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_LT906449	Capnocytophaga haemolytica strain NCTC12947 chromosome 1	5 crisprs	cas3,WYL,DEDDh	0	0	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_LT906449_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906449_1

384469-384589

Orphan

Consensus_repeat	Method
GCAAAGCTGGGGTGGAGATAGTGCATTTGGAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906449_1

>merge|NZ_LT906449|1|384469-384589|CRISPRCasFinder
GCAAAGCTGGGGTGGAGATAGTGCATTTGGAGGAGGTATAATATAATGCACAATGGATAATTGATAATGTATAATATTAGAACTCTTGTGCAAAGCTGAGGTGGAGATAGTGCATTTGGAG

>NZ_LT906449|1|1|384469-384589|CRISPRCasFinder
GCAAAGCTGGGGTGGAGATAGTGCATTTGGAG	GAGGTATAATATAATGCACAATGGATAATTGATAATGTATAATATTAGAACTCTTGT
GCAAAGCTGAGGTGGAGATAGTGCATTTGGAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906449.1\|WP_066429414.1\|377305_377620_+\|DNA-directed-RNA-polymerase-subunit-omega	unknown	unknown	gnl\|CDD\|376482
NZ_LT906449.1\|WP_095114435.1\|373529_375053_+\|DUF4270-domain-containing-protein	unknown	unknown	gnl\|CDD\|379464
NZ_LT906449.1\|WP_066429412.1\|377709_378897_+\|bifunctional-phosphopantothenoylcysteine-decarboxylase/phosphopantothenate--cysteine-ligase-CoaBC	unknown	unknown	gnl\|CDD\|235513
NZ_LT906449.1\|WP_066431839.1\|372717_373527_+\|glycogen/starch-synthase	unknown	unknown	gnl\|CDD\|377972
NZ_LT906449.1\|WP_066429411.1\|378904_381142_+\|glycoside-hydrolase-family-92-protein	unknown	unknown	gnl\|CDD\|377950
NZ_LT906449.1\|WP_066429397.1\|387629_388199_-\|nucleotide-exchange-factor-GrpE	unknown	unknown	gnl\|CDD\|271355
NZ_LT906449.1\|WP_066429400.1\|386509_387619_-\|molecular-chaperone-DnaJ	unknown	unknown	gnl\|CDD\|237660
NZ_LT906449.1\|WP_066429419.1\|375063_375384_+\|translation-initiation-factor	unknown	unknown	gnl\|CDD\|211319
NZ_LT906449.1\|WP_066429409.1\|381420_383211_+\|long-chain-fatty-acid--CoA-ligase	unknown	unknown	gnl\|CDD\|223953
NZ_LT906449.1\|WP_066429393.1\|389571_389772_+\|heavy-metal-associated-domain-containing-protein	unknown	unknown	gnl\|CDD\|238219
NZ_LT906449.1\|WP_095114437.1\|388631_389465_+\|leucine-rich-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|275383
NZ_LT906449.1\|WP_066429402.1\|385627_386356_-\|glycoside-hydrolase-family-16-protein	unknown	unknown	gnl\|CDD\|185683
NZ_LT906449.1\|WP_169792828.1\|394284_394422_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066429388.1\|394503_395307_+\|TIGR02391-family-protein	unknown	unknown	gnl\|CDD\|378194
NZ_LT906449.1\|WP_066429408.1\|383185_384115_+\|bifunctional-riboflavin-kinase/FAD-synthetase	unknown	unknown	gnl\|CDD\|235536
NZ_LT906449.1\|WP_066429404.1\|384771_385440_-\|outer-membrane-beta-barrel-protein	unknown	unknown	gnl\|CDD\|379226
NZ_LT906449.1\|WP_066429390.1\|392373_394266_+\|molecular-chaperone-DnaK	unknown	unknown	gnl\|CDD\|234715
NZ_LT906449.1\|WP_066429417.1\|375427_376174_+\|3-oxoacyl-[acyl-carrier-protein]-reductase	unknown	unknown	gnl\|CDD\|187594
NZ_LT906449.1\|WP_066429416.1\|376495_377293_+\|outer-membrane-protein-assembly-factor-BamD	unknown	unknown	gnl\|CDD\|274513
NZ_LT906449.1\|WP_066429391.1\|389777_392192_+\|copper-translocating-P-type-ATPase	unknown	unknown	gnl\|CDD\|319783

Protein	Function_ID	Function_description	E-value
NZ_LT906449.1\|WP_066429414.1\|377305_377620_+\|DNA-directed-RNA-polymerase-subunit-omega	gnl\|CDD\|376482	pfam01192, RNA_pol_Rpb6, RNA polymerase Rpb6. Rpb6 is an essential subunit in the eukaryotic polymerases Pol I, II and III. This family also contains the bacterial equivalent to Rpb6, the omega subunit. Rpb6 and omega are structurally conserved and both function in polymerase assembly.	1.56884e-05
NZ_LT906449.1\|WP_095114435.1\|373529_375053_+\|DUF4270-domain-containing-protein	gnl\|CDD\|379464	pfam14092, DUF4270, Domain of unknown function (DUF4270). This family of lipoproteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 444 and 534 amino acids in length.	2.01253e-55
NZ_LT906449.1\|WP_066429412.1\|377709_378897_+\|bifunctional-phosphopantothenoylcysteine-decarboxylase/phosphopantothenate--cysteine-ligase-CoaBC	gnl\|CDD\|235513	PRK05579, PRK05579, bifunctional phosphopantothenoylcysteine decarboxylase/phosphopantothenate synthase; Validated.	8.45713e-176
NZ_LT906449.1\|WP_066431839.1\|372717_373527_+\|glycogen/starch-synthase	gnl\|CDD\|377972	pfam08323, Glyco_transf_5, Starch synthase catalytic domain.	7.48531e-55
NZ_LT906449.1\|WP_066429411.1\|378904_381142_+\|glycoside-hydrolase-family-92-protein	gnl\|CDD\|377950	pfam07971, Glyco_hydro_92, Glycosyl hydrolase family 92. Members of this family are alpha-1,2-mannosidases, enzymes which remove alpha-1,2-linked mannose residues from Man(9)(GlcNAc)(2) by hydrolysis. They are critical for the maturation of N-linked oligosaccharides and ER-associated degradation.	0
NZ_LT906449.1\|WP_066429397.1\|387629_388199_-\|nucleotide-exchange-factor-GrpE	gnl\|CDD\|271355	cd00446, GrpE, nucleotide exchange factor GrpE. GrpE is the adenine nucleotide exchange factor of DnaK (Hsp70)-type ATPases. In bacteria, the DnaK-DnaJ-GrpE (KJE) chaperone system functions at the fulcrum of protein homeostasis. GrpE participates actively in response to heat shock by preventing aggregation of stress-denatured proteins; unfolded proteins initially bind to DnaJ, the J-domain ATPase-activating protein (Hsp40 family), whereupon DnaK hydrolyzes its bound ATP, resulting in a stable complex. The GrpE dimer binds to the ATPase domain of Hsp70 catalyzing the dissociation of ADP, which enables rebinding of ATP, one step in the Hsp70 reaction cycle in protein folding. In eukaryotes, only the mitochondrial Hsp70, not the cytosolic form, is GrpE dependent. Over-expression of Hsp70 molecular chaperones is important in suppressing toxicity of aberrantly folded proteins that occur in Alzheimer's disease (AD), Parkinson's disease (PD), amyotrophic lateral sclerosis, as well as several polyQ-diseases such as Huntington's disease and ataxias.	3.90857e-39
NZ_LT906449.1\|WP_066429400.1\|386509_387619_-\|molecular-chaperone-DnaJ	gnl\|CDD\|237660	PRK14289, PRK14289, molecular chaperone DnaJ.	1.27411e-141
NZ_LT906449.1\|WP_066429419.1\|375063_375384_+\|translation-initiation-factor	gnl\|CDD\|211319	cd11567, YciH_like, Homologs of eIF1/SUI1 including Escherichia coli YciH. Members of the eIF1/SUI1 (eukaryotic initiation factor 1) family are found in eukaryotes, archaea, and some bacteria; eukaryotic members are understood to play an important role in accurate initiator codon recognition during translation initiation. The function of non-eukaryotic family members is unclear. Escherichia coli YciH is a non-essential protein and was reported to be able to perform some of the functions of IF3 in prokaryotic initiation.	1.61185e-28
NZ_LT906449.1\|WP_066429409.1\|381420_383211_+\|long-chain-fatty-acid--CoA-ligase	gnl\|CDD\|223953	COG1022, FAA1, Long-chain acyl-CoA synthetases (AMP-forming) [Lipid metabolism].	0
NZ_LT906449.1\|WP_066429393.1\|389571_389772_+\|heavy-metal-associated-domain-containing-protein	gnl\|CDD\|238219	cd00371, HMA, Heavy-metal-associated domain (HMA) is a conserved domain of approximately 30 amino acid residues found in a number of proteins that transport or detoxify heavy metals, for example, the CPx-type heavy metal ATPases and copper chaperones. HMA domain contains two cysteine residues that are important in binding and transfer of metal ions, such as copper, cadmium, cobalt and zinc. In the case of copper, stoichiometry of binding is one Cu+ ion per binding domain. Repeats of the HMA domain in copper chaperone has been associated with Menkes/Wilson disease due to binding of multiple copper ions.	1.71904e-14
NZ_LT906449.1\|WP_095114437.1\|388631_389465_+\|leucine-rich-repeat-domain-containing-protein	gnl\|CDD\|275383	sd00036, LRR_3, leucine-rich repeats. A leucine-rich repeat (LRR) is a structural protein motif of 20-30 amino acids that is unusually rich in the hydrophobic amino acid leucine. The conserved eleven-residue sequence motif (LxxLxLxxN/CxL) within the LRRs corresponds to the beta-strand and adjacent loop regions, whereas the remaining parts of the repeats are variable. LRRs fold together to form a solenoid protein domain, termed leucine-rich repeat domain. Leucine-rich repeats are usually involved in protein-protein interactions.	1.60277e-53
NZ_LT906449.1\|WP_066429402.1\|385627_386356_-\|glycoside-hydrolase-family-16-protein	gnl\|CDD\|185683	cd00413, Glyco_hydrolase_16, glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.	8.57427e-26
NZ_LT906449.1\|WP_066429388.1\|394503_395307_+\|TIGR02391-family-protein	gnl\|CDD\|378194	pfam09509, Hypoth_Ymh, Protein of unknown function (Hypoth_ymh). This entry consists of a relatively rare prokaryotic protein family (about 8 occurrences per 200 genomes). Genes for members of this family appear to be associated variously with phage and plasmid regions, restriction system loci, transposons, and housekeeping genes. Their function is unknown.	5.77209e-45
NZ_LT906449.1\|WP_066429408.1\|383185_384115_+\|bifunctional-riboflavin-kinase/FAD-synthetase	gnl\|CDD\|235536	PRK05627, PRK05627, bifunctional riboflavin kinase/FAD synthetase.	8.60696e-135
NZ_LT906449.1\|WP_066429404.1\|384771_385440_-\|outer-membrane-beta-barrel-protein	gnl\|CDD\|379226	pfam13505, OMP_b-brl, Outer membrane protein beta-barrel domain. This domain is found in a wide range of outer membrane proteins. This domain assumes a membrane bound beta-barrel fold.	2.58603e-06
NZ_LT906449.1\|WP_066429390.1\|392373_394266_+\|molecular-chaperone-DnaK	gnl\|CDD\|234715	PRK00290, dnaK, molecular chaperone DnaK; Provisional.	0
NZ_LT906449.1\|WP_066429417.1\|375427_376174_+\|3-oxoacyl-[acyl-carrier-protein]-reductase	gnl\|CDD\|187594	cd05333, BKR_SDR_c, beta-Keto acyl carrier protein reductase (BKR), involved in Type II FAS, classical (c) SDRs. This subgroup includes the Escherichai coli K12 BKR, FabG. BKR catalyzes the NADPH-dependent reduction of ACP in the first reductive step of de novo fatty acid synthesis (FAS). FAS consists of four elongation steps, which are repeated to extend the fatty acid chain through the addition of two-carbo units from malonyl acyl-carrier protein (ACP): condensation, reduction, dehydration, and a final reduction. Type II FAS, typical of plants and many bacteria, maintains these activities on discrete polypeptides, while type I FAS utilizes one or two multifunctional polypeptides. BKR resembles enoyl reductase, which catalyzes the second reduction step in FAS. SDRs are a functionally diverse family of oxidoreductases that have a single domain with structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet) NAD(P)(H) binding region and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H) binding pattern: TGxxxGxG in classical SDRs. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P) binding motif and an altered active site motif (YXXXN). Fungal type type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P) binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr-151 and Lys-155, and well as Asn-111 (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	6.92912e-129
NZ_LT906449.1\|WP_066429416.1\|376495_377293_+\|outer-membrane-protein-assembly-factor-BamD	gnl\|CDD\|274513	TIGR03302, OM_YfiO, outer membrane assembly lipoprotein YfiO. Members of this protein family include YfiO, a near-essential protein of the outer membrane, part of a complex involved in protein insertion into the bacterial outer membrane. Many proteins in this family are annotated as ComL, based on the involvement of this protein in natural transformation with exogenous DNA in Neisseria gonorrhoeae. This protein family shows sequence similarity to, but is distinct from, the tol-pal system protein YbgF (TIGR02795). [Protein fate, Protein and peptide secretion and trafficking].	6.0523e-29
NZ_LT906449.1\|WP_066429391.1\|389777_392192_+\|copper-translocating-P-type-ATPase	gnl\|CDD\|319783	cd02094, P-type_ATPase_Cu-like, P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B. The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle.	0

