-biogenesis-GTPase-Der
MHDDDEASEQDEALEQALRAGLVDFELSDEDQALVERGELPQEDREDVGGRPVVAVVGRPNVGKSSLVNRILGRREAVVEDVPGVTRDRVSYDAEWSGRRFTLVDTGGWEVDATGIHLRVAEQAEVAIELADAVMFVVDATVGATDTDEQVVRLLRRSGRPVVLVANKVDDQRFEADAAMLWSLGLGQPWPVSALHGRGSGDALDALLDVLPERSAVAGVAPEGGPRRVALLGRPNVGKSSLLNKLAGSDRVVVDDVAGTTRDPVDELIELGDDGRVWRFVDTAGIRRRVHQTKGADFYASLRTQAALEKAEVAVVLVDVSEPIAEQDIRVIQQVVDSGRALVVAYNKWDTLDEERRYYLEREIERELVQITWAPRVNISAATGRNVAKLVPALDTALGSWDRRIPTAKLNAFLGEVVAGQPHPVRGGKQPRVLFATQADTRPPRFVIFASGFIEAGYRRFLERRLREQFGFVGTPIEISVRVREKRRR
>NZ_CP043808.1|WP_022923901.1|1629773_1630637_+|sulfurtransferase
MSSSASDKISAYAHPERLVTTEWLAEHLDDPQVVVLESDEDVLLYDTGHIPGARKLDWHTDLNDPVTRDYVDGERFAQVMGERGVGRDTTVVIYGDRSNWWAAYALWVMTLFGHEDVRLLDGGRAKWVEEGREMTTDAPEVTQAAYPVVERDDSRVRAFKADVLDHLGQPMVDVRSPGEFSGELLHMPDYPQEGAMRGGHIPGATSVPWARAANEDGTFKSREELEAIYQQEQGLATSDDVVAYCRIGERSSHTWFVLTHLLGFEKVRNYDGSWTEWGNSVGVPVER
>NZ_CP043808.1|WP_022923900.1|1628990_1629716_+|(d)CMP-kinase
MPSRPLTIAIDGPSGSGKSSVSKAVARELGLGYLDTGAMYRAVAWRCLDADVDLTDQQAVAQAARDLPLDILTDPDDQTLRVGGTDITDAIRETRVTSQVSAVATNLDVRAELRRRQREIVAAAREQQGGIVAEGRDITTVVAPDAEHRILVTASEEARLTRRSTELHGGADAEQVAATRDQIVRRDQQDSTVSAFMEAADGVVTLDTSDLSFDQVVAAVLALVRGEVEPERSPEHAGEAT
>NZ_CP043808.1|WP_022923899.1|1627808_1628828_+|LD-carboxypeptidase
MRPRFPAPLRPGAVVGVTSPSAGVPAELRARLDVAVESVRSRGYPVVVGRCMDGARHVSAPAADRAAELQRMLLDPGIAAVVPPWGGETAIDLLPLLDWGALTAAEPTWMVGFSDIATLITPLTLRAGWATIHGQNLMDTPYAVPDGLVSWLDLVALPRGATVRQTSPGRYREGFVDWAEHPEDDTDVLDHAGAWTRLDGGGDVDVTGRLVGGCVETLASLAGTTYLDTGALADLGDGLVVYVEAAEHDAFTICRHLHGMRLAGFFDGAAAVLVGRTSAPDGATLTQHEAVMDALDVLGVPVVADVECGHVAPHLPLVNGALARVEHTAATSAITQTLS
>NZ_CP043808.1|WP_028130808.1|1626755_1627592_+|rRNA-pseudouridine-synthase
MPSQGGGAGPRRAGGTRPPRRRRPSTPPDPATRDVHTPDGVRLQKVLAGAGFGSRRACEKLIEEGRVEVDGQVVVELGVRVDAATQTVHVDGDRVVVDTEKLYLAFNKPAGVVSTMEDEEGRPCLTDYVGHLSRRLFHVGRLDVDTEGLLLLTNDGDLAHKLQHPAYGVPKTYVAQVHGVVAPGIGKQLRDGVELEDGLAKADSFRLVDDIPGHSIIEIVLHEGRKHIVRRMMEEVGYPVEALSRVQVGPIKLAELRPGKYRALSAEEVAQLYRAAGE
>NZ_CP043808.1|WP_022923897.1|1626003_1626645_+|SMC-Scp-complex-subunit-ScpB
MSQQDEQPDEPVAGADQAEQEQVAFDVTDFPGGARSAIEAVLMVIDEPVTEEALASALELPLEDVGAVLDELAQEYAQGNRGFMLRRLGGGWRVYSRPEYAPVVEKFLLGGQQARLTQAALETLAVIAYRQPISRARIGAIRGVNVDGVVRTLLARGMVTETGQDPTGGAVLYGTTDLFLQRMGLDSLDDLPALAPYLPSAEVLEELASEGLA
>NZ_CP043808.1|WP_022923896.1|1625120_1626020_+|segregation/condensation-protein-A
MPTAPAADPSSQASGQPGEATPGGVLTATRGGFEVHLDVFSGPFELLLGLIAKHKLDVTEIALARVTDEFVAYLRAAQEGEGEWDLSQASEFVLIAATLLDLKAARLLPSGREDDEEDLALIEARDLLFARLLQYRAFKQVADELRLQMEGKGRIFARDVGVEERFASLLPELVLTVTPEQLAMIAGRAMIPRPPPAVGVDHLHAAQVSVREQASIIVGRLRERGSTSFRDLVADADSTLVIVARFLSLLELFRDTVVSLEQDEALGELTVRWTGPDSGEVGGQVGAEFDEEEADEPAG
>NZ_CP043808.1|WP_022923895.1|1624224_1625109_+|AAA-family-ATPase
MSHDRLPGTETSGVGQEGPTGRPLPDFPVPEPLASHGPARIIAMCNQKGGVGKTTTTINLGAALAEYGRKVLMVDFDPQGALSVGLGVRTHDLDVTIYNLLVERGHDVRDVIQTTSVPGIDILPANIDLSAAEVQLVGEVAREQVLARTLRPVMDDYDVVFIDCQPSLGLLTVNALTASHGVIIPLETEFFAMRGVALLIETIEKITDRLNPRLEIDGILATMYDGRTLHSREVVRSVVDHFGDTVFHTVISRTVKFPDATLAAEPITTYASTHSGAEAYRQLARELVARGGAP
>NZ_CP043808.1|WP_084485068.1|1639402_1640545_-|M20-family-metallopeptidase
MATALVRAPGANPPGEEAATAAVLTSLAAELGLQVAEHDVAPGRPNVRVTLPGGDGPGLLFLGHTDVVPPGDPKDWTGDPYAGSVVEGRLGGRGSADMKGGLAAVLLALAAVREARLVPSGPVHLDALCDEEQNGLGIRALVAGPRPDLLGCVVAEPTDLTTVVAARGASYLHVEVRGVAAHAGRPEDGRNAIGGAARVVADLERWHEELRVDAHPLVGPATLNVGVISGGTSGSAVPDLCRLEVDRRLLPGEPVDGVLDALRHRLDRLDLDERGLTWTLSSPMDMPGFETSPRDPFVTAVDGAMSAAGRGPAPLAGWTAACDGGFVADAWGIPVVVQGPGSVAEQAHRPDESVAVDELVTAARGYARTVLELLGPGATA
>NZ_CP043808.1|WP_022923911.1|1640598_1641816_-|PLP-dependent-aminotransferase-family-protein
MTPVTTASTTLPLASRADLLVGSVIDSSTSLLAQQTHDIVRFAMGSPAAEAIPTDQLNEAARSALHGADAFDYAATEGDPPLRTALLEMLEGTTDATTAERLTITAGGMQGLDLAAKLFIDPGDLVTVESPTYTNGSATALAYQAELAEIPVDEEGMSIDALREAVERAGRTPKLIYTVPTFQNPSGTSMSLTRRQELIGLAQDWGSVVLDDDPYGMLRFAGEALPSLHELADGDPLVFSVRTFSKIIAPGLRVGWVDADPSLGQLLIHAKQTMDTCTNLPAQRLVADFLRAGHLEDHLVTQRQEYRRRKEAMQAALTEHFAGRATWTDPEGGFFLWVSFGGDVDTEALFEVALAEGVAYIPGNAFSPARRFPHDLRLCFASTPPDRIREGVARLARAVDSLAHR
>NZ_CP043808.1|WP_022923912.1|1641812_1643033_-|M24-family-metallopeptidase
MSGLTEITRAAQTAHPHTLRPEHERRMARTQEVLRGRGLDALVVTDPANLYYLTGYNAWSFYMPQALLVPAQGEAHLVLRAMDAKGGHHTATLPRDRIHGYPEHYVHRHDIHPWEWIASTGREVGVLPSGAGTIAMELDAHFFSPRAYLAFGATLPQAEVVDSRELVNWLRVVKSDTEVALLRAAGEVTVRAMTAAIDALRAGRRQCDVVAQIQQAQAHGTEALGGDYPAIVPMLPSGETAGTPHLTWVEEPLRQGEATTIELAGVHRRYHVPLARTVSLGPPPPRLARTAEATGLGLEAALRAVHPGATAADVHAAFTAELTRHGLRKDSRIGYSIGIGYPPDWGERTVSLRAEDDTALEPGMCFHLILGMWMDGWGYETSESVLVTEAGPELLAPLDQGLVIHA
>NZ_CP043808.1|WP_149814673.1|1643029_1643242_-|hypothetical-protein
MQESLTVGAARPRPASAAPVATGASLPEPGIGVVVPYDVEAVGPGQGLLCHRPEVGDGSTVSTSSAEERV
>NZ_CP043808.1|WP_022923914.1|1643307_1644303_+|D-2-hydroxyacid-dehydrogenase
MTGHRPRVVVLTAPGLDPPPQLEEVAAEVDLVVVTADDLATALPGARALLLWDFFSAAVENAWPAADSLEWIHVAAAGVDSLLFDELRASPVMVTNAHGVFDRPIAEFVLASILAHAKRLHESMRLQRDHEWAHRETTLVRGQRVLVVGTGGIGREIARLLRAVGCEVRGAGRRERAADPDFGTVVRSDALVEHVGWADHLVNATPLTPATRGLLDAAVFAAMRREAHVVNIGRGASLVEADLLSALRAGRLAGASLDVFQTEPLPDDSPLWDAPGLVVSAHLSGDVTGWRDRLAEQFVANLRRWRAGEPLTGVVDSRLGYVPGAEATESP
>NZ_CP043808.1|WP_022923915.1|1644299_1645733_+|amidase
MTSGRPTVSELSAAFAYGTSTPLETTERALEAIDRFDPVVHAMVLVDREGALAAAREATRRWAAGTPLSPIDGIPTTIKDILLTRGWPTLRGSLLIDEGQPQDWTEDAPAVARLRAAGCVLLGKNSTPEFAWKGVTDSLRHGPTGNPWDPGLTAGGSSGGAAAAVALGMGAWSIGTDGGGSVRIPASFTGTVALKPTYGRIPLYPASPYGTLSHAGPMTTSVADAALLLDLVGRPDPRDWSALPEASGSFREGLEDGVAGLRVAVSPRLGLDVDNDPAVESAVLATAQRLAEDGARVEQVDPGISDPVDAFHVLWFSGAAKVIEGYGPAALERVDPGLREAVLRHGAGASASAYLDATAVRMDLGRRMGLFHETYDVLLTPTMPIPPFELGHQAPRGDDALWTSWTPYTYPFNMTQQPALSVPCGTTSEGRPIGLQVVGARHADALVLRVGRAIERRAPVGLPPMLYAPSAERGEEA
>NZ_CP043808.1|WP_149814674.1|1646289_1646775_+|hypothetical-protein
MARRWGWIAGMVVVGLLLTLPQVALWRPTPDTPLQQGLFWVAGLSYHVSGLLLGVALVAAAVLVGERGGLVRLTGGSAPRLLLLAMALVVLGTVAGWGVQGLALGVEGQGLVGWSLLLIQVFAWVVGLGYALAGVWLAGRLPAPHREHAPAGPVRDPSQPR
>NZ_CP043808.1|WP_022923917.1|1646827_1647463_+|CDP-alcohol-phosphatidyltransferase-family-protein
MTGVQGDRPGPAPEQRVLPVTDRLWTVPNLLSMVRLALVPVFVWSLLRHELGWAALVLVVAGASDFADGKIARHYGLTSRLGQVLDPVADRLYIAATVLGLAAVSVIPWWLVAVLFAREAFIVLMYPVVRRHALPIPEVTFIGKAATFNLLGGFPLLLLGHVEGWWTVLSLACGWALVWWGTVLYWVTGVTYGWQVAHMVRQRRDAGRVVR
>NZ_CP043808.1|WP_022923918.1|1647459_1648377_+|DUF881-domain-containing-protein
MRWRRGQADPDPAASMALLNEVLDPPLGQGYDSAARSRTQQGLPASSGTRTWLMFGTTLVLGVLLTTAAVTLRTPDPAEAAGRAQLVERIEQVERVGDERSVQVDALRAEVGELERAAIVADSGGSGDAIAAAAVRAGGTAVTGPGVQITLHDAKQPADDTPGEDAEPERINSRDLQLVVNGLWRAGAEAVSVDGHRLTSTSAIRFAGQAIIVDFRGLTPPYDIVAIGAPEELTTELTSGATGAYLQEIDRQLGLRSEVTAARELTVGPGVRLSTRLGTIPSGEAPPAPTPGVLPDRHPRGEEPR
>NZ_CP043808.1|WP_022923919.1|1648373_1648706_+|small-basic-family-protein
MIPVLGLLVGVVLGLVISPEVPIWLQPYLPIAVIAALDAVFGAARASLEGIFNDRVFVISFLSNVVVAALIVFLGNQLGVGAQLSTGVVVVLGLRIFSNVAAIRRHLLGA

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Crispr_ID: NZ_CP043808_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043808_5

2458666-2458751

Orphan

Consensus_repeat	Method
CGACCGGGGATGTCGCGCCCCGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043808_5

>merge|NZ_CP043808|5|2458666-2458751|CRISPRCasFinder
CGACCGGGGATGTCGCGCCCCGGCAGGAGATCCACGGTCGGCTCCACCGAGGTATGCCCGCTCCGACCGGGGACGTCGCGCCCCGG

>NZ_CP043808|5|5|2458666-2458751|CRISPRCasFinder
CGACCGGGGATGTCGCGCCCCGG	CAGGAGATCCACGGTCGGCTCCACCGAGGTATGCCCGCTC
CGACCGGGGACGTCGCGCCCCGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043808.1\|WP_022926228.1\|2447683_2448832_-\|branched-chain-amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|119323
NZ_CP043808.1\|WP_022926230.1\|2449700_2450540_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213191
NZ_CP043808.1\|WP_022926235.1\|2454886_2455552_-\|amino-acid-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223836
NZ_CP043808.1\|WP_022926245.1\|2467575_2468544_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|284659
NZ_CP043808.1\|WP_033419137.1\|2462432_2463410_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|379289
NZ_CP043808.1\|WP_157609223.1\|2460071_2460269_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|234938
NZ_CP043808.1\|WP_022926234.1\|2454143_2454890_-\|amino-acid-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224051
NZ_CP043808.1\|WP_028131247.1\|2450536_2451277_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213186
NZ_CP043808.1\|WP_161600249.1\|2464394_2464997_-\|DUF4245-family-protein	unknown	unknown	gnl\|CDD\|379430
NZ_CP043808.1\|WP_022926236.1\|2455565_2456471_-\|transporter-substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|270431
NZ_CP043808.1\|WP_022926237.1\|2456769_2457819_-\|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase	unknown	unknown	gnl\|CDD\|234893
NZ_CP043808.1\|WP_149814783.1\|2467061_2467571_+\|carbonic-anhydrase	unknown	unknown	gnl\|CDD\|239474
NZ_CP043808.1\|WP_033419131.1\|2460949_2461813_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187578
NZ_CP043808.1\|WP_022926243.1\|2466107_2467034_+\|carbohydrate-kinase	unknown	unknown	gnl\|CDD\|238572
NZ_CP043808.1\|WP_028131252.1\|2461841_2462210_-\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|379266
NZ_CP043808.1\|WP_022926238.1\|2457867_2458632_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_CP043808.1\|WP_022926233.1\|2452861_2454112_+\|DNA-recombination-protein-RmuC	unknown	unknown	gnl\|CDD\|376878
NZ_CP043808.1\|WP_084485252.1\|2451342_2452605_-\|substrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|380551
NZ_CP043808.1\|WP_022926240.1\|2460367_2460634_+\|exodeoxyribonuclease-VII-small-subunit	unknown	unknown	gnl\|CDD\|179195
NZ_CP043808.1\|WP_022926242.1\|2465085_2466108_+\|class-II-fructose-bisphosphatase	unknown	unknown	gnl\|CDD\|236536