>NZ_LT906449.1|WP_066429408.1|383185_384115_+|bifunctional-riboflavin-kinase/FAD-synthetase
MKIITDLSNFTADRGTVVTIGTFDGVHCGHQKIIKRLTEAAKAEGLLSTVFTFFPHPRMIVQHDTQLRLLHTLAEKQTLLAALGVDLLIVQPFDKKFSQMSAEEFVEELLVKHLRVQKVIIGYDHRFGKNRTADIRDMHRFGEHYGFAVEEISAQEVDEVSVSSTKVREALLSGQVEKAESYLGVPYSLTGKVVHGQKLGRTLGYPTANIQVEEDYKLIPADGVYVVYSLLEGRKVYGMMSIGKNPTIADKGSSIEVHFLDYDGDLYDKSLTVYFIKYLRAEQKFASVAALQQQIEQDEEQSRKAIALR
>NZ_LT906449.1|WP_066429409.1|381420_383211_+|long-chain-fatty-acid--CoA-ligase
MNTVTRLFDIPYYQAANYPLEDALATKYNGAWARTSTEEYIKKANTVSRGLLRLGVEKGDKIAVISHNNRTEWHVLDIGLLQIGAQNVPIYPTITLEDYEYIFNHSECKYCFVSNKELLDKITSIKDKLPHLQAIYTFEEVAYAHHWQEIFDLGADESNQGEVEARKAAIGKDDLATIIYTSGTTNRPKGVMLSHWNIISNILNCKERLPLKAGSRAMSFLPVCHVFERMLTYFYQYNGLRLYFAESIDKVSDNLKEVQPDIITAVPRLLEKIFDKIFAKGTELKGLKRSLFFWAIRLGEQYEPYGVNGWWYRFRLGIARKLIFSKWQEALGGHLGMIVCGSAALSPRLARIFSAAGLYVIEGYGLTETAPVVAVNRRAGRLWRIGTVGKPIDNVDVKIAEDGEILCKGENVMLGYYKAPELTAEAITDGYFHTGDIGELDDEGFLKITDRKKEMFKTSGGKYVSPQLIENQLKLSRFIEQVMVVGEGEKMPAAIIQLNFPFVKEWARRHRIKIGKTNEEIIKSDKVFERVKEEVERVNKNLGQWEKIKLFAFTPDEWSIDAGHLTPTLKLKRRVIKEKYIDIYNSFYSENHNGSL
>NZ_LT906449.1|WP_066429411.1|378904_381142_+|glycoside-hydrolase-family-92-protein
MKRILTTFTVLTLAACSHQEPSATEAQPTDYVAYVNPLMGTDSTFELSNGNTYPAIAVPWGMNFFTPQTGKMGDGWAYQYHANKIRGFKLTHQPSPWINDYGAFALMPTTGALKIAEEDRASWFSHKAETAQPHYYKVYLADYDTSVEITPTSRAAQLRFTYPATEEAHLLIDAYFKGSMVKILPEERKIIGYARNNSGGVPENFHHYFVMQFDKDFTAYNTWGDGYKLSNKPEAEGEHTGAVLHFKTQRGEQITAKVATSFISIEQAALNLQREVGSDTFEQTRTKAHRLWQDELSKIAVEDTNTDALRTFYSCLYRVLLFPRTFYEYDKDNKIVHYSPYSGKVEAGYLFTDNGFWDTFRAVFPLFNLVYPEQNKLFMKGLVSTYRESGWLPEWASPGHRNCMIGSNSASIIADAYLKGNINKADAKILLEAMLKNATVSEGRPVKSVGREGVDYYNRLGYVPYNVGINENVARTLEYAYADYCIAQMAEKMGEKAIAAQYRKQSYRYKNVFDKETGWMRGRNEDGSFQRPFNPLKWGDAFTEGNSLHYSWSVFQDIEGLMALMGGKEAFGKKLDEVFSMPPLFDDSYYGFTIHEIREMQIMDMGNYAHGNQPIQHLIYLYPYAGEPRKAQQHIREVMTKLYTPTPDGYCGDEDNGQTSAWYVWSALGFYPVTPASDNYIIGNPIFAKAILHLPNNKNFIIENREKTQGNIYIKSVELNGKPFTDFRLPFKTVREGGKLVFNRD
>NZ_LT906449.1|WP_066429412.1|377709_378897_+|bifunctional-phosphopantothenoylcysteine-decarboxylase/phosphopantothenate--cysteine-ligase-CoaBC
MNILLGITAGIAAYKTPQLVRLLTKKGHTVRVIMTERAQDFVTPLTLSTLSKQPVLTDFQSADHQWNSHVEAALWAEALLIAPATANTMAKMANGICDNLLLATYFSAKAPVFIAPAMDLDMYAHPTVQQNIKRLESFGNYIIPAAYGELASGLIGQGRMEEPENIVAFLENHLSGSQPLSGKKVLITAGPTYEAIDPVRFIGNFSTGKMGIALANEAARQGAEVHLVLGPSAENNIAPSVRVHRVVSAQEMLQATLSEYDNSDLAILSAAVADYRPKEKALEKIKKQGGSLHLELTENPDILTTLGKGKTHQTLIGFALETENELTNAQAKLAKKNLDAIVLNSLKDKGAGFGTDTNKVSFITAEEVVSFPLKSKSEVAKDLLGEALTLMNRKK
>NZ_LT906449.1|WP_066429414.1|377305_377620_+|DNA-directed-RNA-polymerase-subunit-omega
MDFKRIDAPTTTVTYSRTAIEAPTGNIYEAISIIAKRATQINTEIKKELSEKLEEFATANDSLEEIFENKEQIEVSRFYERLPKPQAIAVKEWLEGKIYYREAN
>NZ_LT906449.1|WP_066429416.1|376495_377293_+|outer-membrane-protein-assembly-factor-BamD
MQMKKYILLGLISVLLSSCSEYQKALKSQDAAVKYTMAEKQYQAKKYKKANRLFEVIASEYSGKPQGERVYYMYGKSLYELGQYQLAAYQFERLQKLYPRSEKAAEAGFLEAKSLYNESPKYSVDQTYTYDALEKLQSFLDRYGSSEFAEEANKMTLDLVTRLQKKDFEIAKQYDQIRDYQAAMKSLDNFLANNPGSVFKEDALYVRLHSAYEWAINSVEHKKKERLETAKEAYETLLRTFPETKYKKEAEKMLEKINTSLKSLT
>NZ_LT906449.1|WP_066429417.1|375427_376174_+|3-oxoacyl-[acyl-carrier-protein]-reductase
MKLLEGKTAIITGASRGIGRGIALLFAQHGANVAFTYSASVEKAQALENELKAFGIKAKGYQSDAADFGEAQKLGEEIATEFGSIDILVNNAGITKDNLLMRISEEDFDKVIEVNLKSVFNMTKAVQRTMLKQRSGSIINMSSVVGVKGNAGQSNYAASKAGIIGFTKSIALELGSRNIRCNAIAPGFIETEMTAVLDEKVVQGWRDAIPLKRGGKVEDVANACVFLASDMAAYITGQVLNVDGGMLT
>NZ_LT906449.1|WP_066429419.1|375063_375384_+|translation-initiation-factor
MLKEQLQALFPDHIMEEEPQEEAAPYWMQDDPLLCKYEKRKGKPVTIIEGYNGADADFKALAKDLKTYLGVGGSVKEETILIQGDYRDKIMTFLKEKGFKVKRVGG
>NZ_LT906449.1|WP_095114435.1|373529_375053_+|DUF4270-domain-containing-protein
MIKKLKFVTLFVGGIAFLSACSDDAFNEIESSLPKDPNYNTDVYTATVSVSNIKEKAIQTNGLSGYLLGKYTQAPFGTKNATIASQVILPSANPRFGALTQADETAKNTPENEKVTEAYLYIPFFNINSSNSRATYNKDTEYQLDSIYGNKDASFAINVSELNYYLSNIGTDYQPKTYYSNDTDIPTHIGTSVASVTSYTISNKSITRYQFDDPKTQDDESKKEADVLAPGIRIPLSTSFFQTKIIDKEGSDELSNAEKFSKYFKGLVISTSNFSKDLMMLLNMAGAKIEIVYSYDTTNNGTKSTLKSRYELNLGGGITVNLLSNSDENLSDSTKTYLSGALGQTASITIADTDITKFKEGNWLITDASLYLYVDNSVTYAKEPDRLFVYNAETGNVLVDYQYDPTSAAKTAASSYLIHLGKLQKQNGKGAYYQLRITNHLVDLIKNSTNKNIPLGIAVASSVKVTTSGVYLDTSGANHKIALTTLATPLSTVIKDVQLIIHYTKAK
>NZ_LT906449.1|WP_066431839.1|372717_373527_+|glycogen/starch-synthase
MKDKKVLYVSSEVLPYSPDSEIARMSFEAPRMVNNKGGQLRVFMPRFGNINERRHQLHEVIRLSGMNIIINDIDVPLIIKVASIPKERIQVYFIDNDEYFKRSGTLFDENGTFYADNDERCIFFAKGIVETIKKLNWRPDIIHIHGWLPALLPLYLRTFYKDEPLFSESKIITSVFDKGFDGQLNTTLINKVAFDGISKKVAEPLKEPHYYNLMKMAIKNSDGVIVVSEDMPEDFQTYLRGLRKPVLFNSDKETFQDSYHNFYLQILKR
>NZ_LT906449.1|WP_066429404.1|384771_385440_-|outer-membrane-beta-barrel-protein
MKKIILSLVAIFGFGAAAQAQDGGDFGFNQGNLFLEGNVRFSSQWTAGANSDSKSNLFEVSPAAGYFLSDKFAVGLGLSYKAYKNIKREWDTTSEKYGKVVPNASQKVSSFGFDLFGRYYLLELGQRFKVYGQADLGFDFESDQPVGGGSKDKYTTFNIGAGLGMNYFVTPKLAINFGLSDIISFNSRKPKGSDATNTFKGDFNVFNNFFTTPTFGLTYKLN
>NZ_LT906449.1|WP_066429402.1|385627_386356_-|glycoside-hydrolase-family-16-protein
MKKIIYFMAVMSAMMVSSCGKDDSGSGEWVLDFEDNFDGTQLNKDNWTIYDNAGSTNPDHKRRVEAIEVKDGLLNCIVDKHPTDSSHFMAGGIGCRKNYLYGKFEFRIRMDHDPLYATSGVALTWPESEVWPKDGENDIFETEYETHRWDTYIHYVNDQGEHKTHHHNYDMDKTQWRVVAMEWTPDYIKTYVDGKLMWTLEDRKTIPKVTHHICFQVEKHIDKGLEKPVRLQVDWVKIYKRK
>NZ_LT906449.1|WP_066429400.1|386509_387619_-|molecular-chaperone-DnaJ
MKKDYYEVLEISKTATVAEIKKAYRQQALKYHPDKNPGDKEAEEKFKLAAEAYEVLSDENKRAQYDRFGHAAFEGGAGGGFSSMEDIFAHFGDIFGGHFSSFGFGSSGRSSGQTYIKGENLRIRVKVSLEDIVKGTEKKVKVRRKVKAEGVTYKTCPTCHGQGQVLRQAQTILGMIQTSTTCGHCGGTGQVLDHRPEGSDHNGMKTVEETITVPIPAGVMNGIQLKIDGKGNEAPSKNSIAGDLLVLIEEQEHEKLKREGDNLHYDLYISMPEAALGANKEIETVTGKVRIKIEAGTQSGKILRLRDKGVPSLRGGVGDLIIHVNVWTPKELSKEQKAFFEQMKDDTHFTPNPSKEDKSFFEKVKEMFS
>NZ_LT906449.1|WP_066429397.1|387629_388199_-|nucleotide-exchange-factor-GrpE
MSEYTDHTEEPEEINEELLPEEQEVFDETPEEAQDEEETTTSESNPADELAKERDRYVRLFAEFENYKKRTTKERIELFKTAGQDILSAMLPILDDFDRALAELTKLGDHTALTGVELIYNKLMNMLKAKGLEPVEVNAGDPFDSEHHDAITQIPAPTPDLKGKIIDVVEKGYKLGDKVIRFPKVVVGQ
>NZ_LT906449.1|WP_095114437.1|388631_389465_+|leucine-rich-repeat-domain-containing-protein
MPKIEYILSDDGHTLVEWCLKKTAEIDMPSRVELSGIEAIAPRAFADCNKLTTLVLSEGLTTIGERAFERCKRLNSIVIPEGVVSIGDWAFADCNALVEVHLPQGITHIGERMFSKCESLTNIVLPPKVQTIGDRAFGECISLEEVVLPEGVTSLGKWAFSYCSKLRKVSLPESLTTIADHAFLECHSLTDIHLPDSLEMIGDTAFAFTSLTDLVIPEGVKAIGERAFAGVHLKQLTLLPPYPPTLGEAAFDLRKTIVNLPEEHRALYKEKLNCDGH
>NZ_LT906449.1|WP_066429393.1|389571_389772_+|heavy-metal-associated-domain-containing-protein
MTTYRINGMGCEGCASTVKERLSKVEGVKEVAVDFAGSKATIEMTKEVPLSALQKALEGTSYSITK
>NZ_LT906449.1|WP_066429391.1|389777_392192_+|copper-translocating-P-type-ATPase
MEENNTNNTFTYYIKGMSCAGCVNTVQQALSGVEGVSSVQVDLNEKKATIESAEEVPFEVLEKSLEGTHYTIHKTAEEATEQHSLTLVEEGEEGTGVFYCPMHCEGDKTYDHPGACPICGMDLVEQVSSVEAAAEGERMKLRDLRRKFWGSVIFTLPIFVIAMSEMVPNNPLYEWLPQEYWNWIQFDLSLPVVFGFCWVFFQRAWRSIATLRFNMFTLIGIGAGVAWLFSVVGLLFPNIFPEQFLSHHGTVHVYFEAATVILTLVMLGQYLEAIAHGRTQNAVQSLLSLAPNTAIIVDEEGDIEVPIDEVVIGDLLRVKPGSKIPVDGHIVEGSSSVDESMITGEPIPVEKQVGDKVSAGTLNGTEAFVMEADKVGAETLLSQIVAMVQKASMTQAPIQKLADRVASYFVPVVIGISVLTFVLWAIFGGEHALVYALVNAIAVLIIACPCALGLATPMSVMVGVGKGAQNGILIKNAEGLERMNVVDTLVIDKTGTLTEGKPVVERMVLFSDMTEEELLQIIYSININSEHPLAKATNAYAEERGVEPLKITDFKAIAGKGVVGAYNEQTYYFGNEALLNTAGIMLIGVVKAMVTEEQARGKTISYIATNKKIVGAVVISDPLKATTVDALADLRDLGMEIIMLTGDNQLTAKAVAKAAGITDYKAGMLPQHKQKEVERLQREGKIVAMAGDGINDAPALAQADVGIAMGTGTDIAIENAEITLVKGELNGIVKAKKLSQAVVRNIRQNLFFALIYNAIGIPIAAGVLYPFFGVLLSPMIGALAMSFSSVSVISNALRLRSVKL
>NZ_LT906449.1|WP_066429390.1|392373_394266_+|molecular-chaperone-DnaK
MGKIIGIDLGTTNSCVSVMEGNDPVVITNAEGKRTTPSVVAFVEGGEIKVGDAAKRQAVTNPHNTIYSIKRFMGNKFSELSKEIARVPYKVVRGDNDTPRVDIDGRLYTPQEISAMILQKMKKTAEDFLGQPVTEAVITVPAYFNDAQRQATKEAGEIAGLKVQRIINEPTAAALAYGLDKQHNDHKIVVFDFGGGTHDVSILELGDGVFEVLSTDGDTHLGGDDVDEKIINWLAEEFEKEESLDLRKDPMALQRLKEAAEKAKIELSSSSETEINLPYITATATGPKHLVRKLSRAKFEQLIDDLIQRTIEPCKKALENAGLQVSDINEVILVGGSTRIPAVQNAVEKFFGKKPNKSVNPDEVVAIGAAIQGGVLTGDVKDVLLLDVTPLSLGIETMGGVMTKLIEANTTIPTKKSQIFSTAADNQPSVEIHVLQGERPMANDNKTIGRFHLDGIPPAPRGVPQIEVTFDIDANGIINVSATDKGTGKSHDIRIEASSGLSKEDIEKMKREAEANAEADRKAKEKADKLNEADAMIFQTEKQLKEFGDKLPSDKKSAIESSLEELKKAYNTGDLGTVEQALNKMNDVWRQASEDIYKAQQQGGAQPNASEPQQQSGADNVQDVDFEEVK
>NZ_LT906449.1|WP_169792828.1|394284_394422_+|hypothetical-protein
MSYKLKPGPKPIAKSTGEVDKRRRDNKDTPKNNPALKPSKSSSNK
>NZ_LT906449.1|WP_066429388.1|394503_395307_+|TIGR02391-family-protein
MKRQVLSANILEMISNLIGDTNEGLKGSEITRFLAQAHIDEKEEDKAMTKRMRLFNAFANFQNKERCSNNILNFISLVLSPSRYVNDKSKFDNLRTKINQQLAFVGYELKEDGKYRLIQKASTISDVQIKTENLKQELDKRNAHAEIFKYCKEELLQNNYFHSVLEANKGLFQRIRDLSNISTDGINLIQEVFSSNPILIINNYQSNSEKNEHTGFCNLLRGLCSMFRNPTAHEPKVEWEIKEQDALEILGIISYCHRRLDNAQKIR

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Crispr_ID: NZ_LT906449_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906449_2

1802162-1802283

Orphan

Consensus_repeat	Method
GTTGTTATCAATCACAAAACTACAAAATTTGAAGGCAATTCACAAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906449_2

>merge|NZ_LT906449|2|1802162-1802283|CRISPRCasFinder
GTTGTTATCAATCACAAAACTACAAAATTTGAAGGCAATTCACAACACACTACAACTGTCTCTTAACATCAGTAAAGTTGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC

>NZ_LT906449|2|2|1802162-1802283|CRISPRCasFinder
GTTGTTATCAATCACAAAACTACAAAATTTGAAGGCAATTCACAAC	ACACTACAACTGTCTCTTAACATCAGTAAA
GTTGTTATCAATCACAAAACTACAAAATTTGAAAGCAATTCACAAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906449.1\|WP_066427562.1\|1800365_1801424_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066427547.1\|1806765_1809258_+\|sel1-repeat-family-protein	unknown	unknown	gnl\|CDD\|276807
NZ_LT906449.1\|WP_066427577.1\|1796496_1796703_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372659
NZ_LT906449.1\|WP_143325044.1\|1803574_1803946_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066427551.1\|1805213_1805600_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066431632.1\|1809332_1810208_-\|geranylgeranylglycerol-phosphate-geranylgeranyltransferase	unknown	unknown	gnl\|CDD\|260124
NZ_LT906449.1\|WP_066427545.1\|1810361_1811687_-\|lytic-transglycosylase-domain-containing-protein	unknown	unknown	gnl\|CDD\|381615
NZ_LT906449.1\|WP_066427550.1\|1805886_1806690_+\|DUF3108-domain-containing-protein	unknown	unknown	gnl\|CDD\|378635
NZ_LT906449.1\|WP_066427575.1\|1796792_1797794_-\|diphosphomevalonate-decarboxylase	unknown	unknown	gnl\|CDD\|225941
NZ_LT906449.1\|WP_159429717.1\|1797811_1797982_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066427572.1\|1797986_1798598_-\|DJ-1/PfpI-family-protein	unknown	unknown	gnl\|CDD\|153234
NZ_LT906449.1\|WP_066427567.1\|1798679_1799537_-\|acetyl-CoA-carboxylase-carboxyltransferase-subunit-beta	unknown	unknown	gnl\|CDD\|235547
NZ_LT906449.1\|WP_074860922.1\|1796290_1796572_-\|DKNYY-domain-containing-protein	unknown	unknown	gnl\|CDD\|372659
NZ_LT906449.1\|WP_066427564.1\|1799743_1800163_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066427552.1\|1804731_1805139_+\|SlyB-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066427581.1\|1795924_1796248_-\|DKNYY-domain-containing-protein	unknown	unknown	gnl\|CDD\|372659
NZ_LT906449.1\|WP_066431629.1\|1812143_1814468_+\|penicillin-binding-protein-1C	unknown	unknown	gnl\|CDD\|273954
NZ_LT906449.1\|WP_066427560.1\|1801553_1801991_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|234827
NZ_LT906449.1\|WP_066427554.1\|1804397_1804646_+\|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein	unknown	unknown	gnl\|CDD\|225170
NZ_LT906449.1\|WP_066427559.1\|1802582_1803503_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_LT906449.1\|WP_066427547.1\|1806765_1809258_+\|sel1-repeat-family-protein	gnl\|CDD\|276807	sd00010, SLR, Sel1-like repeat. Sel1-like repeats (SLRs) share similar alpha-helical conformations with Tetratricopeptide repeats (TPRs), but with different consensus sequence lengths and superhelical topologies. SLRs contain 36 to 44 amino acids and are present in bacteria and eukaryotes but not in archaea. SLR proteins are involved in a variety of functions, and many serve as adaptor proteins for the assembly of macromolecular complexes. The SLR family was named after the Caenorhabditis elegans Sel1 protein which is predicted to fold into 11 SLRs, a transmembrane domain, and an N-terminal signal sequence. The human Sel1L protein contains an additional fibronectin type-II domain and an N-terminal PEST sequence. Its downregulation is associated with the development of breast and pancreatic carcinomas.	6.4957e-31
NZ_LT906449.1\|WP_066427577.1\|1796496_1796703_-\|hypothetical-protein	gnl\|CDD\|372659	pfam13644, DKNYY, DKNYY family. This family represents a group of proteins found enriched in fusobacteria. These proteins contain many repeats of a DKNXXYY motif. The repeats are spaced at about 35 amino acid residues intervals. These proteins are likely to be associated with the membrane. The specific function of these proteins is unknown.	0.000540859
NZ_LT906449.1\|WP_066431632.1\|1809332_1810208_-\|geranylgeranylglycerol-phosphate-geranylgeranyltransferase	gnl\|CDD\|260124	cd13961, PT_UbiA_DGGGPS, Geranylgeranylglycerol-phosphate geranylgeranyltransferase. Digeranylgeranylglyceryl phosphate synthase (DGGGPS) transfers a geranylgeranyl group from geranylgeranyl diphosphate to (S)-3-O-geranylgeranylglyceryl phosphate to form (S)-2,3-di-O-geranylgeranylglyceryl phosphate, as part of the isoprenoid ether lipid biosynthesis. Prenyltransferases (PTs) catalyze the regioselective transfer of prenyl moieties onto a wide variety of substrates and play an important role in many biosynthetic pathways.	1.80549e-63
NZ_LT906449.1\|WP_066427545.1\|1810361_1811687_-\|lytic-transglycosylase-domain-containing-protein	gnl\|CDD\|381615	cd16894, MltD-like, Membrane-bound lytic murein transglycosylase D and similar proteins. Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).	1.45963e-65
NZ_LT906449.1\|WP_066427575.1\|1796792_1797794_-\|diphosphomevalonate-decarboxylase	gnl\|CDD\|225941	COG3407, MVD1, Mevalonate pyrophosphate decarboxylase [Lipid metabolism].	2.46253e-63
NZ_LT906449.1\|WP_066427572.1\|1797986_1798598_-\|DJ-1/PfpI-family-protein	gnl\|CDD\|153234	cd03140, GATase1_PfpI_3, Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.	2.57938e-46
NZ_LT906449.1\|WP_066427567.1\|1798679_1799537_-\|acetyl-CoA-carboxylase-carboxyltransferase-subunit-beta	gnl\|CDD\|235547	PRK05654, PRK05654, acetyl-CoA carboxylase carboxyltransferase subunit beta.	4.63118e-151
NZ_LT906449.1\|WP_074860922.1\|1796290_1796572_-\|DKNYY-domain-containing-protein	gnl\|CDD\|372659	pfam13644, DKNYY, DKNYY family. This family represents a group of proteins found enriched in fusobacteria. These proteins contain many repeats of a DKNXXYY motif. The repeats are spaced at about 35 amino acid residues intervals. These proteins are likely to be associated with the membrane. The specific function of these proteins is unknown.	8.1245e-10
NZ_LT906449.1\|WP_066427554.1\|1804397_1804646_+\|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein	gnl\|CDD\|225170	COG2261, COG2261, Predicted membrane protein [Function unknown].	4.347e-05
NZ_LT906449.1\|WP_066427581.1\|1795924_1796248_-\|DKNYY-domain-containing-protein	gnl\|CDD\|372659	pfam13644, DKNYY, DKNYY family. This family represents a group of proteins found enriched in fusobacteria. These proteins contain many repeats of a DKNXXYY motif. The repeats are spaced at about 35 amino acid residues intervals. These proteins are likely to be associated with the membrane. The specific function of these proteins is unknown.	5.29544e-05
NZ_LT906449.1\|WP_066431629.1\|1812143_1814468_+\|penicillin-binding-protein-1C	gnl\|CDD\|273954	TIGR02073, Includes:_Penicillin-insensitive_transglycosylase, penicillin-binding protein 1C. This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	0
NZ_LT906449.1\|WP_066427560.1\|1801553_1801991_-\|hypothetical-protein	gnl\|CDD\|234827	PRK00733, hppA, membrane-bound proton-translocating pyrophosphatase; Validated.	0.00092246
NZ_LT906449.1\|WP_066427550.1\|1805886_1806690_+\|DUF3108-domain-containing-protein	gnl\|CDD\|378635	pfam11306, DUF3108, Protein of unknown function (DUF3108). This is a bacterial family of putative lipoproteins. Structure 3fzx, the first structural template for this large family including several homologs in the human gut microbiome and in metagenomic datasets, folds into a beta barrel that topologically looks like a small-scale porin (such as FepA). Bacteroides fragilis glyA is a putative exported protein, and this fold is of the YmcC-like type, with a predicted signal peptide SpI cleavage site AGAMA\|QNQDC, and a Phobius server prediction of non-cytoplasmic localization for amino acids 21-236. The possibility of it being a membrane protein can be ruled out by the hydrophilic nature of the solvent exposed surface outside the barrels. Analysis of sequence conservation suggests that an area near Glu172/Trp206 is potentially interesting. These two residues are also conserved in Dali hit Structure 2in5, a hypothetical lipoprotein classified as a new YmcC-like fold in SCOP (SCOP:159271, with a 12-stranded meander beta-sheet folded into a deformed beta-barrel) despite large structural differences between the two structures, suggesting similarity in function.	9.71522e-69

>NZ_LT906449.1|WP_066427560.1|1801553_1801991_-|hypothetical-protein
MKKSVQIFLELISAIALYLFINSIAYGDHLVTLPLYLTGVVIMSYLFVRERPQECLQSALRIVLPFTGLMLIAGSLPDANFSLALIYIVSTGVAFLLGMLIATVSKTYQKIGLSALTFLLVVAVRLSFSAEFQYLIGVHWYTLGS
>NZ_LT906449.1|WP_066427562.1|1800365_1801424_-|hypothetical-protein
MKHLFTSLITLLLCACHQERAHKPTDAEKYELKGAVKELEISYYAENDELGEAVKDLRNKLAITFDKEGRQVKETFYEITADAQGKTIAVVASIARTAYDGDVKEVVAYTPDGVQTAKRVFLSDKNGTTIFFDDEEVIITGTAHVKKDTQGRIAERYWQSELGSIEVTFAYKYDAQGNVSEITVSDSMGRHYRTYRFAYDSKGNETEVKSFDRNNKLWAESLYDKKGNLLKTSIYDKEGNLTATAYEYDRKGNVTEELWNLPAGKGEQRNTYTYDRKGNLVKANIESVGVVYTYEYDDKDNVSQMVSTDNATKSSETYRYTYTYDEKGNYTRKTERSSKDFKATEERVIRYY
>NZ_LT906449.1|WP_066427564.1|1799743_1800163_-|hypothetical-protein
MKHFLELISAIAIYLFIGAIAYGDHLVTLPLYLTGVVIVSYLFVRDRPQQKWDSFLRVVSPFAVLMLIAGSLQDAHTSLALGYIAGTVVAYLLGMCIATVSKTYQKIGLSALAFLLIVAVRLSFSAEFQYLIGVHWHTL
>NZ_LT906449.1|WP_066427567.1|1798679_1799537_-|acetyl-CoA-carboxylase-carboxyltransferase-subunit-beta
MSWFKRTAKGIQTSTEEKKDVPKGLWYKSPSGNIVETDELAANAYVSPEDGYHVRIGSKEYFQILFDNNEFKELDENLTSKDPLGFVDTKSYEQRLKEAEQKTGLKDAVRTAVGKSKGEDLVIACMDFAFIGGSMGSVVGEKISRAIGYAIKHKLPFLMISKSGGARMMEAALSLMQMAKTSVKLAQLDEAKLPYISLCTDPTTGGISASFAMLGDINIAEPGALIGFAGPRVVKDTTGQDLPEGFQTAEFVLEHGFLDFIVNRKELKDKVNLYLDLVLNRAVRQ
>NZ_LT906449.1|WP_066427572.1|1797986_1798598_-|DJ-1/PfpI-family-protein
MKKEVVFIILDQFANWESAYLAAALETDFVTNNYTISYASTDKNVKTSIGNMKVLPDLTIDAIPSSAEALVLIGANESWRTLGEEAQSKIITTVQQFKKANKVVAAICDGAYFLAVNGLLNDCKHTTNRLEEIKGVGAYTNEDNYVHTALEAVSDKKIVTAKGDSALHFAASVLRALGDIPEQGIRIFYTAHSLGFEKAMELM
>NZ_LT906449.1|WP_159429717.1|1797811_1797982_-|hypothetical-protein
MDRIYTITDREEEERDDTLMTKEAFFTIIDRARAGKKTEMTIEEMEAYLEDKVARM
>NZ_LT906449.1|WP_066427575.1|1796792_1797794_-|diphosphomevalonate-decarboxylase
MITQKAPSNIALVKYWGKREGQLPANPSVSFTLTNCYTETSVTYNPEHTASFEFFFEGEAKPSFHPKLTTFFERIADLVPFIKEYHLRIDSHNSFPHSSGIASSASAMAALALCLVRMEQQLGTPMTEEEALQKASVLARLGSGSACRSVYSGLVVWGAHKSIAGSSDDYGIPYPLTVNEVFKNYQDSILLIDKGRKQVSSSVGHNLMHGHPFAQARFAQAHQHIEELIPVFAAGDLERFIAIIESEALTLHAMMQTSQPYFILMRPNTLEAINRIWAFRQETKTPVGFTLDAGANVHLLYPAFCKEAVQAFITAELKELCEGGQVIADAVKG
>NZ_LT906449.1|WP_066427577.1|1796496_1796703_-|hypothetical-protein
MLRTATEYDERYSQHPFWTDGKKVYYRHYEIKGVDKDSFEVLGDCMPVIRNIVIFRAIALLGQTVRAL
>NZ_LT906449.1|WP_074860922.1|1796290_1796572_-|DKNYY-domain-containing-protein
MYARDKKHCYFQSNRLAGADRESFVVLNPTYAKDKAMVWAFGSRIKEADAASFEACDAGAQPLSIRKDAIEPYMEITEKGYGKDANNVYYMGF
>NZ_LT906449.1|WP_066427581.1|1795924_1796248_-|DKNYY-domain-containing-protein
MSFGDNYAKDAQRVFYEKYSLPKASPATWDYIHEGFYYTRDGNRIYYMNRLMKGVDVETFELLFDAEEEESGNYYQYARDKNTYYDRGNPITKEAYEKRGELPEGYE
>NZ_LT906449.1|WP_066427559.1|1802582_1803503_+|hypothetical-protein
MSKPKNVKCRAFRISTNNFTDNAKSIFSLLCEQLPKSKANERRMRLNTKDESREEDLICDYEISEGVIFGTLLRIKSSDNIPEIPEEVFEENIVHLEQLRDLDVNSSLFYKDHYYFLLNDKYLIVTLRGNITITHFQTYTNWLLESLRANTLFEFTPIIKENPNISLSDLKSLRIQDPVRKEEDNFDLTETKSISFKLLREMLTDVLSFDEVKASEVISAELLLKFSKPKKMKEKDYQNYFGAQLKPISDLENVTFITKKGKTIKGDEMQEMQEFKVETTDSGKISEPELKQAMEKYLRELEKCFN
>NZ_LT906449.1|WP_143325044.1|1803574_1803946_+|hypothetical-protein
MNTLFTILGIMFSIAMGLLITFNLQGIKNKRIIDLLRSNIKKVRHSYIKYFAFSTLFYLLEKYLRDKGNNLYAFSIREISITINFSLITVVILVYSIIYFIMNFIAMQKLSDSLYDEVNSKNN
>NZ_LT906449.1|WP_066427554.1|1804397_1804646_+|GlsB/YeaQ/YmgE-family-stress-response-membrane-protein
MGIIATLIIGAIAGWLGGTIYKGSGLGLIGNIIIGILGSGVGYWLLGNVFHISLGEGWIGTILTGAIGAIVILFLINLIFKK
>NZ_LT906449.1|WP_066427552.1|1804731_1805139_+|SlyB-protein
MKKTLIISTFVSIFIASCGTSKSPEIKRLEAKKEYLELKTKLNALEIQLVNEENENEALQSEAMKANDNANSHTDKFNDANSASIAAKKARKAERSLRRARKSNRRLANSNKRIYKLRKEIKSLNEKIQKLELGE
>NZ_LT906449.1|WP_066427551.1|1805213_1805600_-|hypothetical-protein
MKKIIALVSVICLSLVAFSCISCSKNDDPADNDLFIGTYKGKVSYSDSQQKKSADNGAVTVIKTGNDYYFRFSDGIPNLTGVSFKKEGDNTLVNIDLKDGVKIIRINASSLNILYTTDGKTWTANAKR
>NZ_LT906449.1|WP_066427550.1|1805886_1806690_+|DUF3108-domain-containing-protein
MKKTLKTITFALVALLCSPVVEAQNDNLPFKNGEWLRFKVKYGVFNASIATMQLTEEMYKGEKVFHAVGKGSTTGLARVFFRVDDIYESYFGVKDGRPRVFVRNIHEGSYTKHLKMFFNYTDNKVKIDNIENGNTTEIDFKPGLQDVISAFYALRHHPEVDNLKVGGQIALDMIFDDDEIYKFKLKFLGKEKVKTRFGTVNTLKFCPLVQDGRVFKEQESITMWITDDKNKVPVKLKASLRVGSLVAELDGFNLLKNDTNLKKIMQK
>NZ_LT906449.1|WP_066427547.1|1806765_1809258_+|sel1-repeat-family-protein
MKNFILAICLLCISMVYGQDSNTKKLIKAAEGGDVKAQTELADLYYKGKGGLKRSFQEGFKWYLKAAEAGDLQAQGQVAEIYFTGRGAPKSPEKGVEWLTKVAESGDAKAKRQLALCYKEGKGVEASNAQYIRWIADVAENEKPEIQMDLAKAYYNGDGVQKDINKAKYWAEKAKKQGYAEADYLIGTWLYEVNPSNPEAIDRLTKAADKGNAEAEYNLSEAYLAGKGVAQSDETALKWLEKAARGGSAEAEYKLATYYFTGENSLIGKSYKKAFEWFQKAAQKGNAEAQFQLAVCYYNGIGVKQSYQDAFNWISKAVASKATPIAENNLGVIYTTGHGAKASNAQALELFEKAANTGDAMAQYNAGVSLLDPQQLDVKKAFDYLEKSAAQNNLLALKKLGDLYFTGKYTNQSAERAFEYYTKVSKLTPKAQEQMLKYFYQQEKEHYAEALFSLAQCYADGKGVKKSTVQACNLAIKAANLDNKAAFDWLNKRVEKNDPKESADVQLAVADGYYYAKLVRKQNDKAFPIYDKLAKQQDNLTAQKRLIEYYFDAKNPDKSDEKALYWAEKVAKKGDVETQRLLGMYYMKEVPDVKKAPAAPASKPVATKPAPKKAKSTPVAATASTTTEPIEIQRETDPVRAELLRRQRGGKPALEVQAHPKKTVQPQRQVVRQAPKAVAPAAPKVAEAPKGPMKRINETKGLFWLSKAAEHNDEEALDALGSYFYNKKDFTQALNNFQRAARRDYAPAQFNLANCYYNGNGVERSFEKAAIYYKQAARRDYAPAQFRLGHCYYHGEGIAQSDNRAADWFDKACDAGVAKSCEMLKIVNKK
>NZ_LT906449.1|WP_066431632.1|1809332_1810208_-|geranylgeranylglycerol-phosphate-geranylgeranyltransferase
MRKKHILLKFLGLFSAVRGYNIAIVCLAQYLAAIFVLSSQSWREVLLDERLFTLVWAGSLAIAGGYIINGFYDTEKDLINKPFKAMIDRLVSQNTRLTLYFLLNFLSVIVASYVSFRAVVFFSLYIFGMWLYSHRLKRLPLWGNLCSAALAIVPFFAVFVYYKNFDRAIFFHATLIYLLLLLKEFVKDLENIKGDLVHNYQTIPVRYGERFSKGMITLCVLLCFIPMGVLTAHFSIGKLWYYFIFTGVCLLLLLVVLWSSNSRRGYAFLHQLIKVILVLGIFSVGLLGLKG
>NZ_LT906449.1|WP_066427545.1|1810361_1811687_-|lytic-transglycosylase-domain-containing-protein
MKFRIYTLGTFFCLLIGNLSAEAQQFAMNDSIVSPAGSLTPKRDEFMRLKDNPKVKKYDEKWLKELSNSDLYFQMSEDIAATPTDVSYDELSTEVLKKRLEKLNQKTPFNIEYNPVLEQVIKSFLKNRRSSLERLMSLSDYYFPMFEQEMSNQKIPLEMKYLAIIESALNPKARSRAGATGLWQFMYSTGRGYGLEVNNYVDERSDPVRSTKAAAKYLNELYKVFGDWDLVLAAYNSGPGNVTKAIRRSNGKQNYWNLRPYLPRETAGYVPAFLATLYIFEYAKEHGFRPQKRTNHLFQTDTIRVKQAVPFKDIADLTGMSVEEIQFFNPSYQLDVVPYVEGRNYALRLPISEIGKFVENEDLIYAYLNEEKEHLEKPLPTVVRGEQYASRNNKKTVYTVKRGDNLGRIASRYGVTVSNLKRWNRMKSTHIRVGQRLVIYK
>NZ_LT906449.1|WP_066431629.1|1812143_1814468_+|penicillin-binding-protein-1C
MVKKHPIKSGIALLLIGWYYFCLPRQLFPEQYATVLESAEGKLLAAKIAPDEQWRFPEVDSVPYRFKMSVLYFEDEYFKYHWGVNPVSVSKALWRNIKSGKVERGGSTLTQQVVRIAREHQQRTYAEKLIEMIWATRLEFRYSKESILKLYASHAPFGGNVIGLEMAAWRYFGVAPHQLSWSECATLAVLPNAPSLIFPGKNQERLREKRDRLLKKLFTAKVIDEETYRLALTEPLPQKPHSIPQIAPHLLTYAAKKHAGERIRSTVPLALQEKVNQVVAGYYTHYSQSEVYNMAALVIDVKTRKVLAYVGNTPTDNEHQNAVDIVHAPRSTGSVLKPLLYAAMLHEGELLPTQLLPDVPTQIGGYSPQNFSNTFEGAVPANVALAKSLNIPFVWLLKQYGTYRFYDILQQLQLKDINKHPDHYGLSIILGGAESNLWDLAQAYTNLASELNEFARRQVYRTEEFQHLQYNAMAKPLTFGSDTRKMPMLRAGALYEMFDAMKEVNRPSTDVAWRYYESSRKIAWKTGTSFGNKDAWAIGATPEYVVAVWVGNATGEGRPTLTGASYAAPVLFSIFGALPPTTWFAKPYDDMREVTVCADSGFLTKEGCPQKAILTTLATKEVGQCPYHKIVHLDASGHYQVNAACEPADKIVSKEWFVLPPVMEWYYKQQHINYLPLPPTREDCRAAEGLRSLDFVYPKHQGIIYTTKDFGGKEQPFIAKAANRTGQVFWYLDATYLGSTDTFHEMQVFATKGKHILRILNEQGDERAIEILVQ

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Crispr_ID: NZ_LT906449_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906449_3

1969098-1969215

Orphan

Consensus_repeat	Method
CCTAAAAAACTTTTTTTAATTGCCGTCCCACGTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906449_3

>merge|NZ_LT906449|3|1969098-1969215|CRISPRCasFinder
CCTAAAAAACTTTTTTTAATTGCCGTCCCACGTCTGTACAAGTGCAAAAAAGTTCAGAAAGTGATCAGCTCACAGCTGTACAAGCCTAAAAAACTTTTTTTAGTTGCCGTCCCACGTC

>NZ_LT906449|3|3|1969098-1969215|CRISPRCasFinder
CCTAAAAAACTTTTTTTAATTGCCGTCCCACGTC	TGTACAAGTGCAAAAAAGTTCAGAAAGTGATCAGCTCACAGCTGTACAAG
CCTAAAAAACTTTTTTTAGTTGCCGTCCCACGTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906449.1\|WP_066431304.1\|1982019_1983207_+\|nicotinate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|235406
NZ_LT906449.1\|WP_066432031.1\|1963159_1964131_-\|acyl-transferase	unknown	unknown	gnl\|CDD\|282319
NZ_LT906449.1\|WP_066431307.1\|1980769_1981303_-\|DUF177-domain-containing-protein	unknown	unknown	gnl\|CDD\|376863
NZ_LT906449.1\|WP_066431346.1\|1962869_1963157_+\|twin-arginine-translocase-TatA/TatE-family-subunit	unknown	unknown	gnl\|CDD\|224739
NZ_LT906449.1\|WP_066431342.1\|1965399_1965879_+\|DNA-starvation/stationary-phase-protection-protein	unknown	unknown	gnl\|CDD\|153102
NZ_LT906449.1\|WP_066431344.1\|1964158_1964665_-\|J-domain-containing-protein	unknown	unknown	gnl\|CDD\|223560
NZ_LT906449.1\|WP_066431323.1\|1975975_1977862_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066432026.1\|1964670_1965072_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066431348.1\|1961812_1962790_-\|M23-family-metallopeptidase	unknown	unknown	gnl\|CDD\|366703
NZ_LT906449.1\|WP_066431352.1\|1960556_1961471_+\|glutaminase	unknown	unknown	gnl\|CDD\|274797
NZ_LT906449.1\|WP_066431336.1\|1967459_1968668_-\|DUF4876-domain-containing-protein	unknown	unknown	gnl\|CDD\|379795
NZ_LT906449.1\|WP_066431326.1\|1974256_1975885_+\|acyl-CoA-carboxylase-subunit-beta	unknown	unknown	gnl\|CDD\|227136
NZ_LT906449.1\|WP_066431350.1\|1961467_1961797_-\|MerR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133393
NZ_LT906449.1\|WP_066431313.1\|1980567_1980762_-\|50S-ribosomal-protein-L32	unknown	unknown	gnl\|CDD\|366808
NZ_LT906449.1\|WP_082753020.1\|1970746_1973467_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|369481
NZ_LT906449.1\|WP_143325054.1\|1965952_1967452_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066431320.1\|1977928_1978171_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066431316.1\|1979441_1980032_+\|peptide-deformylase	unknown	unknown	gnl\|CDD\|234668
NZ_LT906449.1\|WP_066431315.1\|1980050_1980470_+\|DUF5606-domain-containg-protein	unknown	unknown	gnl\|CDD\|375774
NZ_LT906449.1\|WP_066431318.1\|1978326_1979319_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|182059

Protein	Function_ID	Function_description	E-value
NZ_LT906449.1\|WP_066431304.1\|1982019_1983207_+\|nicotinate-phosphoribosyltransferase	gnl\|CDD\|235406	PRK05321, PRK05321, nicotinate phosphoribosyltransferase; Provisional.	0
NZ_LT906449.1\|WP_066432031.1\|1963159_1964131_-\|acyl-transferase	gnl\|CDD\|282319	pfam04443, LuxE, Acyl-protein synthetase, LuxE. LuxE is an acyl-protein synthetase found in bioluminescent bacteria. LuxE catalyzes the formation of an acyl-protein thioester from a fatty acid and a protein. This is the second step in the bioluminescent fatty acid reduction system, which converts tetradecanoic acid to the aldehyde substrate of the luciferase-catalyzed bioluminescence reaction A conserved cysteine found at position 364 in Photobacterium phosphoreum LuxE is thought to be acylated during the transfer of the acyl group from the synthetase subunit to the reductase. The carboxyl terminal of the synthetase is though to act as a flexible arm to transfer acyl groups between the sites of activation and reduction. This family also includes Vibrio cholerae RBFN protein, which is involved in the biosynthesis of the O-antigen component 3-deoxy-L-glycero-tetronic acid.	4.67507e-09
NZ_LT906449.1\|WP_066431307.1\|1980769_1981303_-\|DUF177-domain-containing-protein	gnl\|CDD\|376863	pfam02620, DUF177, Uncharacterized ACR, COG1399. This family is nearly universally conserved in bacteria and plants except the Chlorophyceae algae. Thus far, mutantional analysis in bacteria have not established a function. In contrast, mutants have embryo lethal phenotypes in maize and Arabidopsis. In maize, the mutant embryos arrest at an early transition stage.It has been suggested that family members specifically affect 23S rRNA accumulation in plastids as well as bacteria.	2.00132e-16
NZ_LT906449.1\|WP_066431346.1\|1962869_1963157_+\|twin-arginine-translocase-TatA/TatE-family-subunit	gnl\|CDD\|224739	COG1826, TatA, Sec-independent protein secretion pathway components [Intracellular trafficking and secretion].	7.57636e-13
NZ_LT906449.1\|WP_066431342.1\|1965399_1965879_+\|DNA-starvation/stationary-phase-protection-protein	gnl\|CDD\|153102	cd01043, DPS, DPS protein, ferritin-like diiron-binding domain. DPS (DNA Protecting protein under Starved conditions) domain is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. Some DPS proteins nonspecifically bind DNA, protecting it from cleavage caused by reactive oxygen species such as the hydroxyl radicals produced during oxidation of Fe(II) by hydrogen peroxide. These proteins assemble into dodecameric structures, some form DPS-DNA co-crystalline complexes, and possess iron and H2O2 detoxification capabilities. Expression of DPS is induced by oxidative or nutritional stress, including metal ion starvation. Members of the DPS family are homopolymers formed by 12 four-helix bundle subunits that assemble with 23 symmetry into a hollow shell. The DPS ferroxidase site is unusual in that it is not located in a four-helix bundle as in ferritin, but is shared by 2-fold symmetry-related subunits providing the iron ligands. Many DPS sequences (e.g., E. coli) display an N-terminal extension of variable length that contains two or three positively charged lysine residues that extends into the solvent and is thought to play an important role in the stabilization of the complex with DNA. DPS Listeria Flp, Bacillus anthracis Dlp-1 and Dlp-2, and Helicobacter pylori HP-NAP which lack the N-terminal extension, do not bind DNA. DPS proteins from Helicobacter pylori, Treponema pallidum, and Borrelia burgdorferi are highly immunogenic.	8.13777e-50
NZ_LT906449.1\|WP_066431318.1\|1978326_1979319_+\|hypothetical-protein	gnl\|CDD\|182059	PRK09752, PRK09752, AIDA-I family autotransporter YfaL.	0.00015876
NZ_LT906449.1\|WP_066431348.1\|1961812_1962790_-\|M23-family-metallopeptidase	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	2.66822e-47
NZ_LT906449.1\|WP_066431352.1\|1960556_1961471_+\|glutaminase	gnl\|CDD\|274797	TIGR03814, Glutaminase_1, glutaminase A. This family describes the enzyme glutaminase, from a larger family that includes serine-dependent beta-lactamases and penicillin-binding proteins. Many bacteria have two isozymes. This model is based on selected known glutaminases and their homologs within prokaryotes, with the exclusion of highly-derived (long branch) and architecturally varied homologs, so as to achieve conservative assignments. A sharp drop in scores occurs below 250, and cutoffs are set accordingly. The enzyme converts glutamine to glutamate, with the release of ammonia. Members tend to be described as glutaminase A (glsA), where B (glsB) is unknown and may not be homologous (as in Rhizobium etli). Some species have two isozymes that may both be designated A (GlsA1 and GlsA2). [Energy metabolism, Amino acids and amines].	2.16099e-154
NZ_LT906449.1\|WP_066431336.1\|1967459_1968668_-\|DUF4876-domain-containing-protein	gnl\|CDD\|379795	pfam16215, DUF4876, Protein of unknown function (DUF4876). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 392 and 433 amino acids in length. There is a conserved NNS sequence motif.	3.56667e-51
NZ_LT906449.1\|WP_066431326.1\|1974256_1975885_+\|acyl-CoA-carboxylase-subunit-beta	gnl\|CDD\|227136	COG4799, COG4799, Acetyl-CoA carboxylase, carboxyltransferase component (subunits alpha and beta) [Lipid metabolism].	0
NZ_LT906449.1\|WP_066431350.1\|1961467_1961797_-\|MerR-family-transcriptional-regulator	gnl\|CDD\|133393	cd04765, HTH_MlrA-like_sg2, Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators. Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.	5.83776e-33
NZ_LT906449.1\|WP_066431313.1\|1980567_1980762_-\|50S-ribosomal-protein-L32	gnl\|CDD\|366808	pfam01783, Ribosomal_L32p, Ribosomal L32p protein family.	1.32302e-15
NZ_LT906449.1\|WP_082753020.1\|1970746_1973467_-\|TonB-dependent-receptor	gnl\|CDD\|369481	pfam07715, Plug, TonB-dependent Receptor Plug Domain. The Plug domain has been shown to be an independently folding subunit of the TonB-dependent receptors. It acts as the channel gate, blocking the pore until the channel is bound by ligand. At this point it under goes conformational changes opens the channel.	2.26654e-12
NZ_LT906449.1\|WP_066431316.1\|1979441_1980032_+\|peptide-deformylase	gnl\|CDD\|234668	PRK00150, def, peptide deformylase; Reviewed.	3.10325e-73
NZ_LT906449.1\|WP_066431315.1\|1980050_1980470_+\|DUF5606-domain-containg-protein	gnl\|CDD\|375774	pfam18347, DUF5606, Domain of unknown function (DUF5606). This is a domain of unknown function found at the N-terminal region of bacterial proteins.	1.81782e-17
NZ_LT906449.1\|WP_066431344.1\|1964158_1964665_-\|J-domain-containing-protein	gnl\|CDD\|223560	COG0484, DnaJ, DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones].	5.37722e-26