Protein	Function_ID	Function_description	E-value
NZ_CP043808.1\|WP_022926228.1\|2447683_2448832_-\|branched-chain-amino-acid-ABC-transporter-permease	gnl\|CDD\|119323	cd06581, TM_PBP1_LivM_like, Transmembrane subunit (TM) of Escherichia coli LivM and related proteins. LivM is one of two TMs of the E. coli LIV-1/LS transporter, a Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporter involved in the uptake of branched-chain amino acids (AAs). These types of transporters generally bind type 1 PBPs. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP, which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. E. coli LivM forms a heterodimer with another TM, LivH, to generate the transmembrane pore. LivH is not included in this subgroup. The LIV-1/LS transporter is comprised of two TMs (LivM and LivH), two ABCs (LivG and LivF), and one of two alternative PBPs, LivJ (LIV-BP) or LivK (LS-BP). In addition to transporting branched-chain AAs including leucine, isoleucine and valine, the E. coli LIV-1/LS transporter is involved in the uptake of the aromatic AA, phenylalanine.	1.35896e-57
NZ_CP043808.1\|WP_022926230.1\|2449700_2450540_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213191	cd03224, ABC_TM1139_LivF_branched, ATP-binding cassette domain of branched-chain amino acid transporter. LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.	1.11416e-86
NZ_CP043808.1\|WP_022926235.1\|2454886_2455552_-\|amino-acid-ABC-transporter-permease	gnl\|CDD\|223836	COG0765, HisM, ABC-type amino acid transport system, permease component [Amino acid transport and metabolism].	7.69464e-70
NZ_CP043808.1\|WP_022926245.1\|2467575_2468544_+\|hypothetical-protein	gnl\|CDD\|284659	pfam07291, MauE, Methylamine utilisation protein MauE. This family consists of several bacterial methylamine utilisation MauE proteins. Synthesis of enzymes involved in methylamine oxidation via methylamine dehydrogenase (MADH) is encoded by genes present in the mau cluster. MauE and MauD are specifically involved in the processing, transport, and/or maturation of the beta-subunit and that the absence of each of these proteins leads to production of a non-functional beta-subunit which becomes rapidly degraded.	4.69131e-06
NZ_CP043808.1\|WP_033419137.1\|2462432_2463410_+\|AAA-family-ATPase	gnl\|CDD\|379289	pfam13604, AAA_30, AAA domain. This family of domains contain a P-loop motif that is characteristic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. There is a Walker A and Walker B.	4.6344e-68
NZ_CP043808.1\|WP_157609223.1\|2460071_2460269_-\|hypothetical-protein	gnl\|CDD\|234938	PRK01297, PRK01297, ATP-dependent RNA helicase RhlB; Provisional.	0.000180407
NZ_CP043808.1\|WP_022926234.1\|2454143_2454890_-\|amino-acid-ABC-transporter-ATP-binding-protein	gnl\|CDD\|224051	COG1126, GlnQ, ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism].	2.71269e-145
NZ_CP043808.1\|WP_028131247.1\|2450536_2451277_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213186	cd03219, ABC_Mj1267_LivG_branched, ATP-binding cassette component of branched chain amino acids transport system. The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).	6.11442e-104
NZ_CP043808.1\|WP_161600249.1\|2464394_2464997_-\|DUF4245-family-protein	gnl\|CDD\|379430	pfam14030, DUF4245, Protein of unknown function (DUF4245). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 188 and 235 amino acids in length.	6.43582e-26
NZ_CP043808.1\|WP_022926236.1\|2455565_2456471_-\|transporter-substrate-binding-domain-containing-protein	gnl\|CDD\|270431	cd13713, PBP2_Cystine_like_1, Substrate binding domain of putative ABC transporters involved in cystine import; the type 2 periplasmic binding protein fold. This group contains uncharacterized periplasmic cystine-binding domain of ATP-binding cassette (ABC) transporters. Cystine is an oxidized dimeric form of cysteine that is required for optimal bacterial growth. In Bacillus subtilis, three ABC transporters, TcyJKLMN (YtmJKLMN), TcyABC (YckKJI), and YxeMNO are involved in uptake of cystine. Likewise, three uptake systems were identified in Salmonella enterica serovar Typhimurium, while in Escherichia coli, two transport systems seem to be involved in cystine uptake. Moreover, L-cystine limitation was shown to prevent virulence of Neisseria gonorrhoeae; thus, its L-cystine solute receptor (Ngo0372) may be suited as target for an antimicrobial vaccine. The cystine receptor belongs to the type 2 periplasmic binding fold protein superfamily (PBP2). The PBP2 proteins are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. 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 receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	7.62063e-76
NZ_CP043808.1\|WP_022926237.1\|2456769_2457819_-\|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase	gnl\|CDD\|234893	PRK01045, ispH, 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Reviewed.	0
NZ_CP043808.1\|WP_149814783.1\|2467061_2467571_+\|carbonic-anhydrase	gnl\|CDD\|239474	cd03379, beta_CA_cladeD, Carbonic anhydrases (CA) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism in which the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide is followed by the regeneration of an active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. CAs are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionarily distinct families of CAs (the alpha-, beta-, and gamma-CAs) which show no significant sequence identity or structural similarity. Within the beta-CA family there are four evolutionarily distinct clades (A through D). The beta-CAs are multimeric enzymes (forming dimers,tetramers,hexamers and octamers) which are present in higher plants, algae, fungi, archaea and prokaryotes.	1.20452e-47
NZ_CP043808.1\|WP_033419131.1\|2460949_2461813_-\|SDR-family-oxidoreductase	gnl\|CDD\|187578	cd05269, TMR_SDR_a, triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs. TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	9.15682e-87
NZ_CP043808.1\|WP_022926243.1\|2466107_2467034_+\|carbohydrate-kinase	gnl\|CDD\|238572	cd01167, bac_FRK, Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.	1.05286e-64
NZ_CP043808.1\|WP_028131252.1\|2461841_2462210_-\|DoxX-family-protein	gnl\|CDD\|379266	pfam13564, DoxX_2, DoxX-like family. This family of uncharacterized proteins are related to DoxX pfam07681.	6.04617e-12
NZ_CP043808.1\|WP_022926238.1\|2457867_2458632_-\|alpha/beta-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	1.74285e-15
NZ_CP043808.1\|WP_022926233.1\|2452861_2454112_+\|DNA-recombination-protein-RmuC	gnl\|CDD\|376878	pfam02646, RmuC, RmuC family. This family contains several bacterial RmuC DNA recombination proteins. The function of the RMUC protein is unknown but it is suspected that it is either a structural protein that protects DNA against nuclease action, or is itself involved in DNA cleavage at the regions of DNA secondary structures.	8.87804e-98
NZ_CP043808.1\|WP_084485252.1\|2451342_2452605_-\|substrate-binding-domain-containing-protein	gnl\|CDD\|380551	cd06328, PBP1_SBP-like, periplasmic substrate-binding domain of active transport proteins (substrate binding proteins or SBPs). Periplasmic substrate-binding domain of active transport proteins found in gram-negative and gram-positive bacteria. Members of this group are initial receptors in the process of active transport across cellular membrane, but their substrate specificities are not known in detail. However, they closely resemble the group of AmiC and active transport systems for short-chain amides and urea (FmdDEF), and thus are likely to exhibit a ligand-binding mode similar to that of the amide sensor protein AmiC from Pseudomonas aeruginosa. Moreover, this binding domain has high sequence identity to the family of hydrophobic amino acid transporters (HAAT), and thus it may also be involved in transport of amino acids.	1.96437e-132
NZ_CP043808.1\|WP_022926240.1\|2460367_2460634_+\|exodeoxyribonuclease-VII-small-subunit	gnl\|CDD\|179195	PRK00977, PRK00977, exodeoxyribonuclease VII small subunit; Provisional.	2.46542e-19
NZ_CP043808.1\|WP_022926242.1\|2465085_2466108_+\|class-II-fructose-bisphosphatase	gnl\|CDD\|236536	PRK09479, glpX, fructose 1,6-bisphosphatase II; Reviewed.	0

>NZ_CP043808.1|WP_022926238.1|2457867_2458632_-|alpha/beta-hydrolase
MPEDATARRPAMVLLHGTRMSRAQWEPYRALLPEIDLVTVDLPGHGARVAEPFTRESALATIGAAVAEAGGGAVGRGRPPVLAGHSLGGYLAMMWAARHPDALGGLVLVGASADPRGPLTVVYRGFARALPVLGADRTAGAANALMRLLGARGEHADALPDGAAYAALPAAWDLVMREARPELLRAVRCPVTIVNGQLDQMRIHAGRFARAAGGARVVTVPAATHLMPSTHAEAVASTLREAVVGVHGPSSLST
>NZ_CP043808.1|WP_022926237.1|2456769_2457819_-|4-hydroxy-3-methylbut-2-enyl-diphosphate-reductase
MDVPEAAADRTGRRVLLAAPRGYCAGVDRAVVTVEKALELYGPPVYVRKEIVHNKHVVRTLEKRGAIFVEETDEVPEGARVIFSAHGVSPTVHEEARQLSLKTIDATCPLVTKVHREAVRFADDDYDILLVGHEGHEEVEGTAGEAPDHITLVESPEDVDHVEVRDPEKVVWLSQTTLSVDETMETVRRLREKFPKLQDPPSDDICYATQNRQVAVKQMASDCDLMIVVGSQNSSNSKRLVEVALEYGSRDGHLVDYADEIDEAWLEGVTTVGVTSGASVPEVLVRDVLDWLAARGYADVSAVTAAEESLLFALPNELRRDLKAAGQQTSKVRHDPSSIPSGSGHGPLR
>NZ_CP043808.1|WP_022926236.1|2455565_2456471_-|transporter-substrate-binding-domain-containing-protein
MATTSFRAGLVALAAASSLVLAACGDDGSTDSGAGGGSESGAGSTGDASEAQLINDGELVVAMSGEFQPFSYFEGNTLTGFDHDIGQAIADELGLEMVPQTGAFDTLIGGLGANRYDVLIASMTPTEERATQVEFSDGYYSSGAQAFVASGTECTSLDQMDQPSIGVAAGTTYQDWLNDNGGDWVGEVRTFSSDITALRDVGTGRLDAAMTDRLVGLYQINEAGLDLVPCGDPLYTEEPAFAVKKGNTALVEELNTALATIVENGTYGEISTEYFGQDISGSGGATDDGAGSTDDAATTTD
>NZ_CP043808.1|WP_022926235.1|2454886_2455552_-|amino-acid-ABC-transporter-permease
MGFFDLFVEYAPLFTEAAWVTLRISAAAIAMAMVLGALIAALAMSKVRVLRWLATAYIGLVRGTPLITQIFIIYFGLTMIVTLPAFWAGALALAFHNSAYIAEIIRSGFQAVPKGLTEASRSLGMSKMKTLKRVQAPLALRTTLPVLGNQYIIAVKDSSLVSFIGMTELFQTSRNVAASTYQEMEAYIAVAVFYLAIVLALTAAVNALEHRLSKHRRPATS
>NZ_CP043808.1|WP_022926234.1|2454143_2454890_-|amino-acid-ABC-transporter-ATP-binding-protein
MSDDTPLVRMRGIVKRFGTTTVLDGIDLDVTSGEVVTLIGPSGAGKSTLLRCINGLERITEGSIEVDGEELAYTEKRLNHIRSRIGMVFQAFNLFPHMTVGENIAVAQREVLGRSGEQAREKARSLLERVGLEHKTDAYPDNLSGGQQQRVAIARALAMDPAVMLFDEPTSALDPELVGEVLSVMRDLASEGMTMVVVTHEMRFARQAADRVVLLADGGIAEQGPPTQVLQQPTSERGRAFLQELEEA
>NZ_CP043808.1|WP_022926233.1|2452861_2454112_+|DNA-recombination-protein-RmuC
MSEELTTGAVLPLLLALAVGLVLGWLLARSGAAARSARAQTEVALARASRDQAHAEAAELRLELDGVSSREDQDSRTAAELAPLRAALDRVEQQVRTLERDRVEHFGQVGEHLDQVATQTRALREQTAALSGALSASGTRGTWGEVQLRRVMEHAGMLARCDFDEQVSAISRHDARVRPDAVVRLPGDKVIVVDSKAPLSAFLRAQAPERSGDEVDALLGEHAAALRTHVDGLAAKDYWSAFATSPELVVCFVPSDAVLAAALRAAPDLYDHAQSRKVVLASPATLLAVLRATALAWQQDALAGNARELLALGSELHQRLGTVGRHTRAMGSALRRSVETYNQLVGTLESRVMVTSRRMSELGLAEAGPEPLPVLESAPRPVAEDWLAVELEQGTPSRSEEQDAAAARGTRRREVG
>NZ_CP043808.1|WP_084485252.1|2451342_2452605_-|substrate-binding-domain-containing-protein
MNHLSCSTARRSVPVTARPVRLLTVLTATTALTLSACAPSSTDGGGDDSGASGEGSEGGGTAQVGIIYSETGPLAAYGEQYRQGLEAGIDYATDGTGEVDGTTIEVEYRDDAGNPDTAVAAAKDLIGQDYQILGGTVVSGIATAMAEQAAQNEILYISGPAATDAITGVNEFTFRSGRQSFQDVATAGAMLEDSSGKVVVLAQDNAFGQGNLAAVEAVLGAEGAEVASVLVPEDATEFTGFARQVVDEEPDLIFVAWAGATAGNMWQSLTQQDVFDAAPVVTGLADSATFAAYGDAGEQISFLSHYFPEATDNEVNQALVDSVTEAGGTPDLFTVDGFVAGQMIVQAVAEGGDDVTAMIDALEGWEFEGPKGTTTVREGDHALVQDMFTASLVQDGDAWVPEVIDTVAADEVAPPEASGE
>NZ_CP043808.1|WP_028131247.1|2450536_2451277_-|ABC-transporter-ATP-binding-protein
MEVRDLSLRIGGAQILEDISITVPRGQIVGVIGPNGAGKTTLFNLVSGVHAPTSGQVLLGGRDLTRSSITQRANAGLGRTFQTSSLFPGLTVHENARLAAQVTEGRAISLFSFPRRGDAASRRASELLEEVGLAHRAEHRAGDLPHGDKRKLEIAMLLATDPEVVLLDEPMAGVASGDVPGLTEVIRGLHRDHGCTVLMVEHHMEVLLGLVERVAVLHFGHLLAMDTPEAVMADPTVQSAYLGETV
>NZ_CP043808.1|WP_022926230.1|2449700_2450540_-|ABC-transporter-ATP-binding-protein
MTPAQPTGDLTDAPARSEDVDPVLHVRGLSAHVAGQQVVEHVDLDVAPVGVTALLGRNGVGKTSTIKAVLGLIGRAGEVELAGTDLVPLPTHQIVRLGIGYVPEDREVFAGLTVTDNLRLAERRGGEHRYDLVYDLFPELKQRGAQAAGTLSGGQQQMVSLARALLNDNQVLLVDEPTKGLAPKLVQEVSQVLARAAQVAPILLVEQNLQVVRELAHHAVVLTDGRSVHHGPAQEFLADDALTQRLLGVHGEGGSDPAEEHAQDRDEAGARHTREEHSE
>NZ_CP043808.1|WP_022926228.1|2447683_2448832_-|branched-chain-amino-acid-ABC-transporter-permease
MTTPTTQPSRRSWLGRLVPLALVVLLACLPLLNLHLPGVLPGPTYTPGSLHLMALAMVMAALALSYHLLLGVAGLLSFGHALYFGFGAYVLGIVMSELDLGLVPSALVVLVAGVVFSTLLGAISLRVTGIPFAMVTLAFAQAGSVLVRRDPGRVTGGEEGLRLPTEHVPDALIGVANTRNLYWLALAALVLAFLLTTWVQRSRAGHVAEAVRENELRVRVLGMRPFVVKLAIFVAASVIAIGMGMVHLLLNSGAVPTIVSAEFTISLLLMVVIGGVGSRWGAVTGAVLYVLLNQRLTVLAQAEWVHDLPAVLRIPLSEPMFILGTLFVLVVMFLPGGIAGTVTRLRGRRPSRGGAEPGADRVEQMDDDAREPQHEGAGAARP
>NZ_CP043808.1|WP_157609223.1|2460071_2460269_-|hypothetical-protein
MSDQPQTSEPTPPEPTPSEPRPSEPAPDEPRPSEPGPAEPAPSEPGPMEPEPAPEPAPEGPPTDA
>NZ_CP043808.1|WP_022926240.1|2460367_2460634_+|exodeoxyribonuclease-VII-small-subunit
MSESRDESTPATPVVELSYEQARDELVALVARIESGQVPLEEAMTLWERGEELAAHCQTKLDAAQESLDRSTQDGRPPDGTAAEDPDD
>NZ_CP043808.1|WP_033419131.1|2460949_2461813_-|SDR-family-oxidoreductase
MSDSLIAVTGATGHLGGLVIEKLLESRSAASLVALVRDQKKAEHLAAKGVQVRVASYEDRAALESALTGVETLLLVSGSEVGQRVPQHVNVIDAARTAGVGRVVYTSAPKATTSELVVAAEHKATEEYLTASGLDYTILRNGWYTENYLPQVATARQTGAVVAAVGDGRVASASRADYADGAAAVLVGAGHSGTVYELSGDQAWDYDELAATIGQIIGKPVTYQRVDGPTLVEMLTGTGMPEEVARLMAALDANIADGLLAGATGELSALIGRPTTSLKEGLLAALA
>NZ_CP043808.1|WP_028131252.1|2461841_2462210_-|DoxX-family-protein
MLLALWIINGLLALAFLGAGGMKLLRGKDALAASGMSYVEDFSAGTVKLIGALEVLGAVGLIVPLLTGIVPVLTPIAAIGLAIIMIGAVVTHIRRKEPPLFPAILGVLAVASAVLGFIAVTN
>NZ_CP043808.1|WP_033419137.1|2462432_2463410_+|AAA-family-ATPase
MGWRFASSEDRDAIIGMITDQAEASSLRLTPPELASSPDPFRREDGSSVFRPKASTVYSSEQVLAAEDRLIAAAETRTARGVLLSFIEDAARGTRRQHALTADQEQAIAQVAVSNRVLDVLVGPAGAGKTTAMSALRRAWERQHGRGSVIGLAPSAAAAEVLAGDLGISTENTAKWLYEHRHGAWSLTARQLVIIDEASMAGTLSLDAITRHAAEAGAQVLLVGDWAQLSAVETGGAFGLLVSAREPAPELTDVRRFRNEWEKGASLGLRIGDTDVIDTYLAQDRVHDGGYDDVLDSAYRAWQADPRACLQRLSVGVAECGPRES
>NZ_CP043808.1|WP_161600249.1|2464394_2464997_-|DUF4245-family-protein
MSERPHPTPAGPPAAAPAPDRRRQRLASYTVRNMVYSTVLVLALVLVWWSLTYNPTEQEPRRVEVASTAAYAVDQADWPVWVPEPGQEWSPTVVWFEPLEDVTTWHVSYVTPEGEYLAIHQADGVTPAWRDAVLSGGEQVGQTLLPGPDGEQQWQAWEAESGNAQNAWVLDTEDAGTVIVHGTAQEDEARALLETIQARD
>NZ_CP043808.1|WP_022926242.1|2465085_2466108_+|class-II-fructose-bisphosphatase
MADRSPKTTDQVLPDRNLALELVRVTEAAALAAGRWVGRGDKILADNAAVEAMRKVISQVAMDGVVVIGEGEKDEAPMLFNGESVGDGNGPAVDVAVDPIDGTTPTAKGMDNSIAVMAVSERGTMYDPSAVFYMDKLVVGADVADRVDIRLPVQENLRRIARAKKRYVEDLTVIMLDRPRHDRYTHEVREAGARLRFITDGDVAAAIAAAREGSSVDMLIGIGGTPEGIITACAMKAMGGVIQGRLWPKDDEERQKAIDAGHDLDRVLSTDDLVTGDNCFFVATGITTGELLHGVRYGSGTAVTQSLVMRSRSGTIREITSHHRLDKVAAIADSLAPDAV
>NZ_CP043808.1|WP_022926243.1|2466107_2467034_+|carbohydrate-kinase
MAAVLTVGEALIDIVVPHGDGERSEHVGGSPANVAIGISALDHDSRLTAYLAPDEHGDRVREHLERHDVRLTEGSLRADHTSTATAHLDADAVATYEFDLAWEVGPQDLSGVGHVHTGSIAATLEPGGSEVVRLIERARESATVSYDPNARPSIMGDPRDTRQRIEECLGRSDVVKASLEDVEWLYGEDVDVVQVVHEWGQLGPDLVVVTRGGDGAVVHLSRDDTTLELPSLTVQVVDTVGAGDSFMSGLLSGLLDAGLLGSPQARTRLAHADLEDIAPALERAVACAGFTVARAGAAAPTRADLGLA
>NZ_CP043808.1|WP_149814783.1|2467061_2467571_+|carbonic-anhydrase
MSTSTAFEDLLRANEEYASTHAEELQGFDGVAHAGVAIVTCMDSRIEPLQMLGLTHGDAKIFRNPGGRVTDAALEALVLGVHLLGVERILVVPHTRCAMTTKSENELRETISELTGIDAWFQRFHVVPDQQAVLAEDVHRVTSHPLIQGRVEVGGFLYDVDTGRLTQLV
>NZ_CP043808.1|WP_022926245.1|2467575_2468544_+|hypothetical-protein
MLSALSLAPLTLAALLGWSGAVKLRQPAATAAMVRELRLPRWCAPAAVSRVLPWAELGTAALLLTPWTWTYAVGAGAALALCTAFLVVVARAMGFRPRPVCACFGRVGHHHISARTVVRNAALVGLAALAVGIAVAGSSTGRLVASYRGADWVWLGLAVALAALTAAAVAGGGPDTDLRPSSTPGPASPDRSTLLHSPLVAADLETTTLLTLVLPRPQLVVGVDCWCGSTFAVLQRLPDWRGRAPWLGVHLVHTRPPFAEPRTRGLTDLWWDPDGRLVAALGAGPGPCAVLVDESGVLDGPVTGVEQIERLVDYSASRSRTT