>NZ_LT906449.1|WP_066431336.1|1967459_1968668_-|DUF4876-domain-containing-protein
MRILSKLIIIIIAALSIVSCRKDENTNDGERLLNLTLIALEGEKILSYNELTIRLKELNTGGVITKKYTDLQSLTLSIPLAAGSYEVSVEGRLTYQRGNEKLTGSVSAFSEKIDLTEPSTHKSLQLMLKQTAQDLILEEIFISGTRTPEGKQYIGDSYIKLYNNTDEILYADGLLILQSFFETNAKVQHSPNIIAEAFNVDAVQQIPGSGKDYPVLPYTSIIIATDAIDHREYNKNSIDLRQANFEIKKSDDDEDPDNPQVPNLNNILGELVLSNQGNKSFAIARLPKGMTASQYLAEYKYNYTYRETGMDFDIPQENYKIPNQWIVDAVNLAPKEEFQWLLTSEALDSGWTYSSEHQGDNGRYGMAVRRKVSNSEAGKIYYQDTNNSTVDFIPRVQASLIK
>NZ_LT906449.1|WP_143325054.1|1965952_1967452_-|hypothetical-protein
MRAYFLTPLFIVMSASLWGQVPDTLYRNLKNEYGIRNFVRSITKNPSLMSSWGSDSFSTVEAHYGKSENEAYAKQFPSGTEGFGVRAESFLEYKNGKRLWGSASYQNQKEKDLRWNESIDRTLIYPYFTADSIGGDMQTERYAFAGGYLKHYKRFGWGAALNYAAKLASRNRDPRPKNISSDLRIKAGGALRDFYHLTLALHGSFEKYTQSNDIKFFSETGQPSVYHLNGLGYYNNLLKGNHLRGIYDGYGYGAGAQVVNQRGNWYLAVDYERLQVEKYIPDENNVVASTLVNSQWNAEITKLFHKKSYAYGLKLSYSNRQKAGIEPLLSARNSNGAEVLSTHKNYTLKTADYRLSLIFISEGESQLLISPYVSYQTHREDYTLIESFEHFSYLAAGLHLSYTQAFQRKHYLCYTLDWLSRRTLSKEYLLRNDSQRSLSQMLADNAQYLSSDEHRLTLGIEYNHRLHDNLSLFTRVGSAIALFPKRVNYLHSLSIGIHF
>NZ_LT906449.1|WP_066431342.1|1965399_1965879_+|DNA-starvation/stationary-phase-protection-protein
MSLNSLGLDKAKLGKEIEALNVLLANYQTYYQNLRGVHWNIKGKRFFELHVKFEDLYTAAQEQVDEIAERILTLGGVPYHTFASYVKHATVPVGENVFDDDKTVRLVIDSISELLRVERPLLDLSDELNDEGTNTLISDLVVEQEKNVWMLKSYLNEAI
>NZ_LT906449.1|WP_066432026.1|1964670_1965072_-|hypothetical-protein
MVYYSIFGLCVAYVIYVFATQARTNLKREKAIEEMRKKWEDAVVDEQKTKDIIHGLIKSTYGDPTLHLIEKNQFKEGMSDYLVKMAVGIPNEVQSAAFKSSSTERWHYDALIFTFQNGKLIGWEKNNNPMAKK
>NZ_LT906449.1|WP_066431344.1|1964158_1964665_-|J-domain-containing-protein
MLKDYYEILGVHQTASLDEIKDAYKKLAKAFHPDKHQGDAFFSEKFKSLQEAYAVFTDPVKKQEYDAQWAEFQKSSKKRKGTKQNRTARPENKTERDTTPSSYSAADLPSLVDIYLEKKDKTLQVRKQYDALLASPKKKVVSWVKVAIAVAIIVLNFLLLNPYFGLLK
>NZ_LT906449.1|WP_066432031.1|1963159_1964131_-|acyl-transferase
MNDIFNIQSEGDFKQAALAVFAYQYTHNPVYRDFCNFLGKNPTNVLSIEHIPFLPIEFFKTKKIYCGNTPEEAIFTSSGTTGSQTSKHYVKDLSLYEQSFHKGFELFYGNPADYVILALLPSYLERSGSSLITMVSDLIKASNKPLSGFYLNELNTLADLMNQLDRHEQKVFLIGVSFALLDLVERYQFLLSFTTVMETGGMKGRRKELVREELHRTLRRGFGVAHIHSEYGMTELFSQAYSVGKGIFTPVPWMKILIRDTNDALNLLPHGKTGGVNVIDLANLYSCSFIATQDLGKSYPDGTFEILGRFDNADIRGCNLMVF
>NZ_LT906449.1|WP_066431346.1|1962869_1963157_+|twin-arginine-translocase-TatA/TatE-family-subunit
MGISEIIFILFMVLVLFGADKLPEVARGLGKAMRQVREATNEIKTELTKTTEQGGVNTSIIEDAQQEINKIKDEVANATSVDLKQDSGVEGTVKR
>NZ_LT906449.1|WP_066431348.1|1961812_1962790_-|M23-family-metallopeptidase
MKKIKYYYDPETLSYKRIVSRKRTKVRNVLVFLLAAALFGTLAVFIMMNSNFLLTPREVVLNREIKFLETNFEVLNKKMDLVEEVLANVQERDNNMYRVYFNAAPLTDEERKKVSSDASRYNDLKNYDSSEIVINTIKRLDTLQHQLVAQSKSLDEITKLSKAKEKFLSSIPAIQPVDNKDLKHMASGYGWRTDPFTKARKFHYGMDFTSPQGTFVYATGDGVVTRADNASAGYGNHVRIDHGYGYVTLYGHLSAYNVRPGQHVKRGDLIGRVGSTGRSEAPHLHYEVMKNGEHINPIHFYYGNLTPDEYAEMLRVSTEENQSLD
>NZ_LT906449.1|WP_066431350.1|1961467_1961797_-|MerR-family-transcriptional-regulator
MEITLPNKLYYTTNEVAKAFGVNASLVRFWEKEFKILKPQKDERGTRKFTPDDVRLLQRIYHLVKEQGFTLEGARQKLKEDKHQALSTLEMITKLEAVKQQLLSLKDAL
>NZ_LT906449.1|WP_066431352.1|1960556_1961471_+|glutaminase
MDYQNIIEEVYYYVLEEENVGAKPTYIPELAQVDEHKFGVYFYSLNKRRFGIGDYQERFSIQSIAKVLSTTLAYSILGDRLWERVSVEPSGTSFNSLVQLESDNGIPRNPLINSGAIVVCDILLSTLENAEEDFIEFVRDLANDHSIDYSQRVAQSEKSVGYRNFALCYYIKSLGNIVNDPIKVLDFYFKLCSVELSCEQLAYVFSFLANDGIRLHDREPVLTDTFTKRINAIMQTCGFYDESGEFAFKVGLPGKSGVGGGIVAIMPNQYSIAVWSPKLNAKGNSYRGMKFLEAFTQQTRTSIF
>NZ_LT906449.1|WP_082753020.1|1970746_1973467_-|TonB-dependent-receptor
MVYTCAIQLTFAQIRVDFQVRDTLGRPVQELAIFLGQKAAATDSNGLASLSVAAGKYTLSTSHVGFEAIHKSVTIARDTLIALRVRPSAEQLQEVVVTAREVAAPTSTSVIDRKAMQHLQPSSFTDLVSLLPGRSVSSPVLNRANTLTLREAGISSSQYSTGAMGVGFRVDGVPLNTNANMQETVGYDMLVTPQSSSVDGKRNTTRSGVDMRAIATDEIEKVEVVRGIPSVKYGDLSSGLVQITRKKGATKLSGRIKADGFSKLFYLGKGFEFKDKALTLNTSFDYLNAKIDPRNSFENYKRYTASLRSEKKFGAERRSALSLSLDYTGTFDEEKLDPDNSVRGDAYHSSFSNIRIASAFGTQLSEKWFKEVNVQASLSQSFDQITQDKFVSVKSAKAIATNWQEGEYYGVYMDPNYVSHLLIDGKPLDVFTDLSSTSEFEVFGLKSELLLGATYTYAKNRGRGQVYDIAHPPSEDMNIRPRAFSAVPAMQNAAFYVQDELSKELGSVKITLRAGLQGSSLLGLPANYKMRGRVYLDPRVNAMLRLPLAKFSSGKTLEGSLSAGWGKHSKLPTQEMLYPQDIYDDIEQLNYYHNNKDYRRVHYRTYIFSQTNPALESAVNVKREARLGLSYGGHSLYVTYFNEKMDNGFRKMSDYHKVSYKKYDTSGIDSNNLTEAPRVEQLPFEEKNQLVLRSLESNGSATDKQGVEFQYAGKRLPLLHTRMTLSGAWLRTRYYNSQAALRFASTMTINNRTYYHLGVYPEVERYDRERFQSSFTADTYLEALGLITSLRCDLVWYTLDQNPPVSGVPTHYISEDGVRHPYTESERNDYLLQFLTYPTSRGTSLRVPMSMHLHLKISKQFYHYFTASMYVNNLFNYAESYQSNGLWVNRKGVVDPYFGMEMNINF
>NZ_LT906449.1|WP_066431326.1|1974256_1975885_+|acyl-CoA-carboxylase-subunit-beta
MDIQFNTNEDHNKLALAELRKRLKRVYLGGGAKNLEKLHAAGKLSARERIDYLLDKGARRIEIGAFAGEGMYPEHGGCPSAGVVVVMGYVAGVQCIVVANDATVKAGAWFPITAKKNLRAQEIAMENRLPIIYLVDSAGVYLPLQDEIFPDKEHFGRIFRNNAQMSALGITQIAVVMGSCVAGGAYLPIMSDEAMIVDKTGSIFLAGSYLVRAAIGEDIDNETLGGATTHCEISGVTDYKALDDKDALDRVRRTMGKLGDYQRAGFNRAAAVPPAKDPKEIYGILPTSRSEPYDMKELILRLVDNSEYDEYKVGYGQTLITGYARIDGWAVGIVANQRKVVKTKKGEMQFGGVIYSDSADKATRFIANCNQKRIPLVFLQDVTGFMVGSKSEHGGIIKDGAKLVNAVANSVVPKFTIVVGNSYGAGNYAMCGKAYDPRLIASWPSGNIAVMGGAQAAKVLLQIETATLKKRGEELTPEREAALFEEIKAKYDEQISPYYAAARLWTDAVIDPLETRLWISMGIEAADHAPIERAFNLGIIQV
>NZ_LT906449.1|WP_066431323.1|1975975_1977862_-|hypothetical-protein
MLVALWEAGDLTFDEGPFAQRLYNSIWGFQEEQGVSLVALLAKQPELAEKVLSVLPLYMESLTFDNQLHINFFKQLQEKGILPVEAFVTAAFEALLAPRKKPVLDLLCRLIEVLHPSNALLLCNQERMLALLSLGNSSLINFALPQLRKIAQEKAFDAQAFHDNFFLCANTPRIGKSILIGLEIVEQLIKQEGTKEGTEGTERLGVFFTISDEKVQQRVAQLLTTYYSKAVVDAVVLPYRVYLKEKVAAYLAEAGVTPEEDSSAKGNLSEVYPTRTPEPLKTIATWDELLFAIGDSLREGTTAQLDAIFEAFVSLQDALPANYAEQIAPYVQQLKERFGIYYQYYGSLYKVLTGEVYKDKYSHYYPKEEHDNFSFLRDKAEEVLTRQASHNTLGFLSTPTQQPFYIDPAVLEERLQAYKAAGVSPLAEDVTVAQARCIGAKEAEVYPKYEVKKATVDYYERYQLQFKKHWGAQTMGENIAYQLSLQPNAIDRLVLRYILPIGVGERAEPLHAATRVVQLLLQWQLPVKSGGWLFVATCLIGEKQPLRDMATDYLLWALGAGVDTTYLADCTRRLLASKYAPVKRFLEFTDRPLPYAEVKAFTQAVVQNYKKYVDERDKPSNHKLMLSL
>NZ_LT906449.1|WP_066431320.1|1977928_1978171_-|hypothetical-protein
MQQLDDLKAAMEQYLGINEDFALRFERYLAISYAAMCVCSDLKSLLKVEGKMELSYERNKDLYFLCSEYTTPFLALLHTE
>NZ_LT906449.1|WP_066431318.1|1978326_1979319_+|hypothetical-protein
MKKIITLAAALLFVVACSKNDDKETPTPTPPAPNPPSVTPTPDPTPTPPPTPPEQISMLPKKSVAVGSNGDTETMDYTYEGDKIRTIKRQVKDSKGIRNSIDTYTYEGDLVKMFTTTSEGNSLKTTYFYDGGLLKSRVSKTHQVGKDNAIHTSVSTTSYTYKGQKLVSWYTSVVLTKTLQGEKKPSIIITDSNTLEYISSTEVKIRSEYNGGFLKEISYSKVYFDADGDVLRDEGVKDNGKIEYRVEYTYSNEKTVPWVTFFRIITPEMPFVGASSNKKNILTGKIYNQGSLTSTTKHEYSYDDHNRLTKIINTNQNSIGNFTETITYEY
>NZ_LT906449.1|WP_066431316.1|1979441_1980032_+|peptide-deformylase
MVLPIIAYGDPVLRKVGVEITPDYPNLKALIANMYDTMEASNGVGLAAPQVGLAIRLFVVDAAPFADDEDLSKEERDFLLGFKQTFINAQMIEEVGEEWLFNEGCLSIPGVREDVSRRPKITISYLDENFHPQTLTVDGLVARIIQHEYDHIQGVLFTDKLSSFKKQLIKNKLTNISKGKVKVAYRMKFPDAPKRR
>NZ_LT906449.1|WP_066431315.1|1980050_1980470_+|DUF5606-domain-containg-protein
MNLTKILAISGKPGLYHLEKQTRAGFLATSLVDDSRVSVGLRNNVSLLSEIAIYTNEREVPLAEVFKNMKQVENGQPASVSSKSDGATLEEYFFTVLPTYDSDRVYASDIKKVIQWYNLLLAKGFLEDTEEGDDAAASA
>NZ_LT906449.1|WP_066431313.1|1980567_1980762_-|50S-ribosomal-protein-L32
MAHPKRRQSSTRRDKRRTHDKAAVPQIAKDSVTGELHLYHRAHWYEGKLYYRGQVLIDSTEAAE
>NZ_LT906449.1|WP_066431307.1|1980769_1981303_-|DUF177-domain-containing-protein
MNKLKEYEVSFVGLKQGKHEFVYAIDKRFLALFDYEEVNDIDEKVTLSLDKKSTLMELHFKNKGIVNVNCDVSNEPFDLPVEGELFLVVKFGEEYNDDDDELLILPHGAHQFNVAQYIYELVVLSIPAKRIHPDVVSDKMHSEVLDKLEALSPKEPIDETEHIDPRWESLKNLITDK
>NZ_LT906449.1|WP_066431304.1|1982019_1983207_+|nicotinate-phosphoribosyltransferase
MAVENYSVFNSILDNDFYKFTMQCAVVQLFPTNKGRYTFINRGKHEFPEGFAGALQQGVNAMAQLKLTKDEKLFLQENCPYLSPLYLDFLEGYRYDPSEVKIEQRGADLEVHVEGYWYRTILWEVPLLAMISELYYRLTKAQGWSDERIVENTLEKVRVYNELNVAFAEFGTRRRHSYHVHDIVMRTLTNGAARRFAGSSNVHFAMKYQVKPIGTHAHEWFMFHAAEYSYKMSNALSLEHWVDVYRGDLGVALSDTYTTDVFFKQFDKKFSKLFDGVRHDSGDPIVFAEKTIAHYKRMGIDPLSKYIIFSDGLNTEKVQLITEACRGKIGLSFGIGTDLTNDVGLRPMNIVMKLTEVLTSDNEWVPTVKLSDEPNKHTGDKRMIELAKGILNISV

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Crispr_ID: NZ_LT906449_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906449_4

2369439-2369634

Orphan

Consensus_repeat	Method
TAAAAATTGTTGGCGACACATCAACG	CRISPRCasFinder

4 spacers

The CRISPR arrays of NZ_LT906449_4

>merge|NZ_LT906449|4|2369439-2369634|CRISPRCasFinder
TCAAAAATATGGGCGACATATCAACGCACCGTTGAACCCTCCAAAACAATTTTCGGCGAACTATCAACGTATAGGGAACGTGTACTAAAAATTGTTGGCGACACATCAACGGGTAGTTGATGTGTGTAAAACAATTGTTGGGGAACTATTAACGTATAGGGGACGTACGATAAAACTTGTTGGCGACACATCAACG

>NZ_LT906449|4|4|2369439-2369634|CRISPRCasFinder
TCAAAAATATGGGCGACATATCAACG	CACCGTTGAACCCTCCA
AAACAATTTTCGGCGAACTATCAACG	TATAGGGAACGTGTAC
TAAAAATTGTTGGCGACACATCAACG	GGTAGTTGATGTGTGTA
AAACAATTGTTGGGGAACTATTAACG	TATAGGGGACGTACGA
TAAAACTTGTTGGCGACACATCAACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906449.1\|WP_066430682.1\|2365197_2366382_-\|aminopeptidase	unknown	unknown	gnl\|CDD\|238328
NZ_LT906449.1\|WP_066430688.1\|2361226_2361904_-\|PAS-domain-containing-protein	unknown	unknown	gnl\|CDD\|369881
NZ_LT906449.1\|WP_066430673.1\|2378295_2380602_+\|transglycosylase-domain-containing-protein	unknown	unknown	gnl\|CDD\|227342
NZ_LT906449.1\|WP_066431968.1\|2366481_2367129_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066430677.1\|2369723_2370284_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274948
NZ_LT906449.1\|WP_066430675.1\|2377798_2378287_+\|gliding-motility-lipoprotein-GldH	unknown	unknown	gnl\|CDD\|379474
NZ_LT906449.1\|WP_095114462.1\|2363018_2364716_+\|M23-family-metallopeptidase	unknown	unknown	gnl\|CDD\|366703
NZ_LT906449.1\|WP_066430680.1\|2367716_2368814_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_LT906449.1\|WP_082752995.1\|2370433_2371882_+\|efflux-transporter-outer-membrane-subunit	unknown	unknown	gnl\|CDD\|273830
NZ_LT906449.1\|WP_066430678.1\|2368878_2369424_+\|NAD(P)H-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|376808
NZ_LT906449.1\|WP_066430689.1\|2359310_2361107_-\|long-chain-fatty-acid--CoA-ligase	unknown	unknown	gnl\|CDD\|223953
NZ_LT906449.1\|WP_066430683.1\|2364729_2365107_+\|RidA-family-protein	unknown	unknown	gnl\|CDD\|129116
NZ_LT906449.1\|WP_066430666.1\|2381209_2382133_-\|tyrosine-recombinase-XerD	unknown	unknown	gnl\|CDD\|274043
NZ_LT906449.1\|WP_066430668.1\|2380779_2381151_+\|PUR-family-DNA/RNA-binding-protein	unknown	unknown	gnl\|CDD\|378691
NZ_LT906449.1\|WP_143325018.1\|2367173_2367578_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066430687.1\|2361944_2362643_-\|PAS-domain-containing-protein	unknown	unknown	gnl\|CDD\|369881
NZ_LT906449.1\|WP_066430661.1\|2383272_2383812_-\|DUF1599-domain-containing-protein	unknown	unknown	gnl\|CDD\|377892
NZ_LT906449.1\|WP_082752994.1\|2376417_2377812_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|224688
NZ_LT906449.1\|WP_066430664.1\|2382132_2383227_-\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|225168
NZ_LT906449.1\|WP_066431966.1\|2372931_2376087_+\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911