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Crispr_ID: NZ_CP043808_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043808_6

2664961-2665060

Orphan

Consensus_repeat	Method
GCTGCGGCGGCCCTGAGCGCCCAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043808_6

>merge|NZ_CP043808|6|2664961-2665060|CRISPRCasFinder
GCTGCGGCGGCCCTGAGCGCCCACGCCGCTTCGGTGGGGCTGCGGCGGGCCTGAGCGCCCGCGCCGCTTCGGTGGGGCTGCGGCGGGCCTGAGCGCCCAC

>NZ_CP043808|6|6|2664961-2665060|CRISPRCasFinder
GCTGCGGCGGCCCTGAGCGCCCAC	GCCGCTTCGGTGGGGCTGCGGCGGGCCTGAGCGCCCGCGCCGCTTCGGTGGG
GCTGCGGCGGGCCTGAGCGCCCAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043808.1\|WP_084485173.1\|2648075_2648354_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|370615
NZ_CP043808.1\|WP_022925155.1\|2665557_2666337_-\|DUF4031-domain-containing-protein	unknown	unknown	gnl\|CDD\|379076
NZ_CP043808.1\|WP_022925151.1\|2669826_2670270_+\|universal-stress-protein	unknown	unknown	gnl\|CDD\|238182
NZ_CP043808.1\|WP_028131047.1\|2648485_2649193_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|223816
NZ_CP043808.1\|WP_084485172.1\|2650745_2652107_+\|PDZ-domain-containing-protein	unknown	unknown	gnl\|CDD\|273938
NZ_CP043808.1\|WP_149814809.1\|2657945_2658197_-\|thiamine-binding-protein	unknown	unknown	gnl\|CDD\|376658
NZ_CP043808.1\|WP_022925154.1\|2666443_2666740_+\|WXG100-family-type-VII-secretion-target	unknown	unknown	gnl\|CDD\|274862
NZ_CP043808.1\|WP_149814811.1\|2670266_2671322_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|271363
NZ_CP043808.1\|WP_149814813.1\|2671938_2673606_-\|formate--tetrahydrofolate-ligase	unknown	unknown	gnl\|CDD\|376511
NZ_CP043808.1\|WP_022925152.1\|2668842_2669679_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293840
NZ_CP043808.1\|WP_028131041.1\|2674274_2674952_+\|uracil-DNA-glycosylase	unknown	unknown	gnl\|CDD\|235376
NZ_CP043808.1\|WP_022925156.1\|2663774_2664035_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_149814808.1\|2646087_2647995_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_149814810.1\|2661479_2662865_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274774
NZ_CP043808.1\|WP_022925166.1\|2649210_2650701_+\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP043808.1\|WP_022925153.1\|2666960_2668586_-\|chaperonin-GroEL	unknown	unknown	gnl\|CDD\|234573
NZ_CP043808.1\|WP_022925148.1\|2673692_2673983_-\|DUF3263-domain-containing-protein	unknown	unknown	gnl\|CDD\|378688
NZ_CP043808.1\|WP_022925159.1\|2660496_2661483_-\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|133030
NZ_CP043808.1\|WP_149814812.1\|2671228_2671942_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|271363
NZ_CP043808.1\|WP_022925164.1\|2653985_2655263_+\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187565

Protein	Function_ID	Function_description	E-value
NZ_CP043808.1\|WP_084485173.1\|2648075_2648354_-\|hypothetical-protein	gnl\|CDD\|370615	pfam09683, Lactococcin_972, Bacteriocin (Lactococcin_972). These sequences represent bacteriocins related to lactococcin. Members tend to be found in association with a seven transmembrane putative immunity protein.	4.99288e-05
NZ_CP043808.1\|WP_022925155.1\|2665557_2666337_-\|DUF4031-domain-containing-protein	gnl\|CDD\|379076	pfam13223, DUF4031, Protein of unknown function (DUF4031). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and viruses. Proteins in this family are typically between 91 and 130 amino acids in length. There is a conserved HYD sequence motif.	1.14228e-28
NZ_CP043808.1\|WP_022925151.1\|2669826_2670270_+\|universal-stress-protein	gnl\|CDD\|238182	cd00293, USP_Like, Usp: Universal stress protein family. The universal stress protein Usp is a small cytoplasmic bacterial protein whose expression is enhanced when the cell is exposed to stress agents. Usp enhances the rate of cell survival during prolonged exposure to such conditions, and may provide a general "stress endurance" activity. The crystal structure of Haemophilus influenzae Usp reveals an alpha/beta fold similar to that of the Methanococcus jannaschii MJ0577 protein, which binds ATP, athough Usp lacks ATP-binding activity.	6.3719e-24
NZ_CP043808.1\|WP_028131047.1\|2648485_2649193_+\|response-regulator-transcription-factor	gnl\|CDD\|223816	COG0745, OmpR, Response regulators consisting of a CheY-like receiver domain and a winged-helix DNA-binding domain [Signal transduction mechanisms / Transcription].	1.42758e-82
NZ_CP043808.1\|WP_084485172.1\|2650745_2652107_+\|PDZ-domain-containing-protein	gnl\|CDD\|273938	TIGR02037, Probable_periplasmic_serine_protease_do/HhoA-like, periplasmic serine protease, Do/DeqQ family. This family consists of a set proteins various designated DegP, heat shock protein HtrA, and protease DO. The ortholog in Pseudomonas aeruginosa is designated MucD and is found in an operon that controls mucoid phenotype. This family also includes the DegQ (HhoA) paralog in E. coli which can rescue a DegP mutant, but not the smaller DegS paralog, which cannot. Members of this family are located in the periplasm and have separable functions as both protease and chaperone. Members have a trypsin domain and two copies of a PDZ domain. This protein protects bacteria from thermal and other stresses and may be important for the survival of bacterial pathogens.// The chaperone function is dominant at low temperatures, whereas the proteolytic activity is turned on at elevated temperatures. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides].	8.72192e-92
NZ_CP043808.1\|WP_149814809.1\|2657945_2658197_-\|thiamine-binding-protein	gnl\|CDD\|376658	pfam01910, Thiamine_BP, Thiamine-binding protein. The crystal structure of two of these members shows that this domain has a ferredoxin like fold and is likely to exists as at least homodimers. Sulphate ions are are located at the dimer interfaces, which are thought to confer additional stability. Although the function of this domain remains to be identified, its structure suggests a role in protein-protein interactions possibly regulated by the binding of small-molecule ligands. Solution of the structure of the hyperthermophilic anaerobic Thermotoga maritima sequence, UniProtKB:Q9WYV6, shows that this has a beta-alpha-beta-beta-alpha-beta ferredoxin-like fold and assembles as a homotetramer. It was possible to identify a pocket in each monmer that bound an unidentified ligand. It was also found that it bound charged thiamine though not hydroxymethyl pyrimidine. It is proposed that it is transporting charged thiamine around the cytoplasm. Under oxidative conditions this bacterium is under stress, and the transcriiptional unit within which this protein is expressed is up-regulated in these conditions, suggesting that the chelation of cytoplasmic thaimine is part of the response mechanism to such oxidatvie stress, which is mediated by this family.	1.46933e-29
NZ_CP043808.1\|WP_022925154.1\|2666443_2666740_+\|WXG100-family-type-VII-secretion-target	gnl\|CDD\|274862	TIGR03930, WXG100_ESAT6, WXG100 family type VII secretion target. Members of this protein family include secretion targets for the two main variants of type VII secretion systems (T7SS), one found in the Actinobacteria, one found in the Firmicutes. This model was derived through iteration from pfam06013. The best characterized member of this family is ESAT-6 from Mycobacterium tuberculosis. Members of this family usually are ~100 amino acids in length but occasionally have a long C-terminal extension.	7.45824e-14
NZ_CP043808.1\|WP_149814811.1\|2670266_2671322_+\|hypothetical-protein	gnl\|CDD\|271363	cd10329, SLC5sbd_SGLT1-like, Na(+)/glucose cotransporter SGLT1 and related proteins; solute binding domain. This subfamily includes the solute-binding domain of SGLT proteins that cotransport Na+ with various solutes. Its members include: the human glucose (SGLT1, -2, -4, -5 ), chiro-inositol (SGLT5), and myo-inositol (SMIT) cotransporters. It also includes human SGLT3 which has been characterized as a glucose sensor and not a transporter. It belongs to the solute carrier 5 (SLC5) transporter family.	8.72747e-95
NZ_CP043808.1\|WP_149814813.1\|2671938_2673606_-\|formate--tetrahydrofolate-ligase	gnl\|CDD\|376511	pfam01268, FTHFS, Formate--tetrahydrofolate ligase.	0
NZ_CP043808.1\|WP_022925152.1\|2668842_2669679_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293840	cd16282, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities 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.	4.32879e-59
NZ_CP043808.1\|WP_028131041.1\|2674274_2674952_+\|uracil-DNA-glycosylase	gnl\|CDD\|235376	PRK05254, PRK05254, uracil-DNA glycosylase; Provisional.	3.25355e-121
NZ_CP043808.1\|WP_149814810.1\|2661479_2662865_-\|hypothetical-protein	gnl\|CDD\|274774	TIGR03766, hypothetical_protein_lp_2141, conserved hypothetical integral membrane protein. Models TIGR03110, TIGR03111, and TIGR03112 describe a three-gene system found in several Gram-positive bacteria, where TIGR03110 (XrtG) is distantly related to a putative transpeptidase, exosortase (TIGR02602). This model describes a small clade that correlates by both gene clustering and phyletic pattern, although imperfectly, to the three gene system. Both this narrow clade, and the larger set of full-length homologous integral membrane proteins, have an especially well-conserved region near the C-terminus with an invariant tyrosine. The function is unknown.	1.81062e-13
NZ_CP043808.1\|WP_022925166.1\|2649210_2650701_+\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	2.98328e-60
NZ_CP043808.1\|WP_022925153.1\|2666960_2668586_-\|chaperonin-GroEL	gnl\|CDD\|234573	PRK00013, groEL, chaperonin GroEL; Reviewed.	0
NZ_CP043808.1\|WP_022925148.1\|2673692_2673983_-\|DUF3263-domain-containing-protein	gnl\|CDD\|378688	pfam11662, DUF3263, Protein of unknown function (DUF3263). This family of proteins with unknown function appears to be restricted to Actinobacteria.	3.02756e-31
NZ_CP043808.1\|WP_022925159.1\|2660496_2661483_-\|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.	1.05103e-69
NZ_CP043808.1\|WP_149814812.1\|2671228_2671942_+\|hypothetical-protein	gnl\|CDD\|271363	cd10329, SLC5sbd_SGLT1-like, Na(+)/glucose cotransporter SGLT1 and related proteins; solute binding domain. This subfamily includes the solute-binding domain of SGLT proteins that cotransport Na+ with various solutes. Its members include: the human glucose (SGLT1, -2, -4, -5 ), chiro-inositol (SGLT5), and myo-inositol (SMIT) cotransporters. It also includes human SGLT3 which has been characterized as a glucose sensor and not a transporter. It belongs to the solute carrier 5 (SLC5) transporter family.	9.02894e-68
NZ_CP043808.1\|WP_022925164.1\|2653985_2655263_+\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|187565	cd05255, SQD1_like_SDR_e, UDP_sulfoquinovose_synthase (Arabidopsis thaliana SQD1 and related proteins), extended (e) SDRs. Arabidopsis thaliana UDP-sulfoquinovose-synthase ( SQD1), an extended SDR, catalyzes the transfer of SO(3)(-) to UDP-glucose in the biosynthesis of plant sulfolipids. Members of this subgroup share the conserved SDR catalytic residues, and a partial match to the characteristic extended-SDR NAD-binding motif. 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_CP043808.1|WP_022925156.1|2663774_2664035_-|hypothetical-protein
MQSLAGGARPRGAGAPDLLAALARTLARLHDLQPLLVRRAAFLVHETFVIQPHLHRVAALTTDASRRQTYLEAVAQLRDGLEVCLG
>NZ_CP043808.1|WP_149814810.1|2661479_2662865_-|hypothetical-protein
MSLLVLVLLGRALLRPGAGVGGGEARSGTLWASAAAGTLLAGAHAALALIPFGFDARRIFSSASTLAVGEPLPAEALTYYARYPHNVRLLWLEQVAVEAGSVVSLPALGAVLLPHVLCVGVVLWSLGRAAQLLGHPRAVLPVQALALVLVGLSPNVAVPYTDLPAAAAVSVAALAMVRCGGAAGWSWPWALTGAVSLGLGVALKPYVVVVAIALVLVVLWSRQWRRVVAVALLGAVSWGTVALLDGASARGTGLDAQRLAQVEAPFPPEHFLAMGTWDSAEDSPVRRWGAYRQDQVDATAAMDPASRAADLRAQAWDQVGGRGLVGNLRFVGAKALWVWGDGTFWAHGEGADSRQASSLPESLSGMTAASRGAGELYDERAGVVQGLWVAVVLLTGAVLLRARADPLLTTWALALGGLTAYLLIFEARPRYVLALVPVVLLVLLRAGLGSADHPTATREAR
>NZ_CP043808.1|WP_022925159.1|2660496_2661483_-|glycosyltransferase-family-2-protein
MSAPQAGPIALSVVVPMFDEQDVLPLLVRRLRPVLDGLGLDYEVLVVDDGSSDATPVLLARERHSWAQLRVVRLRANAGHQAAISAGLERARGELVVTIDADLQDPPELIADMVRLARAESLDVVYAVRDDRTTDTRFKRVTASGYYDTMRRLGADHGPSNAGDYRLMSRATVEAVTALPEHHRVLRLVVPSLGFPSGVLTYRRDARAAGRSKYPLSSMVRLALDSITGASIAPLRLATWLGFVGAVVALGLLVYALVGYAVGLNVPGWTSTFMVVTAVGGVQLLCLGILGEYVGRTYTMQLGRPTYYVAHDSLSGQEPPPPPGPTTG
>NZ_CP043808.1|WP_149814809.1|2657945_2658197_-|thiamine-binding-protein
MSAAVADALRVVRDSGLPYELTSMFTTIEGEWDEVMPVIKAACDAVAEHSPRVSLVVKADLRPGYTGQLTEKVERVTDRLADG
>NZ_CP043808.1|WP_022925164.1|2653985_2655263_+|NAD-dependent-epimerase/dehydratase-family-protein
MLIAVLGGDGFCGWPAALHLSDLGHEVVIVDNLVRRRIDEELGAQSLTPIAGIEERLAAWHEVSGQQMRFRDIDLAQDYDGLRSFLETERPDVVVHFAEQRSAPYSMKSPRHKRYTVDNNTGATHNLLCALVETGLDAHLVHLGTMGVYGYGTAGMAIPEGYLDVQITGDDGAQVDQQILYPTNPGSVYHMTKCLDQQLFAYYAKNDALRITDLHQGIIWGTHTDQTLRDERLINRFDYDGDYGTVLNRFLMQAAVGYPLTVHGTGGQTRAFIHLRDMARCVQIAVENPPARGDRVKIFNQMTQTHRVRDLAELVARISDAEVELVPNPRHEAAENELHVHNETFLDLGLEPTLLEEGLLMEVEDVARRYADRADLEKIPCTSTWTSAQEAGVPASRSALAGAGAAVSVEGNPGDRAGDRAEHPA
>NZ_CP043808.1|WP_084485172.1|2650745_2652107_+|PDZ-domain-containing-protein
MTTPQHDPQDRSADQASRADATSPIHPDATAPVPRAEGSRAEESRAESPRAEESQAETSATQAPPAAPPAAPRRERRRVGDIAVASVLAALLASGGTYAAIQLAEDGSGQAAQESTQETEDEQASGDAEGTTVSLTGEQDWASVADAVTPSTVSIAVAGAQGEASGSGVVWDDEGHVVTNSHVVEGAQEVQVTLPGGRSYSAEVVGSDPSSDLAVLQLDSVPDELTPIAVGDDSALGVGDPVMAVGNPLGLSGTVTTGIVSALDRPVTTQGSSQNPADPNSAVFTNAIQTSAAINPGNSGGALVNAAGELVGINSSIASLGSAMGGQSGSIGIGFAIPSSKVQLIADQLIETGTATHAFLGVGLDDATAETDGATVSGAVVTQVEPDSPAAEVGLESGDLIVGIDDEPITSSTALVGQVRERGAGDEATIAYIRDGERAEVTVTLVTRPDEEG
>NZ_CP043808.1|WP_022925166.1|2649210_2650701_+|HAMP-domain-containing-histidine-kinase
MLQHLRRAAYSKLHRLSLTRRLVTVLVLLVLAAYLLTTSVTITMLRGYLVDRVDADLKTYIDPLAERVSAQLLEDATGQQSSSAELWLPPNSYYILLTPGERSSRTITLASRGMDDTPDLRRVDLDDDRLGTPFTVGSTEGVGTWRVLAVPLDERQDVFTGTIAVALPLDEVDSTARQLAFLTVVIGLTTMVVVGVLGWFAVRRAFRPLSRMEDTAAAIAAGDLTRRIPPPGARDEVSSLSESLNGMLAHIEHSFAVREASEQRMRDFVADASHELRTPLATVKGYAELHRFGAMTDPEDVAGAMRRIEDEATRMTRLVEDLLTLTRWDSQPEMAPTRVDLTVLASDVVQDARVRAPQRAVRLVPLDGAEPDAAPVVTGEDGALRQVLTNLVANALAHTPDGTPVEVAVGRTGERVVVEVRDHGQGLSDGTADRVFERFYRADKSRSRASGGTGLGLAIVAAIVGRHQGSVRHTPTPGGGATFRVELPADRRPGNS
>NZ_CP043808.1|WP_028131047.1|2648485_2649193_+|response-regulator-transcription-factor
MSATATEPEATLLVVEDETNIRELLTTSLRFAGFAVHAAADGRSALQLSGEHDFDLAVLDIMLPDMDGFTVTRTLRERGLDLPIVFLTAKDSLDDKIKGLTVGGDDYVTKPFSLEEVVARIRAVLRRTRVAEEGDDHALRVADLELDEDSHEVRRAGKVIEVSPTEFKLLRYLMLNPGRVLSKSQILDHVWDYDFRGEMNIVESYISYLRRKIDVVGEPLIHTKRGVGYVLREPR
>NZ_CP043808.1|WP_084485173.1|2648075_2648354_-|hypothetical-protein
MSALTLAWTLSVVGASPSNAIEVEYPNEGGEWRYGYSWQKAVSRYNHPSQCHGSTVTDPNGAESRSIQTAAGNFSEAGLWWSWNRSYYYWLC
>NZ_CP043808.1|WP_149814808.1|2646087_2647995_-|hypothetical-protein
MNKLVIAAVAAVTALLCYVAATFMAIDEQLRPLGATVSISVDVGDPPPAKREFVATLERVAADRGLFIVKPVVGAESPARARDLFVAGPEAPEERRAFSWYDGRLRGDLVPLTDLGSSSMAGKIYLVGASDADLSEVEDALGGIGVAATSYSVSTPTVWATVLLDTGAGPASLAGLLLLVLTVAAWSASRARRRALLVLHGEPLTRVVLYEGRAFLRLAAPAGLLVSVCAWALLLVRRGPEHLPGYLVISSTLVGALVVGGVLSASLSTLLNLPRAQHLAERSVPRRGHKRAADVLRSLTMVTVALALPALVVSVHVQRQQARGLETWEPLSSHVVTRLGGLSIETQKLEHAAGEVIARTPAEDSALSYVLFEEDPGFWRGDNFDGLVIVDQTYLELMNLEGDVSALEGVSDVTRSQLQASWDLWSERPLPTMQTAEADSRFLGGAGAQEFSNLERPLVLVVPDVEVMKPAFVLSAMSTGNILFEDAGSLATHIADEGLGSSLLSIERVADVALLQAQQAERAALLRTVAVGMLVTAWLVAASLGARVYWAVRATRLTVNRTAGRPWLALLRTPIIVDVGIALAASAILLLFQDHTPVVLVTASLLPFIAGMVSAAVHRAAAQAQVISVLTRASS
>NZ_CP043808.1|WP_022925155.1|2665557_2666337_-|DUF4031-domain-containing-protein
MTVLVDPPLWRAHGRLWSHLASDISLAELHAFAQRSGIPRRSFEGDHYDIPQERYAEVVAAGAAEVSGTELARRLRDSGLRFRKRKGERPLARVEDGLAGAAPTPHLLEVVASPLERLGAGASVVLARAQGVPERMALVRNSTREGWGAPGGKREVTDASARAAAVREVAEEIAVELEQERLVAVGYQRITLPPGHGARSWDEGDNYVQVYAATLPSPVPLRPDGVEVLEARWLSLAEARGVAGQAAWWPLAEWWWARG
>NZ_CP043808.1|WP_022925154.1|2666443_2666740_+|WXG100-family-type-VII-secretion-target
MSNTFAVDTARIAAASGDIERIATSIEGEVRAMMAKLNALQDCWRGSAAGSFHSVTQDWSATQEKVRTSLQQISTTLRTAGQDYELVEQTNRTRFTPA
>NZ_CP043808.1|WP_022925153.1|2666960_2668586_-|chaperonin-GroEL
MAKTIAFDEEARRGLEKGMNTLADAVKVTLGPKGRNVVLEKKWGAPTITNDGVSIAKEIELEDPYEKIGAELVKEVAKKTDDVAGDGTTTATVLAQAMVKEGLRNVAAGANPMALKRGIEVAVKAVNDDLLEMAKPVETKEQIAQSASISAADTEIGGMIAEAMDKVGNEGVITVEESNTFGLELELTEGMRFDKGYISPYFVTDTERMEAVLEDAYVLVVNSKISSVKDLLPLLEKVMQSGKPLMIIAEDVEGEGLATLVVNKIRGNFKSVAVKAPGFGDRRKAMLADIAILTGGQVISEEVGLKLENAELDMLGTARKVVVTKDETTIVEGGGDADQIAGRVSQIRTEIDNSDSDYDREKLQERLAKLAGGVAVIKAGAATEVELKERKHRIEDAVRNAKAAVEEGIVAGGGVALIQASRAFDGLSVEGDEATGANIVRVAIEAPLKQIAINAGLEGGVVAEKVRNLTPGEGLNAATGEYGDMLGFGVADPVKVTRSALQNAASIAALFLTTEAVIADKPEKAPAMPAGADGGMGGMDF
>NZ_CP043808.1|WP_022925152.1|2668842_2669679_-|MBL-fold-metallo-hydrolase
MSEATWREVAPGVHVRRHEELKLNCGLVVGEERSLVVDTRSFHAQGQDLLEAVRRITDTELVVVNTHAHYDHCFGNAAFRDSQIYAHSGAAEGLRRTGEHQRQQVVDHLRSTDREHLAEQVENTEIVLPFYLIEDDTALDLGGRTVELQYAGRGHTDHDLAVGVPDAGVVFAGDLVEEGADPAMEDAFPMEWAPTLRSLLERRSGETADTWVPGHGHVVDRTFVEAQAEQLAAMAERFTEVLGTGIAGVDSLANAGRGLGLGEDTLRLAAIRALELRH
>NZ_CP043808.1|WP_022925151.1|2669826_2670270_+|universal-stress-protein
MFPTRILLATDGSPSAALARERVIDLVRHTEAEVHVVHVALVSPWTNPTPLSPSLRERVEAEARPVLADAVSQLQGAHVAVAGSHLRTGRATDEILRLRDEIDADLVVIGSRGQNAFVRVLLGNDAEGIVRHAPCAVLVVRTEEETR
>NZ_CP043808.1|WP_149814811.1|2670266_2671322_+|hypothetical-protein
MTADVMLPLADAGGGMPDFTVRALDLSVIIGYLVLSRIIPLVVGSRMQKKAHAEAKASGKESDASEDYFLGGRNFIWPFVGLSLVATNMSGATFVGLAGGAYEQGISIFAYEWMSAVILVVFIFFILPFYLRSKVFTLPEFLEQRYDRRARMAFAGFNLFANMFIDMAAALFAGAVVVKVLYPDIPMIVSVAVLAILAAIYTVIGGLGAVMVSDSIQATVTLLGGVIVLIATFNAIESWDSMAQVAGDEKMSLILPADHPDLPWPGLLTGVLIVGLYYWTTNQLVVQRTLGAKSLDHGRWARCWPASSSWPSSSSSSSPGSWRSRCTRTSRVPTRSSRRSSSTCCRWACAA
>NZ_CP043808.1|WP_149814812.1|2671228_2671942_+|hypothetical-protein
MALSLYPNLESPDTVFPTLVFDLLPVGLRGLILAAVIAAITSTVDSILNSASTIVTMDFVKTLRPNTSQRGLVLTGRVATVVALVVAIIWAPFIAQFDTLYNYLQSVLSFLVPPVVAVFLVGIASKRISATAAFLTLVIMQPLGLLMFILTQVLPEEPSIQFLYAAGISTAASILLLVVISLLGPSPDESKTAELTWKSDYWTEESQALQGTAVWANYRVLSIVLLVTTAVIVVIWA
>NZ_CP043808.1|WP_149814813.1|2671938_2673606_-|formate--tetrahydrofolate-ligase
MLTDVQIAQGATLERIADIAAGLGLTEDEFEPYGHDKAKIALQVLDRLADRPDGKLILVTAINPTAAGEGKTTTNVGLSMALNRIGARAITTLREPSLGPCFGMKGGAAGGGYAQVVPMDDINLHFTGDFHAITSAHNLLAALLDNSLHQGNPLGLDPKRITWTRVLDMNDRALRNIVVGMGKKGDGVVRESGFEITVASEIMAALCLATGLEDLKERFGRIVVGYTYDKEPVTAGQLEAAGAMAMLMKDAVKPNLVQTLENTPAIIHGGPFANIAHGNNSVLATRTALKLADYVVTEAGFGADLGAEKFFDIVCPAGGLRPDAAVIVATIRALKLNGGAPKSDLGTEDVEALGAGLANLEQHLENLAKFGVPVVVALNRFPSDSDAELDLVRERCGQLGVEVARSEVFTRGGEGGEELARAVVQLCERGSDYAPLYAADADLQTKIETVAREVYRADGVSFAPAAQTQLTQLTEQGYGDLPVCMAKTQYSFSDDPTLLGAPRGFTITVRELVVNAGAGFVVALTGDIMRMPGLPKVPAALGMDIAEDGTITGLS
>NZ_CP043808.1|WP_022925148.1|2673692_2673983_-|DUF3263-domain-containing-protein
MGAARHVQQVEPPAGLSERDQEILDFENRHWTYAGSKEQGIKDLFDLSSTRYYQLLNQLIDDEAALAYKPLLIKRLRRDRSRRQRARSMRRLGIES
>NZ_CP043808.1|WP_028131041.1|2674274_2674952_+|uracil-DNA-glycosylase
MTPTPLRDLVHPSWAEALAPVEETVAELGEFLRGEVAAGRGYLPGGDHVLRVFTRPLDDVRVLIVGQDPYPTPGHAVGLSFSVAPDVSPVPRSLQNIYTELVDDLGIPRPTTGDLSPWADAGVMLLNRVLTVRPGTPASHRGKGWEKVTDLAIDALVRRGGPLVAILWGRDARNLASRLGDVPRVESAHPSPLSARGGFFGSRPFSRADELLRQQGGEAIDWRLP