Protein	Function_ID	Function_description	E-value
NZ_LT906449.1\|WP_066430682.1\|2365197_2366382_-\|aminopeptidase	gnl\|CDD\|238328	cd00585, Peptidase_C1B, Peptidase C1B subfamily (MEROPS database nomenclature); composed of eukaryotic bleomycin hydrolases (BH) and bacterial aminopeptidases C (pepC). The proteins of this subfamily contain a large insert relative to the C1A peptidase (papain) subfamily. BH is a cysteine peptidase that detoxifies bleomycin by hydrolysis of an amide group. It acts as a carboxypeptidase on its C-terminus to convert itself into an aminopeptidase and peptide ligase. BH is found in all tissues in mammals as well as in many other eukaryotes. Bleomycin, a glycopeptide derived from the fungus Streptomyces verticullus, is an effective anticancer drug due to its ability to induce DNA strand breaks. Human BH is the major cause of tumor cell resistance to bleomycin chemotherapy, and is also genetically linked to Alzheimer's disease. In addition to its peptidase activity, the yeast BH (Gal6) binds DNA and acts as a repressor in the Gal4 regulatory system. BH forms a hexameric ring barrel structure with the active sites imbedded in the central channel. The bacterial homolog of BH, called pepC, is a cysteine aminopeptidase possessing broad specificity. Although its crystal structure has not been solved, biochemical analysis shows that pepC also forms a hexamer. .	3.96884e-20
NZ_LT906449.1\|WP_066430688.1\|2361226_2361904_-\|PAS-domain-containing-protein	gnl\|CDD\|369881	pfam08447, PAS_3, PAS fold. The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.	1.62056e-11
NZ_LT906449.1\|WP_066430673.1\|2378295_2380602_+\|transglycosylase-domain-containing-protein	gnl\|CDD\|227342	COG5009, MrcA, Membrane carboxypeptidase/penicillin-binding protein [Cell envelope biogenesis, outer membrane].	5.72661e-156
NZ_LT906449.1\|WP_066430677.1\|2369723_2370284_+\|hypothetical-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	5.45447e-05
NZ_LT906449.1\|WP_066430675.1\|2377798_2378287_+\|gliding-motility-lipoprotein-GldH	gnl\|CDD\|379474	pfam14109, GldH_lipo, GldH lipoprotein. Members of this protein family are predicted lipoproteins, exclusive to the Bacteroidetes phylum. Proteins in this family are typically between 155 and 167 amino acids in length. Members include GldH, a protein linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Not all Bacteroidetes with members of this protein family may have gliding motility.	5.02781e-48
NZ_LT906449.1\|WP_095114462.1\|2363018_2364716_+\|M23-family-metallopeptidase	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	4.28805e-21
NZ_LT906449.1\|WP_066430680.1\|2367716_2368814_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	8.16339e-55
NZ_LT906449.1\|WP_082752995.1\|2370433_2371882_+\|efflux-transporter-outer-membrane-subunit	gnl\|CDD\|273830	TIGR01845, Outer_membrane_protein_OprM, efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family. Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins].	2.64938e-70
NZ_LT906449.1\|WP_066430678.1\|2368878_2369424_+\|NAD(P)H-dependent-oxidoreductase	gnl\|CDD\|376808	pfam02525, Flavodoxin_2, Flavodoxin-like fold. This family consists of a domain with a flavodoxin-like fold. The family includes bacterial and eukaryotic NAD(P)H dehydrogenase (quinone) EC:1.6.99.2. These enzymes catalyze the NAD(P)H-dependent two-electron reductions of quinones and protect cells against damage by free radicals and reactive oxygen species. This enzyme uses a FAD co-factor. The equation for this reaction is:- NAD(P)H + acceptor <=> NAD(P)(+) + reduced acceptor. This enzyme is also involved in the bioactivation of prodrugs used in chemotherapy. The family also includes acyl carrier protein phosphodiesterase EC:3.1.4.14. This enzyme converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine residue from ACP. This family is related to pfam03358 and pfam00258.	1.43512e-44
NZ_LT906449.1\|WP_066430689.1\|2359310_2361107_-\|long-chain-fatty-acid--CoA-ligase	gnl\|CDD\|223953	COG1022, FAA1, Long-chain acyl-CoA synthetases (AMP-forming) [Lipid metabolism].	0
NZ_LT906449.1\|WP_066430683.1\|2364729_2365107_+\|RidA-family-protein	gnl\|CDD\|129116	TIGR00004, RutC_family_protein, reactive intermediate/imine deaminase. This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other].	5.69119e-59
NZ_LT906449.1\|WP_066430666.1\|2381209_2382133_-\|tyrosine-recombinase-XerD	gnl\|CDD\|274043	TIGR02225, Tyrosine_recombinase_XerD, tyrosine recombinase XerD. The phage integrase family describes a number of recombinases with tyrosine active sites that transiently bind covalently to DNA. Many are associated with mobile DNA elements, including phage, transposons, and phase variation loci. This model represents XerD, one of two closely related chromosomal proteins along with XerC (TIGR02224). XerC and XerD are site-specific recombinases which help resolve chromosome dimers to monomers for cell division after DNA replication. In species with a large chromosome and with homologs of XerD on other replicons, the chomosomal copy was preferred for building this model. This model does not detect all XerD, as some apparent XerD examples score below the trusted and noise cutoff scores. XerC and XerD interact with cell division protein FtsK. [DNA metabolism, DNA replication, recombination, and repair].	1.92954e-123
NZ_LT906449.1\|WP_066430668.1\|2380779_2381151_+\|PUR-family-DNA/RNA-binding-protein	gnl\|CDD\|378691	pfam11680, DUF3276, Protein of unknown function (DUF3276). This bacterial family of proteins has no known function.	1.7209e-51
NZ_LT906449.1\|WP_066430687.1\|2361944_2362643_-\|PAS-domain-containing-protein	gnl\|CDD\|369881	pfam08447, PAS_3, PAS fold. The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.	4.91517e-11
NZ_LT906449.1\|WP_066430661.1\|2383272_2383812_-\|DUF1599-domain-containing-protein	gnl\|CDD\|377892	pfam07659, DUF1599, Domain of Unknown Function (DUF1599).	8.17001e-31
NZ_LT906449.1\|WP_082752994.1\|2376417_2377812_+\|hypothetical-protein	gnl\|CDD\|224688	COG1774, COG1774, Uncharacterized homolog of PSP1 [Function unknown].	1.33137e-50
NZ_LT906449.1\|WP_066430664.1\|2382132_2383227_-\|DoxX-family-protein	gnl\|CDD\|225168	COG2259, COG2259, Predicted membrane protein [Function unknown].	2.8939e-06
NZ_LT906449.1\|WP_066431966.1\|2372931_2376087_+\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0

>NZ_LT906449.1|WP_066430678.1|2368878_2369424_+|NAD(P)H-dependent-oxidoreductase
MSKTLVIVIHPDIEHSMVNKRWIAALEEQPEKYTVHQLYKTYPDSRIDVGHEQQLVEAHQRIIFQFPLYWFSCPPLLKQWLDEVLTYGWAYGSKSGYKVGGKKIALAISAGIDDYEYAHGQKYKYTLEELTRPFEITFEYVHANYQPLFAYYGIERNPSEEWVEKSVPLYLAYLEKFGADE
>NZ_LT906449.1|WP_066430680.1|2367716_2368814_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MNKTLLTLAAAALAASCNNAPQQNAMGAPSYPVITVGTSNAVSDLQYPVNIEGTVNSAVQAKVSGYITKVLVDEGQRVVQGQPLFQLETQTLNQSAQSAKAQVDAARVEVNKLKPLVEKNIVSAVQLATAQANLARAQAAYNEVAANIGYGVVKAPVSGVVGAINYREGALVTANNTVLTTVSDVKDVYAYFSMSEKDYLQFLERAPGKSPAEKLKNMPPAKLVLADGQTYAHSGKIAAITGQIDKTTGSMQFRVTFPNPEGLLTNGNSGTVLIPQQFNDVVVIPEVATFEQQGKVFAYKVEHDTIKQVIITLKNRANNFAVVEEGINKGDVILVQGLNAVRTGMVIKPQQVDMDSLVKAIQPIF
>NZ_LT906449.1|WP_143325018.1|2367173_2367578_+|hypothetical-protein
MKYILLSMTLLALSCKSAQPQTKAEPQPQQEVITFKEMDITAQKKEAPERTRNLIIYYKDDADLQPLLNVAKKEKLELIYQYKNFKAIAVKVPDDRDLEGVKSYLQTLAGVLSVNYDEVNQIQGAGTSEGSFQQ
>NZ_LT906449.1|WP_066431968.1|2366481_2367129_+|hypothetical-protein
MNRIIILFMMLLGGQFLMQAQPFEIQRRQIPVVVPLEKAPEVNKPSNLMKLPVAPKNENNPFMKLPEKQIDFTGKSNLVHRKIDFQPNYGVLNDHKQEEYDAPKGDQFFGDFTNNGKYVNVYCRDFQAIDGDRVSIFVNGVEEVRDIMLVGEFRGFQIALKPGFNKIEFLALNQGESGPNTAEFQVLDDQGNVIAKNQWNLATGSKAHFVIIKDK
>NZ_LT906449.1|WP_066430682.1|2365197_2366382_-|aminopeptidase
MKRIALFIALSVVSYVSAQDNLINSLSGNQTDNAGFKFTKIIDLSHTEVKDQGSSGTCWSYAGASFLESEMIRMGKKTVDLAEIFTARNSYIEKAKQYVRMHGYLDYGQGGELHDVINMYAKYGALPQSVYTGLNYGTNRNDFSESHAVFKGFLEGLMKHDSKKPLTPSWLPAFTATVDAYLGAVPETFTFEGKKYTPKSFAKEVVGINPADYVEMVSYEDQPKYQNVFMAVSDNWSFDWAYNVAMTDLTKVIDNALKKGFTVGWSSDVSERYFSWKNGVAFVPEQDIATLSMADQLNLFLAPPKAERTITPEMRQKAFDNYETQDDHGMHIVGLAKDQTGREYYIVKNSWGAKNDYQGFIYVSKAYVQYKTTAIMVHKDGVPKDILKNWKKQQ
>NZ_LT906449.1|WP_066430683.1|2364729_2365107_+|RidA-family-protein
MNRVIFTEKAPAPIGPYNQAILAGNTLYVSGQIPVDPTTGEVVWGIEAATVQVMENLRAVLAEAGATFKDVVKTTIFLNDMGQFAQVNEVYGRYFEEETAPARETVQVAKLPKGVEVEISCIAVI
>NZ_LT906449.1|WP_095114462.1|2363018_2364716_+|M23-family-metallopeptidase
MMKKSLWLMAFCGFLAVSEVDAQRFAPSYPLDVPPLLAGNFAELRPNHFHGGLDFKTQGKEGQYVRAVDDGYISRIKVSPFGYGKTMYVTHPSGYITTYSHLQQYAPEIEAYVKQQQYAKKTYEIDIFPSKKEFVVKRGDWIALSGNTGGSQGPHLHFEVHDANNNGLNPFLFGYQDMEDTIAPEVLQVLAYPLGGNSQVEGSELPRVLPRTKQPDGSYRTAKISASGTLGFGIVAFDRMNGSYNRNGIYKVTLKLNGEPQLQTVFDKVNYDDTRYINELLDYQRLVEHKGYVQRLFKTKGNKLESIYPLLKPNKGYLPIEEGASYEVTIVVEDFKGNATTVHIPVEGKPMVVKTFRPRPKTNKQLVADRDNLYEFEEGSVYFPANTFFEDMAIFLESKKDTLRVHDYKTPINKAFTVTIKNQTFTEDEIPKVFIARSSGGRFGAERTTYKDGVFMAKSKYLGNFYLRKDVTPPTLRPLNFKNNGVVKGNTLKVAMSDNLTGIASWSASINGQWVLFEYEPKNHTLTFNFDDIDTTKVDTYQLEMSATDGVGNIQRLSATVIKRD
>NZ_LT906449.1|WP_066430687.1|2361944_2362643_-|PAS-domain-containing-protein
MIKDYRDIELTVQRPAPIDREVVWDKSKVIISETDIYGRITNVNDIFCSVCGYSADELIGQPHSIIRHPDMPKITFKLLWDNLKLGNNFAGVVKNLAKSGEYYWVITDFEMRRDASGNITHYIARRKSVPKKVIDNYVTPLYETLLKLEKIGGMELSARFFKNYLAKQGKDYMDFIIDVMNKNREDAVFEEIPMATFSSNKEPELVTDDIVTVGVGGSMDEKRKNFFGKLFQ
>NZ_LT906449.1|WP_066430688.1|2361226_2361904_-|PAS-domain-containing-protein
MADFQSPVPTIPRPAPIDKEVSWDKTKTLISETDVAGTITNVNDVFCNVSHYSSAELIGQPHNLIRHPDMPKLIFKLLWDNLKQGNNFVGVIKNLAKTGEYYWVVTDFEMRRDASGNITHYIGRRKSVPEKAINDYLAPFYESLLKLEKIGGVDLSSRFFKNYLAKQGKDYVDFVIGVMSETQSSFTAENVTAIDSNNVSVPDDIYNVDESMDEKRKNFFGRLFN
>NZ_LT906449.1|WP_066430689.1|2359310_2361107_-|long-chain-fatty-acid--CoA-ligase
MNLISYHYINVFQENTQKYSTKNALMGKEGEVWCGTTWQQLGEITRRLSKALLSLEVGVQESVGIFSQNTPQWTMADLATLQIRARVVPIYTTNIPEQALYVLNHAEVKVLFVGDKTQYEKAIEVADNCPSLIKIITFKDDFQLENDGGRSMHWADFLALGEGTAQEEALSHRISERSLDDLFTIIYTSGTTGDPKGVMLTYANLAHQMVAHNKRLSVSEADSSLSFLPLSHVYERAWTFYCLFKGVTVYYLEDTNQVREALSEVKPTLMCAVPRFYEKIFATVHDRANASSFAKRSLFRLAVRTGRQMLKAKEEGRKPGLLLQKAYNLFDKLVYSKFKTLLGGRIRFMPCGGANLEPSIGRFFQSIGINVKLGYGMTETTATVSCWGDDTFNLQSVGEVMPDIEVKIGEDNEILVKGGMVMKGYYKNPEETAKAFTADGFLRTGDAGSVDAHNNLFITERIKELMKTSNGKYIAPQLIENKVGKYNLIEQIAIIADGKKFVSALIVPNFEMLTQALKELNIKCKNTAEMIRHSAVIEYIAKQLQRFQSDLSDYEQIKKFTLLPAAFSIERNEITPTLKLRRKVIYANYSNEIEAMYH
>NZ_LT906449.1|WP_066430677.1|2369723_2370284_+|hypothetical-protein
MYVKQKIVLLIAFIGGVLLTGGLQAQITVYGTLTDHNKHPLVGVRVDVEGDSIRTHTDAEGKYSLTVRRWQLVHYWIQPSRCVPITDSGTRQRIDLAEPKIVSESELEGGRCRVVYVLDGKKADARAFGKLEEEGRLHQHLVLQGAMLSALTSGQYGDARTVVLGFTEKGWRQYQRDKKRKKNVLR
>NZ_LT906449.1|WP_082752995.1|2370433_2371882_+|efflux-transporter-outer-membrane-subunit
MKIMIYRTIAVMGVTIALVACAGRKQYERPDAYSDKLFRTETVDTANTSAGAIEWRELFTDSQLQGLISRALDRNLDVKVALENVRASHAYLKQSRMAFAPTLSASASYTRSTPSVNASGGMGERTYNNLFDLSGSASWELDVWGKLTAQNRAQYASFLASAEAYKAAQSEVVATLATAYYQLLMYDAQREILQHTIDLRQKSLETTKELKKAGSTTEVATQQTEALVLNAQSQLISIENSVWALENSICVLLGEEPHPIERGKLAEQKFPAQLHTGYAMTTLYNRPDIRRAELQLINAFELTNVACAGFYPSLTLTARGGVSSTELDTWFSAKSLFANFVAGLAQPILSARQVRTKYEVQRSAQEQALLTFKKALLTAGKEVSDALHNFAAQDEFIRLKTQEMEAYNKATDYSKQLFNSGMVNYLEVITAEVNRLNAELAVANAQFTKLQQGVVLYKALGGASQVNIDPATLSRGRKENKK
>NZ_LT906449.1|WP_066431966.1|2372931_2376087_+|efflux-RND-transporter-permease-subunit
MIKNFINRPVLSTVISILIVILGVLGIISLPISQYPDIAPVTVQVSANYGGANAETVLKSVVVPLEEQINGVENMDYISSSASNSGAANISVFFKQGTDGDVAAVNVQNAVSRANALLPAEVKQAGVTVRKQNSGNLMFLSFYSENPKLDDVFLQNYLNINVIPALKRISGVGDASVFGGKTYSMRVWLDPQKLQAYKLSPTEVTAAISSQSLEAAAGTLGQNSGQSYEYVIKYKGKYNKVEEYENIVLKALDGGKVLRLKDVATIQLDALSYSGFSESGGKADVAMGISQTPGSNAHEIIQNIETYLKEAEKSFPEGISYSINYNANTFLDAAISKVVSTLLEAFLLVFLAVYLFLQDFRSTLIPAIAVPVSIVGTFFFLNLFGYSINMLTLFALVLAIGIVVDDAIVVVEAVHAKMEHGAGDAKESTVEAMNEIAGAIISITLVMAAVFIPVTFIGGTTGVFYKQFGITLMVAIAISAINALTLSPVLCSLFLKPHGDKAYEEKGWLGKFFHKFNIAFAEGTRRYGKAFTFLLRHKWLTLVMFAVAVGSLLFMNKQLKSGFVPSEDQGFVMMNVEMIPGASMERVANVMRQLEKKVSNIPGVDRVTFVTGRGMLSGEGSNNGMGFFRLKPFEERAKAEGQDIQTIIQRAFVATAGIKDAKIIFFQPPSVPGFGIGSGASFVLLDKSGGEISQVSKDADAFMAALMQRPEIQYVQTSFNTNYPQYQMDINVERAMQSGVSVSNILGTLQNFIGGYYASDFTLYGKQFRVMVQALPDDRKNVESLSSMYVKTATGEMAPISQFVSLKRVFGPQSLSRYNLFTSVAMTASNNASYSTGDAIAAVEEVAAKTLNANYSIDYTGLTREEQNAGSQTVIIFMLSLVFTYFILAAQYESYIVPLSVLLSLPFGIFGAYLGQWLFGLENNIYFQISLIMLMGLLAKNAILIVEFALQRRRTGDSLSKSAIDAAMARLRPILMTSFAFIVGLLPLVFASGVGAAGNRSVATGAAAGQLIGTFFGLVVIPVLFVVFQHLQEKITGKSPKKKVVAWIEKE
>NZ_LT906449.1|WP_082752994.1|2376417_2377812_+|hypothetical-protein
MSCNTCTKGNTNDYRTTDCGDLGGPSSFGSVKLSVFDWLANTSLAGGLDFFDCVEVRFKNSRKEYFRNVDKLPLQAGDVVATEANSGHDVGVVTLTGELVRMQMKKRSIDWNNEDLPRVYRKANQKDIDVWQESRKREISVQKRSRELAIALGLEMKISDVEFQGDGSKATFYYTAEGRVDFRQLIKDMARAFGIRIEMRQIGFRQEAARLGGIGSCGRELCCATWLTDFRSVSTSAARYQQLSLNPQKLAGQCGKLKCCLNFELDTYLDALKDFPKTETKLHTQRGLATCQKIDIFKRLMWYTYDESPMTWYKLSVDSVKEIIELNKEGQQIEELEEYTIINDLSSKRSSSSMGLEMKPVEEDSITRFDTPRRRKKKNNQAKKAQNRPDRASQSPEGKVSQKAENVQGQGKKQGQNPNAQKQRRGQGQQQAATEGQSQKRKPNNNKNQKRPNNNSEISKDEKN
>NZ_LT906449.1|WP_066430675.1|2377798_2378287_+|gliding-motility-lipoprotein-GldH
MRRISLLLLLIVLVGCNKQLEYAQYVSLPNGWVEHQSIPFYLDENDTLTPKNLFIMLRNDEQYEFSNIFLITKMEVPHSNKVIIDTLEYEMANAEGQWLGDGFSAVKESKLWYKENFRFPAKGKYVVKIEQAMRKIGTNQGIEVLKGITEVGLRVENPQLNK
>NZ_LT906449.1|WP_066430673.1|2378295_2380602_+|transglycosylase-domain-containing-protein
MKKTTENEETDTSKKRFLKWFWGVFAAGVLLVILLFLSASLGLLGEMPDFKHLENPDTNLATEIVSADGKSLGKFYLDENRTPIKFKDLPKPLVDALIATEDERFYQHSGIDVRGTMRALFFLGTKGGASTISQQLAKQLFHKTKTRGLQRYTQKIKEWVIATRLERQYTKEEILAMYFNIYDFNNNADGIRSAARIYFGKEPKDLKIEEGAMLVGMFKNSALYNPLKNKEGVTNRRNVVLSQMAKNNYITQEEKDSLQALPLKIKYTPESHNDGIATYFREYLRSYMKAWIEANPKPDGSKHNLYLDGLKVYTTIDSKMQAYAEEAVKAHMKQLQKAFDAENNPKKNKTFPFVRVSNDEYKSLMEKAMKNSNRWIHLKYLGYSEDEIRATFDKKVEMRVFSWKGEKDTIMTPRDSILYYKAYLRAGVMSMETNTGHIKAWVGGINYKHFQYDQVIQGARQTGSTFKPFVYATAIDQLHYSPCLELPDIQTCVEAGKYGNPQPWCPRNSTGNFTGRMMTLKYALANSVNSITVNLMDKVGPMPVINLVKKLGISTKIPEVPSIALGTSEATVFEMTAAYGTFANEGVYVKPVLITRIEDKNGTVLFENTPETHDVVSAEVSRAVINLMEGVTRYGSGARLRTKGAETYNVIYKNVMTGYPYSFTNAIAGKTGTTQNNSDGWFIAMVPNLVTGVWVGGEDRAVHFRTTAYGQGATMALPIWGYYMKKCYADRDLSVSKEAFPPPQNKQIQIDCSKEKESEGEESPQIDF
>NZ_LT906449.1|WP_066430668.1|2380779_2381151_+|PUR-family-DNA/RNA-binding-protein
MEEREFIDNEEIFSKVLRAGRRTYFFDVRATRANDYYLTITESKKFTHEDGSFHFKKHKIYLYKEDFELFKEFLNEVTAYVFDEKGTEVISDTHQRDFKREPYGAQTREDKSSSFTNLSFEDI
>NZ_LT906449.1|WP_066430666.1|2381209_2382133_-|tyrosine-recombinase-XerD
MTTHLWHTTKEAYQNYLRLQRGMSKNSVISYGLDIEKLIGYLAQYEIDESPDTIGVDTLREFVYEVSKDLNARSQARLISALKSFFRFMMSERGREDFPMDLIDSPKIGVKLPDTLSLQEIDMMLNSIDLSTDEGHRNRAIIETLYGCGLRVSELTSLRLSDLFFNEDFIRVIGKGSKQRLIPIGKFTQQQISNYINNQRKQLKIARGFEDIVFLNRRGKQLTRAMIFTIVREVAKQAGIQKKISPHTFRHSFATHLLENGANLRAIQLMLGHENITTTEVYVHVEKSYLREMLVKYHPRQKMSFTQ
>NZ_LT906449.1|WP_066430664.1|2382132_2383227_-|DoxX-family-protein
MKYVINCIRVVVGIIFIISGLVKLNDPVGFAIKLEEYFSKPVLNMPVFEPFAMAIGILVCITEVTLGVMLLVGYLKKLTLWLLIAMTVYFGFLTFYSAYFNKVTDCGCFGDAIKFTPWQSFTKDMVLLALVLILFWGQKYIKPIAKGMIPLYFTLAGIIVSALVVNYTYKHLPIKDFRPYKIGANIPEGMVVPEGAPLPKYEYHWRFIVNGKEKVVTTNGKYPKVNGEFKDVTTEMIDKGYVPPIHDFYIEDKDRKSYFDDFMKEEKLMMVVSEDIGKADVEAFKAVKVTTDRALKEGYTVIGLTSTLDKADKLVKDYELNFRFYYNDEKTLKTMIRSNPGVIILNKGTIKMKKHYYDLEKLKL
>NZ_LT906449.1|WP_066430661.1|2383272_2383812_-|DUF1599-domain-containing-protein
MNKTIEQYNNVVKECQALFSKKMKDYGSAWRILRLPSLTDQIFIKAQRIRGLQENSVHKIEEDETAEFIGIVNYAVMALIQIDRGIATQPDLDAEEATLLYEKEIAETRTLMENKNHDYGEAWRDMRVSSLTDLILQKILRVKQIEDNEGKTLVSEGIRANYQDMLNYAVFALIHLGLA