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Crispr_ID: NZ_CP043808_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043808_7

2718787-2718887

Orphan

Consensus_repeat	Method
CCTTCGACGACCGGGTGCTCGAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043808_7

>merge|NZ_CP043808|7|2718787-2718887|CRISPRCasFinder
CCTTCGACGACCGGGTGCTCGACCGTGCCGTGGGGGCGGCCGCGGCCGGTGCCGTCGGCGTGGCACGCAGGGCGGCCACGTTCGACGACCGGGTGCTCGAC

>NZ_CP043808|7|7|2718787-2718887|CRISPRCasFinder
CCTTCGACGACCGGGTGCTCGAC	CGTGCCGTGGGGGCGGCCGCGGCCGGTGCCGTCGGCGTGGCACGCAGGGCGGCCA
CGTTCGACGACCGGGTGCTCGAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043808.1\|WP_022926324.1\|2724229_2724808_+\|DUF305-domain-containing-protein	unknown	unknown	gnl\|CDD\|367619
NZ_CP043808.1\|WP_022926322.1\|2727648_2727972_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_149814581.1\|2729725_2730727_-\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|366234
NZ_CP043808.1\|WP_028131277.1\|2731880_2732201_-\|transposase	unknown	unknown	gnl\|CDD\|366690
NZ_CP043808.1\|WP_022925110.1\|2706889_2707180_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_149814581.1\|2732740_2733742_-\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|366234
NZ_CP043808.1\|WP_149814815.1\|2728255_2729401_-\|IS110-family-transposase	unknown	unknown	gnl\|CDD\|376564
NZ_CP043808.1\|WP_084485264.1\|2722299_2722623_-\|NlpC/P60-family-protein	unknown	unknown	gnl\|CDD\|366353
NZ_CP043808.1\|WP_084485263.1\|2713130_2713481_+\|cation-transporter	unknown	unknown	gnl\|CDD\|225328
NZ_CP043808.1\|WP_022926303.1\|2713744_2714089_+\|NADH-quinone-oxidoreductase-subunit-A	unknown	unknown	gnl\|CDD\|376344
NZ_CP043808.1\|WP_084485271.1\|2731185_2731878_-\|IS3-family-transposase	unknown	unknown	gnl\|CDD\|222853
NZ_CP043808.1\|WP_022926299.1\|2716872_2717175_+\|NADH-ubiquinone-oxidoreductase	unknown	unknown	gnl\|CDD\|180218
NZ_CP043808.1\|WP_022926305.1\|2712065_2712983_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|374209
NZ_CP043808.1\|WP_022926332.1\|2732385_2732757_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_022925108.1\|2707578_2707908_+\|DUF3618-domain-containing-protein	unknown	unknown	gnl\|CDD\|378834
NZ_CP043808.1\|WP_022925111.1\|2706448_2706721_-\|DUF4235-domain-containing-protein	unknown	unknown	gnl\|CDD\|379422
NZ_CP043808.1\|WP_033419151.1\|2720622_2722017_+\|NADH-quinone-oxidoreductase-subunit-N	unknown	unknown	gnl\|CDD\|235603
NZ_CP043808.1\|WP_028131268.1\|2716312_2716876_+\|NADH-quinone-oxidoreductase-subunit-J	unknown	unknown	gnl\|CDD\|223909
NZ_CP043808.1\|WP_168714909.1\|2707154_2707598_+\|phage-holin-family-protein	unknown	unknown	gnl\|CDD\|377816
NZ_CP043808.1\|WP_143553825.1\|2707991_2708984_+\|YihY-family-inner-membrane-protein	unknown	unknown	gnl\|CDD\|224214

Protein	Function_ID	Function_description	E-value
NZ_CP043808.1\|WP_022926324.1\|2724229_2724808_+\|DUF305-domain-containing-protein	gnl\|CDD\|367619	pfam03713, DUF305, Domain of unknown function (DUF305). Domain found in small family of bacterial secreted proteins with no known function. Also found in Paramecium bursaria chlorella virus 1. This domain is short and found in one or two copies. The domain has a conserved HH motif that may be functionally important. This domain belongs to the ferritin superfamily. It contains two sequence similar repeats each of which is composed of two alpha helices.	2.25839e-47
NZ_CP043808.1\|WP_149814581.1\|2729725_2730727_-\|IS3-family-transposase	gnl\|CDD\|366234	pfam00665, rve, Integrase core domain. Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.	3.36609e-28
NZ_CP043808.1\|WP_028131277.1\|2731880_2732201_-\|transposase	gnl\|CDD\|366690	pfam01527, HTH_Tnp_1, Transposase. Transposase proteins are necessary for efficient DNA transposition. This family consists of various E. coli insertion elements and other bacterial transposases some of which are members of the IS3 family.	6.233e-08
NZ_CP043808.1\|WP_149814581.1\|2732740_2733742_-\|IS3-family-transposase	gnl\|CDD\|366234	pfam00665, rve, Integrase core domain. Integrase mediates integration of a DNA copy of the viral genome into the host chromosome. Integrase is composed of three domains. The amino-terminal domain is a zinc binding domain pfam02022. This domain is the central catalytic domain. The carboxyl terminal domain that is a non-specific DNA binding domain pfam00552. The catalytic domain acts as an endonuclease when two nucleotides are removed from the 3' ends of the blunt-ended viral DNA made by reverse transcription. This domain also catalyzes the DNA strand transfer reaction of the 3' ends of the viral DNA to the 5' ends of the integration site.	3.36609e-28
NZ_CP043808.1\|WP_149814815.1\|2728255_2729401_-\|IS110-family-transposase	gnl\|CDD\|376564	pfam01548, DEDD_Tnp_IS110, Transposase. Transposase proteins are necessary for efficient DNA transposition. This family includes an amino-terminal region of the pilin gene inverting protein (PIVML) and of members of the IS111A/IS1328/IS1533 family of transposases. The C-terminus is represented by family pfam02371.	7.32124e-19
NZ_CP043808.1\|WP_084485264.1\|2722299_2722623_-\|NlpC/P60-family-protein	gnl\|CDD\|366353	pfam00877, NLPC_P60, NlpC/P60 family. The function of this domain is unknown. It is found in several lipoproteins.	6.7637e-27
NZ_CP043808.1\|WP_084485263.1\|2713130_2713481_+\|cation-transporter	gnl\|CDD\|225328	COG2608, CopZ, Copper chaperone [Inorganic ion transport and metabolism].	1.71499e-05
NZ_CP043808.1\|WP_022926303.1\|2713744_2714089_+\|NADH-quinone-oxidoreductase-subunit-A	gnl\|CDD\|376344	pfam00507, Oxidored_q4, NADH-ubiquinone/plastoquinone oxidoreductase, chain 3.	2.42301e-26
NZ_CP043808.1\|WP_084485271.1\|2731185_2731878_-\|IS3-family-transposase	gnl\|CDD\|222853	PHA02517, PHA02517, putative transposase OrfB; Reviewed.	1.37997e-66
NZ_CP043808.1\|WP_022926299.1\|2716872_2717175_+\|NADH-ubiquinone-oxidoreductase	gnl\|CDD\|180218	PRK05715, PRK05715, NADH-quinone oxidoreductase subunit NuoK.	4.38888e-12
NZ_CP043808.1\|WP_022926305.1\|2712065_2712983_-\|hypothetical-protein	gnl\|CDD\|374209	pfam15902, Sortilin-Vps10, Sortilin, neurotensin receptor 3,. Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1.	0.00307951
NZ_CP043808.1\|WP_022925108.1\|2707578_2707908_+\|DUF3618-domain-containing-protein	gnl\|CDD\|378834	pfam12277, DUF3618, Protein of unknown function (DUF3618). This domain family is found in bacteria, and is approximately 50 amino acids in length.	3.30906e-09
NZ_CP043808.1\|WP_022925111.1\|2706448_2706721_-\|DUF4235-domain-containing-protein	gnl\|CDD\|379422	pfam14019, DUF4235, Protein of unknown function (DUF4235). This family of integral membrane proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 88 and 119 amino acids in length.	1.10967e-17
NZ_CP043808.1\|WP_033419151.1\|2720622_2722017_+\|NADH-quinone-oxidoreductase-subunit-N	gnl\|CDD\|235603	PRK05777, PRK05777, NADH-quinone oxidoreductase subunit NuoN.	1.95687e-90
NZ_CP043808.1\|WP_028131268.1\|2716312_2716876_+\|NADH-quinone-oxidoreductase-subunit-J	gnl\|CDD\|223909	COG0839, NuoJ, NADH:ubiquinone oxidoreductase subunit 6 (chain J) [Energy production and conversion].	1.35754e-07
NZ_CP043808.1\|WP_168714909.1\|2707154_2707598_+\|phage-holin-family-protein	gnl\|CDD\|377816	pfam07332, Phage_holin_3_6, Putative Actinobacterial Holin-X, holin superfamily III. Phage_holin_3_6 is a family of small hydrophobic proteins with two or three transmembrane domains of the Hol-X family. Holin proteins are produced by double-stranded DNA bacteriophages that use an endolysin-holin strategy to achieve lysis of their hosts. The endolysins are peptidoglycan-degrading enzymes that are usually accumulated in the cytosol until access to the cell wall substrate is provided by the holin membrane lesion.	1.6445e-27
NZ_CP043808.1\|WP_143553825.1\|2707991_2708984_+\|YihY-family-inner-membrane-protein	gnl\|CDD\|224214	COG1295, Rbn, Ribonuclease BN family enzyme [Replication, recombination, and repair].	8.49228e-61

>NZ_CP043808.1|WP_022926299.1|2716872_2717175_+|NADH-ubiquinone-oxidoreductase
MTLEAALLLSAAIFSVGLYGAISQQVVVMVMMGLELMINGVILAAAACWWFLAPGPTGQVLLMVVIAAMTLEMAMGFAVAVLLHRARQTDMTDMATDLSR
>NZ_CP043808.1|WP_028131268.1|2716312_2716876_+|NADH-quinone-oxidoreductase-subunit-J
MLVDIAFVALGVLAVLSGAAVFVVDSMARATYALAVSFVAVGAQVLFLQQSYVGVVIILMMVMEMAVMAVYMVMFMGMNPALMPMSMVHSNRTAVATAVLTFLLLAAGILVVDWPARRGSPPPDVTEALGEALMGPQMLVMAVISPVMVATIVAGVVLAAPRTRYDRFGDDLRQRPPDDPQPGGVGR
>NZ_CP043808.1|WP_022926303.1|2713744_2714089_+|NADH-quinone-oxidoreductase-subunit-A
MYLGLIGVAISCLVALAGMFALHRATAVAADPLHTLPFESGWVPQQHALSRYHVRWYLASLVFLAFDVEMLFMYPWAVVVAQVGWSAVVEMFLFLGALLVAVVWAWREGAFRWV
>NZ_CP043808.1|WP_084485263.1|2713130_2713481_+|cation-transporter
MCTSRTQSTQVGERPTTAEATSCDCCATEAGSATGSAERSLALVQTTYLVTGLTCHHCATSVTEELEALDEVSAVRVDVVPGGESSVRVASTEALGTERVRTALSAAGDYAVSGRR
>NZ_CP043808.1|WP_022926305.1|2712065_2712983_-|hypothetical-protein
METAIRTLSRTTKKHLGTAKSATIALAASLVLSACSSDITPASEQSGASGGTAGQKAGVLDQPITHIHGVARDPITQSVVMATHEGAFERRDGGWYGRGDVVDLMGFAIAPDGTWFASGHPGFDTDLPQPVGLIASTDRGQTWQTLSRGGESDFQVLAVGPAGVLGFDGTLRASADGTRWDEASIPAPPVDLAVNRATGAVLATTEQGLLQSTDDLATWAPLDPPESVVLVDWVDEETIVATTAANRVLLSHDAGQSWEAGSPLSVEVQALGAHLLPSGKTEILVATQNGLLKSLDFGSTFVQVP
>NZ_CP043808.1|WP_143553825.1|2707991_2708984_+|YihY-family-inner-membrane-protein
MTGPAWKYTAVKAFREFLDDECTDLAAALTYYAVLAIFPALIAIFSLLGLVGQSQQVVSAVMPVLSSVLGESGSSTLEPVVQSLATSPGAGLALVIGLATALWSASGYVTAFSRAMNRVYEIEEGRPVWKLRPVMLLITLVMVLMVVLIALMLIVSGPVATALGEAIGLGSTVVTVWQVAKWPVVLVLVMLLVALLYYSTPNVKQPKFRWLSIGAAFAILVWVLISVAFGFYIANFSSYGATYGSFAGVIIFLLYLWITNLALLLGAEVDAELERSRQLIAGIEAEEDIQLPPRDDAKIVASEEKEQADQDKARALRRSGGDTTDPDQTR
>NZ_CP043808.1|WP_022925108.1|2707578_2707908_+|DUF3618-domain-containing-protein
MSATPHENPDSDNTQDEASSDPAQIEADIARHRQELGDTVDELTERLDVKKQARDKVQSIKTRADAGLGEVKTRLNSDDHRDVLSVLAPALGAVAAVVLIIGVARRVRR
>NZ_CP043808.1|WP_168714909.1|2707154_2707598_+|phage-holin-family-protein
MSRRGLVAERFTPDTDHASTGELIARMSEQTSTLIRDEMRLAQAELSAKAKDAGVGIGMFGAGGLLAFFGIAALITTAILALALVLPPWAAAGIVTLLLFAAAAVVSLVGKKRVQEATPAAPERAVDNVKQDIEQVKGQPSHERHTA
>NZ_CP043808.1|WP_022925110.1|2706889_2707180_+|hypothetical-protein
MSKIMMATAFGAGYVLGARAGRERYEQLSAKAQELWGHPKVQEQADKAKQQAGRVTEQAKGRLSNAQDGDRDSTDDPWEVDTDTALAGDEQEGPRG
>NZ_CP043808.1|WP_022925111.1|2706448_2706721_-|DUF4235-domain-containing-protein
MGDKMWSLATTAAAIGGGVMAKNVIETTWKFVTGSNSPSNPEDPEVDWGEAMAFALVSGAIVQLVRVSINHKSTQAFAKRKGRLPESVAS
>NZ_CP043808.1|WP_033419151.1|2720622_2722017_+|NADH-quinone-oxidoreductase-subunit-N
MRPALLLPEIVLFLGALAALLGGSFLPRTRQWVTRVVAAAALVLAAAMAAVALAGPTAVAMEGSFTVDPTTGVARLVATLGALVVLALAADEIDGSPRESETYALLLLSTTGTLVLAGADDLLVVAVGFLLTSVPLYGLIGITGTAVAAEAAMKTYLLGALFGILLLAGVTLLYGVSGTTSYAGLADPLAAAPRAVVAAGVVGILGGLLFKAGGVPAHFWVPDAAQGAGGAVAAFLTTVPKIGAVLAAYRLVAALPDTLAWPLLVAVLAVASMTVGNLAAYTQTDPRRLLGWSTVSQVGYLLVPVTVAGRSDLALPSLLLYLAGYTVTNLAAFAVTTAFPRRRELSAYRGVGRRYPWLAAALVVALLGLVGTPPTAVFVGKLTTTAAAWDAGDAWLAVLVLLNTLASLFYYLRWIAPLYARPTAEHPEDGDPPAPWSRWTAVATANLSVLVGVAAGVLWAVATA
>NZ_CP043808.1|WP_084485264.1|2722299_2722623_-|NlpC/P60-family-protein
MLGVAAGLTGIPYQWGGSTPAGFDCSGFTSYVFAQVGISLPRTAAQQQAFATPVSNPQPGDLVFYGYPAYHIGIYAGDGMMYDSPTPGNYSGYRPVFSGVSGYGRVG
>NZ_CP043808.1|WP_022926324.1|2724229_2724808_+|DUF305-domain-containing-protein
MLSMPAMALAALFTISACTTETAQDPSSSAASEEHNDADVQFATEMIPHHQQAVEMSDMALEQGGTEVRELAERIQAAQAPEIETMTEWLQAWGEDVPETDGHGSMEGMDHSQMEGMMSPEDMEDLGGAQGSQFDTMWLEMMIEHHDGAITMAQTQVADGLDPEAVALAEDIAESQEAEIEEMEALLQGSNG
>NZ_CP043808.1|WP_022926322.1|2727648_2727972_+|hypothetical-protein
MKALQSQGGLADALETLDRLAPFAEALGLDTESDMPSSGQLDAFRSLSKNITVPLVVVGDDYDGDSDWKVAGTLRTEFLADAEALDGPSIVVGKVRNESPRVSWRLG
>NZ_CP043808.1|WP_149814815.1|2728255_2729401_-|IS110-family-transposase
MPSMQLRRDDVIVGVDTHKDNHVAVAIDGLGGRLGDLVVPATLAGFEELVAFCVAFIGPEGRLVAFGVEGTGSYGVGLARYLRRQGHEVHEIARPARAVERRLAGKNDTLDAEHAARQLLAGHGLSTPKTADGEVETIRLVKIAYDGAVQARTTAMITLKATLATGSEALRTELEKLTDHQLVLACAALEGPTPLPPVRRGAPTVVLPTEPDAAMRHVLSSMARRWLSLHEEAKAHAASLKALTAAAAPRLVEAVGVGYDTAAQMLITAGDNTDRIKSEAAFAKMCGACPIPAGSGKTNNRHRLYRGGNRQANAALYRVIIVRMRWHQPTIDYVARRTAEGLSKREIIRCLKRYLARELFRLLPAPDTTAHNRDEELEMVA
>NZ_CP043808.1|WP_149814581.1|2729725_2730727_-|IS3-family-transposase
MINPAVDEVAEHVGTARACALLGRSRAGHYRAKNPPPPRARAPRPVPANKLTPAERAHVLSVLTSERFADKSVAQVWATLLDEGTYLCSQSTMHRILRENAMAGERRRQATHPARTRPELVATGPGQVWSWDITKLRGPERGVYYDLYVVLDIFSRFVVAWTIAAREDADIAKNLLEQAMGIHGVPDALHADRGTSMTSKPVAQLLVDLGVARSHSRPHVSNDNPYSEAAFKTLKYAPIFPEHFGSLADAGAFAEQFFAYYNHEHRHSGIGLHTPASVHYGTATQVRAQRQATLDAAYAAHPERFGHRRPQAPNLPTAAWINQPSQEALIQTA
>NZ_CP043808.1|WP_084485271.1|2731185_2731878_-|IS3-family-transposase
MPTAVLVDYIDQHRDRFGVEPICTVLRDAGMQVAPSTYYAAKTRPASARSVRDAELTEDIRTAHKANLGVYGARKIYAELTREGVTVARCTVERLMKAEGLRGIPREKTRRTTIGDGAETERPEDLVARKFVATAPNQLWVADLTYVRTHAGWTYVAFVLDVFSRMIVGWQVSTSLRTDLALDALDMGLWARQRAGQDVTGLVHHSDRGVQYRAIRYTERLAEALCVRMG
>NZ_CP043808.1|WP_028131277.1|2731880_2732201_-|transposase
MPAPRKYSVELQQRATRMAIDARKDPDSARGAIKRVADQLGVHPEALRNWVRQAEIDGGVRAGTTTDDAQRLAELEREVRELRRANEILMTSAAFFAAAELDRKIR
>NZ_CP043808.1|WP_022926332.1|2732385_2732757_+|hypothetical-protein
MVNEEIDMTDASTSTTEPTVGANRGVKRGLPPRALPEAAEDAATLWEVARLGTAPYMTFATKLGRRSASGGGWDQLMAVLRGFGLVRFEGDQQIGLTPLGQELVNGSAEGVKAGETVSVRRSV
>NZ_CP043808.1|WP_149814581.1|2732740_2733742_-|IS3-family-transposase
MINPAVDEVAEHVGTARACALLGRSRAGHYRAKNPPPPRARAPRPVPANKLTPAERAHVLSVLTSERFADKSVAQVWATLLDEGTYLCSQSTMHRILRENAMAGERRRQATHPARTRPELVATGPGQVWSWDITKLRGPERGVYYDLYVVLDIFSRFVVAWTIAAREDADIAKNLLEQAMGIHGVPDALHADRGTSMTSKPVAQLLVDLGVARSHSRPHVSNDNPYSEAAFKTLKYAPIFPEHFGSLADAGAFAEQFFAYYNHEHRHSGIGLHTPASVHYGTATQVRAQRQATLDAAYAAHPERFGHRRPQAPNLPTAAWINQPSQEALIQTA

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Crispr_ID: NZ_CP043808_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043808_8

2943102-2943189

Orphan

Consensus_repeat	Method
CAACCATTCGCGACGCTCGGTCGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043808_8

>merge|NZ_CP043808|8|2943102-2943189|CRISPRCasFinder
CAACCATTCGCGACGCTCGGTCGGGAGATGTGGCGGCGGAGCCGGGGCCGGCCGGGTCGGGGGCAACCATTCGCGACGCCCGGTCGGG

>NZ_CP043808|8|8|2943102-2943189|CRISPRCasFinder
CAACCATTCGCGACGCTCGGTCGGG	AGATGTGGCGGCGGAGCCGGGGCCGGCCGGGTCGGGGG
CAACCATTCGCGACGCCCGGTCGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043808.1\|WP_022926062.1\|2937340_2938123_-\|CPBP-family-intramembrane-metalloprotease	unknown	unknown	gnl\|CDD\|376806
NZ_CP043808.1\|WP_022926075.1\|2953408_2954212_-\|HAD-IIB-family-hydrolase	unknown	unknown	gnl\|CDD\|319784
NZ_CP043808.1\|WP_149814954.1\|2947401_2948169_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223779
NZ_CP043808.1\|WP_022926065.1\|2939597_2940383_+\|thioesterase-family-protein	unknown	unknown	gnl\|CDD\|379298
NZ_CP043808.1\|WP_052327899.1\|2949010_2950132_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340828
NZ_CP043808.1\|WP_022926077.1\|2955465_2955720_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_149814841.1\|2948114_2949014_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|224137
NZ_CP043808.1\|WP_149814840.1\|2936982_2937333_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_149814839.1\|2935535_2936102_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379642
NZ_CP043808.1\|WP_022926070.1\|2945909_2947040_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340832
NZ_CP043808.1\|WP_022926067.1\|2941533_2942724_-\|O-succinylhomoserine-sulfhydrylase	unknown	unknown	gnl\|CDD\|236103
NZ_CP043808.1\|WP_052327897.1\|2938501_2939572_-\|DUF2891-family-protein	unknown	unknown	gnl\|CDD\|378592
NZ_CP043808.1\|WP_022926063.1\|2938127_2938427_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_022926066.1\|2940647_2941229_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_022926079.1\|2956446_2958114_+\|polysaccharide-biosynthesis-protein	unknown	unknown	gnl\|CDD\|224011
NZ_CP043808.1\|WP_161600265.1\|2958194_2959109_+\|glycosyl-transferase	unknown	unknown	gnl\|CDD\|133464
NZ_CP043808.1\|WP_028131215.1\|2943941_2945570_-\|iron-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224099
NZ_CP043808.1\|WP_022926078.1\|2955883_2956165_+\|DUF4235-domain-containing-protein	unknown	unknown	gnl\|CDD\|379422
NZ_CP043808.1\|WP_022926059.1\|2935064_2935463_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_022926060.1\|2936144_2936774_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP043808.1\|WP_022926062.1\|2937340_2938123_-\|CPBP-family-intramembrane-metalloprotease	gnl\|CDD\|376806	pfam02517, Abi, CAAX protease self-immunity. Members of this family are probably proteases (after a isoprenyl group is attached to the Cys residue in the C-terminal CAAX motif of a protein to attach it to the membrane, the AAX tripeptide being removed by one of the CAAX prenyl proteases). The family contains the CAAX prenyl protease. The proteins contain a highly conserved Glu-Glu motif at the amino end of the alignment. The alignment also contains two histidine residues that may be involved in zinc binding. While they are involved in membrane anchoring of proteins in eukaryotes, little is known about their function in prokaryotes. In some known bacteriocin loci, Abi genes have been found downstream of bacteriocin structural genes where they are probably involved in self-immunity. Investigation of the bacteriocin-like loci in the Gram positive bacteria locus from Lactobacillus sakei 23K confirmed that the bacteriocin-like genes (sak23Kalphabeta) exhibited antimicrobial activity when expressed in a heterologous host and that the associated Abi gene (sak23Ki) conferred immunity against the cognate bacteriocin. Interestingly, the immunity genes from three similar systems conferred a high degree of cross-immunity against each other's bacteriocins, suggesting the recognition of a common receptor. Site-directed mutagenesis demonstrated that the conserved motifs constituting the putative proteolytic active site of the Abi proteins are essential for the immunity function of Sak23Ki - thus a new concept in self-immunity.	2.22776e-14
NZ_CP043808.1\|WP_022926065.1\|2939597_2940383_+\|thioesterase-family-protein	gnl\|CDD\|379298	pfam13622, 4HBT_3, Thioesterase-like superfamily. This family contains a wide variety of enzymes, principally thioesterases. These enzymes are part of the Hotdog fold superfamily.	1.24934e-25
NZ_CP043808.1\|WP_052327899.1\|2949010_2950132_+\|glycosyltransferase	gnl\|CDD\|340828	cd03798, GT4_WlbH-like, Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.	2.36284e-07
NZ_CP043808.1\|WP_161600265.1\|2958194_2959109_+\|glycosyl-transferase	gnl\|CDD\|133464	cd06854, GT_WbpL_WbcO_like, The members of this subfamily catalyze the formation of a phosphodiester bond between a membrane-associated undecaprenyl-phosphate (Und-P) molecule and N-acetylhexosamine 1-phosphate, which is usually donated by a soluble UDP-N-acetylhexosamine precursor. The WbcO/WbpL substrate specificity has not yet been determined, but the structure of their biosynthetic end products implies that UDP-N-acetyl-D-fucosamine (UDP-FucNAc) and/or UDPN-acetyl-D-quinosamine (UDP-QuiNAc) are used. The subgroup of bacterial UDP-HexNAc:polyprenol-P HexNAc-1-P transferases includes the WbcO protein from Yersinia enterocolitica and the WbpL protein from Pseudomonas aeruginosa. These transferases initiate LPS O-antigen biosynthesis. Similar to other GlcNAc/MurNAc-1-P transferase family members, WbpL is a highly hydrophobic protein possessing 11 predicted transmembrane segments.	3.20568e-59
NZ_CP043808.1\|WP_149814841.1\|2948114_2949014_+\|glycosyltransferase	gnl\|CDD\|224137	COG1216, COG1216, Predicted glycosyltransferases [General function prediction only].	3.19909e-06
NZ_CP043808.1\|WP_149814839.1\|2935535_2936102_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379642	pfam14542, Acetyltransf_CG, GCN5-related N-acetyl-transferase. This family of GCN5-related N-acetyl-transferases bind both CoA and acetyl-CoA. They are characterized by highly conserved glycine, a cysteine residue in the acetyl-CoA binding site near the acetyl group, their small size compared with other GNATs and a lack of of an obvious substrate-binding site. It is proposed that they transfer an acetyl group from acetyl-CoA to one or more unidentified aliphatic amines via an acetyl (cysteine) enzyme intermediate. The substrate might be another macromolecule.	6.50332e-26
NZ_CP043808.1\|WP_022926070.1\|2945909_2947040_+\|glycosyltransferase	gnl\|CDD\|340832	cd03802, GT4_AviGT4-like, UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.	1.31833e-77
NZ_CP043808.1\|WP_022926067.1\|2941533_2942724_-\|O-succinylhomoserine-sulfhydrylase	gnl\|CDD\|236103	PRK07810, PRK07810, O-succinylhomoserine sulfhydrylase; Provisional.	0
NZ_CP043808.1\|WP_052327897.1\|2938501_2939572_-\|DUF2891-family-protein	gnl\|CDD\|378592	pfam11199, DUF2891, Protein of unknown function (DUF2891). This is a bacterial family of uncharacterized proteins.	7.83109e-117
NZ_CP043808.1\|WP_149814954.1\|2947401_2948169_+\|hypothetical-protein	gnl\|CDD\|223779	COG0707, MurG, UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell envelope biogenesis, outer membrane].	3.74102e-08
NZ_CP043808.1\|WP_022926079.1\|2956446_2958114_+\|polysaccharide-biosynthesis-protein	gnl\|CDD\|224011	COG1086, COG1086, Predicted nucleoside-diphosphate sugar epimerases [Cell envelope biogenesis, outer membrane / Carbohydrate transport and metabolism].	1.36594e-178
NZ_CP043808.1\|WP_028131215.1\|2943941_2945570_-\|iron-ABC-transporter-permease	gnl\|CDD\|224099	COG1178, ThiP, ABC-type Fe3+ transport system, permease component [Inorganic ion transport and metabolism].	1.34358e-75
NZ_CP043808.1\|WP_022926078.1\|2955883_2956165_+\|DUF4235-domain-containing-protein	gnl\|CDD\|379422	pfam14019, DUF4235, Protein of unknown function (DUF4235). This family of integral membrane proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 88 and 119 amino acids in length.	2.37333e-17
NZ_CP043808.1\|WP_022926075.1\|2953408_2954212_-\|HAD-IIB-family-hydrolase	gnl\|CDD\|319784	cd02585, HAD_PMM, phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM. PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid biosynthesis. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	4.14943e-34

>NZ_CP043808.1|WP_022926067.1|2941533_2942724_-|O-succinylhomoserine-sulfhydrylase
METPDGWRPDTLAVRGGLMRSPFDETAEALYPTSGYVYSSAEEAQAAFEEKIERFVYSRYGNPTVAMLEERMRVMHGAEAAQATASGMSAVFTALGGLCAAGDRIVASRALFGSCFVIIDEVLRRWGVESTFVDGTDLDAWREALATPAEAVFFETPSNPTQELVDIAAVSELAHAAGATVVVDNVFGTPVFSRPLDHGADIVVYSTTKHIDGQGRVMGGMILGPEELVAGPIQTLLRHTGPAMSPFNAWVTLKGLETMALRVERQAATALTLAQELEADPRVLAVHHPWLESHPQAELARRQMTGGGTVVTFTLDAGQEETFAFMNALQVVDISNNLGDTKSLTTHPATTTHRRLPEEARRAAGITEGTIRLSVGLEDIDDLRADLARGFAAAFG
>NZ_CP043808.1|WP_022926066.1|2940647_2941229_+|hypothetical-protein
MTRTRPITLALAALSLSAALAGCGDTDATAGAEPTASSAGASDEAAGESGDETGDETSEDGSTVTKDEPIGDKPIQTGPAGEASLPLGAVPDAIVQRDDVQAAIDAEAKRAGVGREAVTVAGYADVTWSDGSIGCPREGMMYTQALVPGHQLVLEVDGEHASYHAAQGKDFSFCAQPVGPATSESSGGPVTDR
>NZ_CP043808.1|WP_022926065.1|2939597_2940383_+|thioesterase-family-protein
MTADGRHYFTALGEGRYQPTEHVQGAWSPDEQHVAPVIGLLLHTLELNHPREDLQWARLSVDILGFIRREEMTVTTRVLRPGRTIELLESSVEIAGRAAVRMTAWRLVTGDTTAVAETEHADLPGPEGLEAWTGMDHWDGGFIRSLDFRSVPGSRAGRGRTWVRTSVPLVGGAEEASALASWVGLLDTANGTAGRAAPHDWAFPNVDLTLHLHRLPEGAWVGLDTRVSWGPTGVGQTSSVVHDEAGPVGTLVQALTLRPAR
>NZ_CP043808.1|WP_052327897.1|2938501_2939572_-|DUF2891-family-protein
MPSRATTPGDPTGARSAAARHAADWSRIAREVIGTAYPWAPAHVVTGPDDTDVTPHRLHPAFHGALDWHSCVHMQWSLVTLLTRYAGALGAREAAAARSLLEERLTPEHLQVEVAYLRARPGFERPYGWAWAAQLAAATRELGGRDEQAARWAQALVPLSDLLAERVLGHLPRQAYPVRHGKHQNDAFALLLLRDAYGRLGRDDVVRACEEAARAWFADDGPAPTDAEPGGSDFLSPALTEALLMTAVLEPGDARRWLERVLPGLGEGRHAPLLAVPEVRDPTDGQGAHLLGLALSRAWALRALAPWGHERAAARLRAAADDQEAAVLGHITDGDFMATHWLVSFALLADGALDRS
>NZ_CP043808.1|WP_022926063.1|2938127_2938427_-|hypothetical-protein
MEQELRRSGGAEPTVTGLAAVHAFCPLVARSPAGQGGRRTGRCPAAEQEAARQVEQSQPAPVQPGPVQCWDDDGWGECDDDWDDDFDGTTTDARWPHLV
>NZ_CP043808.1|WP_022926062.1|2937340_2938123_-|CPBP-family-intramembrane-metalloprotease
MSTQGPPTPPTALARRSLLVETLLVLGVSLGASAIWSVLSLIRKLTAEGGLAAQTTSMNTSATPDRPWLDLAYQLVGIGLALVPVLLAVHLLGRDVARPWRLLGLDRSRPVRDLAQGTMLAAVIGIPGLGLYLVARGLGVNTTVAPSNLADVWWAVPVLVLAAVQNAVVEEVVVVGYLFTRWAQAGWSTWAIILTSALLRGSYHLYQGFGGFVGNVAMGVILGWFYTRTRRVMPLVVAHTLLDVVAFVGYAALAGRVDWL
>NZ_CP043808.1|WP_149814840.1|2936982_2937333_+|hypothetical-protein
MAADRRPAAWHAALLLCLLPTVSACLGDPPPDPASAPLEVVLDGCGLNRDKVAPGEHEVSVVGEGRLVVTDAAGQEVLRLPGGTSTLATTAQTYTMTCVVEGEETTATLTSVAEGG
>NZ_CP043808.1|WP_022926060.1|2936144_2936774_-|hypothetical-protein
MKTSTATATALGVTGLTAAVIGFGVAVPSLAEDSDNGTSTSTAAAADTVEPDGSAAPADGGVPGGHGTRGTARPHGVSLATAAETLGLTEDDLLARLAEGTTLGAIADAQGVDRQEVVDALMVQAQERLTALLDEPMAGMVGPGGGMVPPGGPQGEVGGTVPGREGADLPWDPEDQGEPDGTGSPDETEQDTEGSTDEDADATTGGGTA
>NZ_CP043808.1|WP_149814839.1|2935535_2936102_-|GNAT-family-N-acetyltransferase
MTQIDHLPERERWVARSEDREIGYLSYELEGGVLDLQHTVVEPEARGQGLGGRLVEEALGYARDEGLRVRPTCPFVPRYVAEHPEHADLIVGAGDVAQPRHDDEVVGEDEPDDGAGDVPTVEIRDQSIRLGQLLKLAGLVPDGAMARMVIENGEVAVDGETVMRRGTQVRPGQVVTYAGESVSPVSGG
>NZ_CP043808.1|WP_022926059.1|2935064_2935463_-|hypothetical-protein
MTLSPHGSSAVATGSLRKGLPIMLLGGVLAWVAGQSWSVQRGSGEVFQVLMAYGNLAVMAVAAQLVAGPRGRAWMMATAGAVGMTVPWFFGLAFAQQGQGVLLPSLVVLVTSWGMTWVVSTLTRVTVRRRGR
>NZ_CP043808.1|WP_028131215.1|2943941_2945570_-|iron-ABC-transporter-permease
MALGLAALIPLAFLTVFFALPVGGMLARGLWPEGRLDLSAVPEVLGRARTLRVLTFTLVSSLAGTVVTLLLGIPVAFVLYRLRFPGRTLLRAVVVMPFVLPTVVVGVMFRSLLSDGGPLGGLGLDGTWVPILLAFVFFNLAVVVRTVGGLWEGMDRRAEESAATLGATPWQVWRTVTLPALAPGVISAGTLVFLFCSTAFGVVLTLGGLRYGTIETEIYLLTVQFLDLQGAAVLSVLQLVAVVAMLAVAARARSTREQALRRVDVQASARRPRRDDTPALAVTALVVGFVLLPVGTLVARSLRVGQGWGLAHYRALTDPEATNALRVSVTEAMANSLRTAVDATVLAMVLGLVVAVIVSRRPRRPGWARTVSVLDGVFMLPLGISAVTVGFGFLITLDRPPLDLRTSPILVPIAQAMVALPLVVRTLAPVLRSVDPRQREAAATLGAGPWRAAWTAEAPVLARPLLAATGFAFAVSLGEFGATSFLARPDRPTVPVVIYQLISRPGADHLGMALAASVLLALVTVVVMGVVERLRVGSVGAF
>NZ_CP043808.1|WP_022926070.1|2945909_2947040_+|glycosyltransferase
MHVVVVAHTRHPISQPFAGGLESVTWHLARGLVARGHRVSVFADRHSDPIPGVDYLWPDRLELSEAARRDVSMPEEGWMERHHAYLQLMLHLARRTDVDLVHTHALHHLPAAMAPSLGVPTVLTLHTPPTPWLESAIAIAGTAPRRDRLHVTAVSRWTAAAWRHVTPARVVRNGVDVREWTPGPGGPGLVWSGRIVPEKAPHLAARIARRAGLPLTIAGPVSDEDYAREMLWPWCGRDGGVSYAGHLPTAELARLVGRSAALLVTPAWDEPFGLVAAEALACGTPVLGFARGGLPEVVGPGVGRLVPPGDDATLVEQAAALVPDVVRLPRARARAHAVAHHSMDRMVEDYLGVYDDVLAAAPPRPLGAAVGPAAAR
>NZ_CP043808.1|WP_149814954.1|2947401_2948169_+|hypothetical-protein
MPGDREDQPHRLARSLAEAVLAPWPPGAHGDGAASGPAPRTWEVGGISALAVAGGASGEGSARPGTGQGEPGALPAGSGQGATGAVEPGRGPLGAVEPRRGGVLVVWGSGGAGPGEHDVEAARASTGRRWLVRGGDHPPSPDLLAEMRAAEVVVCHAGQGAVADVALAGRPAVVLAQPRPHGEQEATARALERRGLAATASGWPAAEAWPGLLDRALATGGEGWSAWGSQQGAARAAQCLDEAATRLQEQRCWPS
>NZ_CP043808.1|WP_149814841.1|2948114_2949014_+|glycosyltransferase
MPRRGRHPAAGAAVLAVLTLAHGRHDHLRAQVAGLAAGVRRPDLHVVVAMDDPAVAQVAHRAWRAAGNPPPVLVEPLAADPLGLPLAAARNAAARVATAAGADRLVFLDVDCIPGPTTLTTYARHLHPSPSRPSPAVLGADVAYLPPRQPGCGGWEHQLYRLAEVGVHRPDRVRPAPGETRAEPDLTRFWSLSFALTAADFARTGGFCPLFVGYGGEDTDFAQVVGSLGGSLTWVGGATAYHQHHPTRTPPVDHVEAVVRNAGVFADRWGWWPMLGWLEQLRERGLAAPDGDGRWQVTR
>NZ_CP043808.1|WP_052327899.1|2949010_2950132_+|glycosyltransferase
MTIRVRQIPAGHAYVAALLPVRPDPRTEPAVVHLPDPPVPGAPPGQWWPHPALDPAWLREHASEQDLVHVHFGLEGQDTARLRTWLDMLREQRLPLVHTVHDLDHPQLRDQRRHREHLELLVEHAAGLLTLTEGAAEAVQRTLGRRPLVVPHPHVAPLPLVGRPRPARSGPLTVGLHLKSLRANLAPLRSLPALAAAVREVDSVLPSGARLEVRAHPEVLDPDRPGHDPRVVGLLTELGGPAWGVVDVRVAPRLPDDQLWDYLRGLDVSVLPYAWATHSGWVEACRDLGTWVLAPEVGHLREQGGVLSWGPASRPPDPGRLAQLLLRAAGSPPPRVDREERVRQREAGAALHTAVYAAVLSGRRVDAETEGVL
>NZ_CP043808.1|WP_022926075.1|2953408_2954212_-|HAD-IIB-family-hydrolase
MSGSGSPAVRAVAFDLDDTLAPSKSPVPEVTATALSELTAVVPVCVISGGSFEQFRDQLLARLPTPATGWGGLHLMPTCGTRYYRRAAGAADWALVESRELDPARRRRAVHVVEETARELGLWEPEDRVTGARIEDRGSQVTFSALGQLAAIADKQAWDPDGARRALLARHLAQRLPDLEVRVGGSTSVDLTERGVDKAYGVGRFAREVGADPREVLFVGDRLDPLGNDYPVLRLGVQARPVADHHETVQVLRELLQRLPGTAPGRA
>NZ_CP043808.1|WP_022926077.1|2955465_2955720_-|hypothetical-protein
MPFELPGWAVLLLWILLAVAALAVFLGSARGTLRGMDVVLGPPQRDEEHGDVGEQGDSGEGRDGDDRDDGDSVGDDHDRGAPER
>NZ_CP043808.1|WP_022926078.1|2955883_2956165_+|DUF4235-domain-containing-protein
MGNLVAKAMTVGAVLAASSIARKATDGTWKFVTGNDSPTNPEDPDIDFKEAVAFAVLSGALVGLARMLANRESTKVIAKASGKSPKQIADETN
>NZ_CP043808.1|WP_022926079.1|2956446_2958114_+|polysaccharide-biosynthesis-protein
MGLVASIHAIVGLLTGPYLVRHMRGSFDEITALTRTALITALALMAIAWLTPAVFIPRSSALLAPALAIVLMLAARVFVRTYRSRLMSRNPNGEKVIVFGAGLAGRRLVHNMLHDDRSEFTPVALLDDDRSKRRLKIEGVRVVGTFAKLATTVEKTSATYLAVAVPRATPELLRDVQRQARELNLKVQVLPPIEDWLRQTDPQATDLRDINLEDLLGRRAVELDQETIADHLTGKVVLVTGAGGSIGSELCRQIAKFAPARLIMLDRDESALHAVQLSLTGRGLLEGEDLMLADIRDADNLRTQFSVTRPDVVFHAAALKHLSLLERYPKEAWQTNVLGTLNVLTAAAEHGVGTFVNISTDKAASPTSVLGTSKRMAERLTAEFALREPGRYVSVRFGNVLGSRGSVIPAFTEQIRQGGPVTVTHKDVERYFMLIPEAAQLVLQAGAIGCDGDVLVLDMGTPVKIVDVARDLIRTSGKDIEIRYTGLRPGEKLSEVIFTEGERFRTTEHPLITAVNVPRMEPEQVRSRHFGTAERAAAWLAEHINEDATPLNTSR
>NZ_CP043808.1|WP_161600265.1|2958194_2959109_+|glycosyl-transferase
MDVPNTRSSHDTPVARGGGIAVVAAVVGAALCAFLTSWPAPWWPALAAAIVLAGVGLWDDVAGLGSLPRLALQISVGAALGIALSATEGTQLLLWATLSVILVPLSVNVINFMDGVNGITAVTMLVWGASMWWAADRYNEPTVAALGVITAGASMGFLPYNAPRATLFLGDVGSYGLGTLVGATTLLALSRGLTPALVLAPLVPYFSDVLITLLRRRIRGTALLSAHREHAYQLLVRPGGWPHFAVALLWGALSVVCTLAAMSEKTYLSICIFTLIAMTTWLISVRLSRRLLNTQTQMPTVIDG

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Crispr_ID: NZ_CP043808_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043808_9

3304589-3304676

Orphan

Consensus_repeat	Method
AGTCTCGCCGGGGCAGGCATTCCAC	CRISPRCasFinder

1 spacers

WYL

The CRISPR arrays of NZ_CP043808_9

>merge|NZ_CP043808|9|3304589-3304676|CRISPRCasFinder
AGTCTCGCCGGGGCAGGCATTCCACCGTCGGCGGGCGGCCGCAGCGAGTGTGGTGACCGTAAGAGTCTCGCCGGGGCAGGCATTCCAC

>NZ_CP043808|9|9|3304589-3304676|CRISPRCasFinder
AGTCTCGCCGGGGCAGGCATTCCAC	CGTCGGCGGGCGGCCGCAGCGAGTGTGGTGACCGTAAG
AGTCTCGCCGGGGCAGGCATTCCAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043808.1\|WP_022923560.1\|3308494_3309544_+\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187575
NZ_CP043808.1\|WP_022923572.1\|3297350_3297848_-\|DUF2087-domain-containing-protein	unknown	unknown	gnl\|CDD\|378279
NZ_CP043808.1\|WP_149814897.1\|3300931_3302218_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|376311
NZ_CP043808.1\|WP_149814900.1\|3312612_3314655_+\|FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|239240
NZ_CP043808.1\|WP_022923565.1\|3303936_3304539_+\|rhomboid-family-intramembrane-serine-protease	unknown	unknown	gnl\|CDD\|366759
NZ_CP043808.1\|WP_022923571.1\|3298065_3299040_-\|YafY-family-transcriptional-regulator	WYL	COG2378_WYL_CAS-I:CAS-III	gnl\|CDD\|225253
NZ_CP043808.1\|WP_084485030.1\|3296715_3296943_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|319906
NZ_CP043808.1\|WP_022923561.1\|3308041_3308449_+\|glyoxalase/bleomycin-resistance/dioxygenase-family-protein	unknown	unknown	gnl\|CDD\|319924
NZ_CP043808.1\|WP_022923559.1\|3309533_3310568_-\|beta-propeller-fold-lactonase-family-protein	unknown	unknown	gnl\|CDD\|378416
NZ_CP043808.1\|WP_022923557.1\|3311954_3312515_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043808.1\|WP_022923573.1\|3297001_3297190_-\|PspC-domain-containing-protein	unknown	unknown	gnl\|CDD\|377200
NZ_CP043808.1\|WP_022923567.1\|3302269_3303412_+\|citrate-(Si)-synthase	unknown	unknown	gnl\|CDD\|99862
NZ_CP043808.1\|WP_022923558.1\|3310602_3311847_-\|alpha-amylase	unknown	unknown	gnl\|CDD\|200491
NZ_CP043808.1\|WP_022923564.1\|3304785_3305802_+\|LLM-class-flavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|225052
NZ_CP043808.1\|WP_022923570.1\|3299141_3299720_+\|TIGR03086-family-protein	unknown	unknown	gnl\|CDD\|274424
NZ_CP043808.1\|WP_161600286.1\|3303428_3303890_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|185696
NZ_CP043808.1\|WP_149814896.1\|3299742_3300897_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_CP043808.1\|WP_149814899.1\|3305924_3307334_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340863
NZ_CP043808.1\|WP_022923562.1\|3307458_3307941_-\|winged-helix-DNA-binding-protein	unknown	unknown	gnl\|CDD\|197670
NZ_CP043808.1\|WP_161600287.1\|3314685_3314868_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP043808.1\|WP_022923560.1\|3308494_3309544_+\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|187575	cd05265, SDR_a1, atypical (a) SDRs, subgroup 1. Atypical SDRs in this subgroup are poorly defined and have been identified putatively as isoflavones reductase, sugar dehydratase, mRNA binding protein etc. Atypical SDRs are distinct from classical SDRs. Members of this subgroup retain the canonical active site triad (though not the upstream Asn found in most SDRs) but have an unusual putative glycine-rich NAD(P)-binding motif, GGXXXXG, in the usual location. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	5.79726e-54
NZ_CP043808.1\|WP_022923572.1\|3297350_3297848_-\|DUF2087-domain-containing-protein	gnl\|CDD\|378279	pfam09860, DUF2087, Uncharacterized protein conserved in bacteria (DUF2087). This domain, found in various hypothetical prokaryotic proteins and transcriptional activators, has no known function. Structural modelling suggests this domain may bind nucleic acids.	3.0191e-20
NZ_CP043808.1\|WP_149814897.1\|3300931_3302218_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|376311	pfam00285, Citrate_synt, Citrate synthase, C-terminal domain. This is the long, C-terminal part of the enzyme.	1.51531e-49
NZ_CP043808.1\|WP_149814900.1\|3312612_3314655_+\|FAD-dependent-oxidoreductase	gnl\|CDD\|239240	cd02930, DCR_FMN, 2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.	0
NZ_CP043808.1\|WP_022923565.1\|3303936_3304539_+\|rhomboid-family-intramembrane-serine-protease	gnl\|CDD\|366759	pfam01694, Rhomboid, Rhomboid family. This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.	8.28926e-21
NZ_CP043808.1\|WP_022923571.1\|3298065_3299040_-\|YafY-family-transcriptional-regulator	gnl\|CDD\|225253	COG2378, COG2378, Predicted transcriptional regulator [Transcription].	1.28135e-45
NZ_CP043808.1\|WP_084485030.1\|3296715_3296943_-\|hypothetical-protein	gnl\|CDD\|319906	cd07242, VOC_BsYqjT, vicinal oxygen chelate (VOC) family protein similar to Bacillus subtilis YqjT. 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.	1.13364e-05
NZ_CP043808.1\|WP_022923561.1\|3308041_3308449_+\|glyoxalase/bleomycin-resistance/dioxygenase-family-protein	gnl\|CDD\|319924	cd07263, 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.	3.1982e-10
NZ_CP043808.1\|WP_022923559.1\|3309533_3310568_-\|beta-propeller-fold-lactonase-family-protein	gnl\|CDD\|378416	pfam10282, Lactonase, Lactonase, 7-bladed beta-propeller. This entry contains bacterial 6-phosphogluconolactonases (6PGL)YbhE-type (EC:3.1.1.31) which hydrolyze 6-phosphogluconolactone to 6-phosphogluconate. The entry also contains the fungal muconate lactonising enzyme carboxy-cis,cis-muconate cyclase (EC:5.5.1.5) and muconate cycloisomerase (EC:5.5.1.1), which convert cis,cis-muconates to muconolactones and vice versa as part of the microbial beta-ketoadipate pathway. Structures of proteins in this family have revealed a 7-bladed beta-propeller fold.	4.49147e-46
NZ_CP043808.1\|WP_022923573.1\|3297001_3297190_-\|PspC-domain-containing-protein	gnl\|CDD\|377200	pfam04024, PspC, PspC domain. This family includes Phage shock protein C (PspC) that is thought to be a transcriptional regulator. The presumed domain is 60 amino acid residues in length.	1.16243e-21
NZ_CP043808.1\|WP_022923567.1\|3302269_3303412_+\|citrate-(Si)-synthase	gnl\|CDD\|99862	cd06109, BsCS-I_like, Bacillus subtilis (Bs) citrate synthase CS-I_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). 2MCS catalyzes the condensation of propionyl-coenzyme A (PrCoA) and OAA to form 2-methylcitrate and coenzyme A (CoA) during propionate metabolism. The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. This group contains proteins similar to BsCS-I, one of two CS isozymes in the gram-positive B. subtilis. The majority of CS activity in B. subtilis is provided by the other isozyme, BsCS-II (not included in this group). BsCS-I has a lower catalytic activity than BsCS-II, and has a Glu in place of a key catalytic Asp residue. This change is conserved in other members of this group. For E. coli CS (not included in this group), site directed mutagenesis of the key Asp residue to a Glu converts the enzyme into citryl-CoA lyase which cleaves citryl-CoA to AcCoA and OAA. A null mutation in the gene encoding BsCS-I (citA) had little effect on B. subtilis CS activity or on sporulation. However, disruption of the citA gene in a strain null for the gene encoding BsCS-II resulted in a sporulation deficiency, a characteristic of strains defective in the Krebs cycle. This group contains proteins which functions exclusively as either a CS or a 2MCS, as well as those with relaxed specificity which have dual functions as both a CS and a 2MCS. Many of the gram-negative species represented in this group have a second CS isozyme which is in another group.	1.20127e-135
NZ_CP043808.1\|WP_022923558.1\|3310602_3311847_-\|alpha-amylase	gnl\|CDD\|200491	cd11354, AmyAc_bac_CMD_like, Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	0
NZ_CP043808.1\|WP_022923564.1\|3304785_3305802_+\|LLM-class-flavin-dependent-oxidoreductase	gnl\|CDD\|225052	COG2141, COG2141, Coenzyme F420-dependent N5,N10-methylene tetrahydromethanopterin reductase and related flavin-dependent oxidoreductases [Energy production and conversion].	7.97007e-37
NZ_CP043808.1\|WP_022923570.1\|3299141_3299720_+\|TIGR03086-family-protein	gnl\|CDD\|274424	TIGR03086, TIGR03086, TIGR03086 family protein. This family, like pfam07398 and TIGRFAMs family TIGR030834, belongs to the larger set of probable enzymes defined in family TIGR03083. Members are found primarily in the Actinobacteria (Mycobacterium, Streptomyces, etc.). The family is uncharacterized.	1.30434e-31
NZ_CP043808.1\|WP_161600286.1\|3303428_3303890_+\|hypothetical-protein	gnl\|CDD\|185696	cd09019, galactose_mutarotase_like, galactose mutarotase_like. Galactose mutarotase catalyzes the conversion of beta-D-galactose to alpha-D-galactose. Beta-D-galactose is produced by the degradation of lactose, a disaccharide composed of beta-D-glucose and beta-D-galactose. This epimerization reaction is the first step in the four-step Leloir pathway, which converts galactose into metabolically important glucose. This epimerization step is followed by the phosophorylation of alpha-D-galactose by galactokinase, an enzyme which can only act on the alpha anomer. A glutamate and a histidine residue of the galactose mutarotase have been shown to be critical for catalysis, the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. Galactose mutarotase is a member of the aldose-1-epimerase superfamily.	9.07251e-49
NZ_CP043808.1\|WP_149814896.1\|3299742_3300897_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	1.1848e-14
NZ_CP043808.1\|WP_149814899.1\|3305924_3307334_-\|MFS-transporter	gnl\|CDD\|340863	cd06173, MFS_MefA_like, Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters. This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	9.83772e-53
NZ_CP043808.1\|WP_022923562.1\|3307458_3307941_-\|winged-helix-DNA-binding-protein	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	8.32172e-09

>NZ_CP043808.1|WP_022923565.1|3303936_3304539_+|rhomboid-family-intramembrane-serine-protease
MSQPATRRPDLPAWARRVMPVLVLVALMWVSEIVDLVLPLRLDQFGIRPRDPGHLAGIVLSPFLHLGFGHLLANTVTLLVLGSLLALTTRHLWLVTGGVVLLGGLGVWLLGGPGTVHIGASGVVYGYAAFLAVYGFVARRVWQAVLGLLVVVVYGSMLWGVLPVREGVSWQAHLFGAAAGVALAVWLGRRDRSRVPLAPR
>NZ_CP043808.1|WP_161600286.1|3303428_3303890_+|hypothetical-protein
MTPDPTQHTLTTAGLRLSTLSTGDSVTSCEVEDADGGWSEVVLGHRDLRSYARGGYLGATIGRVGNRIASGSFELDGTAYDLTVNDRGNTLHGGAAGFDLQEWLVEEGPAHVTWGLVSPDGDQGFPGEVEVEVRYALAPETFTSCTLWRLSTS
>NZ_CP043808.1|WP_022923567.1|3302269_3303412_+|citrate-(Si)-synthase
MTSTVQHAPPGLKGLVVARTRTGGVEGQEGFYHFREYSALDLSRHRSFEDVVHLMIEGHLPDAAESRAFADELAAASMLPHELLEQLLAIARSGPDRASLARLRTAVSLLGSVEDFPATYGATHEKVRAGVLRLVGVVPVLQAALFRLRAGMPPLEPRPELGAAGSWLWMLTGQEPAPEHAEAVTAYLISTVDHGFSASTFTARVVTSAGADVASAVCAALGTFSGPLHGGAPDRALDALDEIGTPDRARDWVRERVSKGERIMGFGHAVYRTTDPRAVLMREHAQRLGGPLAELAVAVEREVVGALAELKPGHELHTNVEYYAGVVMEQCGIPRAMFTPTFAVARVVGWGAHILEQTEDPRIIRPSAEYAGPPAPAPLP
>NZ_CP043808.1|WP_149814897.1|3300931_3302218_-|helix-turn-helix-domain-containing-protein
MSGPVALLSTAQAADYLGVKVQTVYAYVSRGVLTPVRREPGVGSLFDVEEVSALAGRPGRSGHRGSRGGGRATSDDVRTRITQVGPGSLAYRGHDVRDLAGSRTFEEVRDLLTGVPLADASRASDGRGVRSGEGPDGRGIRSGVLAALPAGTPSLDRMKHAVLLAAQDDLGRHDRSAEGFAAAGARAAAAMAGSPASSGAGPARASSGPSAACGSDPSTGSPGAGALAEALRAYLDLPSDLVDVALVLLADHDLAVSTTAVRVAVSAGSDAYSALLAGLAAADSPLHGGASMRAVDWLRPALQDPRSALDAALTGGPPPGFGHVVYTEQDPRAQLLLERILPGAALEVRASLELLEGELLERRGWVLTVDIALALLTLEHGLPRDAGAVIFACARTAGWTAHAIEELAEPGMRFRLRGIYTGPRQAKP
>NZ_CP043808.1|WP_149814896.1|3299742_3300897_-|alpha/beta-fold-hydrolase
MTWDDLLRTIGGLLAPFGGSWAQGDVGADGGGPSDVGFCCAHDLLADALPHIPQITDVSGNEGGCGDLWLTGEGDHLLAAHFEGFSPGESLARLGLLAEARRYAACAPGPVDLAGRVRALTLILTPDDLRGVEDAPYRVVGDGDPLVVLPGGPVRDGHYLGDLGGLAASRRMVVPVLPRTRVEDLVPVVEAVRNDLGLSRIDVLAHSAGAVLALAYLAAHPDRVARLVLMSPAVRAMGIADDVDGAARIVRARRAEPGFEESRKVRWLEGATYPEELRLTFGRWDDQVAALAGTGSVDQGERLAAYYAAPRPDPGRLRAAATAFPGDVTVMTGRLDVGPTPRQADELATLFPRGRVVEIQGAAHYPWLDAPDEVCRAVLSGLTP
>NZ_CP043808.1|WP_022923570.1|3299141_3299720_+|TIGR03086-family-protein
MTQQPDLRPVLARTQEWVADLVDGVRADQMQTRTPCAQWNVAELVEHLFAVEHRVAVLPEKGTVDDEPVAIPLPNDVSAGFRDAVRRAQDAWADDAVMDAELSPPWGTMPGRAVLGGYVQEHLVHGWDLASATGQDGEALAEVSEQVLPMIKAFLPAETRSEDWIPFDAPVEPASDAGPTERLANWLGRTTR
>NZ_CP043808.1|WP_022923571.1|3298065_3299040_-|YafY-family-transcriptional-regulator
MRTERLLQLVGLLRAHGRLSATELARRLEVSRRTVMRDVEALSLAGVPVYAERGRGGGYTLLPGYRPDVEELTDAESRALFVAGGAGVADALGMGQDYAAALRKLATGLPQRRTGDIGHALERVVVDPGGWSGSRHQPARLRELMAAVEADRRIRAVYRAASSGWSGRRTLDPWGLVLAGQSWYLVAAHRGRPHTYRVDRFERLEVLDAQARRPAGLDLLATWHELRDTWQQRPSMPVTLRVRADQAYLARRQLAMVLRGPVERTDDGPGHVLLRAPVGSLRGLVGMMAGFGSWVQVVEPPEAVALMREVAREVLEAHPAEPTS
>NZ_CP043808.1|WP_022923572.1|3297350_3297848_-|DUF2087-domain-containing-protein
MTTDADLKARVRERMARTGENYTTARAALLSAPPPRALVVETDLAADRAVRSFFDGERLPIPTRRRPRAAVLMELLTRFERGREYAEREVNAILATAHDDVASLRRELVDYRWFTRTDGVYRVADEVPQRHPNEAQEVPTDEVARLARVPRAAAGHTPHPGVTTG
>NZ_CP043808.1|WP_022923573.1|3297001_3297190_-|PspC-domain-containing-protein
MASAPALARPRHDRVIAGVCAGLGRRFGMSPTLVRVLFVLSCLLPGPQVLAYLVLWVVMPSD
>NZ_CP043808.1|WP_084485030.1|3296715_3296943_-|hypothetical-protein
MPGTRVSNPVHHIELWTHDLAEVEDRPTLDALRAGAAENGWSELIADAYPHAGSPGHTALFVENVQGSALEIVVA
>NZ_CP043808.1|WP_022923564.1|3304785_3305802_+|LLM-class-flavin-dependent-oxidoreductase
MKRIGFLSFGHWTPHPQSATRSASDVLLQSIDLAVAAEELGADGAYYRVHHFARQLASPFPLLAAVGARTERIEIGTGVIDMRYENPLYMTEDAGAADLISGGRLQLGISRGSPEQVVEGYRHFGHEPREGETDADMARRHTARFLDALSGEGFAEPNPRPMFPNPPGMLRLEPHSEGLRERIWWGAGTRGTAEWAAEQGMNLMSSTLLTEDTGVPFHQLQAEQIQRYRDAWTAAGHTREPRVSVSRSVFPLRTDQDHAYFGLERRSTDQVGIIDGARATFGKTYAAEPEDLARQLAADEAVAAADTLLLTVPNQLGVDYCAHVIEGVLEVAAELGWR
>NZ_CP043808.1|WP_149814899.1|3305924_3307334_-|MFS-transporter
MGREVSPRGALIDLTPLRHSQAYRRIWAGGALSGLGHQVAVVAVLFQVWEMTRNPFSVALIGVAQAVPMIVFGLVGGPVADVLDRRRVALAATTGQALAATTLAAQLVVGLYPLPLLLGVLSLQTACSALGSPARRTFIVRLLPRALVPAGIALHMISFQAAMMVGPALGGLLLGVASPAACYLVNAVALALSAWTVWALPLLPPERGESSDRGTPPEQDTPPERGESSDHGSDAAPDRRPVPRTETGGRAYPGARGARLRRRVRTALVLLAEGVAQVRRDPVLRGSFLLDLAATLLAFPVALFPMVNQALFGGDPRTLGLFLTCIAIGGVSAGLMSGLVTRRRRLGVVQLLAVGVWGLALLGFGLAALTGLAWAALGSLVVAGAADTVSVTSRAAMVQLATPDSHLGRVSSVEHVIGVAGPDIGNARAGLVAGLTTPAWSALLGALTCLGAATWVALTHRGRGVRVDD
>NZ_CP043808.1|WP_022923562.1|3307458_3307941_-|winged-helix-DNA-binding-protein
MTSPDPTRESRFEQLFAVLGDMDAAVAAVYRERGEGEVRPRFALPLIRLARLGPMTITALAAEVDRSHSALSQTIAQMRRAGLVTSEAGQDGRTRIVTLTDRGRALVPFAEAEWRATEAAIAEVEAELPYALSQAAADLAAALGRRSFAERLADHLNGPE
>NZ_CP043808.1|WP_022923561.1|3308041_3308449_+|glyoxalase/bleomycin-resistance/dioxygenase-family-protein
MSTDLPPALLGLDDAFNGFSVDDLDAAEAFYRDTLGIPVERSEEPMAMLSLRLGARSVLVYPKGPVHTPASYTVLNFPSDDVRATVQELTDRGLEFLRYDGMPHDELGVMTGGGPLIAWFTDPAGNVHSVIQREG
>NZ_CP043808.1|WP_022923560.1|3308494_3309544_+|NAD-dependent-epimerase/dehydratase-family-protein
MRLLLLGGTAFLGRAVATEAAGRGHDVTCLARGSAPPPDDVTFVRGDRDEPDGLAQVRDEEWDAVIDVTRQPGQVRRAVAELRTPHWVFVSTANVYAPAPGVRPVETDALVEPLAGDVMGSMEEYGPAKVACEKAVQDGMAAAGRSGTLARAGLIGGPGDVSGRLGYWPWRFAHPSGPDVIVPDDPDFPVAVIDVRDLAAWLVDAAEQRLDGAFNITGEVVPLGEVLAAAARAAGARVRARPVDLPTLAELGVNAWMGPRSLPLWIDDPDLRQAMALDISRAVASGLRLRPLAETLADTLAWEETRDAPRAAGLTDAEEQEIRTRLDSPLTTPGGSEGNHSRRPVEVRR
>NZ_CP043808.1|WP_022923559.1|3309533_3310568_-|beta-propeller-fold-lactonase-family-protein
MTELVLVANAGDSTVSTFRVDPDGPALQRIAVSEVGQGCGTFAIDAERDLVYAAAKGDPPGIDVFALERSSGRLEHLSRTDVESSMTYLALAYGGTLLVGASYGGGSAQVFGVDGDGHVEEPTAAVSWPNAHCVAVAGDGRHVYVVALGGDVVAQYALSPAGVLSPLAPPTAAAPEGSGPRHLVLDADESHAYVMTEFSGEVLTYARDGSGDLVLTGQVPAYAQDRGLSRSELGADPIEGHLVWGADLHLAWEGRVLLASERCESTLASLPVADDGSVGEPVSIIDTVTQPRGFTVLAGGELAVVTGEQDTDVALVSVDADGGLTEVGRYDTGAGANWARSITV
>NZ_CP043808.1|WP_022923558.1|3310602_3311847_-|alpha-amylase
MAHTPAPGAQRLLDHAIWWHVYPLGAVGAPAVLEGGVDAPVEHRLPRLVAWLDHVVELGCSGVLLGPVFAASSHGYDTLDHDRVDPRLGDEGDLDQLIEEARERGLSVLLDGVFNHVGADHPMVHDPDRAHLLKQGEDGRPAAWEGHEGLVELDHGSPDVEHLVVDVMLRWLRRGIAGWRLDVAYAVPADFWARVTARVREEFPDALFVGEVIHGDYAQVVADSDLDTVTQYELWKAVWSSIHDTNCWELAHALGRHDALLDSFVPQTFVGNHDVTRIATQVGEEGAALALAVLMTVGGMPSIYYGDEQAYQGLKEERLGGDDAIRPELPATPADLDPAGEWMRSLHRRLVGLRRQHAWLARARTEVETQSNEAITYVSSGQDQWLRVELSLAPQAQVIVTGADGELFRWAAGD
>NZ_CP043808.1|WP_022923557.1|3311954_3312515_-|hypothetical-protein
MRTTPRALLASALLAGLALAPVTLAAPAATAAPYCGITWGSLPKVTGYDTEPAPLTDVRAGRHSCFDRVVLDVSGDAGEYSVRYVSTYRAPGSGQALSLRGGAKIEVVVGNPTYDGDGDPVYDPRRPAELVGTDGYRTLRQARLGGSYEGQTSIGLGVRARLPMRAFVLDGPGSGQRLVIDVAHRW
>NZ_CP043808.1|WP_149814900.1|3312612_3314655_+|FAD-dependent-oxidoreductase
MTPGASAYPHLLRPLDLGHLTLRNRVVMGSMHTKLEDRARDIDKLAAYLGARAEGWVGLMVTGGYAPSWRGWLLPFGSSMVRAAQARRHRTVTDAVHEHDGAILLQLLHAGRYAYHPFAQGASREKSPITPFRPSALSTREVGRTVDDFARSARLAQRAGYDGVEIMGSEGYLVNQMLTARTNDRTDEWGGSAAARMRFPLEIVRRTRELVGDDFVVQYRMSLLDLVPDGQSWAETVDLAHGLVEAGVTLLNTGIGWHESRIPTIVTSVPRAAFTWVTARLRQEVDVPVIASNRINRPEVAEEILAAGEADLVSMARPLLADADWVRKTEQGREAEIIPCIACNQACLDHTFDNKRATCILNPRSAHETELVLHPTRSARRVAVVGAGPAGLACAVELAGRGHTVEMFEAADEVGGQFRLAAQIPGKEEFRQAIAYYEHMLGVRGVRVHLGMRVVASDLEGFDEVVVSTGVAPRVPDIEGIDHPSVLTYPEAIREPDRAGRRVAVIGAGGIGFDVSRALLHEPDETVDAWRERWGVADPWEERAGLGDKEHPPVPREVHLVQRKTSRHGTGLGKTSGWVHRTELRDAGVGFVGGAEYVRIDDDGLHLTLPVEGGDKGERRPHVLAVDTVVLCAGQESVTDLVEPLAALGVPVHVVGGADVAAELDAKRAIAQATELAARL
>NZ_CP043808.1|WP_161600287.1|3314685_3314868_-|hypothetical-protein
MLELTDQGRELYAQSDRIQRRVVEDVGIPLEEAHDLQRRLRRITATLEAGEDHEDGTAQA

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP043808_2	2.1\|1088782\|41\|NZ_CP043808\|CRISPRCasFinder	1088782-1088822	41	NZ_CP043808.1	1088867-1088907	2	0.951

1. spacer 2.1|1088782|41|NZ_CP043808|CRISPRCasFinder matches to position: 1088867-1088907, mismatch: 2, identity: 0.951

gcacgacgtgccggtgggaccgtgcgctcgtgcgtcagcgc	CRISPR spacer
gcactgcgtgccggtgggaccgtgcgctcgtgcgtcagcgc	Protospacer
**** .***********************************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	NZ_CP030074	Streptomyces sp. ZFG47 plasmid unnamed1, complete sequence	733881-733909	5	0.828
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	NZ_LR594667	Variovorax sp. SRS16 plasmid 2	357937-357965	6	0.793
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	NZ_LR594690	Variovorax sp. WDL1 plasmid 2	341879-341907	6	0.793
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	NZ_LR594672	Variovorax sp. PBL-E5 plasmid 2	358071-358099	6	0.793
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	NZ_LR594660	Variovorax sp. PBL-H6 plasmid 2	442437-442465	6	0.793
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	NC_008271	Rhodococcus jostii RHA1 plasmid pRHL3, complete sequence	5643-5671	6	0.793
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	NZ_CP035511	Haematobacter massiliensis strain OT1 plasmid pOT1-1, complete sequence	17156-17184	6	0.793
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	MK977706	Corynebacterium phage Dina, complete genome	41098-41126	7	0.759
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	MH926061	Corynebacterium phage Troy, complete genome	41326-41354	7	0.759
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	NC_048069	Corynebacterium phage SamW, complete genome	41326-41354	7	0.759
NZ_CP043808_1	1.1\|236390\|29\|NZ_CP043808\|CRISPRCasFinder	236390-236418	29	NC_048790	Corynebacterium phage Lederberg, complete genome	41711-41739	7	0.759

1. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to NZ_CP030074 (Streptomyces sp. ZFG47 plasmid unnamed1, complete sequence) position: , mismatch: 5, identity: 0.828

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
cgtcgccggtcacgtcgcgcaggcgcagg	Protospacer
 *.** .************ *********

2. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to NZ_LR594667 (Variovorax sp. SRS16 plasmid 2) position: , mismatch: 6, identity: 0.793

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
ggccggtggtcttgtcgcggagggcgaag	Protospacer
*********** .**********   *.*

3. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to NZ_LR594690 (Variovorax sp. WDL1 plasmid 2) position: , mismatch: 6, identity: 0.793

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
ggccggtggtcttgtcgcggagggcgaag	Protospacer
*********** .**********   *.*

4. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to NZ_LR594672 (Variovorax sp. PBL-E5 plasmid 2) position: , mismatch: 6, identity: 0.793

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
ggccggtggtcttgtcgcggagggcgaag	Protospacer
*********** .**********   *.*

5. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to NZ_LR594660 (Variovorax sp. PBL-H6 plasmid 2) position: , mismatch: 6, identity: 0.793

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
ggccggtggtcttgtcgcggagggcgaag	Protospacer
*********** .**********   *.*

6. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to NC_008271 (Rhodococcus jostii RHA1 plasmid pRHL3, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
ggccggtggtcacgtcgtcgaggtgtgag	Protospacer
*****************. ****.*...*

7. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to NZ_CP035511 (Haematobacter massiliensis strain OT1 plasmid pOT1-1, complete sequence) position: , mismatch: 6, identity: 0.793

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
agccggtggtcaggtcgcggagttccaga	Protospacer
.*********** ********* . ***.

8. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to MK977706 (Corynebacterium phage Dina, complete genome) position: , mismatch: 7, identity: 0.759

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
ggccggtggtggcgtcgcggaggcagtcc	Protospacer
********** .************.

9. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to MH926061 (Corynebacterium phage Troy, complete genome) position: , mismatch: 7, identity: 0.759

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
ggccggtggtggcgtcgcggaggcagtcc	Protospacer
********** .************.

10. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to NC_048069 (Corynebacterium phage SamW, complete genome) position: , mismatch: 7, identity: 0.759

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
ggccggtggtggcgtcgcggaggcagtcc	Protospacer
********** .************.

11. spacer 1.1|236390|29|NZ_CP043808|CRISPRCasFinder matches to NC_048790 (Corynebacterium phage Lederberg, complete genome) position: , mismatch: 7, identity: 0.759

ggccggtggtcacgtcgcggaggcgcagg	CRISPR spacer
ggccggtggtggcgtcgcggaggcagtcc	Protospacer
********** .************.

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

2639773 : 2646076

Staphylococcus_phage(33.33%)

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_022925174.1\|2639773_2640235_-	6,7-dimethyl-8-ribityllumazine synthase	A0A2H4PQS3	Staphylococcus_phage	6.3e-16	39.5
WP_022925173.1\|2640231_2641473_-	3,4-dihydroxy-2-butanone-4-phosphate synthase	A0A2H4PQS2	Staphylococcus_phage	3.5e-69	38.9
WP_022925172.1\|2641469_2642069_-	riboflavin synthase	A0A2I2L4R9	Orpheovirus	1.3e-16	36.8
WP_052327849.1\|2642068_2643301_-	bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD	A0A1V0SE20	Indivirus	2.3e-28	31.7
WP_022925170.1\|2643770_2645450_+	DEAD/DEAH box helicase	B2CRJ8	Acidianus_filamentous_virus	3.9e-15	22.4
WP_022925169.1\|2645395_2646076_-	ATP-binding cassette domain-containing protein	G9BWD6	Planktothrix_phage	2.1e-20	35.2

DBSCAN-SWA_2

2707154 : 2733742

Shigella_phage(40.0%)

transposase,holin

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_168714909.1\|2707154_2707598_+\|holin	phage holin family protein	NA	NA	NA	NA
WP_022925108.1\|2707578_2707908_+	DUF3618 domain-containing protein	NA	NA	NA	NA
WP_143553825.1\|2707991_2708984_+	YihY family inner membrane protein	NA	NA	NA	NA
WP_022926305.1\|2712065_2712983_-	hypothetical protein	NA	NA	NA	NA
WP_084485263.1\|2713130_2713481_+	cation transporter	NA	NA	NA	NA
WP_022926303.1\|2713744_2714089_+	NADH-quinone oxidoreductase subunit A	NA	NA	NA	NA
WP_028131268.1\|2716312_2716876_+	NADH-quinone oxidoreductase subunit J	NA	NA	NA	NA
WP_022926299.1\|2716872_2717175_+	NADH-ubiquinone oxidoreductase	NA	NA	NA	NA
WP_022926298.1\|2717171_2719109_+	NADH dehydrogenase	NA	NA	NA	NA
WP_033419151.1\|2720622_2722017_+	NADH-quinone oxidoreductase subunit N	NA	NA	NA	NA
WP_084485264.1\|2722299_2722623_-	NlpC/P60 family protein	A0A2P1CIC9	Actinomyces_phage	6.4e-15	44.3
WP_022926324.1\|2724229_2724808_+	DUF305 domain-containing protein	NA	NA	NA	NA
WP_022926322.1\|2727648_2727972_+	hypothetical protein	NA	NA	NA	NA
WP_149814815.1\|2728255_2729401_-\|transposase	IS110 family transposase	NA	NA	NA	NA
WP_149814581.1\|2729725_2730727_-\|transposase	IS3 family transposase	U5P429	Shigella_phage	1.5e-09	31.3
WP_084485271.1\|2731185_2731878_-\|transposase	IS3 family transposase	A0A1B3AZE5	Gordonia_phage	9.3e-80	65.9
WP_028131277.1\|2731880_2732201_-\|transposase	transposase	A0A1B3AZF8	Gordonia_phage	2.9e-36	76.4
WP_022926332.1\|2732385_2732757_+	hypothetical protein	NA	NA	NA	NA
WP_149814581.1\|2732740_2733742_-\|transposase	IS3 family transposase	U5P429	Shigella_phage	1.5e-09	31.3

DBSCAN-SWA_3

2932610 : 3017681

Gordonia_phage(18.75%)

transposase,holin,integrase,protease

attL 2973442:2973457|attR 3017862:3017877

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_022926055.1\|2932610_2932988_-\|holin	phage holin family protein	NA	NA	NA	NA
WP_022926056.1\|2933111_2933387_+	type II toxin-antitoxin system VapB family antitoxin	NA	NA	NA	NA
WP_022926057.1\|2933383_2933773_+	type II toxin-antitoxin system VapC family toxin	NA	NA	NA	NA
WP_022926058.1\|2933963_2935055_+	histidinol-phosphate transaminase	A0A1X6WGT4	Pacmanvirus	1.5e-15	25.2
WP_022926059.1\|2935064_2935463_-	hypothetical protein	NA	NA	NA	NA
WP_149814839.1\|2935535_2936102_-	GNAT family N-acetyltransferase	NA	NA	NA	NA
WP_022926060.1\|2936144_2936774_-	hypothetical protein	NA	NA	NA	NA
WP_149814840.1\|2936982_2937333_+	hypothetical protein	NA	NA	NA	NA
WP_022926062.1\|2937340_2938123_-\|protease	CPBP family intramembrane metalloprotease	NA	NA	NA	NA
WP_022926063.1\|2938127_2938427_-	hypothetical protein	NA	NA	NA	NA
WP_052327897.1\|2938501_2939572_-	DUF2891 family protein	NA	NA	NA	NA
WP_022926065.1\|2939597_2940383_+	thioesterase family protein	NA	NA	NA	NA
WP_022926066.1\|2940647_2941229_+	hypothetical protein	NA	NA	NA	NA
WP_022926067.1\|2941533_2942724_-	O-succinylhomoserine sulfhydrylase	NA	NA	NA	NA
WP_022926068.1\|2942862_2943942_-	ABC transporter ATP-binding protein	G3M9Y6	Bacillus_virus	4.7e-22	31.7
WP_028131215.1\|2943941_2945570_-	iron ABC transporter permease	NA	NA	NA	NA
WP_022926070.1\|2945909_2947040_+	glycosyltransferase	NA	NA	NA	NA
WP_149814954.1\|2947401_2948169_+	hypothetical protein	NA	NA	NA	NA
WP_149814841.1\|2948114_2949014_+	glycosyltransferase	NA	NA	NA	NA
WP_052327899.1\|2949010_2950132_+	glycosyltransferase	NA	NA	NA	NA
WP_022926075.1\|2953408_2954212_-	HAD-IIB family hydrolase	NA	NA	NA	NA
WP_022926077.1\|2955465_2955720_-	hypothetical protein	NA	NA	NA	NA
WP_022926078.1\|2955883_2956165_+	DUF4235 domain-containing protein	NA	NA	NA	NA
WP_022926079.1\|2956446_2958114_+	polysaccharide biosynthesis protein	A0A1V0SAI8	Catovirus	2.2e-26	31.0
WP_161600265.1\|2958194_2959109_+	glycosyl transferase	NA	NA	NA	NA
WP_084485241.1\|2959227_2961303_+	glycosyltransferase	NA	NA	NA	NA
WP_168714883.1\|2961769_2961961_+	hypothetical protein	NA	NA	NA	NA
WP_149814844.1\|2962183_2962423_+\|transposase	transposase	A0A1B3AZF8	Gordonia_phage	2.0e-18	82.1
WP_022926083.1\|2962376_2963318_-\|transposase	IS3 family transposase	U5P429	Shigella_phage	2.8e-34	33.2
WP_149814845.1\|2963331_2963604_-\|transposase	transposase	NA	NA	NA	NA
WP_157609225.1\|2963671_2964097_+	hypothetical protein	NA	NA	NA	NA
WP_161600266.1\|2967152_2968004_+	sulfotransferase	NA	NA	NA	NA
WP_149814848.1\|2968463_2969213_+	hypothetical protein	NA	NA	NA	NA
WP_161600267.1\|2970081_2970969_+	glycosyltransferase	NA	NA	NA	NA
WP_161600268.1\|2971106_2972147_+	O-antigen ligase family protein	NA	NA	NA	NA
WP_161600269.1\|2972335_2972506_+	hypothetical protein	NA	NA	NA	NA
2973442:2973457	attL	NA	NA	NA	NA
WP_149814955.1\|2974376_2974640_-\|transposase	IS3 family transposase	NA	NA	NA	NA
WP_161600270.1\|2974652_2974865_-	hypothetical protein	A0A2P1JR32	Mycobacterium_phage	6.9e-10	50.7
WP_161600271.1\|2974867_2975062_-	hypothetical protein	A0A1B3AZF8	Gordonia_phage	1.7e-10	70.4
WP_022926308.1\|2975075_2975366_+\|transposase	transposase	NA	NA	NA	NA
WP_149814851.1\|2975362_2976244_+\|transposase	IS3 family transposase	U5P429	Shigella_phage	8.6e-22	31.9
WP_149814852.1\|2976341_2977505_+\|transposase	IS110 family transposase	NA	NA	NA	NA
WP_161600272.1\|2978257_2978533_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_149814957.1\|2978893_2980138_-	sulfate adenylyltransferase	A0A1V0SGC3	Hokovirus	9.6e-35	25.9
WP_149814853.1\|2980161_2981073_-	sulfate adenylyltransferase subunit CysD	NA	NA	NA	NA
WP_022926316.1\|2981242_2982661_+	polysaccharide biosynthesis tyrosine autokinase	NA	NA	NA	NA
WP_149814855.1\|2983235_2983526_+	hypothetical protein	NA	NA	NA	NA
WP_149814958.1\|2983550_2984681_-	UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing)	A0A1V0SAG5	Catovirus	5.5e-21	29.1
WP_084485269.1\|2984698_2985994_-	UDP-N-acetyl-D-mannosamine dehydrogenase	NA	NA	NA	NA
WP_149814959.1\|2987517_2988762_-	sulfate adenylyltransferase	A0A1V0SGC3	Hokovirus	7.4e-35	25.9
WP_022926277.1\|2988785_2989697_-	sulfate adenylyltransferase subunit CysD	NA	NA	NA	NA
WP_022926278.1\|2989837_2990284_-	histidine triad (HIT) protein	NA	NA	NA	NA
WP_084485262.1\|2990498_2991509_+	adenylyl-sulfate kinase	A0A2K9L4R9	Tupanvirus	3.3e-33	46.7
WP_022926280.1\|2991550_2992315_+	3'(2'),5'-bisphosphate nucleotidase CysQ	NA	NA	NA	NA
WP_022926281.1\|2992319_2994086_-	SLC13 family permease	NA	NA	NA	NA
WP_149814857.1\|2995453_2996209_-	WecB/TagA/CpsF family glycosyltransferase	NA	NA	NA	NA
WP_149814858.1\|2998970_2999660_+	hypothetical protein	NA	NA	NA	NA
WP_161600273.1\|2999644_3000055_+	hypothetical protein	NA	NA	NA	NA
WP_052327922.1\|3000010_3000937_-	sulfotransferase	NA	NA	NA	NA
WP_022926285.1\|3001084_3002629_+	asparagine synthase (glutamine-hydrolyzing)	R4TIC1	Phaeocystis_globosa_virus	5.0e-33	27.7
WP_028131264.1\|3002621_3003071_+	adenylyltransferase/cytidyltransferase family protein	A0A222YWT0	Streptomyces_phage	7.3e-09	30.5
WP_149814860.1\|3003142_3004261_+	hypothetical protein	NA	NA	NA	NA
WP_022926294.1\|3004298_3005216_-\|transposase	transposase	A0A1P8CWQ3	Bacillus_phage	2.4e-06	29.9
WP_028131265.1\|3005389_3005734_-	hypothetical protein	NA	NA	NA	NA
WP_161600274.1\|3005862_3007284_-	cellulase family glycosylhydrolase	NA	NA	NA	NA
WP_149814861.1\|3009985_3012502_-	PKD domain-containing protein	NA	NA	NA	NA
WP_149814862.1\|3012528_3013956_-	hypothetical protein	NA	NA	NA	NA
WP_149814863.1\|3014145_3014532_-	hypothetical protein	NA	NA	NA	NA
WP_084485220.1\|3015168_3016005_+\|transposase	transposase	A0A1B3AZF8	Gordonia_phage	5.5e-34	80.0
WP_149814960.1\|3017072_3017681_+\|integrase,transposase	DDE-type integrase/transposase/recombinase	NA	NA	NA	NA
3017862:3017877	attR	NA	NA	NA	NA

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP043808

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