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Crispr_ID: NZ_LT906449_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LT906449_5

2506562-2506665

Orphan

Consensus_repeat	Method
TAGCAGTACACAACTAATTGGCTGTCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LT906449_5

>merge|NZ_LT906449|5|2506562-2506665|CRISPRCasFinder
TAGCAGTACACAACTAATTGGCTGTCGCCCTGCGACCCCTCATACCTCATACCCCGCACCTCACACCTTCAACGCTGTAGCAGTGCACAACTAATTGGCTGTCG

>NZ_LT906449|5|5|2506562-2506665|CRISPRCasFinder
TAGCAGTACACAACTAATTGGCTGTCG	CCCTGCGACCCCTCATACCTCATACCCCGCACCTCACACCTTCAACGCTG
TAGCAGTGCACAACTAATTGGCTGTCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LT906449.1\|WP_066430492.1\|2505346_2506504_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|226957
NZ_LT906449.1\|WP_066430468.1\|2517249_2517555_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066430490.1\|2506676_2507366_-\|SMUG2-DNA-glycosylase-family-protein	unknown	unknown	gnl\|CDD\|379812
NZ_LT906449.1\|WP_066430495.1\|2502504_2503089_-\|5-formyltetrahydrofolate-cyclo-ligase	unknown	unknown	gnl\|CDD\|274270
NZ_LT906449.1\|WP_066430475.1\|2511551_2513642_+\|M13-family-metallopeptidase	unknown	unknown	gnl\|CDD\|341056
NZ_LT906449.1\|WP_095114465.1\|2504040_2505285_-\|DUF1343-domain-containing-protein	unknown	unknown	gnl\|CDD\|377768
NZ_LT906449.1\|WP_066430494.1\|2503107_2503965_-\|glycoside-hydrolase	unknown	unknown	gnl\|CDD\|119384
NZ_LT906449.1\|WP_066430501.1\|2501806_2502544_+\|shikimate-dehydrogenase	unknown	unknown	gnl\|CDD\|223247
NZ_LT906449.1\|WP_066430508.1\|2498096_2498834_-\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|376777
NZ_LT906449.1\|WP_066431953.1\|2515523_2516966_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066430509.1\|2497674_2498016_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066430476.1\|2511323_2511530_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066430470.1\|2517044_2517287_+\|addiction-module-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066430484.1\|2510890_2511322_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066430506.1\|2498931_2500464_-\|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase	unknown	unknown	gnl\|CDD\|234854
NZ_LT906449.1\|WP_066430503.1\|2500555_2501803_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|182528
NZ_LT906449.1\|WP_066430511.1\|2496731_2497577_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LT906449.1\|WP_066430486.1\|2510315_2510894_+\|flavin-reductase-family-protein	unknown	unknown	gnl\|CDD\|224766
NZ_LT906449.1\|WP_066430472.1\|2513717_2515196_-\|NAD(P)/FAD-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|224154
NZ_LT906449.1\|WP_066430467.1\|2517560_2519372_+\|HEAT-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|379311

Protein	Function_ID	Function_description	E-value
NZ_LT906449.1\|WP_066430492.1\|2505346_2506504_+\|ABC-transporter-permease	gnl\|CDD\|226957	COG4591, LolE, ABC-type transport system, involved in lipoprotein release, permease component [Cell envelope biogenesis, outer membrane].	3.23815e-44
NZ_LT906449.1\|WP_066430467.1\|2517560_2519372_+\|HEAT-repeat-domain-containing-protein	gnl\|CDD\|379311	pfam13646, HEAT_2, HEAT repeats. This family includes multiple HEAT repeats.	7.43029e-07
NZ_LT906449.1\|WP_066430490.1\|2506676_2507366_-\|SMUG2-DNA-glycosylase-family-protein	gnl\|CDD\|379812	pfam16265, DUF4918, Domain of unknown function (DUF4918). This family consists of uncharacterized proteins around 230 residues in length and is mainly found in various Listeria species. The function of this family is unknown.	1.84052e-129
NZ_LT906449.1\|WP_066430495.1\|2502504_2503089_-\|5-formyltetrahydrofolate-cyclo-ligase	gnl\|CDD\|274270	TIGR02727, Uncharacterized_protein_YqgN, 5,10-methenyltetrahydrofolate synthetase. This enzyme, 5,10-methenyltetrahydrofolate synthetase, is also called 5-formyltetrahydrofolate cycloligase. Function of bacterial proteins in this family was inferred originally from the known activity of eukaryotic homologs. Recently, activity was shown explicitly for the member from Mycoplasma pneumonia. Members of this family from alpha- and gamma-proteobacteria, designated ygfA, are often found in an operon with 6S structural RNA, and show a similar pattern of high expression during stationary phase. The function may be to deplete folate to slow 1-carbon biosynthetic metabolism. [Central intermediary metabolism, One-carbon metabolism].	8.71285e-43
NZ_LT906449.1\|WP_066430472.1\|2513717_2515196_-\|NAD(P)/FAD-dependent-oxidoreductase	gnl\|CDD\|224154	COG1233, COG1233, Phytoene dehydrogenase and related proteins [Secondary metabolites biosynthesis, transport, and catabolism].	6.77451e-46
NZ_LT906449.1\|WP_095114465.1\|2504040_2505285_-\|DUF1343-domain-containing-protein	gnl\|CDD\|377768	pfam07075, DUF1343, Protein of unknown function (DUF1343). This family consists of several hypothetical bacterial proteins of around 400 residues in length. The function of this family is unknown.	0
NZ_LT906449.1\|WP_066430494.1\|2503107_2503965_-\|glycoside-hydrolase	gnl\|CDD\|119384	cd06524, GH25_YegX-like, YegX is an uncharacterized bacterial protein with a glycosyl hydrolase family 25 (GH25) catalytic domain that is similar in sequence to the CH-type (Chalaropsis-type) lysozymes of the GH25 family of endolysins.	4.28254e-69
NZ_LT906449.1\|WP_066430501.1\|2501806_2502544_+\|shikimate-dehydrogenase	gnl\|CDD\|223247	COG0169, AroE, Shikimate 5-dehydrogenase [Amino acid transport and metabolism].	1.97577e-61
NZ_LT906449.1\|WP_066430508.1\|2498096_2498834_-\|ABC-transporter-permease	gnl\|CDD\|376777	pfam02405, MlaE, Permease MlaE. MlaE is a permease which in E. coli is a component of the Mla pathway, an ABC transport system that functions to maintain the asymmetry of the outer membrane. In NMB1965 it is involved in L-glutamate import into the cell. In Arabidopsis thaliana TGD1 it is involved in lipid transfer within the cell.	3.77301e-61
NZ_LT906449.1\|WP_066430475.1\|2511551_2513642_+\|M13-family-metallopeptidase	gnl\|CDD\|341056	cd08662, M13, Peptidase family M13 includes neprilysin and endothelin-converting enzyme I. The M13 family of metallopeptidases includes neprilysin (neutral endopeptidase, NEP, enkephalinase, CD10, CALLA, EC 3.4.24.11), endothelin-converting enzyme I (ECE-1, EC 3.4.24.71), erythrocyte surface antigen KELL (ECE-3), phosphate-regulating gene on the X chromosome (PHEX), soluble secreted endopeptidase (SEP), and damage-induced neuronal endopeptidase (DINE)/X-converting enzyme (XCE). Proteins in this family fulfill a broad range of physiological roles due to the greater variation in the active site's S2' subsite allowing substrate specificity. NEP is expressed in a variety of tissues including kidney and brain, and is involved in many physiological and pathological processes, including blood pressure and inflammatory response. It degrades a wide array of substrates such as substance P, enkephalins, cholecystokinin, neurotensin and somatostatin. It is an important enzyme in the regulation of amyloid-beta (Abeta) protein that forms amyloid plaques that are associated with Alzeimers disease (AD). ECE-1 catalyzes the final rate-limiting step in the biosynthesis of endothelins via post-translational conversion of the biologically inactive big endothelins. Like NEP, it also hydrolyzes bradykinin, substance P, neurotensin, and Abeta. Endothelin-1 overproduction has been implicated in various diseases including stroke, asthma, hypertension, and cardiac and renal failure. Kell is a homolog of NEP and constitutes a major antigen on human erythrocytes; it preferentially cleaves big endothelin-3 to produce bioactive endothelin-3, but is also known to cleave substance P and neurokinin A. PHEX forms a complex interaction with fibroblast growth factor 23 (FGF23) and matrix extracellular phosphoglycoprotein, causing bone mineralization. A loss-of-function mutation in PHEX disrupts this interaction leading to hypophosphatemic rickets; X-linked hypophosphatemic (XLH) rickets is the most common form of metabolic rickets. ECEL1 is a brain metalloprotease which plays a critical role in the nervous regulation of the respiratory system, while DINE is abundantly expressed in the hypothalamus and its expression responds to nerve injury. A majority of these M13 proteases are prime therapeutic targets for selective inhibition.	0
NZ_LT906449.1\|WP_066430506.1\|2498931_2500464_-\|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase	gnl\|CDD\|234854	PRK00881, purH, bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; Provisional.	0
NZ_LT906449.1\|WP_066430503.1\|2500555_2501803_+\|ABC-transporter-permease	gnl\|CDD\|182528	PRK10535, PRK10535, macrolide ABC transporter ATP-binding protein/permease MacB.	4.00348e-38
NZ_LT906449.1\|WP_066430486.1\|2510315_2510894_+\|flavin-reductase-family-protein	gnl\|CDD\|224766	COG1853, COG1853, Conserved protein/domain typically associated with flavoprotein oxygenases, DIM6/NTAB family [General function prediction only].	1.85737e-16

>NZ_LT906449.1|WP_066430492.1|2505346_2506504_+|ABC-transporter-permease
MAITAIAVGVVVMLIAIATGVGLQQKIREKLVVFHGHIQIFNYDNNASEVSIKPISLEQPFYPQFKDVPAVKHIQAVATKGGILRTPTTYEAILAKGVGKDYDWHLLQDFITEGRIPDFTTDEISNEVLISTYLANRLGLKLGDRCQAIFLKDESAQVPSQRSFVIVGLYNSGFQEFDASYLFVDLRQIQHINKWKADEIGTFELFIDDFNHITEVGNEVYARTNSHLDSQTILQKYPFIFEWLSMFDFNIYLIIGIMLIVGVFNMITALLVLILEKTPMVGTLKSLGAADRSIRNIFLYNATYIITLGLLWGNGIGFALLWLQQQYGIVKLDPATYYVSQVPIAIPWVGALLVNVGVLVVCLLMLLLPSFVIAKISPTKAMKFD
>NZ_LT906449.1|WP_095114465.1|2504040_2505285_-|DUF1343-domain-containing-protein
MKYSKFKSICEFRGAKVTLFLLIALLSCKNNGQEHRSSMTQKTESQQKEIIPAANRMYLYIKDLRDKNVAVVTNQTGVVERKDGSLVHLVDTLLAKKVKLTKVFAPEHGFRGDADAGEVVKDGKDARTGLPIISLYGKNKKPTAEQLKGIDLVLFDLQDVGARFYTYISTLHYVMEACAEQHIPLIVLDRPNPNGHYIDGAVLEPSCQSFIGMHPVPVVYGMTIGEYAQMINGEGWLAQRAKSDLKVIPLAHYTHQKAYHLPVKPSPNLPNDVAINLYPSLCFFEGTEVSMGRGTDKQFQIYGSPYLEKTDFSFTPQPNAGDKNPKFNGKLCYGEDLSSSVRLSALNLSWLKKAYEQSKGVKMAFFTASFNKIAGTPALKQQLIDGKSEQEIRASWQKDIEKFKEVRKKYLLYP
>NZ_LT906449.1|WP_066430494.1|2503107_2503965_-|glycoside-hydrolase
MRRKSSKQRRSAHKGGSHWKSFLWGFFLCIFVVGVGGALYIRTYYPAMYQKILNKISSRKINTTYESQRIERIVSLHSDKILGIDLSHYQDKGEIIWDSLHIKVNEHKYPLQFAVFRATMGNDGSDKNFTYFWKEAKQHTLIRGAYHYYRPDEDPELQARSYLKNAQLEKGDLPPILDVEKLPKKKSTEAFLADIQKWLDIVEQKYKRKPIIYTYISFYEDYLSQKFKKYPFWVANYNNVEVPTTIFKWQMWQFTENGISPGAKVKIDLNIYNGSYEEMEAILIK
>NZ_LT906449.1|WP_066430495.1|2502504_2503089_-|5-formyltetrahydrofolate-cyclo-ligase
MTKKELRKHYMQLRLALTQEQRDNLSMQIANRLLTLPIWDKSTYHIFLTVERLGEINTEYLLDILYGKDKNVVVPKMHTKEKRLSSILLTEQTLLRLNSWGIAEPDGGIEVPPNAIEVVFVPLLAYDRQGNRVGYGGGYYDRFLSECKDETLKVGLSFFPPEDDMSAVMSPTDITLDYVVFPQGCLHIPQAASA
>NZ_LT906449.1|WP_066430501.1|2501806_2502544_+|shikimate-dehydrogenase
MKNLYALVGRNIAYSFSRAYFAEKFQREGLADCQYVNFDIQRIEELPALIAAHPHLRGFNVTIPYKRDILPLLSSIDPVAEAIGAVNTVKITPEGLVGYNTDAYGFAESLKPLLKPQHTHALILGTGGASQAVAYVLKSLGIAYRFVSRTPHLGQFAYTDLNGSLLKKYTLIINCTPLGTFPNTEACPPLPYQHLTEAHLLYDLIYNPEKTTFLQKGAAKGAHICNGQQMLELQAEAAWGIWRQP
>NZ_LT906449.1|WP_066430503.1|2500555_2501803_+|ABC-transporter-permease
MFIYLQLLKESFNFAIKSLRDNKLRTVLSLLGVTVGIFSIISVLAAVDSLNKMIQDQLSGLDKNMITLCKFSFAPTDVPQWKRFQFPQVTYQEFEQLQREMTNTEVVVYQIFGVNSSLKYGGKTIENVSVEAVSAGVEMLNDIKIAKGRFFTDTEANTGSAVIVLGHNIAQQLFGSEEPLDKEIRAFGRKMRVVGVLKRYGDMGDDTDEKAYTDANFVRTFIPTGPNGYPAAVTFKPKKGTDAIAYEETLRARVRTMRGLKPEQIDNFFLNKVSSFTDMIDETISMMNLIGWIIGGFSILVGGFGIANIMFVSVKERTNLIGVQKSLGAKNQFILFQFLFEAVLLAIIGGLAGLLLVWLLTFALSGISETFHFILSFKNIAIGLGISFVVGLLSGIIPASSAARLNPVEAIRTGQ
>NZ_LT906449.1|WP_066430506.1|2498931_2500464_-|bifunctional-phosphoribosylaminoimidazolecarboxamide-formyltransferase/IMP-cyclohydrolase
MSTTKQAKSALISVFDKTGLEPIVHRMKTLGITIYSTGGTESFLKNLGVEVIPVESVTDYPSILGGRVKTLHPKIFGGILNRQDNDNDVEEMKQYTIPQIDIVIVDLYPFEKTVHSGASEAEIIEKIDIGGISLIRAAAKNFADVLCISSVNQYDALLNILVEQHGATTLEERRHFAAEAFAVSSHYDTAIFNYFNQKEQIPCLKISESEGQVLRYGENPHQKGEYYGNLNALFKKMHGKELSYNNLLDIDAAVNLMAEFSHDDPTFAILKHNNACGVATRKTIAEAYQATLAGDPVSAFGGILISNTKIDSATAELIHPLFFEVIIAPSYSDEALTILEQKKNRIILVKRSADLPKMSLRSCLNGYLVQEKDLKTDKEEDITYVTSAKPTVKAMEDLLFASKICKHSKSNTIVLAKDKQLIASGVGQTSRVDALKQAIEKAKEFKADLRGAVMASDAFFPFPDCVEIAYNEGIKDVIQPGGSVKDQESIDFCNHHDVAMVFTGIRHFKH
>NZ_LT906449.1|WP_066430508.1|2498096_2498834_-|ABC-transporter-permease
MKHIAAVGGYFIMLYDIFRKRTRWSITKDLILREIDDLIFGSIGIVAFISFFVGGVVAVQTALNIDNPFIPKYLIGFATRQSIVLEFAPTFTAIILAGKIGSFVTSSIGTMRVTEQIDALDIMGVNSVNYLVFPKIVALMLLPFLIALGMYLGVLGGWAASVMSGYTTSSEFVQGVQYDFKAYSLVYAFTKTIVFAFFLATIPSYHGYYMKGGALDVGKASTVSFVWTSIVIILSNSVITQLFYT
>NZ_LT906449.1|WP_066430509.1|2497674_2498016_+|hypothetical-protein
MKDYSTEIAKCSLWLMGISVVGVLLCVIFDAANSFMRLLIGVEAVLLLLLLFGFPLYYLYHLVLRFIFKKERKGFRLLCYAAICYLVSIAFYVVLFWIIYNYSYNDAIRRHHP
>NZ_LT906449.1|WP_066430511.1|2496731_2497577_+|hypothetical-protein
MKRILLLLVVVSISFLTSFAQNKLSNPEMYTDHNKGKFFLFWGGNRDYYTNSDIRFKGADYDFTIYDVEAVDKPKGWHIDYINPLRMTIPQTNVHLGYFVSDHYYISAGVDHMKYVMKQDQMVRMNGYINNSGTAHDGVYNNAEKVLTEDFLTFEHTDGLNYVVLEGARVDDISRLFGIRNTDAFQVQLTEGLGFGMVYPRSNTKLLKKERYDEFHIAGVGVNAKAGLHLTFLKHLLIVGELKGGYINMYDVRTTYSIADKAQHDFFFFETVLGIGWTWRF
>NZ_LT906449.1|WP_066430490.1|2506676_2507366_-|SMUG2-DNA-glycosylase-family-protein
MKATFGERVIDFNRHLRYDEALPEGFAVLNPYVDNPETMQVMRAFYERFYSDNAPRRFIIGINPSRNGAGVTGVPFTDTKRLESACGIVMHSAHTHEVSSVFLYEMIAAYGGVAAFYKDFYINSPFPLAIVRRGSDGNWLNANYYDDNALFASVRPYMIETLRKHITLGLDTAKVYILGKKNADFIAKLNKEASLFGQMVVLEHPRYIQQYKSKEKELYIDKYITALKV
>NZ_LT906449.1|WP_066430486.1|2510315_2510894_+|flavin-reductase-family-protein
MQTFLPNMFYYGFPVVLLSTVDSEGNQDVTPVSCTWTLGNNAVIGLVRLNQAYENVKQVPEAVFNLPTATMWQQVEGIARYTGKNPVPEQKAAKYTYTDNKFAIGGFTTLPSEKVKPLRIAECPIQAEAEVLRINERDSYAIVELRFLTVHVADDLVMEGNKINPERWHPLIYNFKNYQEVGALLGKNFSIK
>NZ_LT906449.1|WP_066430484.1|2510890_2511322_+|hypothetical-protein
MSYPRYTYKAGKYLTSFEFVSVGKRGSIKKVVGYAPMSNPRIYNLGFGDWNEETQEVDDSNGDMVKVLSTVVATMYEFTEVYPEIAVYATGSNETRTRLYRINIAKHLAILQQDFYVYGQNSDGSFETFEVNKEYIGFMVKRK
>NZ_LT906449.1|WP_066430476.1|2511323_2511530_+|hypothetical-protein
MTVGKAAIEIEGADIQYSEFLDSLKEKLGRSNLFPKKLALAEEQLRNAVLPWETKEKPKGVGKKRVKE
>NZ_LT906449.1|WP_066430475.1|2511551_2513642_+|M13-family-metallopeptidase
MKKINRKVMVLSAACLLAACGTKKPVSTTTPTITETVSTTTEMTTPEKGLDLSAMDPSVRPQDDFYNYVNGGWMKTAKIPADKPRWGAFDMLREETDKHCLLILDEILKENYPTGTEGQKIKDLYASYIDWDKRNAEGLKPIAARLAAIEKIKTLSDLQAYLEKTTPQGGNPICGWGVYADMKNSSQNAVYLGAFDLGMGRDYYQKESKENAEALAKYQEFVADIFKVLKDPKATQKAKQIVDFERSVAKLMLTNEEDRDPNLSYNPQTMAELKKLVKSLNIPAYLEKVGVKTDKVVVGEIRLYKEYDKFINKKNLPLLRDYLRYTLVANNTGSLNKELDELSFEFYNKYLRGQQEQRAMNKRALDLINGILGEAFGKLYVEKYFPAQAKEEMVELIGYLKKSFAQHINDLTWMSAETKEKALAKLDKFKVKVGYPDKWKDYSKLTILPASETVYYDNLQQVIKWAYQRKLDKVGKPVDKSEWEMSPQTVNAYYNPLNNEIVFPAAILQRPFFSFEADPAVNFGGIGAVIGHEMTHGFDDSGAEFDAEGNLKNWWTAADKENFKKVTKALAEQYDKYEPVKGVFVNGTFTSGENIADLGGVNIAFDALQMYLKDKGAVDKISDLTQDQRFFISWGTVWRTLSTEKYLINQTKTDPHTPGYYRAFGPVVNVDAWYKAFDVKEGDKLYKAPEQRVKIW
>NZ_LT906449.1|WP_066430472.1|2513717_2515196_-|NAD(P)/FAD-dependent-oxidoreductase
MNRYDTIVIGSGLSGLYTALLLAKRGKKVAIVEKNNQYGGNLQTFSRNKVLFDTGVHYLGSLAEGEVLYNYFKEVGIMEDLTLERLNTDAYDRICFGDTPAIEYPHAQGYENFIRQLLVYFPEEETALRRYAEEMQAVCDRFPLYRNRRETERYDIDLLSRKLLPFLDAITTNERLKAVLLGSNFLYAGVSEQTPLYVHALSVNSYIQSAWRLKKGGSQITNLLIKQLRKLRVELFKNTEITGFQLDTQHSITGAISADNAVFEADSFVSAIDIKALLQLTGKTPFKPSFYNRVMRLQPVASVFSLHLVLKPKSFPYLPYNVYWFSDEASVYRTYPEAGAAPHTYMLSMSPPREEDGYSDNATILTYMSPEEVAPWADTFNTKNAPNDRTEEYEAFKAAKAEALLAVVCEKYPTLREAIAYSYTSTPLTYRDYIGNPTGAIYGYQKNADRIMESVIMPQTHIKNLYLTGQSIGMHGLVGVTIKAVVCAEVIP
>NZ_LT906449.1|WP_066431953.1|2515523_2516966_+|hypothetical-protein
MEITEQKIEELAPNAEAAKKGRELEKKKKFVNLKISAEGDLIWGECAGSGKNPYYCSVDFKDAYNPISRCNCPSRQFPCKHGLGLLYCYAADASQFTVGEVPEDILSKREKIEKKQEKKAQEKESIKEKAEKPKKVNVAALTKKIDAQLSGIAIAQKLLQDIVHTGLSSIDAKLRKTLSEQVKELGNYYIGGIQTAFNKLLLLLEEVKGEEYTPVVDQLNYIGALLKKATDYLTARKEDPQSPPELNSAIEEQIGTVWKLVELMQNGLYEENAELLQLSFNSLDKAARREFVDEGIWLNLKSGRIFKTLNYRPYKAAKYVKEDNSVFNVLCLKDLYLYPGDQNPRIRWEAEAASERKVGAEDLAKVHQFASANFAETIKSAKNTMKNPLMDKNPVVLLALHKAYRFGEDLVVEDKHGNALTLRDLSDAPVASTIALKAILPADAQGLALTVMLHNDVASGLLSGQPLSLITKEKIVRLLY
>NZ_LT906449.1|WP_066430470.1|2517044_2517287_+|addiction-module-protein
MDTERNTYGEVSTSNEASPCCVAEAAATYEVGIPYAHKLIIDERLKELEKDPTRGIPLEEAARMIEEKYGIRSNFRPAGF
>NZ_LT906449.1|WP_066430468.1|2517249_2517555_+|hypothetical-protein
MVYEVILDPLASDEWIAILSRYNAIREGLGTEAYDEVKVYLFALAEDAFLYQKRYGEVRVSFTKRFHFAIYYVIRETDVYVIAVKHQREDPDAVLWRAKNK
>NZ_LT906449.1|WP_066430467.1|2517560_2519372_+|HEAT-repeat-domain-containing-protein
MKQLYELQQEINRLFIAGSKFAGGDPRLAKHVPVLKKLGEKAPVFAKIASDVEALLQAAAKESAERLLAVSTLLYSVLYTQGKTTEEGTGEAKVTPQEPNVALAQVNTAYSYLQLKPVMQALTESKSGRLEVLKEAQERGLFADSRTFAYLSKGLGDKYGELADYVEQEIIPSLGTGMLPFLVQDFAFEDSTQNVRRLRLLQHFNYEGLKAIEDKVFEENLPNLQAAALTSIVARGGAEVEALIISLTGDKNKTVRGAAYKALAKLGTDTAIDKLYEVYSKNKKKSDTELLAAAIGSVALPRHYKAFLQTLEAHFDAFMAMDKSDQKKVGTALDNFQEELPLLKGKDYAEVYDFIAKLYTTQDFWNFQRREYGYRIVMYIREILGSLDAKKVLAFYEQHLSELPKLNEYFNPLSQYLEKAATVYSKEQLFDSFSKYLNNGLQLEHFYNVFTNGHANYYYDLAQVEVYKERIDPRWAYKFVNYIKNFNKYDYTYLHTMVMLEAIDPKREEVLEMLLFLLPKVPLDSREPYYQMLLKQETPEKYALIYEAIEKTPKNNYYAPSLYKRLIEKGFFTTFPKEYAEKLNTLAESRKEEIFEKIAREIK

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

513397 : 530866

Riemerella_phage(38.46%)

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_066429213.1\|513397_514117_-	ParB N-terminal domain-containing protein	F5A3C9	Riemerella_phage	9.2e-22	34.0
WP_066429212.1\|514094_514784_-	phosphoadenosine phosphosulfate reductase family protein	F5A3D0	Riemerella_phage	1.3e-57	49.5
WP_066429210.1\|515040_515526_-	hypothetical protein	NA	NA	NA	NA
WP_066429208.1\|515681_515882_-	hypothetical protein	NA	NA	NA	NA
WP_066429205.1\|515981_516302_-	DUF2693 domain-containing protein	F5A3D3	Riemerella_phage	7.9e-34	70.7
WP_095114476.1\|516667_517333_-	phage antirepressor KilAC domain-containing protein	F5A3A8	Riemerella_phage	1.4e-40	55.7
WP_066429199.1\|517379_517724_-	hypothetical protein	NA	NA	NA	NA
WP_066429197.1\|518115_518523_-	hypothetical protein	NA	NA	NA	NA
WP_066429196.1\|518570_518756_-	type II toxin-antitoxin system HicA family toxin	NA	NA	NA	NA
WP_066429194.1\|518948_519593_-	antA/AntB antirepressor family protein	F5A3D4	Riemerella_phage	3.7e-30	65.0
WP_066429193.1\|519594_519861_-	hypothetical protein	NA	NA	NA	NA
WP_082752977.1\|519880_520324_-	VRR-NUC domain-containing protein	A0A0D4DBJ8	Acinetobacter_phage	3.2e-09	36.3
WP_066429191.1\|520298_520514_-	hypothetical protein	NA	NA	NA	NA
WP_143324998.1\|520527_520728_-	hypothetical protein	NA	NA	NA	NA
WP_143324999.1\|520750_520942_-	hypothetical protein	NA	NA	NA	NA
WP_143325000.1\|520964_521870_-	hypothetical protein	NA	NA	NA	NA
WP_066429183.1\|521766_522738_-	hypothetical protein	A0A2I7RTS8	Vibrio_phage	3.4e-11	50.0
WP_066429181.1\|522954_525234_-	DNA methylase	A0A218M4Z8	Flavobacterium_phage	9.3e-169	42.3
WP_066429179.1\|525387_526122_-	hypothetical protein	A0A088C3D3	Flavobacterium_sp._phage	2.0e-24	30.6
WP_066429178.1\|526139_526556_-	hypothetical protein	S0A3Z9	Cellulophaga_phage	1.0e-17	40.6
WP_066431811.1\|526588_527344_-	KilA-N domain-containing protein	A0A0H4A783	Pseudoalteromonas_phage	3.1e-12	34.1
WP_066431808.1\|527379_527763_-	hypothetical protein	NA	NA	NA	NA
WP_066429177.1\|527765_528014_-	hypothetical protein	NA	NA	NA	NA
WP_066429176.1\|528016_528268_-	hypothetical protein	NA	NA	NA	NA
WP_066429174.1\|528280_528757_-	DUF3127 domain-containing protein	I6R165	Nonlabens_phage	7.4e-20	46.6
WP_066429172.1\|528769_529423_-	hypothetical protein	NA	NA	NA	NA
WP_066429171.1\|529424_530099_-	MBL fold metallo-hydrolase	NA	NA	NA	NA
WP_082752976.1\|530104_530866_-	phage recombination protein Bet	A8ATK8	Listeria_phage	5.7e-54	45.8

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_LT906449

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection