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_LS483461	Clostridium perfringens strain NCTC2837 chromosome 1	5 crisprs	DEDDh,cas14j,cas2,csa3,cas3,DinG,c2c9_V-U4	0	0	4	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_LS483461_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LS483461_1

277985-278080

Orphan

Consensus_repeat	Method
GCTTTATATTAATTAAGTTTGATTCATATG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LS483461_1

>merge|NZ_LS483461|1|277985-278080|CRISPRCasFinder
GCTTTATATTAATTAAGTTTGATTCATATGCAAATACTAGAGTAAGTATAAATGCAATTAATCTTTGCTTTATATTAATTAAATTTGATTCATATG

>NZ_LS483461|1|1|277985-278080|CRISPRCasFinder
GCTTTATATTAATTAAGTTTGATTCATATG	CAAATACTAGAGTAAGTATAAATGCAATTAATCTTT
GCTTTATATTAATTAAATTTGATTCATATG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LS483461.1\|WP_003472388.1\|275294_275924_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|274656
NZ_LS483461.1\|WP_110003193.1\|277510_277609_+\|heavy-metal-associated-domain-containing-protein	unknown	unknown	gnl\|CDD\|238219
NZ_LS483461.1\|WP_003472341.1\|290275_291499_+\|exonuclease-SbcCD-subunit-D	unknown	unknown	gnl\|CDD\|223497
NZ_LS483461.1\|WP_003457483.1\|265736_266600_-\|5'-nucleotidase,-lipoprotein-e(P4)-family	unknown	unknown	gnl\|CDD\|273674
NZ_LS483461.1\|WP_003458319.1\|287841_288657_-\|mechanosensitive-ion-channel	unknown	unknown	gnl\|CDD\|182386
NZ_LS483461.1\|WP_003457595.1\|265335_265533_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003457507.1\|263923_264781_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|184196
NZ_LS483461.1\|WP_003458357.1\|278316_278898_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003458296.1\|276465_276735_+\|metal-sensing-transcriptional-repressor	unknown	unknown	gnl\|CDD\|197394
NZ_LS483461.1\|WP_003458282.1\|286892_287663_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003458291.1\|279035_281411_-\|PAS-domain-S-box-protein	unknown	unknown	gnl\|CDD\|223715
NZ_LS483461.1\|WP_003458341.1\|289230_289875_-\|biliverdin-producing-heme-oxygenase	unknown	unknown	gnl\|CDD\|350856
NZ_LS483461.1\|WP_003472342.1\|283303_284185_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003452599.1\|262843_263155_+\|energy-coupling-factor-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|179494
NZ_LS483461.1\|WP_111693567.1\|266822_268022_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	unknown	unknown	gnl\|CDD\|366703
NZ_LS483461.1\|WP_096071742.1\|263138_263909_+\|cobalt-ECF-transporter-T-component-CbiQ	unknown	unknown	gnl\|CDD\|274139
NZ_LS483461.1\|WP_003458280.1\|282936_283164_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003472367.1\|284212_286411_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003472002.1\|268707_269364_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003458257.1\|281777_282836_+\|acyltransferase-family-protein	unknown	unknown	gnl\|CDD\|226122

Protein	Function_ID	Function_description	E-value
NZ_LS483461.1\|WP_003472388.1\|275294_275924_+\|hypothetical-protein	gnl\|CDD\|274656	TIGR03570, NeuD_NnaD, sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family. This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.	3.25857e-25
NZ_LS483461.1\|WP_110003193.1\|277510_277609_+\|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.	6.90956e-05
NZ_LS483461.1\|WP_003472341.1\|290275_291499_+\|exonuclease-SbcCD-subunit-D	gnl\|CDD\|223497	COG0420, SbcD, DNA repair exonuclease [DNA replication, recombination, and repair].	5.67576e-60
NZ_LS483461.1\|WP_003457483.1\|265736_266600_-\|5'-nucleotidase,-lipoprotein-e(P4)-family	gnl\|CDD\|273674	TIGR01533, Lipoprotein_E, 5'-nucleotidase, lipoprotein e(P4) family. This model represents a set of bacterial lipoproteins belonging to a larger acid phosphatase family (pfam03767), which in turn belongs to the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases. Members are found on the outer membrane of Gram-negative bacteria and the cytoplasmic membrane of Gram-positive bacteria. Most members have classic lipoprotein signal sequences. A critical role of this 5'-nucleotidase in Haemophilus influenzae is the degradation of external riboside in order to allow transport into the cell. An earlier suggested role in hemin transport is no longer current. This enzyme may also have other physiologically significant roles. [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides].	5.10353e-84
NZ_LS483461.1\|WP_003458319.1\|287841_288657_-\|mechanosensitive-ion-channel	gnl\|CDD\|182386	PRK10334, PRK10334, small-conductance mechanosensitive channel MscS.	3.14587e-61
NZ_LS483461.1\|WP_003457507.1\|263923_264781_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|184196	PRK13636, cbiO, cobalt transporter ATP-binding subunit; Provisional.	0
NZ_LS483461.1\|WP_003458296.1\|276465_276735_+\|metal-sensing-transcriptional-repressor	gnl\|CDD\|197394	cd10159, CsoR-like_DUF156_2, Uncharacterized family 2; belongs to a superfamily containing transcriptional regulators CsoR (copper-sensitive operon repressor), RcnR, and FrmR, and related domains; this family was previously known as part of DUF156. Uncharacterized family 2, belonging to a larger superfamily that contains various transcriptional regulators that respond to different stressors such as Cu(I), Ni(I), sulfite, and formaldehyde, and includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily, including this family, and a conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are also conserved.	8.30868e-38
NZ_LS483461.1\|WP_003458291.1\|279035_281411_-\|PAS-domain-S-box-protein	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	3.70887e-48
NZ_LS483461.1\|WP_003458341.1\|289230_289875_-\|biliverdin-producing-heme-oxygenase	gnl\|CDD\|350856	cd19165, HemeO, heme oxygenase in eukaryotes and some bacteria. This subfamily contains heme oxygenase (HO, EC 1.14.14.18) found in eukaryotes as well as some proteobacteria, including cyanobacteria. Heme oxygenase (HO) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling of iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. In vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1, HO-2 and HO-3. HO-1 is ubiquitously expressed after induction while HO-2 expression is constitutive, mostly limited to certain organs, such as the brain, testes, and the vascular system. HO-3 is non-functional in humans, suggesting that the Hmox3 gene is a pseudogene derived from HO-2 transcripts. In higher plants and cyanobacteria, heme oxygenase is required for the synthesis of light-harvesting pigments, which contain tetrapyrrols derived from biliverdin. Candida albicans expresses a heme oxygenase that is required for the utilization of heme as a nutritional iron source, whereas Saccharomyces cerevisiae responds to iron deprivation by increasing Hmx1p transcription, which is controlled by the major iron-dependent transcription factor, Aft1p, and promotes both the re-utilization of heme iron and the regulation of heme-dependent transcription during periods of iron scarcity. In pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme. In Leptospira interrogans, a pathogenic spirochete that causes leptospirosis, HO is required for iron utilization when hemoglobin is the sole iron source, thus making HO an interesting target for novel antimicrobial agents. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology.	2.93206e-64
NZ_LS483461.1\|WP_003452599.1\|262843_263155_+\|energy-coupling-factor-ABC-transporter-substrate-binding-protein	gnl\|CDD\|179494	PRK02898, PRK02898, energy-coupling factor ABC transporter substrate-binding protein.	5.38206e-49
NZ_LS483461.1\|WP_111693567.1\|266822_268022_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	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.	9.19482e-54
NZ_LS483461.1\|WP_096071742.1\|263138_263909_+\|cobalt-ECF-transporter-T-component-CbiQ	gnl\|CDD\|274139	TIGR02454, Uncharacterized_protein_MJ1089, cobalt ECF transporter T component CbiQ. This model represents the CbiQ component of the cobalt-specific ECF-type. CbiQ is now recognized as the T component of energy-coupling factor (ECF)-type transporters. The S component confers specificity (CbiM-N for cobalt systems), which CbiO is the ABC-family ATPase. In general, proteins found by this model reside next to the other putative subunits of the complex, identified as CbiN, CbiO, or CbiM. Note that the designation of cobalt transporter has been spread excessively among ECF system transporters with many other specificities. [Transport and binding proteins, Cations and iron carrying compounds].	2.60571e-56
NZ_LS483461.1\|WP_003458257.1\|281777_282836_+\|acyltransferase-family-protein	gnl\|CDD\|226122	COG3594, NolL, Fucose 4-O-acetylase and related acetyltransferases [Carbohydrate transport and metabolism].	3.83782e-14

>NZ_LS483461.1|WP_110003193.1|277510_277609_+|heavy-metal-associated-domain-containing-protein
MIGKIECASCAATIENMLNKMGGVENVSLDFF
>NZ_LS483461.1|WP_003458296.1|276465_276735_+|metal-sensing-transcriptional-repressor
MNAEKKKALQCLKTAKGQIEGIIRMIEDERYCIDISNQVMASQALLKKANKLILQQHMHNCVKSAFENNESKDEKIEEILSVLNKLIDK
>NZ_LS483461.1|WP_003472388.1|275294_275924_+|hypothetical-protein
MKDIVIIGTENIGKEVVKIIEAINSKRNTLNVLGFISLKKDEEGSNIEGYSVLGSIDSMFNYFEGRKKDKFYFFKKLESQNELFTIIAIDNCKLKKEIENKLKDKIKFATIIHPDVSFFNKQEVGEGTIIYPGLISVGRFKLGKHVILKQKCSLGNNIEIGDYSFISFNSNIDSNVMVKEGSYIEANTTILANSNIDKNTYIKEGSILY
>NZ_LS483461.1|WP_003472002.1|268707_269364_+|hypothetical-protein
MARKSSKKYLKEANAQIILFVLIMIIMRMVVLNFMSEISGIEFDELSKARIYNGDITATLFLESLVNFFGNFILETYKGIILLAIINVFIASYILTKKDFTGNSYFNMVIAYLFSAIITVFLLLAGIILFFGIMQCMVVINSLKIDVSSEILWLAISVLVGVVFIKYFRKSVVFSLFAFLIISVYASYYTDIGKKAINTDYTQYSLEEFANNLNLVGE
>NZ_LS483461.1|WP_111693567.1|266822_268022_-|peptidoglycan-DD-metalloendopeptidase-family-protein
MNKLKIVSLFMSSFLMISAFSAPLITKANPEVNKLQEEKKQITEEKEIKKGKLDEIKDSIDAKQAELNSAQAKVTEYEEKIKTLNNEISSTDSEISKVEKSIEENTTEIEKAKKEQELKQEILGERLRNVYKSNLNDKFLYMILESKNFGELFSNIANIRTLVKTDNKLIEEIEALKNELEVRQAELETSKSTLASKKAELLSKEKSLNEVKAEHENTLNTYKSQLNELEELEAEKNAELKELADREDEIEKEIQSYFTKTPSTSSPTSNSSSGFIRPVASSTITSSYGPRVHPVTGQYKVHTGVDFAASTGTPFVAAKDGVVTAAEYHPAYGNMVIIDHGGGFSTLYAHASQLKVSVGQKVKQGQVVSLVGSTGYSTGPHAHFEIRINGQHVNPMDYI
>NZ_LS483461.1|WP_003457483.1|265736_266600_-|5'-nucleotidase,-lipoprotein-e(P4)-family
MRNSKITAIVLSAIIGIGVGTGGTLVYENNQEAKQISKLEQTTKANAVEEIVKGNVLATLWQQNSGEVKALRYEAYNSGKRYVDELVKEPTAKPYAVTLDIDETIIDNSPHAGYEIKHNELFSKENFGEWVQMADAAAIDGAKDFTDYAKSKGFEVFYVSNRSEEKELDATIKNMQKLGFVNSDKDHILLKTDTSSKDARWDKIKENYNLAIYCGDNLGDFPDGYDNKSNEQRREIVDKEAQFFGTKYIVLPNPTYGDFENAVYGYDFKKSPEQKLEDRLNSIKSFK
>NZ_LS483461.1|WP_003457595.1|265335_265533_+|hypothetical-protein
MILKIKKGEYDKMFTNELKDLLAGLYQKYGCTQEVLQLSNIIDEIIVKEQRERLKEYYKSRKNNI
>NZ_LS483461.1|WP_003457507.1|263923_264781_+|ATP-binding-cassette-domain-containing-protein
MEDYILKVEELNYNYSDGTHALKGINMNIKRGEVTAILGGNGVGKSTLFQNFNGILKPSSGRILFDNKPIDYSRKGIMKLRESIGIVFQDPDNQLFSASVYQDVSFGAVNMKLPEDEIRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLILDEPTAGLDPMGVSEIMKLLVEMQKELGITIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEVIRKVNLRLPRIGHLMEILKEKDGFVFDELDLTIGQARKTINSWKNKIFND
>NZ_LS483461.1|WP_096071742.1|263138_263909_+|cobalt-ECF-transporter-T-component-CbiQ
MINIDKYAYASKLKNINPSEKMFFALITLCVCLWANNFIVSMLIISIMTFLITKVGRTKIRVFIKLMMVPIAFLIIGILTIVVSYSLKQDTFLVSFKLFNGWIGVSKSGIIQGLNMFLKVMGSLSCLYFISLTTPMIDVISVLAKLKVPSFLIELISLVYRFIFIILETSEMMFISQNSRLGYRDIKTSYKSLGALASTLFIRSFKRANDLYTALEARGYNGELKVLEEQVQKRNYIYIITIIINLIFIGIAIFIK
>NZ_LS483461.1|WP_003452599.1|262843_263155_+|energy-coupling-factor-ABC-transporter-substrate-binding-protein
MKNKRVLTNVILLLLVVFITIIPFFVAKNGEFGGSDDQAEEAITQIDENYEPWFSPLFEPASGEIESLLFALQAAIGAGVIGFGLGYLKGKKKVNDEVNDKHR
>NZ_LS483461.1|WP_003458357.1|278316_278898_+|hypothetical-protein
MENLLKDYSNEEVLKALKIVTELKLEREQGDLPEFIRGRVSEVSEDEFDLIQAYNYYMRELRRGSVLLSEEETEKCGFNSRLAIDVELKDLIIFLNTQPNIKTLYSCSGHQFVRGQITFEGLLKFPQVDDFKIEYADERDETKVSFDIPERSYDYLNKLRKLYNYFYLINYNNLKTLTRDEVSAIKIKENCTA
>NZ_LS483461.1|WP_003458291.1|279035_281411_-|PAS-domain-S-box-protein
MDNPIFFHIFNDDKNKLETQRIIKLSIFIVFSIFFILLIDLSYKVLIRKNIEFIPGNSMPSFSLSLSLILGTMAYISSLIYYSSTKKDDFFIISLIYMNLSVELLITKGHNLIIFDKFIFIHAIFRIILLFYVAFNKKGISPLITKHKIITSIVVFLFSVITPMINYRIFSNNLFAKDIYFYATLMTMIIILYIIACIFLSKKSLDDCELIYSFIIASILLIALRGLYWICEVLLPNITLLKTNNVVLLLTILSFLLAISGVFNEITAKNKRSSLLQNELQVFYHLVEFNTSSSIILYDNKKKVIYTNKTIRERYCKSTKLKDQLKEVEKLFVDSIFIDDSEKNATKALFNKGNWEGKLILKNGKIVSAYIQILNVENKNYFAVNLKDITEEYTLTKNIKRNEQLLSCINNNVQDLIISVDNNGLITYVNDSVLKTLNYTYEEIIGMPIINLLGKNDEILNQLKLEDEEDSIKCKLVGKHSFVYVESIIRTLNDNNEIPYGKVIVAKNLTSKKRLENLAIKFKEAKAYEQIRNEFFANISHELRTPLNIIYSTIQLLNSKHETDPMDFNNFYDKYKQGLKINCYRMLRLINNLIDVSKIEVGFLKADFTNRDIVFLVENIVSLVIPHSENKDINIIFDTNVEENIIKCDPVKIERLILNLLSNAIKFTQNHGEIFVDLNISKDWVKISIKDNGIGIPKEMQASIFDRFVQADKSLKRRNEGSGIGLSIVKSIAELHDGKIELISDGIKGSEFIVWLPNVKLNYTEESNNLVDYITDDKNIELELSDIYEVH
>NZ_LS483461.1|WP_003458257.1|281777_282836_+|acyltransferase-family-protein
MNTVLKQRKRLDYLDIAKGLLIISVVLCHSPFENAYYLYWFHMPAFFIISGMLYKRGMNIKEQAIKFFVPYAIFSLIDISFNYIMYYHGNFSLGDLIHEIIKYAYGGKATWGVFWFIPVMFVTKVVFDQLNKRLTSKKLAFVCILSYILAHIYSMSFIPSSVTEITENQFVFWNLDTVLITLPYYALGYYITKLNIQRVFKETSTLILSSIGVVAMFILNSSIGIYYYLNIKYSYYKDPIFDILMPVTITIFILSLSYQISKFKYKKLFTIIGANSLVIMYLHKQVATLFMDVFNYGYIMFTIIGVCLPLLMMVLINKSIVSKFLFNGDLTFYRKIKDIKDIEPKDIIIDNK
>NZ_LS483461.1|WP_003458280.1|282936_283164_+|hypothetical-protein
MLRREKACIKEFYLNNRRGLVDTNGCVYLDGRYAGILKPSGAIYIEGRRGFIKKNGDIYLDGILIGTLNNYSIVY
>NZ_LS483461.1|WP_003472342.1|283303_284185_+|hypothetical-protein
MAMERKNFNNYKEVSLLIMLIPMLFILIDTLGRMNSKINNKNLFEIIFNEIFLYREVIVKFIMAIVVIFVITKIKIIKEKFILGDFKIIIGYTTLGVISYKFFGSEYGLSKSLDVYVMCIIAMIFILSGIREIMSSIDNININIEEKSNFERLVYTRVKYLGIIYFIIFSILIAIENLNSIMSSDFIVSLISNYNQHYNNMARVISVLGVVLIVALILIIKKSFSNLNLCYEEYIYIIKHKTVTEEIKKDIDFVNLKVEANKKYINNKFKKLEDKKAQVLLKGIFDLFKDNKH
>NZ_LS483461.1|WP_003472367.1|284212_286411_+|hypothetical-protein
MESKKSTNFDFILKTSIESYYDLLKNAEKAWETHAALTYIALRMVVEDLLIKLEEKYEVNRDKEANFKSTLNNLKEYVPSWIIEYGEYIRIKGEKSANKEIDSNLEENSTLLALKKVHEILIWYLKNVTKEMSLEADYSFITPESIKESECDLAIDKKVLENKEKFIISLEKQIKTNSDDEKKQEELEELLRNVKEEKKELTEKLEKKELELQEVLNSFKELQVKLTTYIEKDQSAEENNNKYPDFYKGFLSLQGYELRVVYAFLKSLSLGSIFLNKSKSIFLKSQRKEFLKFIEKEVEDLKKYSDGILKLKLYYILLKLTNTPVASVADKETFDKSLDSIVEKAYFIIESRNGFNGKVDKLEAIINYYLIVIMNSLSAEINHEEDNKDKVSDIIYEVLRTIPLDERKIILNKMNFTDISEGAIKENIRLNQVEFLKAALDCGISESSEFVIRSVFSIYVAFQKDFDFYEFRTRHDMLRAYIGPLLLVILLKEFKISRENLVPIFVMEISISNKILRKERREKIYYNQLVQAWLEEKEKYDKILSEKNNLEKNLKEVQEARELLLTNERKFVAEKDNTENAIKSQWDMFKEKALQSEEIKSFNSYEEYRRAVNQKNLIEVSEEHSLKDRGIIKNFFSLDTWKYKLNKLEISKNIKVLEEKLIEEAKESGVFENELLTIRELEKILADKESGLEDIRVDLKENSAENEKLNRLISNSNKLMEKFKEDNFDFAK
>NZ_LS483461.1|WP_003458282.1|286892_287663_+|hypothetical-protein
MKRFLAVGIIGVLVAGISVFGIEEFKHKRVKGLEAKVFQAKTYINHGDLVNAEIMLNIIKEENLDLKDKNVQEDILEIENSIDSNKDSFRDKPIKNLEDLSVDQKKVELLNIYLENNEFSPDVRSIESAGKEYYIQFRKSKKLPLDKNKDFSNKKGYILKPIRTSKRFFEDTCLIFDVEKPYYINKNIYYKFVEMPVSSYFGEDDKEIWYFADLNFNIISKENLEFYMNNKDVLDSNNNILSNYNLTNYIEDEYLY
>NZ_LS483461.1|WP_003458319.1|287841_288657_-|mechanosensitive-ion-channel
MKFDLSKMYEKLLSWITTNGFKLVIGLILLYIGWKIINKVIKILANIMKSRNVDPTLTSFAEAFSEVSLKVLLVITLMSYVGFDIAGLAALIASAGLAVGLALQGSLSNFAGGVIILLLRPFRVNDFIEASGYSGTVERITVFYTHLVTPDNKEILIPNGTLANGSLINYSSKDTRRVDLVFSVGYDDDIIKVKNVLWDIINKNELILKTPEAFVGISQHAASSIDFTVRVWTKQEDYWKVHFSLLEEVKLRFDEENITIPYPQMDVTLTK
>NZ_LS483461.1|WP_003458341.1|289230_289875_-|biliverdin-producing-heme-oxygenase
MNSFMMDIKNNSNDLHAVAEKTGFLKRLLEGKASTESYAEYLYNLYEVYNAIEVNLEKCKDNKVVKDFVLPEIYRAEAILKDLKFLLGENLNTMKPLASTRAYVARINEIGETAPELLVAHAYTRYLADLFGGRTIYGMVKDLYKIDEEGLNYYKYETLSDGPEMKGFVMNYHNKLNNIELNEEMKERFINEVANSYVYNIAISNELDFIRFNR
>NZ_LS483461.1|WP_003472341.1|290275_291499_+|exonuclease-SbcCD-subunit-D
MRILHTADWHLGKNLEGLSRMDEQERFLEDFVHIVKDNNIDLVIIAGDVYDSSNPPARAEKMFYDTLKKISANGERMTLVISGNHDNPERLVAAGPLAREHGIVMVGTPKSIVEVGEYGRNKVLNSGEGFIELDINGEKSVILTVPYPSEKRLNEVLYGAMDETCERIKSYSDRIKLLFDSLKGNFKEDTINLVVSHLFATGAENTGSERNIELGGSFIVDKECFPKEAQYIALGHIHKPMILPGTNKKIRYAGSPLQYNKKEISFEKKCFIVDVKANEEANIDEIKFDVYKPIEVWKCDSIDEAIYKCEENKDRECWVYLEIKTDRYIREDEIKAMKKLKGDIIEIIPKITLDEEENDEISFSEKSFQELFTDFYEKERGVKPEEDLLELLLNIVKEEGDEENETN

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Crispr_ID: NZ_LS483461_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LS483461_2

341447-341535

Orphan

Consensus_repeat	Method
AGTTTTATATAAATCAATATAAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LS483461_2

>merge|NZ_LS483461|2|341447-341535|CRISPRCasFinder
AGTTTTATATAAATCAATATAAATTTAAAATTGCAATTTCAAAAGCTAGATTAGGTATTGATAAAGAGTTTTATATAAATCAATGTAAA

>NZ_LS483461|2|2|341447-341535|CRISPRCasFinder
AGTTTTATATAAATCAATATAAA	TTTAAAATTGCAATTTCAAAAGCTAGATTAGGTATTGATAAAG
AGTTTTATATAAATCAATGTAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LS483461.1\|WP_003458368.1\|334384_334570_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003464293.1\|339200_339413_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003453458.1\|352291_353464_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|213187
NZ_LS483461.1\|WP_003458249.1\|341572_342250_-\|uracil-DNA-glycosylase	unknown	unknown	gnl\|CDD\|235376
NZ_LS483461.1\|WP_003473105.1\|358893_359547_-\|HAD-family-phosphatase	unknown	unknown	gnl\|CDD\|223710
NZ_LS483461.1\|WP_003464290.1\|336390_336897_+\|CarD-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224248
NZ_LS483461.1\|WP_025648473.1\|356028_357210_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213187
NZ_LS483461.1\|WP_003472405.1\|338213_338837_+\|copper-homeostasis-protein-CutC	unknown	unknown	gnl\|CDD\|225684
NZ_LS483461.1\|WP_003472403.1\|333800_334247_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_111693571.1\|341068_341365_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003472378.1\|337080_338217_+\|mechanosensitive-ion-channel-family-protein	unknown	unknown	gnl\|CDD\|366370
NZ_LS483461.1\|WP_003458352.1\|334582_334831_+\|spore-coat-protein	unknown	unknown	gnl\|CDD\|377935
NZ_LS483461.1\|WP_111693572.1\|357324_358758_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340856
NZ_LS483461.1\|WP_003470229.1\|349102_349570_-\|peroxiredoxin	unknown	unknown	gnl\|CDD\|224146
NZ_LS483461.1\|WP_003453460.1\|351461_352274_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224596
NZ_LS483461.1\|WP_003460434.1\|353477_354761_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340856
NZ_LS483461.1\|WP_003453475.1\|350251_350998_+\|peptidylprolyl-isomerase	unknown	unknown	gnl\|CDD\|234605
NZ_LS483461.1\|WP_003472324.1\|339536_340847_-\|DUF1576-domain-containing-protein	unknown	unknown	gnl\|CDD\|377881
NZ_LS483461.1\|WP_003453477.1\|354779_356015_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340856
NZ_LS483461.1\|WP_003472385.1\|335366_336098_-\|NAD-dependent-protein-deacylase	unknown	unknown	gnl\|CDD\|234777

Protein	Function_ID	Function_description	E-value
NZ_LS483461.1\|WP_003453477.1\|354779_356015_+\|glycosyltransferase	gnl\|CDD\|340856	cd04950, GT4_TuaH-like, teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	1.34702e-58
NZ_LS483461.1\|WP_003453458.1\|352291_353464_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|213187	cd03220, ABC_KpsT_Wzt, ATP-binding cassette component of polysaccharide transport system. The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.	7.45112e-115
NZ_LS483461.1\|WP_003458249.1\|341572_342250_-\|uracil-DNA-glycosylase	gnl\|CDD\|235376	PRK05254, PRK05254, uracil-DNA glycosylase; Provisional.	3.08574e-148
NZ_LS483461.1\|WP_003473105.1\|358893_359547_-\|HAD-family-phosphatase	gnl\|CDD\|223710	COG0637, COG0637, Predicted phosphatase/phosphohexomutase [General function prediction only].	6.61705e-50
NZ_LS483461.1\|WP_003464290.1\|336390_336897_+\|CarD-family-transcriptional-regulator	gnl\|CDD\|224248	COG1329, COG1329, Transcriptional regulators, similar to M. xanthus CarD [Transcription].	2.01008e-14
NZ_LS483461.1\|WP_111693572.1\|357324_358758_+\|glycosyltransferase	gnl\|CDD\|340856	cd04950, GT4_TuaH-like, teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	2.29211e-55
NZ_LS483461.1\|WP_003453460.1\|351461_352274_+\|ABC-transporter-permease	gnl\|CDD\|224596	COG1682, TagG, ABC-type polysaccharide/polyol phosphate export systems, permease component [Carbohydrate transport and metabolism / Cell envelope biogenesis, outer membrane].	2.59948e-37
NZ_LS483461.1\|WP_003472378.1\|337080_338217_+\|mechanosensitive-ion-channel-family-protein	gnl\|CDD\|366370	pfam00924, MS_channel, Mechanosensitive ion channel. Two members of this protein family of M. jannaschii have been functionally characterized. Both proteins form mechanosensitive (MS) ion channels upon reconstitution into liposomes and functional examination by the patch-clamp technique. Therefore this family are likely to also be MS channel proteins.	1.6784e-42
NZ_LS483461.1\|WP_003458352.1\|334582_334831_+\|spore-coat-protein	gnl\|CDD\|377935	pfam07875, Coat_F, Coat F domain. The Coat F proteins, which contribute to the Bacillales spore coat. It occurs multiple times in the genomes it is found in.	2.38946e-13
NZ_LS483461.1\|WP_003472405.1\|338213_338837_+\|copper-homeostasis-protein-CutC	gnl\|CDD\|225684	COG3142, CutC, Uncharacterized protein involved in copper resistance [Inorganic ion transport and metabolism].	2.44152e-89
NZ_LS483461.1\|WP_003470229.1\|349102_349570_-\|peroxiredoxin	gnl\|CDD\|224146	COG1225, Bcp, Peroxiredoxin [Posttranslational modification, protein turnover, chaperones].	9.8243e-79
NZ_LS483461.1\|WP_025648473.1\|356028_357210_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213187	cd03220, ABC_KpsT_Wzt, ATP-binding cassette component of polysaccharide transport system. The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.	2.31139e-120
NZ_LS483461.1\|WP_003460434.1\|353477_354761_+\|glycosyltransferase	gnl\|CDD\|340856	cd04950, GT4_TuaH-like, teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.	4.52699e-51
NZ_LS483461.1\|WP_003453475.1\|350251_350998_+\|peptidylprolyl-isomerase	gnl\|CDD\|234605	PRK00059, prsA, peptidylprolyl isomerase; Provisional.	1.6338e-32
NZ_LS483461.1\|WP_003472324.1\|339536_340847_-\|DUF1576-domain-containing-protein	gnl\|CDD\|377881	pfam07613, DUF1576, Protein of unknown function (DUF1576). This small family is found in several undescribed proteins. The alignment is distinguished by the frequent occurrence of conserved glycine and aromatic residues.	4.57673e-64
NZ_LS483461.1\|WP_003472385.1\|335366_336098_-\|NAD-dependent-protein-deacylase	gnl\|CDD\|234777	PRK00481, PRK00481, NAD-dependent deacetylase; Provisional.	3.29219e-134

>NZ_LS483461.1|WP_111693571.1|341068_341365_-|hypothetical-protein
MKNYKDNDENFKLIPMNMKCNQEYSFMPMNKFNSNSMNLNPMINKNSNHSCCCMHNYVMKPSPYNNNYYENQMFPQNHTDNMMVKTLITVKKKSDLFD
>NZ_LS483461.1|WP_003472324.1|339536_340847_-|DUF1576-domain-containing-protein
MKRLPQEYLIHLILYISFIIFAFFLESPKEILNGLYNIISNSDILITDYISIGGFGATLINSALLGLIFIFLFYITDTKSTGKSIMSLWFLTGFGMFGKNIINIWPIVLGTFIYSKVKKKPFKDYLVIASLGTALAPTVSQFSFFPGVHPISGAIMGALVGIIVGFILPPIAKNASKIHSGFSLYNVGFAGGIIAIAVMSLMRAVGHDFETNSIWHKGNNILYMLFLFTISAYFIICSLILDKSKKSVLKDQIGINKEHGIFPSDFFSIYGSSCYFNMGVLCIFSTLFVLLINGDLNGPTIGAIFSMAGFGCYGKNLANSVPLIIGASLASLISISDINSPVTVVCILFSTGLAPISGYYGWPYGIIAGFLHIFMVFNIGELHGGLNLYNNGLASGFVAAIIVPVIESLQVTNTKNNLKDSSKKHPISLGIKKEAD
>NZ_LS483461.1|WP_003464293.1|339200_339413_+|hypothetical-protein
MLEKMILSDKECEYLAKSIAGGVLIGLALGAIFNNPQFGFALGGVTGIVASLIYTLVKRAKIKSDKKLIN
>NZ_LS483461.1|WP_003472405.1|338213_338837_+|copper-homeostasis-protein-CutC
MTIKLEACVGNYKEGKRAEELGANRIELCDNLAQGGTTPSYGTILQCKKDINIDINVIIRPRGGNFVYSKEELSIMKNDIKLCKDIGVTGVVFGFLKEDNTLDYETTKEFVELAKPLSVTFHMAFDEIENKVDALGKLIDLGVDRVLTKGGLDNAFKNKDTLKELVEHAKDKIIILPGGGVTKDNFLKLKDYTNAREFHGTKIVGNL
>NZ_LS483461.1|WP_003472378.1|337080_338217_+|mechanosensitive-ion-channel-family-protein
MKELERLLGRITIINIKEIIIILVIMIIVLIINKILINNLFKLLMRGARRTKNYLDNNIVRALENPLKLIVSFVGIYSIFKVINLDSLGIDFLSTYKILRVGIIVSFIYFAYNLTLENSLLYSKLHKNDGGNTIVFPFVSIIIRLIILLVGIIIIANEFGLTGFIAGLGVSGVAFALAAQDTCSNLFGGMVIVLDRPFSIGDWIQAGDVEGVVEEITFRSTRIRTFSMAIATVPNSKLANSNIINWTQRKLRRIHFKFTMDCKTPIESIKNSVNKIENMLKKHDKIDKNLIIVSFNELSTYGFGVFIYFYTDEFEYLKYEKLKEEINIKILEILREENVSLMFLNFDFKGFERRSGNCNLENTELESIKNITEEERGV
>NZ_LS483461.1|WP_003464290.1|336390_336897_+|CarD-family-transcriptional-regulator
MFKINDYIMYGTVGVCQVIDITKETLMNNIEKEYYVLSPVYSKYPKKTVIKIPVDNKKISMRTLLSKEDVNSIINSIPETETLWIDNDRQRNDEFKTMLRSGNCDDLIVLIRSIYLDKKKRKLDGKKACKGDDEIMQTAEKLINEEFAVILDIRPEEVKSYIKSHIPQ
>NZ_LS483461.1|WP_003472385.1|335366_336098_-|NAD-dependent-protein-deacylase
MDDKINKLKEIIKNSNNIVFFGGAGVSTESGIPDFRSANGLFNEKLNITFTPEQLVSHSFFERYPEEFFNFYKAKLIYPNAKPNDAHIALAKLEEMGKLKAIVTQNIDGLHQMAGSKNVFELHGSVLRNYCVDCHTFYDEKFILESKGVPKCTKCGGIVKPDVVLYEEPLDDNVIRGAIDAISKADTLIIGGTSLVVYPAAGLINYFRGKNLVLINKSSTQADSKADLVINDSIGKVLGKVID
>NZ_LS483461.1|WP_003458352.1|334582_334831_+|spore-coat-protein
MQEKEMISDYLAGINASLAGYGGIISQCENQELRETIQNMRNQDEVRQYALFKIAKEKGYYIPAQQATPEEVATVKQQVSQG
>NZ_LS483461.1|WP_003458368.1|334384_334570_+|hypothetical-protein
MANLNELELQNLRHLIGAHCTIEKKLECYSEQCTDPTLKNMLKKDAQDAKNSKEKLMSFLG
>NZ_LS483461.1|WP_003472403.1|333800_334247_-|hypothetical-protein
MIFLCIFLILLGVCAVAFVLYQCNIKITEYKRQILTLNNQLSKYKDTTYKKSNNDSKKTLIINFNKPEFKYGITLPYTSIFIAPSEESIAISKIKEKSQVKIIDEAEINNEIWYYSLLNTESKINCNGWIKKSQFSMLMEDTNNIISE
>NZ_LS483461.1|WP_003458249.1|341572_342250_-|uracil-DNA-glycosylase
MAAEFNNDWDDLLKDEFEKEYYLNLRKFLINEYKTQKIHPSMYDIFNALKFTPYKDVKVVILGQDPYHGPNQAHGFSFSVKPGVQTPPSLRNMFKELNSDLGCYIPNNGFLESWAKQGILLLNTVLTVREGQANSHKGKGWEIFTDRVIELLNKREEPIVFILWGRNAISKEALITNPIHKIIKSVHPSPLSATRGFFGSKPFSKTNDFLVSINKEPIDWQIPNI
>NZ_LS483461.1|WP_003470229.1|349102_349570_-|peroxiredoxin
MSIEINKLAPDFKLMGSDGKEHSLSDYKGKNIVLYFYPKDNTAGCTTEACDFRDNIQNFHDLNAIILGVSRDSLASHDKFITKLSLPFVLLSDPDETVCKLYDVIKEKNMYGKKYMGVERSTFLINKEGILIEEFRKVRVKGHIEKVLDKLKEIN
>NZ_LS483461.1|WP_003453475.1|350251_350998_+|peptidylprolyl-isomerase
MEKKVLATVGNTEITSDYIDEIIARYPAQQQAMLASDEGKRQVLEQAIAFELMSEFAKETGLDKTEEFKDQLNKFAKELLAQMVMKKTLSSVTVTDDEAKAFYEEHKENFVELETVTAKHILVASEEEAKKVEEEIASGSITFEDAANKYSSCPSKEQGGNLGSFSKGMMVPEFEEAAFNLELGVVSAPVKTQFGYHLIKVEDKTEAKTKAFEDVKEQVVNMLIQERQQKKYLELIKELREKYGVKLA
>NZ_LS483461.1|WP_003453460.1|351461_352274_+|ABC-transporter-permease
MKDWLEIEKSIFSHWRMIFSISKKEFKKEFAGSKLGMAWAIIRPLAMITVFWMIFSTGMRTTSSNVQVNYLVWLVSAYIPWIFISDVIMSGAGSIRVNSFLVKKVKFPVEILPTIRIVISFYTFLILLVISFIIFAVNGNLNLINIPKLIYAIIITIIFLAALSRLLSTWVVMSIDILHGISVFMQFLFWMCPVMWQAGELPVGSSMPWIEKILKLNPLYYLAVLFRDAYLGTHTVSLAYGVYFWVVTIILFIFGSKVFKKFRPEFDDVL
>NZ_LS483461.1|WP_003453458.1|352291_353464_+|ATP-binding-cassette-domain-containing-protein
MSVAIRVKDLTKKYKLYQKRSERLANAFGKEKNIKEFYALKGVSFEISKGECVGIIGHNGAGKSTLLKLLTGVAFPTSGEIEINGRLASMLELGSGFNPELTGMENIYFNGSLNGLTKEEIDGKLKDILEFADIGNFIEQPVKNYSSGMFARLAFAVAINVDPDILIVDEILSVGDVGFQVKCMEKFNEFKKKGKTILYVSHGLGTVKKFCDRAIWLQKGEVVDDGNSVIVVERYYNLNFNPANIEQLKDHKSDIINSIAVKSNTKNVEYLEKLDLEVEYDLISNDLKDPNIVLEFRKTDYEPGTTRGNDQFVCGINSKDNIKNIPFNLGVNKLKVSLNKVNLVAGVYYIDFVLRDGEEEVYRKINGYSFTLNDKYRGEGFLILGHSWGN
>NZ_LS483461.1|WP_003460434.1|353477_354761_+|glycosyltransferase
MSVGRIARRTTEVLKEDGLIEVIKRVLRYIKRRIKDKLDNNALTYRKNYEEANAIFHKILKKEKFKAVVVFDSRVGWNIPLFQRSQHMANELTDDGYLYFYRTSEQFDPHVKTVEKLKDRLYLVNMANFALQNAMFDLLKEYKGHKFLSLYSTDVYLDEQYIKEKYINNGFKIIYEYIDELSDEISGHLPDFVYDRHKNIIEDKSNIAVGSADKLIEEIEEIRGKENVAMITNGVQYDHWQYRSDEVPEKLKDIVSKGNPIIGYFGALAKWFDYELLKKVAKERPNYEIVLIGFLYDNSFKDSKIDELENVHYLGIVDYKELNQYSQYFTISTIPFLLNDITESTSPVKLFEYMAMGHPIVTTDMRECRKYKSVLIGKSHEDFIEKLDFALTLDKKDEYYNYLKEEALANTWREKAAILDRLIEKNI
>NZ_LS483461.1|WP_003453477.1|354779_356015_+|glycosyltransferase
MSLKRSLKNLLRPILKPMLLKYREKGHEDQKQVFFDEITGAIKNGNYDAIVIFDVYFGFEVKMFQRPQHIALNLAKENVLYFYKASPYVDKDIKTYKKMEENLYLVNTDLYWLQECLIDIVSQSGVPAFGQIYSTSFVEYDSWLKKFTDRNFKIIYEYVDDLSDDIAGFKISDEIKASHKRMLEDTEKVYVVTTADKLYQEAKELRGENKLALVTNGVQYEHFANIDCKKIPDKMKNIVNSKKKIIGYFGALASWFDYDLIKELAEEFKDDYEIVLIGIDYDQSLGKSGILKLDNVHYLGTVNYNELPTYSKFFNVSIIPFVVNEITEATSPVKLFEYMALGKPIVTTALPECRKYESPLVSDSHEDFINNIKKAAELENSKEYIELLRKEGNQNTWRQKAKDIKELILNS
>NZ_LS483461.1|WP_025648473.1|356028_357210_+|ABC-transporter-ATP-binding-protein
MEKAIEVKNLCKNYRVYDSKSSRIRNIINPFAKKEVKEFKALTDVSFHVNKGEIVGIIGNNGAGKSTLLKILTGVSFPSSGEVNVNGRVSSLLELGTGFNPELTGEENIYFNGSLMGLTQDEIDKVKDNIIEFADIGEFINQPVKSYSSGMYARLAFAVAININPDILIVDEILSVGDVGFQKKCMDKFNEFKEAGKTVLYVSHGLETVQTFCERAIWLEKGRVVDIGPSFDIVEKYYDKLMKSDDEEELETGKFVELINVEILDDKKVYKKGESIEFLVEYEVFNPSVKNAGITIEMRKAYREPCEYRNADQFIFSVNSNVDEFTIPWKKGRNKITFKIDSLDVKEGIYYLDAIFSESQNLVALETQEDVVSFEVKNEGESEGFVFLDSTWT
>NZ_LS483461.1|WP_111693572.1|357324_358758_+|glycosyltransferase
MSNIFEVMLKKNIGDFTYEEKRELNNWLIENLKLKELIYSGLELTKVINEDGEETAYYDNKITEEDILSGNFNELCSKTSKYIDDAISSILFEGQFNCFYEKIKSILELEDFDEIIVFHASFGWNIEMKQRPQHLAEALSKKKVLYIYRSDVKNDNIYSIKKIKDNLYVLNLDMYSLNVAFFEAIKSINKPKFVHVYATCLNSVDYEKIKTYMDKGFKVIYDFVDELSSEISGYNITSKMIEDHEKLLRDKENVLVVSTAKKLKDIANKFRGENENNILAPNAVNLEDFKNHGHEIGEKIQPIVNKRKPIIGYYGALAKWFDYKLIEQLAKEREDYEIVLIGMDYDGSYDQSNLKNYSNISYLGMIDYKYLINYSRYFDVCIVPFIKNDITDSTSPLKIFEYMALEKPIVTTDINECKNYESCLISKDYDEFIRNIDKALKLEVDNKEYFNILRREAEENTWDNRAELIKEAIKNLE
>NZ_LS483461.1|WP_003473105.1|358893_359547_-|HAD-family-phosphatase
MLSNIKGVIFDLDGTLVDSMGVWAKIDSDYLTDLGLEVPKNLKEEITHLGFKEVAKYFKKRFNIASSEEEIMKTWHDMAYVEYKNNIKLKPGAREFLEQLKESNIKIGLATSNSYPLLEVCLKSNDIFHLFDSITITGEVPRGKDFPDVYLLAAERLGLEPKECAVFEDILPAVKGALSAGMKVFAVEEHTVSEEEKSQIKEIVHEYIDSFNDLLVN

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Crispr_ID: NZ_LS483461_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LS483461_3

1160494-1160696

Orphan

Consensus_repeat	Method
TTTTAAGCAATATTTGTTTTTAGGT	CRISPRCasFinder

3 spacers

The CRISPR arrays of NZ_LS483461_3

>merge|NZ_LS483461|3|1160494-1160696|CRISPRCasFinder
TTTTAAACAAGCTTTATTTTTTAGGTGCACAGACCATACTTTCTTTTGGCATTACAATAGATGATTTTAAGCAATATTTGTTTTTAGGTCTATTTACGAGCAAATATTAAATAAAATCTAAACTAGATACTTTTAAACAATATTTGTTTTTAGGTGCTAACAGCTTTTTAGTAGTTACTATTAATAGAATATTGATTTTAGGT

>NZ_LS483461|3|3|1160494-1160696|CRISPRCasFinder
TTTTAAACAAGCTTTATTTTTTAGG	TGCACAGACCATACTTTCTTTTGGCATTACAATAGATGA
TTTTAAGCAATATTTGTTTTTAGGT	CTATTTACGAGCAAATATTAAATAAAATCTAAACTAGATAC
TTTTAAACAATATTTGTTTTTAGGT	GCTAACAGCTTTTTAGTAGTTAC
TATTAATAGAATATTGATTTTAGGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LS483461.1\|WP_003453880.1\|1154638_1155415_+\|ethanolamine-utilization-cobalamin-adenosyltransferase	unknown	unknown	gnl\|CDD\|227149
NZ_LS483461.1\|WP_003453912.1\|1159151_1159625_+\|DUF861-domain-containing-protein	unknown	unknown	gnl\|CDD\|114941
NZ_LS483461.1\|WP_003453956.1\|1157172_1157445_+\|EutN/CcmL-family-microcompartment-protein	unknown	unknown	gnl\|CDD\|377017
NZ_LS483461.1\|WP_111693874.1\|1169661_1170447_-\|phosphorylase	unknown	unknown	gnl\|CDD\|350158
NZ_LS483461.1\|WP_003453793.1\|1160901_1161447_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_LS483461.1\|WP_003453976.1\|1154270_1154561_+\|ethanolamine-utilization-microcompartment-protein-EutM	unknown	unknown	gnl\|CDD\|132899
NZ_LS483461.1\|WP_057231030.1\|1168365_1169088_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_111693869.1\|1156267_1157026_+\|ethanolamine-utilization-protein	unknown	unknown	gnl\|CDD\|274184
NZ_LS483461.1\|WP_111693875.1\|1170654_1171173_+\|ClbS/DfsB-family-four-helix-bundle-protein	unknown	unknown	gnl\|CDD\|226733
NZ_LS483461.1\|WP_111693870.1\|1161738_1162050_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_111693871.1\|1162363_1164004_+\|EAL-domain-containing-protein	unknown	unknown	gnl\|CDD\|225110
NZ_LS483461.1\|WP_111693867.1\|1152437_1153916_+\|acetaldehyde-dehydrogenase-(acetylating)	unknown	unknown	gnl\|CDD\|131570
NZ_LS483461.1\|WP_003454016.1\|1158051_1159149_+\|ethanolamine-utilization-protein-EutH	unknown	unknown	gnl\|CDD\|237906
NZ_LS483461.1\|WP_003454035.1\|1157446_1158001_+\|BMC-domain-containing-protein	unknown	unknown	gnl\|CDD\|131578
NZ_LS483461.1\|WP_111693868.1\|1155424_1156060_+\|phosphate-propanoyltransferase	unknown	unknown	gnl\|CDD\|237899
NZ_LS483461.1\|WP_011590444.1\|1167712_1168171_+\|4Fe-4S-cluster-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|379137
NZ_LS483461.1\|WP_003454005.1\|1159992_1160469_+\|glutathione-peroxidase	unknown	unknown	gnl\|CDD\|238207
NZ_LS483461.1\|WP_011590441.1\|1165148_1165574_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|341244
NZ_LS483461.1\|WP_111693872.1\|1164085_1164706_+\|flavodoxin-family-protein	unknown	unknown	gnl\|CDD\|223728
NZ_LS483461.1\|WP_111693873.1\|1165904_1167716_+\|ribonucleoside-triphosphate-reductase	unknown	unknown	gnl\|CDD\|236212

Protein	Function_ID	Function_description	E-value
NZ_LS483461.1\|WP_003453880.1\|1154638_1155415_+\|ethanolamine-utilization-cobalamin-adenosyltransferase	gnl\|CDD\|227149	COG4812, EutT, Ethanolamine utilization cobalamin adenosyltransferase [Amino acid transport and metabolism].	1.25082e-69
NZ_LS483461.1\|WP_003453912.1\|1159151_1159625_+\|DUF861-domain-containing-protein	gnl\|CDD\|114941	pfam06249, EutQ, Ethanolamine utilisation protein EutQ. The eut operon of Salmonella typhimurium encodes proteins involved in the cobalamin-dependent degradation of ethanolamine. The role of EutQ in this process is unclear.	1.30397e-93
NZ_LS483461.1\|WP_003453956.1\|1157172_1157445_+\|EutN/CcmL-family-microcompartment-protein	gnl\|CDD\|377017	pfam03319, EutN_CcmL, Ethanolamine utilisation protein EutN/carboxysome. The crystal structure of EutN contains a central five-stranded beta-barrel, with an alpha-helix at the open end of this barrel (Structure 2HD3). The structure also contains three additional beta-strands, which help the formation of a tight hexamer, with a hole in the center. this suggests that EutN forms a pore, with an opening of 26 Angstrom in diameter on one face and 14 Angstrom on the other face. EutN is involved in the cobalamin-dependent degradation of ethanolamine.	5.50579e-37
NZ_LS483461.1\|WP_111693874.1\|1169661_1170447_-\|phosphorylase	gnl\|CDD\|350158	cd09007, NP-I_spr0068, uncharacterized subfamily of the nucleoside phosphorylase-I family. This subfamily is composed of uncharacterized members including Streptococcus pneumoniae hypothetical protein spr0068. The nucleoside phosphorylase-I (NP-I) family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of the NP-I family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.	1.09927e-22
NZ_LS483461.1\|WP_003453793.1\|1160901_1161447_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	1.47125e-09
NZ_LS483461.1\|WP_003453976.1\|1154270_1154561_+\|ethanolamine-utilization-microcompartment-protein-EutM	gnl\|CDD\|132899	cd07059, BMC_PduA, 1,2-propanediol utilization protein A (PduA), Bacterial Micro-Compartment (BMC) domain. PduA is encoded within the 1,2-propanediol utilization (pdu) operon along with other homologous carboxysome shell proteins PduB, B', J, K, T, and U. PduA is thought to be required for the formation of the outer shell of bacterial pdu polyhedral organelles which are involved in coenzyme B12-dependent degradation of 1,2-propanediol. Although it has been suggested that PduA might form hexamers and further assemble into the flat facets of the polyhedral outer shell of pdu organelles, like PduU does, at present no experimental evidence directly supports this view.	4.19683e-40
NZ_LS483461.1\|WP_111693869.1\|1156267_1157026_+\|ethanolamine-utilization-protein	gnl\|CDD\|274184	TIGR02536, putative_ethanolamine_utilization_protein, ethanolamine utilization protein. This family of proteins is found in operons for the polyhedral organelle-based degradation of ethanolamine. This family is not found in proteobacterial species which otherwise have the same suite of genes in the eut operon. Proteobacteria have two genes that are not found in non-proteobacteria which may complement this genes function, a phosphotransacetylase (pfam01515) and the EutJ protein (TIGR02529) of unknown function.	2.69076e-72
NZ_LS483461.1\|WP_111693875.1\|1170654_1171173_+\|ClbS/DfsB-family-four-helix-bundle-protein	gnl\|CDD\|226733	COG4283, COG4283, Uncharacterized conserved protein [Function unknown].	2.14458e-72
NZ_LS483461.1\|WP_111693871.1\|1162363_1164004_+\|EAL-domain-containing-protein	gnl\|CDD\|225110	COG2200, Rtn, c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms].	1.12886e-56
NZ_LS483461.1\|WP_111693867.1\|1152437_1153916_+\|acetaldehyde-dehydrogenase-(acetylating)	gnl\|CDD\|131570	TIGR02518, Acetaldehyde_dehydrogenase_acetylating, acetaldehyde dehydrogenase (acetylating).	0
NZ_LS483461.1\|WP_003454016.1\|1158051_1159149_+\|ethanolamine-utilization-protein-EutH	gnl\|CDD\|237906	PRK15086, PRK15086, ethanolamine utilization protein EutH; Provisional.	5.41583e-166
NZ_LS483461.1\|WP_003454035.1\|1157446_1158001_+\|BMC-domain-containing-protein	gnl\|CDD\|131578	TIGR02526, putative_ethanolamine_utilization_protein, PduT-like ethanolamine utilization protein. This gene shows up in ethanolamine utilization operons in which a proteinaceous coat organelle is also encoded. It is closely related to the PduT protein in propane-diol operons with the same structure.	7.32798e-92
NZ_LS483461.1\|WP_111693868.1\|1155424_1156060_+\|phosphate-propanoyltransferase	gnl\|CDD\|237899	PRK15070, PRK15070, phosphate propanoyltransferase.	5.15896e-115
NZ_LS483461.1\|WP_011590444.1\|1167712_1168171_+\|4Fe-4S-cluster-binding-domain-containing-protein	gnl\|CDD\|379137	pfam13353, Fer4_12, 4Fe-4S single cluster domain. This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.	7.10084e-10
NZ_LS483461.1\|WP_003454005.1\|1159992_1160469_+\|glutathione-peroxidase	gnl\|CDD\|238207	cd00340, GSH_Peroxidase, Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.	8.48351e-99
NZ_LS483461.1\|WP_011590441.1\|1165148_1165574_+\|hypothetical-protein	gnl\|CDD\|341244	cd05920, 23DHB-AMP_lg, 2,3-dihydroxybenzoate-AMP ligase. 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.	0.000422593
NZ_LS483461.1\|WP_111693872.1\|1164085_1164706_+\|flavodoxin-family-protein	gnl\|CDD\|223728	COG0655, WrbA, Multimeric flavodoxin WrbA [General function prediction only].	3.01642e-51
NZ_LS483461.1\|WP_111693873.1\|1165904_1167716_+\|ribonucleoside-triphosphate-reductase	gnl\|CDD\|236212	PRK08270, PRK08270, ribonucleoside triphosphate reductase.	0

>NZ_LS483461.1|WP_003454005.1|1159992_1160469_+|glutathione-peroxidase
MEIYDISVKDINGENVSLERYRGKVLLIVNTASKCGFTKQFDGLEELYEKYKDEGFEVLGFPCNQFKEQDPGSNSEIMNFCKLNFGVTFPMFEKIDVNGENESLLYSYLKEQKSGMFGSKIKWNFTKFLVDREGNVIKRFSPQTTPKSIEKDIEELLA
>NZ_LS483461.1|WP_003453912.1|1159151_1159625_+|DUF861-domain-containing-protein
MENISKELLEKLVRQIIEEKLAGAGNNDSVDFIRNKDKSGIMSIKLPTVKVDESNRLDTGNPRDVVYTKDLFTLEESPRLGAGIMEMKETTFDWTLNYDEIDYVIEGHLDIIIDGRKISADAGEIILIPKGSKIQFSVPDYARFIYVTYPADWASQA
>NZ_LS483461.1|WP_003454016.1|1158051_1159149_+|ethanolamine-utilization-protein-EutH
MSINEIIVYIMVACMALGAIDKCLGNKFGIGEQFEEGIMAMGSLALAMVGVICLAPVLASVLGPIVTPVFNALGADPAMFAGSILANDMGGAPLAASLAQDPQAGMFSGLIIGAMMGATIVFTIPVSLGIIEKKDHKFLATGILAGIITIPVGAFVGGLVAGFPAMMVLKNLVPIIIFAILIAIGLAFAEEAMIKGFNIFGKIVVIIITLALAAAIIEALTGFVIIPGMAPITDGIEIVGSIAIVLAGAFPLVYIITKVFKKPLMGLGKILGMNEIAAAGMIASLANNIPMFGMLKDMDDRGKIINVAFAVSASFVLGDHLGFTAGFNPEMIFPMIVAKLVGGITAVILAMFIAKKTLGKIEEAK
>NZ_LS483461.1|WP_003454035.1|1157446_1158001_+|BMC-domain-containing-protein
MKKSIGALEFRSISKGIEVSNEVVKKAFVEVSYLKSICPGKFFLIVNGDAGEVKEAIEFGEKLGEKYLVGSFIINSIHHDIINALKGKYSQKNIEDKAIGIMETGKVSSGILALDKTLKSSEVNLVKLQLAFGIGGKLVYIVSGDLSSVENGMREGQSILQEKDIINVSIIPFVHSEIAKNLIK
>NZ_LS483461.1|WP_003453956.1|1157172_1157445_+|EutN/CcmL-family-microcompartment-protein
MEIGRVVGNVWATRKDEKLNGQKFLIVKLLVSKDKEKEGLFVAADNAGAGIGDIVLITKGGAARQSIGNREVPIDAAIVGIVDSIDIEED
>NZ_LS483461.1|WP_111693869.1|1156267_1157026_+|ethanolamine-utilization-protein
MKGGKDNMDYEKLVEFLVDEIYKRIQEENSKSNSLEKRKSIVVIGESNVSFYREVLKGFDINPLTSECKDCDILLISKLCIKGLSNIAQGTCTTKAENFALEMLLKGKKVYILEDGIEYRKYKNTAPKVLYNKYIKFEEELLAYGIEVIDDLNRISIESKDEKVSFSGIKEEISKNICLCSENKVEGKKDLDTTAIADEFTINLSNKKLVSESDLRKPHINGVRTLIVDKKAIITPLAKDYIRINNLNVVLS
>NZ_LS483461.1|WP_111693868.1|1155424_1156060_+|phosphate-propanoyltransferase
MDNLLQDIIEEVVRRVKDEAFIEVEASGRHVHLTREHIDILFGEGHELTRIKDLSQPGQYACKERVTISGPRGKIDNVVVLGPPRNETQVEVSFTDALVLGSIPPVKLSGDLENTPEITISTERASIALNRGLMVAKRHIHMTPEDSIKFGVSNNESVKVKVLGKRPLIFDDVIVRVSKDYRTFMHIDYDEANACGFSKGTFALIVGKDKK
>NZ_LS483461.1|WP_003453880.1|1154638_1155415_+|ethanolamine-utilization-cobalamin-adenosyltransferase
MAVLTEGEVRKRLSREDLKALKEFKVVKGEIITPSAKSYLAEHNINLVYVNSEEEKLNKETEPKEIIREVVREKEYKYETVFGAKLDEKPEHMTHLTGNLLVFKDHKRIIFRGKIDSLEARIVETQVLCHKQGMNKLVEDLQEILNLIGRILRCEVLSEPLEGFSLQGMTEKDLREKSHNPKKYFGIGHEMPTYEMGEIVAALNILRTLTRETELSAYEAFKGEYGQVEREDLIRALNRLSSVFWIMIFKVRTGKYEK
>NZ_LS483461.1|WP_003453976.1|1154270_1154561_+|ethanolamine-utilization-microcompartment-protein-EutM
MANANALGMIETRGLVGAIEAADAMVKAANVQLVGKEQVGGGLVTVMVRGDVGAVKAATDAGAAAAERVGDLISVHVIPRPHFEVDAILPKAPKAE
>NZ_LS483461.1|WP_111693867.1|1152437_1153916_+|acetaldehyde-dehydrogenase-(acetylating)
MEFLDKDLVSIQETRGLIRKAKEAQSKLARMSQQDIDRIVKAISDAAYENSEKLAKMANEETGFGKWEDKVLKNVFAARTVYESIKDTKTVGIVEENVEKRAFKIMVPVGVVAGLIPSTNPTSTAIYKAMISIKARNAIVLSPHPSAKKCIIETAKIIAKAAERAGCPEGAIGCITVPSIEGTNELMKNKDTSLILATGGEAMVRAAYSSGTPAIGVGPGNGPAFIDKSADVKLAVKRILDSKTFDNGTICASEQSIVVEKAMEDEVVRELKEQGAYFLTEEQANQLSKFVMRANGTMNPQIVGKTPQDIAKLAGLEGIPSWARVLIPRECHVGHKYPFSREKLTTILTFFVEENVDAVLNRCREILLNEGAGHTFCMHANNEEIVKKFALEMPVSRMVVNSPGALGGIGATINLVPALTLGCGAVGGSSTSHNIGPLDLMNTRNVAYGVRELEDIRELAVGATKEVASSLDLGDKEELINLLVKKIIEELK
>NZ_LS483461.1|WP_003453793.1|1160901_1161447_+|GNAT-family-N-acetyltransferase
MNLKRINSNDNCFNKAMEIYNGSFPIFERRTMDDQIKALDDTNYHFEVIYDKEEIVGILLYWDMGRYKYIEHFAIDSKLRGKNYGSRVLKEFCDHNKNVILEIDPPIDEISIKRLNFYLKLGFKLQDFDYTHPSYRKGCKRHSLKIMTFNHNMPKEDYDTFNILLKRDIMKYSEFKDRLNN
>NZ_LS483461.1|WP_111693870.1|1161738_1162050_+|hypothetical-protein
MKKVLIGVLVFLICIISVFLFFDREEESIVTDVVEKSQYGLLVNYEDGLIAVDTGDAEIVDRDGKENTLDCVNEGDRIEIIYDGKIEETYPAQINNVYKIIIF
>NZ_LS483461.1|WP_111693871.1|1162363_1164004_+|EAL-domain-containing-protein
MKKRVFWVSIVFLIIITVLGITIKFDGKKVNCNRKTIKVGFYEYYPYYYLNKNSVPDGYYNEILELICNKLDLNYKYVDCNVTDALEKLKSGQIDLVFGISKTPDREKEYEFTDHYLNNDNFAIYTNKNIKNGDLKALNGLKMGFLKGEENNEWILRLLKDKGINVKPIYVSNYPEDEEYLYNNKVDFVVENTRSNINYENKNIKKIFEFSSGPVYIVSRKGNEKLIEGIDSVLGELEEDGEQKDTNLYSKYFDEHLDKLKNEKLLVVIFLIIISLFIYKKRKNKIFAIRTKRKIRDYMKNDKYILYYQPIVDPKKNRVKGFESLLRLNKDGKILTPYSFIKEIEDNNMSLEVSLWLLKKVISDYRIIKDYDMVKGNDFYISLNVSFKEIENPKFLRSLMKIAKDYKIDDCNICLEIVEKFGMEDIGRIQSAIRIIKEYGFLIAIDDFGVEYSNLDLLNKIDSDIVKLDKYFADNLDKSIINEKTVEFISEICIIANRTIVFEGIEEQYQVDIVKAFPYEKIYIQGYFYSKPVDIETLKDFKFKDS
>NZ_LS483461.1|WP_111693872.1|1164085_1164706_+|flavodoxin-family-protein
MKVLLVNGSPNKEGCTYTALKEVSKTLEENGIDTEIFQVGNKPIGGCIGCGSCKKTGECFMKDGVNEFVEKAKDADGFVFGSPVYYAAASGSITSFLDRAFYSGGKHMAFKPGAVICSARRAGTTSTLDQLSKYLTICNMPVVSSQYWNMVHGNTPEEVKKDLEGMQTMRVLGRNMAWLIKCIELGKKNNILKPELEERERTNFIR
>NZ_LS483461.1|WP_011590441.1|1165148_1165574_+|hypothetical-protein
MESKEMRLAKKAKKLIDEFERVQSVLLSGELSDQEVEIRDDGATIVLKNIMPGYSGEAMFKLTHISDVVKAYIDHMDEENDEMIKSYEVENTNWHESDLGDIYRESAMEHLEKVEVVGDKVRHTYKELKKIEEKAREIEGL
>NZ_LS483461.1|WP_111693873.1|1165904_1167716_+|ribonucleoside-triphosphate-reductase
MYNVSINKRDVKKDVKNMLSSKKIVDDYIKKIDWRVNENSNSPYSFGSLNKHIIAEVSKDYWLNEVYKDKRIIDAYKNGDMHIHDLGGLTLYCCGYSLRNIILMGVQGIPNIPTSSPAKHFDAILNQIANLVTIYQNEIMGAVAFNSFDTLLAPYIKKDNLTYEEVKQNLQNFIFSINSNSRAGAEPAFTNITFDLFPPKDLENDPALIGDKIQEFTYKECQKEMDMLNKAFYELMNEGDYNGRPFSYPIPTYNINSNFDFDNPNNDMLFEMTGKFGYPYFANFVNSDMDQSDVRSMCCRLNLDLRELRKRNGGLFGSGDSTGSIGVVTINLPRLAYKHKNNEKEFFNALKEILIIAKDSLEKKRKWLNDNIINKDMLPAFSTYVGTLKNHFSTIGIVGLNEMCENFNGNNILTEEGMEFSIKVCNFIREELINFQEETGNLYNFEATPAESTCYRLAKKDVEDFEDIIVRGVREYPYYTNSCHMPPNEVKNLKQLFDHQDKLQVLFTGGTVVHIYCDGAISGEKAKHIVKTVCKKYRTPYVSISPLNRYCEEHGYVKERVEECPICGKKLDLYQRITGYLRKVEFFNDGKKSEFKDRNQLSL
>NZ_LS483461.1|WP_011590444.1|1167712_1168171_+|4Fe-4S-cluster-binding-domain-containing-protein
MIIKTKGIVHERVEDAPFMGALISAVDCNLNCKGCFNQHLKDLPNIEMDSEDILDKVTNDPFNEGIILAGLEWSLQPKELREMVNSARKRNLKVIVYSGLSEEDFKKKFPDIYGLKGDMYFKFGKYDEKLKVNNNIQYDVKLATSNQKILKK
>NZ_LS483461.1|WP_057231030.1|1168365_1169088_+|hypothetical-protein
MKDRKASKYHSRSSRVFAPVHINSKGVIDYKLPLCDLMDSILSKKSFNTSVITETLDGNQYYYDYDFDGKNIIVSKSQIIKDSPGLKLIERYKGNYLGKELYNDSIVLVLYKDDKKVTETISYKKDLGLNVDMVIEVGSYFYKLPLCEFMDNIIRKTPDILKFIYFGFEGDMYYITLEFDGKDINYIKYSVNNSKLDEIEKAIGNRLVKEFSGHNNIILSLYDDNTRVKDIVAYSSKFLY
>NZ_LS483461.1|WP_111693874.1|1169661_1170447_-|phosphorylase
MYNFLIDGHKKYGLKKDTLCKSVLKCNDEAIKENVIIAPWWEPTIFKDIESELIVDTSIKIWNCKLFDKNITYIKTGIGASVCTDVILALGNSNCKKIIFIGSVGALDEKINIGDIIIPTLSVCGDGVCRYLEKDLTKDCFGEKYYPDTKLNKILIKNTEKICKDNNISYHIVPNFSVDTIFAQFAHLDYIMKLGCKSIEMETAAAFKACSICNIPISAIFNVSDNSIKNKSIYNGKTESELKYRKKVRNEIIPKIIYSLL
>NZ_LS483461.1|WP_111693875.1|1170654_1171173_+|ClbS/DfsB-family-four-helix-bundle-protein
MRTYENKEELKKEIDKYYKKYIAEFDNIPNDLKDVRCEEVDRTPAENLAYQIGWTTLILKWEKDEKAGLKVKTPSDKFKWNQLGDLYNWFNEEYAFLSLSQLKLLLAENIENIYKMIDSMSNDELFKPHQRIWADEATKTAVWEVYKFIHVNTVAPFGTFRTKIRKWKKLML

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Crispr_ID: NZ_LS483461_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LS483461_4

1179493-1179713

Orphan

Consensus_repeat	Method
GTTAAAAAGATATTATGATAAATTT	CRISPRCasFinder

3 spacers

The CRISPR arrays of NZ_LS483461_4

>merge|NZ_LS483461|4|1179493-1179713|CRISPRCasFinder
TCTAATGAGCTTTTGTGATAAATCTTTCCTTAAATTTTCTTATTAAAGAAACTTACATAGCAAGGGTTAAAAAGATATTATGATAAATTTACTTGTGAGAATCAAGCTTATACCTAATCAATTTAGTAATGTTAAGAAGATATTATGATAAATTTTCTTTTAAATGATGCTAATATATTAAGTGTAGGAAAATAAGTTTAATAAGTTCTTATAATAAATAC

>NZ_LS483461|4|4|1179493-1179713|CRISPRCasFinder
TCTAATGAGCTTTTGTGATAAATCT	TTCCTTAAATTTTCTTATTAAAGAAACTTACATAGCAAGG
GTTAAAAAGATATTATGATAAATTT	ACTTGTGAGAATCAAGCTTATACCTAATCAATTTAGTAAT
GTTAAGAAGATATTATGATAAATTT	TCTTTTAAATGATGCTAATATATTAAGTGTAGGAAAATAAG
TTTAATAAGTTCTTATAATAAATAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LS483461.1\|WP_111693884.1\|1182958_1184722_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|183088
NZ_LS483461.1\|WP_111693877.1\|1172068_1172383_+\|DUF3784-domain-containing-protein	unknown	unknown	gnl\|CDD\|378903
NZ_LS483461.1\|WP_111693886.1\|1186292_1186676_+\|SdpI-family-protein	unknown	unknown	gnl\|CDD\|379303
NZ_LS483461.1\|WP_041702640.1\|1178644_1179265_-\|CPBP-family-intramembrane-metalloprotease	unknown	unknown	gnl\|CDD\|376806
NZ_LS483461.1\|WP_111693889.1\|1188059_1188836_+\|DUF1311-domain-containing-protein	unknown	unknown	gnl\|CDD\|226278
NZ_LS483461.1\|WP_111693874.1\|1169661_1170447_-\|phosphorylase	unknown	unknown	gnl\|CDD\|350158
NZ_LS483461.1\|WP_111693879.1\|1173445_1174192_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_111693890.1\|1188885_1189188_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_111693875.1\|1170654_1171173_+\|ClbS/DfsB-family-four-helix-bundle-protein	unknown	unknown	gnl\|CDD\|226733
NZ_LS483461.1\|WP_111693876.1\|1171209_1172013_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293837
NZ_LS483461.1\|WP_111693885.1\|1184725_1186267_+\|McrC-family-protein	unknown	unknown	gnl\|CDD\|370821
NZ_LS483461.1\|WP_111693888.1\|1187368_1187758_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_111693883.1\|1182452_1182764_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_111693880.1\|1174405_1175551_-\|exo-alpha-sialidase	unknown	unknown	gnl\|CDD\|271234
NZ_LS483461.1\|WP_111693882.1\|1181151_1182306_+\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_111693887.1\|1186766_1187324_-\|flavin-reductase-family-protein	unknown	unknown	gnl\|CDD\|224766
NZ_LS483461.1\|WP_011590494.1\|1177960_1178254_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|183800
NZ_LS483461.1\|WP_003454100.1\|1180430_1180823_+\|DUF4440-domain-containing-protein	unknown	unknown	gnl\|CDD\|227327
NZ_LS483461.1\|WP_111693878.1\|1172541_1173270_-\|carbon-nitrogen-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|143587
NZ_LS483461.1\|WP_111693881.1\|1176328_1177537_+\|YkgJ-family-cysteine-cluster-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_LS483461.1\|WP_111693884.1\|1182958_1184722_+\|AAA-family-ATPase	gnl\|CDD\|183088	PRK11331, PRK11331, 5-methylcytosine-specific restriction enzyme subunit McrB; Provisional.	1.26629e-39
NZ_LS483461.1\|WP_111693877.1\|1172068_1172383_+\|DUF3784-domain-containing-protein	gnl\|CDD\|378903	pfam12650, DUF3784, Domain of unknown function (DUF3784). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 96 and 110 amino acids in length.	2.61808e-14
NZ_LS483461.1\|WP_111693886.1\|1186292_1186676_+\|SdpI-family-protein	gnl\|CDD\|379303	pfam13630, SdpI, SdpI/YfhL protein family. This family of proteins includes the SdpI and YfhL proteins from B. subtilis. The SdpI protein is a multipass integral membrane protein that protects toxin-producing cells from being killed. Killing is mediated by the exported toxic protein SdpC an extracellular protein that induces the synthesis of an immunity protein.	1.454e-16
NZ_LS483461.1\|WP_041702640.1\|1178644_1179265_-\|CPBP-family-intramembrane-metalloprotease	gnl\|CDD\|376806	pfam02517, Abi, CAAX protease self-immunity. Members of this family are probably proteases (after a isoprenyl group is attached to the Cys residue in the C-terminal CAAX motif of a protein to attach it to the membrane, the AAX tripeptide being removed by one of the CAAX prenyl proteases). The family contains the CAAX prenyl protease. The proteins contain a highly conserved Glu-Glu motif at the amino end of the alignment. The alignment also contains two histidine residues that may be involved in zinc binding. While they are involved in membrane anchoring of proteins in eukaryotes, little is known about their function in prokaryotes. In some known bacteriocin loci, Abi genes have been found downstream of bacteriocin structural genes where they are probably involved in self-immunity. Investigation of the bacteriocin-like loci in the Gram positive bacteria locus from Lactobacillus sakei 23K confirmed that the bacteriocin-like genes (sak23Kalphabeta) exhibited antimicrobial activity when expressed in a heterologous host and that the associated Abi gene (sak23Ki) conferred immunity against the cognate bacteriocin. Interestingly, the immunity genes from three similar systems conferred a high degree of cross-immunity against each other's bacteriocins, suggesting the recognition of a common receptor. Site-directed mutagenesis demonstrated that the conserved motifs constituting the putative proteolytic active site of the Abi proteins are essential for the immunity function of Sak23Ki - thus a new concept in self-immunity.	7.04878e-19
NZ_LS483461.1\|WP_111693889.1\|1188059_1188836_+\|DUF1311-domain-containing-protein	gnl\|CDD\|226278	COG3755, COG3755, Uncharacterized protein conserved in bacteria [Function unknown].	4.41958e-08
NZ_LS483461.1\|WP_111693874.1\|1169661_1170447_-\|phosphorylase	gnl\|CDD\|350158	cd09007, NP-I_spr0068, uncharacterized subfamily of the nucleoside phosphorylase-I family. This subfamily is composed of uncharacterized members including Streptococcus pneumoniae hypothetical protein spr0068. The nucleoside phosphorylase-I (NP-I) family members accept a range of purine nucleosides as well as the pyrimidine nucleoside uridine. The NP-1 family includes phosphorolytic nucleosidases such as purine nucleoside phosphorylase (PNP, EC. 2.4.2.1), uridine phosphorylase (UP, EC 2.4.2.3), and 5'-deoxy-5'-methylthioadenosine phosphorylase (MTAP, EC 2.4.2.28), and hydrolytic nucleosidases such as AMP nucleosidase (AMN, EC 3.2.2.4) and 5'-methylthioadenosine/S-adenosylhomocysteine (MTA/SAH) nucleosidase (MTAN, EC 3.2.2.16). Members of the NP-I family display different physiologically relevant quaternary structures: hexameric (trimer-of-dimers arrangement of Shewanella oneidensis MR-1 UP); homotrimeric (human PNP and Escherichia coli PNPII or XapA); hexameric (with some evidence for co-existence of a trimeric form) such as E. coli PNPI (DeoD); or homodimeric such as human and Trypanosoma brucei UP. The NP-I family is distinct from nucleoside phosphorylase-II, which belongs to a different structural family.	1.09927e-22
NZ_LS483461.1\|WP_111693875.1\|1170654_1171173_+\|ClbS/DfsB-family-four-helix-bundle-protein	gnl\|CDD\|226733	COG4283, COG4283, Uncharacterized conserved protein [Function unknown].	2.14458e-72
NZ_LS483461.1\|WP_111693876.1\|1171209_1172013_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293837	cd16279, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).	1.71173e-16
NZ_LS483461.1\|WP_111693880.1\|1174405_1175551_-\|exo-alpha-sialidase	gnl\|CDD\|271234	cd15482, Sialidase_non-viral, Non-viral sialidases. Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates, they play vital roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed, beta-propeller fold with the non-viral sialidases containing 2-5 Asp-box motifs (most commonly Ser/Thr-X-Asp-[X]-Gly-X-Thr- Trp/Phe). This CD includes eubacterial and eukaryotic sialidases.	3.09796e-66
NZ_LS483461.1\|WP_111693887.1\|1186766_1187324_-\|flavin-reductase-family-protein	gnl\|CDD\|224766	COG1853, COG1853, Conserved protein/domain typically associated with flavoprotein oxygenases, DIM6/NTAB family [General function prediction only].	6.16502e-36
NZ_LS483461.1\|WP_011590494.1\|1177960_1178254_-\|hypothetical-protein	gnl\|CDD\|183800	PRK12863, PRK12863, YciI-like protein; Reviewed.	0.000563911
NZ_LS483461.1\|WP_003454100.1\|1180430_1180823_+\|DUF4440-domain-containing-protein	gnl\|CDD\|227327	COG4994, COG4994, Uncharacterized protein conserved in bacteria [Function unknown].	7.57805e-30
NZ_LS483461.1\|WP_111693878.1\|1172541_1173270_-\|carbon-nitrogen-hydrolase-family-protein	gnl\|CDD\|143587	cd07197, nitrilase, Nitrilase superfamily, including nitrile- or amide-hydrolyzing enzymes and amide-condensing enzymes. This superfamily (also known as the C-N hydrolase superfamily) contains hydrolases that break carbon-nitrogen bonds; it includes nitrilases, cyanide dihydratases, aliphatic amidases, N-terminal amidases, beta-ureidopropionases, biotinidases, pantotheinase, N-carbamyl-D-amino acid amidohydrolases, the glutaminase domain of glutamine-dependent NAD+ synthetase, apolipoprotein N-acyltransferases, and N-carbamoylputrescine amidohydrolases, among others. These enzymes depend on a Glu-Lys-Cys catalytic triad, and work through a thiol acylenzyme intermediate. Members of this superfamily generally form homomeric complexes, the basic building block of which is a homodimer. These oligomers include dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers, as well as variable length helical arrangements and homo-oligomeric spirals. These proteins have roles in vitamin and co-enzyme metabolism, in detoxifying small molecules, in the synthesis of signaling molecules, and in the post-translational modification of proteins. They are used industrially, as biocatalysts in the fine chemical and pharmaceutical industry, in cyanide remediation, and in the treatment of toxic effluent. This superfamily has been classified previously in the literature, based on global and structure-based sequence analysis, into thirteen different enzyme classes (referred to as 1-13). This hierarchy includes those thirteen classes and a few additional subfamilies. A putative distant relative, the plasmid-borne TraB family, has not been included in the hierarchy.	1.92717e-20
NZ_LS483461.1\|WP_111693885.1\|1184725_1186267_+\|McrC-family-protein	gnl\|CDD\|370821	pfam10117, McrBC, McrBC 5-methylcytosine restriction system component. Members of this family of bacterial proteins modify the specificity of mcrB restriction by expanding the range of modified sequences restricted.	2.06825e-94

>NZ_LS483461.1|WP_041702640.1|1178644_1179265_-|CPBP-family-intramembrane-metalloprotease
MLVYLLIYKCKKYNKNKIINKLPRKDIPKYALISMGMGGLSALWLIFADTILSSITLVKNSLQNFSQISESLNNEAYIFIFLSVILFGPIVEELLFRGLIFNEIDKIKGGAAPIILSGLLFGLFHREPVQVVYASILGIILGFVYSKTRSLPLVIFMHMLNNLVATLPPPLAKHEILQFVNGFQIISIVPMAYLLSKLYKKGSLTN
>NZ_LS483461.1|WP_011590494.1|1177960_1178254_-|hypothetical-protein
MKYFIVEGILKDSDKINEDIMKKHMAYTQKAMDEGMILVSGLKSDMSGGIFVIKSESVEKLESYLSKEPFKLYGIQDYKFVEFNAHYFNPSPSEWFK
>NZ_LS483461.1|WP_111693881.1|1176328_1177537_+|YkgJ-family-cysteine-cluster-protein
MKVRVPNYFNEFKCIASECEDTCCAGWEIVIDDETHKRYENVEGDFGNILRSKIVKSDGENIFLLNNGNCSFLNEKKMCEIYINLGEDHLCYTCQQFPRYTEEFLDLKEVGLSLSCPEAARIILRKAENTTFNLSASENSECFDSSNNAVDSFTEDEDCFDEGIDEEVLSEFLECRNIVFNIIERNDLDLGTKAALALEFVKEVQNKIDLGDMDEIPELMEEYRDENFINTLLKELECFKGKESIKHKNLCEYLNVYKSIKHINSNDPLGLEKALKYFEGNEEFYLRKHKEFNEYYKENLYKFKNILVYFIFRYFMKAIFDYDVSAKIKLAIISTLMIKELAVVRFIENNNEFTEEDMVEVSRIYSKDIEHSDENIENLQEIFETEEIFEVDEILPMLMNDF
>NZ_LS483461.1|WP_111693880.1|1174405_1175551_-|exo-alpha-sialidase
MCNKNNTFEKNLDISHKPEPLILFDRDNNIWNSKYFRIPNIQLLNDGTILTFSDIRYNGPDDHAYIDIASARSTDFGKTWNYDIAMKNNRIDSTYSRVMDSTTVITNTGRIILIAGSWNTNGNWAMTTSTRRSDWSVQMIYSDDNGLTWSNKIDLTKDSSKVKNQPSNTIGWLGGVGSGIVMDDGTIVMPAQISLRENNENNYYSLIIYSKDNGETWTMGNKVPNSNTSENMVIELDGALIMSTRYDYSGYRAAYISHDLGNTWEIYEPLNGKVLTGKGSGCQGSFIKATTSNGHRIGLISAPKNTKGEYIRDNIAVYMIDFDDLSKGVQEICIPYPEDGNKLGGGYSCLSFKNGHLAIVYEANGNIEYQDLTPYYLLINN
>NZ_LS483461.1|WP_111693879.1|1173445_1174192_+|hypothetical-protein
MRRYKMVIISIIILLLINNIMHSKVSYALDIANSKNQVLLSEIPNEEIYLYALDSDEGKGVYEDILLNVKGKKKRFNWIVDSGLSFRPELMLTDINNDGKKELVIIITTGHGTGINTQEVHIFKEETLEEINVQNPFDIISKNVKTKVYKDENSVKVYININGKESVISSKKLNELYNDQNNKKNFGDTLFFRDFLIYEVHNEKLKAIVGGDIFFWNYIIDVKIEYKFESNMLVVDKIYFDVTEYFKD
>NZ_LS483461.1|WP_111693878.1|1172541_1173270_-|carbon-nitrogen-hydrolase-family-protein
MKIGLASKEFINKDIEKNTDTIIKSMIEAKENNAHMICFGEAFLQGFDSLSWNYEKDKEIALSLSSLPIKTLCDYAKKIGICVSFGYIENYKGLLYCSYITINENGEIINNFKRVSPGWKESYADPTHYKEGDTFPTFKYKDLTFSVGLCGDFWHEKNIDMVSKIKKDIVLWPLFVDFNIQEFESQYKKEYAEQANKLKSKVLFINSISKESKAFGGCFEFLNGDILNKLPIGTEGILYVEI
>NZ_LS483461.1|WP_111693877.1|1172068_1172383_+|DUF3784-domain-containing-protein
MSIKILMIALFILLGIMFSLGKWSFLIAGFNTMTKEEKAKYDVMSLCKFMGKLMFIIAFCITLFTLSDIFMMKILFNIGTVILIVSIIFVIIYANTGNRFERKN
>NZ_LS483461.1|WP_111693876.1|1171209_1172013_+|MBL-fold-metallo-hydrolase
MKFRIVGSGGCISLPKPLCNCEVCKEARSKGRPYSRCGCSLFLDDINLLVDTPEDITYGINYCDIKEIDRVLFSHVDPDHTLGMRVFEHLRLNWLDVSCGKNCEKPIEVFALEDVMKDINSIGFKFGSYLDYYENVRNLIKRKSVEDYISIKDIKVSFIKVNHATVFVFEKEGKKLIYAPCDVKPFPKSKLFLDADCLIIGNTIVGGVLKDGFILKEDNPLRDELFTISDIEELKNKYNIKRVIITHLEEDWGKSYDDYVELEKGLD
>NZ_LS483461.1|WP_111693875.1|1170654_1171173_+|ClbS/DfsB-family-four-helix-bundle-protein
MRTYENKEELKKEIDKYYKKYIAEFDNIPNDLKDVRCEEVDRTPAENLAYQIGWTTLILKWEKDEKAGLKVKTPSDKFKWNQLGDLYNWFNEEYAFLSLSQLKLLLAENIENIYKMIDSMSNDELFKPHQRIWADEATKTAVWEVYKFIHVNTVAPFGTFRTKIRKWKKLML
>NZ_LS483461.1|WP_111693874.1|1169661_1170447_-|phosphorylase
MYNFLIDGHKKYGLKKDTLCKSVLKCNDEAIKENVIIAPWWEPTIFKDIESELIVDTSIKIWNCKLFDKNITYIKTGIGASVCTDVILALGNSNCKKIIFIGSVGALDEKINIGDIIIPTLSVCGDGVCRYLEKDLTKDCFGEKYYPDTKLNKILIKNTEKICKDNNISYHIVPNFSVDTIFAQFAHLDYIMKLGCKSIEMETAAAFKACSICNIPISAIFNVSDNSIKNKSIYNGKTESELKYRKKVRNEIIPKIIYSLL
>NZ_LS483461.1|WP_003454100.1|1180430_1180823_+|DUF4440-domain-containing-protein
MDSIKEQIFQLENDLIKSEVRKSAEKINEILSNDFVEFSSSGSEYHYKCGDVFQDEEDERTLDWEILNFKVKKVAENCILATYRVIKHDELDERKRYSLRSSLWTEENGKWKMSFHQGTLLAGKEGRSIF
>NZ_LS483461.1|WP_111693882.1|1181151_1182306_+|hypothetical-protein
MKHKKEVFIAALIIVFLIAIGPSIKKQVGIYTKGKNIDKSYSKDSLYDIYITNGEGLGLIQISNVQKGNINYSKIDNINVKYDSANFLFIEKDSRGNIYVPYSSDIENPKNANRLLIFNGGKLEDEIEFDDIRNPQTVISDRENNRVFLEQNITVQPEDSQGLKLKVIDTTSKEVIKELYLKGYIRDYYVGEKEIVLSLEGAKKLGFLDAQDRSLYAINRKTLDGREISKEPICNVVNALCGDSKGNNVIFANITLKESGDLDKNEIIVMDSQGEIKERKEVLYDMNGNFYGNEKYEYVLNGKIHNKNNGFLIFNKETLEFEKLVDDVKDISYIESLDDYLFILTRDSKLFIYDENTLEQIGSIELKGEVSHRMKVINRKVKLS
>NZ_LS483461.1|WP_111693883.1|1182452_1182764_+|hypothetical-protein
MGKGSVEINIDRVIFIGLIIEFICTAFIFFYFTTLYENLNLIIDCLMILNVIIFILSIIYFKYNKKLALRYTIISLIFFFFSDKSMYSLILVIILIMQGKGMY
>NZ_LS483461.1|WP_111693884.1|1182958_1184722_+|AAA-family-ATPase
MDKIKNEVTKEVKDLTKEDYLSILEFLKNHAGEEYSNPENEENIEEKNKYIALREEAQETLSKFRAIGDLFKEEGLVYEKKGASKWLVAARVTRVRNYLWIELKEPEKIGFSTSISIFADKIEEGNKLRFRVVLETKDLKSDEGDYVRHFRFLEELDPYEDKFEYWDNYSDYSYLERGKTSDIRALIQDVKERKELKLQIGRTLYYEEVKRISKEEIREFFEEAVRELKPYYDLAVEGEYFLSSEEELGINEDGEEYLEEPKILKVKNQILYGPPGTGKTYNAINRALEIIDFKKYKELIGNEGKRGEAIKVFNELLDEGQIAFCTFHQSYGYEDFVEGLRSNESGAGFVPKDGIFKKLCRKASKSPKNHVLIIDEINRGNISKIFGELITLIEDDKRLGEKNQLKVTLPYSNESFGVPKNLYILGTMNTADRSIALLDTALRRRFEFFEYMPKEELLPEDACGINLREFLRVINERIEYLFDREHTIGHSYFLKEDLTFEELVSIMKNKIIPLVQEYFYGDWEKVELVLGGACKKGRANRFIEKSRIDTRKLFKGMGVDSYGEEYKYSIVENPEKEAFLNIYEDEE
>NZ_LS483461.1|WP_111693885.1|1184725_1186267_+|McrC-family-protein
MRHIIIKESYESLRIVDDFILDKIREQGDLESRKDSEKDRNHLERLNLGDEKSNDFYNHIEKDYDKEDYGKEILKNKSDFIKKNSGETFYESRDVFNEGEEDFYGNYSCEKIISRREAHELYNYAMSKKLDMDNILWERDTLRFINYVGYMRLSTVSIEILPKISINHSAELERKALLNMLSKCGVLKVNYSEISSLKLYKQSLNEILAYLFSEKLQKELGKGVYGEYVYIEENINSLKGSLRVQEQIKNMASHSSKAFCRFEEFSRDNKLNKILSFFVKEVMKSVKNRETLRLLRISEMILGDVDERNVTLNEVNNFSFNRLNKPFEDAFTLGKMIVLGESALGNLGGNKAYSILFKMNEIFEIYIGKLLRELLYKETVHMQHSKYKLLVKEESNRGVFKLIPDIVIEKNGIERVIIDTKWKSVESKFNRHGVKREDLYQMYAYLTRYKNARTVILIYPYNERIEGEDGEYLESWYLEDDQHKRLRVYAVNLENEKETLKSLDKIVRKYVEE
>NZ_LS483461.1|WP_111693886.1|1186292_1186676_+|SdpI-family-protein
MGFWIFMMVMELLIPLIMIIFGKLFSKKAPKEINHFYGYRTSMSMKNKDTWEFAHKYCGRLWLKIGSIMFAISFIIMLFVLGRGEQAIGTLGGALCMIQCVVLVASIFPTERALRKNFDKYGNRKNV
>NZ_LS483461.1|WP_111693887.1|1186766_1187324_-|flavin-reductase-family-protein
MSKVKFNKLPLVYPIPSVLIGTVINDKSNFATIGNCGIISVNPAVIYISMEKDHYTNKGIRENQVFSINIPSADLVDKVDYCGLVSGNNIDKSQVFKCFYESNNKIPLIEECPINMECKVTKIIEIYDMEVFIGEIIETYVNEDLLTNGFPDTKKINPLIYSMDNNYWEIGDFVGNAFNIGKNIK
>NZ_LS483461.1|WP_111693888.1|1187368_1187758_-|hypothetical-protein
MDDLILKRCKYCDKTYEGTNESCCCSEPCNIKYQKYMKQREKTETPVKIFSIILLLIFFINIMFLPNNPISKYLFIAISLIAPALHVIFPFGEDKGLQKRGVKKTKILFRTIWGTVLIYILTYYFLEQF
>NZ_LS483461.1|WP_111693889.1|1188059_1188836_+|DUF1311-domain-containing-protein
MKKRNYLISLLAVVLSLGVLVGCGDKTNTSNEGASVNSSENSDAASSKDSADVVKDKGESDKAQAKDADSKDKEATNKDESEKKEEDIKNDSSTKETAKVDNSNKKESKGASNSSKKEESKSASKKENSKDESSLAKAKSEYLKKMKKIDSESEKLDKEYDSNRGSTQAGMNGISGEQAKLYDNELNKIYDYLKQNLSKEKAKELEKSEMAWIKEKESNIAEIKKQYEGGSVTPLMVNSEVAKESKERCYYLIDNYMK
>NZ_LS483461.1|WP_111693890.1|1188885_1189188_+|hypothetical-protein
MKEFFLDILPSILLVIVLFLVLNDFRNNKNLKRNKRYSKESDDINKKEGKRVDYMSIGMCFGVAISIFFIRKFGSIALTYGILCGMLLGKFVGVIVKRNF

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Crispr_ID: NZ_LS483461_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_LS483461_5

2316688-2316800

Orphan

Consensus_repeat	Method
TTCTATTTAAATCTATTACTTTACATAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_LS483461_5

>merge|NZ_LS483461|5|2316688-2316800|CRISPRCasFinder
TTCTATTTAAATCTATTACTTTACATAAGAAATTATTCTAATTATTTTTAAAATAATAAATCTTTTTTGGAGACCTCTTCTTCTCTTCTATTTAAATTTATTACTTTACATAA

>NZ_LS483461|5|5|2316688-2316800|CRISPRCasFinder
TTCTATTTAAATCTATTACTTTACATAA	GAAATTATTCTAATTATTTTTAAAATAATAAATCTTTTTTGGAGACCTCTTCTTCTC
TTCTATTTAAATTTATTACTTTACATAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_LS483461.1\|WP_003470736.1\|2312010_2312616_-\|stage-III-sporulation-protein-AG	unknown	unknown	gnl\|CDD\|274319
NZ_LS483461.1\|WP_003451406.1\|2314378_2314765_-\|stage-III-sporulation-protein-AD	unknown	unknown	gnl\|CDD\|131896
NZ_LS483461.1\|WP_003451536.1\|2311487_2311985_-\|SpoIIIAH-like-family-protein	unknown	unknown	gnl\|CDD\|378918
NZ_LS483461.1\|WP_003451671.1\|2314852_2315050_-\|stage-III-sporulation-protein-AC	unknown	unknown	gnl\|CDD\|131895
NZ_LS483461.1\|WP_003458670.1\|2315125_2315641_-\|stage-III-sporulation-protein-SpoAB	unknown	unknown	gnl\|CDD\|131880
NZ_LS483461.1\|WP_003451649.1\|2317346_2317904_-\|elongation-factor-P	unknown	unknown	gnl\|CDD\|234788
NZ_LS483461.1\|WP_003470903.1\|2320226_2320739_-\|type-II-secretion-system-protein	unknown	unknown	gnl\|CDD\|225076
NZ_LS483461.1\|WP_003458748.1\|2318074_2318422_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003471076.1\|2318818_2319430_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003471039.1\|2320758_2321187_-\|prepilin-type-N-terminal-cleavage/methylation-domain-containing-protein	unknown	unknown	gnl\|CDD\|236714
NZ_LS483461.1\|WP_003470631.1\|2313195_2314368_-\|stage-III-sporulation-protein-AE	unknown	unknown	gnl\|CDD\|213743
NZ_LS483461.1\|WP_003451410.1\|2311013_2311403_-\|Asp23/Gls24-family-envelope-stress-response-protein	unknown	unknown	gnl\|CDD\|377129
NZ_LS483461.1\|WP_070957028.1\|2318418_2318859_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003470719.1\|2310487_2310895_-\|transcription-antitermination-factor-NusB	unknown	unknown	gnl\|CDD\|234686
NZ_LS483461.1\|WP_003470769.1\|2321179_2322199_-\|type-II-secretion-system-F-family-protein	unknown	unknown	gnl\|CDD\|224376
NZ_LS483461.1\|WP_003451464.1\|2316870_2317233_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003451372.1\|2319404_2319755_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003470945.1\|2319801_2320092_-\|hypothetical-protein	unknown	unknown	unknown
NZ_LS483461.1\|WP_003470968.1\|2315787_2316672_-\|stage-III-sporulation-protein-AA	unknown	unknown	gnl\|CDD\|274324
NZ_LS483461.1\|WP_003470595.1\|2312630_2313188_-\|stage-III-sporulation-protein-AF	unknown	unknown	gnl\|CDD\|131942

Protein	Function_ID	Function_description	E-value
NZ_LS483461.1\|WP_003470736.1\|2312010_2312616_-\|stage-III-sporulation-protein-AG	gnl\|CDD\|274319	TIGR02830, Stage_III_sporulation_protein_AG, stage III sporulation protein AG. CC A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is found in a spore formation operon and is designated stage III sporulation protein AG. [Cellular processes, Sporulation and germination].	1.54475e-69
NZ_LS483461.1\|WP_003451406.1\|2314378_2314765_-\|stage-III-sporulation-protein-AD	gnl\|CDD\|131896	TIGR02849, Stage_III_sporulation_protein_AD, stage III sporulation protein AD. Members of this family are the uncharacterized protein SpoIIIAD, part of the spoIIIA operon that acts at sporulation stage III as part of a cascade of events leading to endospore formation. Note that the start sites of members of this family as annotated tend to be variable; quite a few members have apparent homologous protein-coding regions continuing upstream of the first available start codon. The length of the alignment and the scoring cutoff thresholds for the model have been set to try to detect all valid members of the family, even if annotation of the start site begins too far downstream. [Cellular processes, Sporulation and germination].	5.58273e-33
NZ_LS483461.1\|WP_003451536.1\|2311487_2311985_-\|SpoIIIAH-like-family-protein	gnl\|CDD\|378918	pfam12685, SpoIIIAH, SpoIIIAH-like protein. Stage III sporulation protein AH (SpoIIIAH) is a protein that is involved in forespore engulfment. It forms a channel with SpoIIIAH that is open on the forespore end and closed (or gated) on the mother cell end. This allows sigma-E-directed gene expression in the mother-cell compartment of the sporangium to trigger the activation of sigma-G forespore-specific gene expression by a pathway of intercellular signaling. This family of proteins is found in bacteria, archaea and eukaryotes and so must have a wider function that in sporulation. Proteins in this family are typically between 174 and 223 amino acids in length.	3.45938e-23
NZ_LS483461.1\|WP_003451671.1\|2314852_2315050_-\|stage-III-sporulation-protein-AC	gnl\|CDD\|131895	TIGR02848, Stage_III_sporulation_protein_AC, stage III sporulation protein AC. Members of this protein family are designated SpoIIIAC, part of the spoIIIA operon of sporulation genes whose mutant phenotype is linked to sporulation stage III. Members of this family are encoded by the genome of a species if and only if that species is capable of endospore formation, as in Bacillus subtilis. The molecular function of this small, probable integral membrane protein is unknown. [Cellular processes, Sporulation and germination].	1.97477e-14
NZ_LS483461.1\|WP_003458670.1\|2315125_2315641_-\|stage-III-sporulation-protein-SpoAB	gnl\|CDD\|131880	TIGR02833, Stage_III_sporulation_protein_AB, stage III sporulation protein AB. A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is designated stage III sporulation protein AB. [Cellular processes, Sporulation and germination].	1.85407e-76
NZ_LS483461.1\|WP_003451649.1\|2317346_2317904_-\|elongation-factor-P	gnl\|CDD\|234788	PRK00529, PRK00529, elongation factor P; Validated.	2.22205e-107
NZ_LS483461.1\|WP_003470903.1\|2320226_2320739_-\|type-II-secretion-system-protein	gnl\|CDD\|225076	COG2165, PulG, Type II secretory pathway, pseudopilin PulG [Cell motility and secretion / Intracellular trafficking and secretion].	0.00148505
NZ_LS483461.1\|WP_003471039.1\|2320758_2321187_-\|prepilin-type-N-terminal-cleavage/methylation-domain-containing-protein	gnl\|CDD\|236714	PRK10557, PRK10557, prepilin peptidase-dependent protein.	0.00475385
NZ_LS483461.1\|WP_003470631.1\|2313195_2314368_-\|stage-III-sporulation-protein-AE	gnl\|CDD\|213743	TIGR02829, Stage_III_sporulation_protein_AE, stage III sporulation protein AE. A comparative genome analysis of all sequenced genomes of shows a number of proteins conserved strictly among the endospore-forming subset of the Firmicutes. This protein, a member of this panel, is found in a spore formation operon and is designated stage III sporulation protein AE. [Cellular processes, Sporulation and germination].	1.69594e-149
NZ_LS483461.1\|WP_003451410.1\|2311013_2311403_-\|Asp23/Gls24-family-envelope-stress-response-protein	gnl\|CDD\|377129	pfam03780, Asp23, Asp23 family, cell envelope-related function. The alkaline shock protein Asp23 was identified as an alkaline shock protein that was expressed in a sigmaB-dependent manner in Staphylococcus aureus. Following an alkaline shock Asp23 accumulates in the soluble protein fraction of the S. aureus cell. Asp23 is one of the most abundant proteins in the cytosolic protein fraction of stationary S. aureus cells, with a copy-number of >25000 per cell. A second Asp23-family protein, AmaP, which is encoded within the asp23-operon, is required to localize Asp23 to the cell membrane. The overall function for the family is thus a cell envelope-related one in Gram-positive bacteria.	5.69298e-30
NZ_LS483461.1\|WP_003470719.1\|2310487_2310895_-\|transcription-antitermination-factor-NusB	gnl\|CDD\|234686	PRK00202, nusB, transcription antitermination factor NusB.	2.7207e-50
NZ_LS483461.1\|WP_003470769.1\|2321179_2322199_-\|type-II-secretion-system-F-family-protein	gnl\|CDD\|224376	COG1459, PulF, Type II secretory pathway, component PulF [Cell motility and secretion / Intracellular trafficking and secretion].	2.94558e-51
NZ_LS483461.1\|WP_003470968.1\|2315787_2316672_-\|stage-III-sporulation-protein-AA	gnl\|CDD\|274324	TIGR02858, Stage_III_sporulation_protein_AA, stage III sporulation protein AA. Members of this protein are the stage III sporulation protein AA, encoded by one of several genes in the spoIIIA locus. It seems that this protein is found in a species if and only if that species is capable of endospore formation. [Cellular processes, Sporulation and germination].	1.0031e-161
NZ_LS483461.1\|WP_003470595.1\|2312630_2313188_-\|stage-III-sporulation-protein-AF	gnl\|CDD\|131942	TIGR02896, Stage_III_sporulation_protein_AF, stage III sporulation protein AF. This family represents the stage III sporulation protein AF of the bacterial endospore formation program, which exists in some but not all members of the Firmicutes (formerly called low-GC Gram-positives). The C-terminal region of this protein is poorly conserved, so only the N-terminal region, which includes two predicted transmembrane domains, is included in the seed alignment. [Cellular processes, Sporulation and germination].	3.2592e-24

>NZ_LS483461.1|WP_003470968.1|2315787_2316672_-|stage-III-sporulation-protein-AA
MKEIFDVLPDKINSCLKDKSNLNKLQEIRVKVGKPLNIVLDNTETIFNYVIRREDVKAIIQKISNYSLYAFEEDIRQGYITIQGGHRVGLAGQCVIEDNSIKTIRNITSLNIRVCREIVGCSNSLMNSLVENNRVNNTLIISPPKCGKTTLLRDITRNISNGISQIGFKGKRTVVIDERSEIAACYNGIPQMNVGMRTDVYDNCIKSEGMMMAVRGLSPEVIICDEIGTYKDMEGLMMAYNSGVSIIATLHGRNVEELYRRPVFREIVENNIINRVVVLSGKKGIGTIEGIYNV
>NZ_LS483461.1|WP_003458670.1|2315125_2315641_-|stage-III-sporulation-protein-SpoAB
MKVFFLLIIVLLSSLIGYLYGEGFRNRLSQLRELKRALIDFENDIVYTYTPLPESIESIALKAKSPIKELFNEISFKLKNNEVENVYMAFKESINEHKKEMNLRNKDFEILLDLSKSLGETNVEGQIKIFNLAKEKLDIELEIAEDECNKNTKVYRYLGVAVGAMIAIFLV
>NZ_LS483461.1|WP_003451671.1|2314852_2315050_-|stage-III-sporulation-protein-AC
MSDLSLIFQIAGVGIVLVILDKVLDQSGKKEYATLANIVGVVIILTMMIQLISRLFSSVKSMFLF
>NZ_LS483461.1|WP_003451406.1|2314378_2314765_-|stage-III-sporulation-protein-AD
MDVVIQVISFVLISLFLYLVLKDNKSTFAVFLLLGAGIVIFLFVMPYVNEIIAFMQDIARESGMDSSYIAIVMKIIAIAYLSTFCSYICNDAGVTVLGKKVEFTGKIMILLLAIPIMANILNSILSIM
>NZ_LS483461.1|WP_003470631.1|2313195_2314368_-|stage-III-sporulation-protein-AE
MKKLINIILLSLIFVFCFNLKVLANDNLESSKEKIDNDSRIERFYDYINNLETEEDILGNMSAKEYIMNYLESGEDPITLKKIGASILSYIFRELNIVLKFIASILVIALLSALLKNLQDAFNIEEGVTQIAFFACYALLIMLLTKSFFISLNLGKEVLTSIIDFMNVIVPVIVMLIATSGGVTSAVTIDPIVLGAVSITPRIYTYFLFPLILAYFTLQFVNNLSSEFKIDRMCKFIKQVVMISQGFILTIFVGILTLRGMTADTLDAVAVKTVKFAVDNFVPIVGKAFSDAITTVAGYSLAMKSVITSLGVIVLVVIVIYPIIKIGLMAICFKLTSAIIEPVVDSKISSSVETVGEALFMIMSCIISVSIMFFIMASMMATAGNFIVGG
>NZ_LS483461.1|WP_003470595.1|2312630_2313188_-|stage-III-sporulation-protein-AF
MELLKNWISTLCVVIVIISIAHIILPNSSIKKHVKFAFSLIILSVMLSPIIGILTMNKDIDETVFQEKISDVTRSDEEKKSLYDEEAILKSVEKNLEKSLKDEFYENEFEVNLIGKIDFDEVKFNIEKAEITVLDEKKVKKVDKVVVGKEKVNKEEKKDSFLEKIEKFVEKELEISHENIIVSYA
>NZ_LS483461.1|WP_003470736.1|2312010_2312616_-|stage-III-sporulation-protein-AG
MHELKKKIANLFKQKNITNLIILLLLVIMFYLVVSYFTGVNNITKSEKTNLEKVSKEDMNSNSQKDSEVLSYQEKQEKDLERILGKINGVGSVDVVINFQSSEVKVPAVDNSSQKSTTEETDSEGGTRVNSQETDGDKIVMSNSSNGSEPVILKTEKPEVLGVMVVAEGAEDSKIKYEITKAISSLYNISVDKVNVLAMKK
>NZ_LS483461.1|WP_003451536.1|2311487_2311985_-|SpoIIIAH-like-family-protein
MNRKQAGIILTLLALIVCTGVLATRVNNQIKESMGEVPTAFGENDDNATETSSNYFYESRNLREQKDSKTIDNLKAIVEDKNTSAEQKEEAEKELTEKTMARDYETRIELSIKSKGYEDVICFIDGDNAKVVVKTNEELTQEKMVEIQDIVMNVSKVYDVDIEKK
>NZ_LS483461.1|WP_003451410.1|2311013_2311403_-|Asp23/Gls24-family-envelope-stress-response-protein
MNEMNRDEANLGIVNISDEVIGVVAGIAASEIDGILEINHNNSTGIGHKFSKKSLGKGIKVNVENGEAVIEIGVTVQYGIKIPDVVSQVQENVRRTVEAITGLKVALVNIYVQNIIILKEEDKNEILKK
>NZ_LS483461.1|WP_003470719.1|2310487_2310895_-|transcription-antitermination-factor-NusB
MNRVKSREYLLQLAYQMEITSETALETFNSFMENEDISKDDLDLAYIKSGLLGIEENKEKLDSLIESQLVKWKLNRISKVNLSILRISTYEILFAEDVPGKVSINEAIELCKKYSDNKSVSFINGVLDKVYKNMK
>NZ_LS483461.1|WP_003451464.1|2316870_2317233_-|hypothetical-protein
MKDIKNNISNLLKAMDKNTELDKEFKDSLLNVISSLVDKVEELQVNVETLDENVNLLNDDLSGVQDELFEELTLEELEEYDDEYCEVVCDKCHKPIYIEKDILNRSESIPCPYCGNEFEV
>NZ_LS483461.1|WP_003451649.1|2317346_2317904_-|elongation-factor-P
MISGSDLRKGTTFELDGQVYTVIDFLHVKPGKGAAFVRTKLRNVIMGGVTDRTFNPTDKLQEAIIERKEMQYLYSDGELYYFMDQETFEQIPLNHEKVEDAIKFLKENMNAVIKFYKGEAFSVEAPNFVELLITECEPSVKGNTATTAMKTAVVETGATVMVPMFVEEGNTIRIDTRTGEYMERV
>NZ_LS483461.1|WP_003458748.1|2318074_2318422_-|hypothetical-protein
MKKLKLDVTLATIFIVILLVQGIELFQLRNYEIPVLTNSIGEMDLNTVLKNIENKDCTVLQLEYKEGWIGKVLFTGSLEDLSNYVNLLKNNNINIKNYKIEKSEELRCFLELKVV
>NZ_LS483461.1|WP_070957028.1|2318418_2318859_-|hypothetical-protein
MRLEVRRIYIKKYKNFLPIEYVEEYNRKIKKKLNIYILLLLLFNLFFYGKIKTENNKIKNYLSEIKGVNRERSLDKEFLEDINKLKEIIKDEKILNLNLERKSFEVEVNSIYKNSLINYINKINGRVYDISLNESNNTYRLKGELR
>NZ_LS483461.1|WP_003471076.1|2318818_2319430_-|hypothetical-protein
MLIKTLVINDTNDISKLKELKDKRVKIILLNEKIFIETLRVDKKCNIEEKIEQLIRDRFFNYTPLVHYEVLKYNKSLFLIVYFIGCDERFKSLLYERKDFSLTFPELKNKNILSFKKATFELKNLKISIYIKGKLVLLKSVKDSNIIEVIEESLKGLEKDFGVSLKDFTFKIQKEYLKEEIKELFKGLKLNEIRGEENLYQKI
>NZ_LS483461.1|WP_003451372.1|2319404_2319755_-|hypothetical-protein
MIVTILMDNSFQRRKELDRSFKITCHNIDKNNSEEQFLKYMLKEKILNKDTFQELKFSLNNMKAEYSKKARILNIKNKDKISGLSRDTYYEIKVINDDIILSKRGNYEFVNKDLSN
>NZ_LS483461.1|WP_003470945.1|2319801_2320092_-|hypothetical-protein
MYLNHRFWDNMVEYIKINKEKNYIVVKFWRKGIVEENKIEKKEDKLHVYYISSGENRNHILIENVEEFDVVEKKNLFYIKLKVKNQEERIYCYEKA
>NZ_LS483461.1|WP_003470903.1|2320226_2320739_-|type-II-secretion-system-protein
MEDKINKKKGYLLVDMVLALALISILFLGIGKSYSTYIKNNYYIKEKIKVAEIINSLALELKHNISFEDLRSINSGTYKISSLKINDLINSDIKEFLRKNLILHNKNHNDFGWTINISHFDQYESIINIIYKNEKPYISENKEVKIYKFLEKSSQNLENQLQKEEEKHIY
>NZ_LS483461.1|WP_003471039.1|2320758_2321187_-|prepilin-type-N-terminal-cleavage/methylation-domain-containing-protein
MYRKRKGFTLSEVIIYLGITSLILAIPTSFMIIKDRGYELKVEGEISKIHDFLMEAKQLSKKDNLYGEIIFNILDNKLIYENALRTTSLKLNGVKVSFNRDNLITINETGMISIAGTITIIDKNNKQREITIVPGIWKINVK
>NZ_LS483461.1|WP_003470769.1|2321179_2322199_-|type-II-secretion-system-F-family-protein
MFGFKDEASYICLNLSTYVKSGMPIGRSLDLIKNTVKDKKYKESLKRIEKKVLNGEALSKAFKEEGNLYPDLMKDMMKIGEESGNLEEVLEKCARNILAEKEIKNKIIKSLRYPVSLLIGLIIMIFGYVTYILPQFVDMYELREIEGSKIMTLLNNYINFVEENPNVEVIVFCYFSCALILLYLLFKVIPSEKILEKIEVYRMYYEIRILFLINMILNSGISLNNSLSVFGESLSDVKLRKYIKSINEELIKGTTLSSSIGKINVISHVSKGFLITGEESGLFSKNIEELLKIREKDFDRALNKTVGKIEPAMFIILGFVISAMMLLVLVPTFEGMKYV

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

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

853235 : 863421

Synechococcus_phage(28.57%)

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_111693745.1\|853235_857036_+	phosphoribosylformylglycinamidine synthase	A6N228	Microbacterium_phage	1.5e-33	25.0
WP_003453078.1\|857348_857828_+	5-(carboxyamino)imidazole ribonucleotide mutase	A0A2P0VNU7	Tetraselmis_virus	2.6e-28	47.4
WP_003452912.1\|857827_858535_+	phosphoribosylaminoimidazolesuccinocarboxamide synthase	M4SM18	Cyanophage	2.1e-47	43.8
WP_003453151.1\|858853_860299_+	amidophosphoribosyltransferase	A0A1B1ISH6	uncultured_Mediterranean_phage	3.0e-56	32.7
WP_111693746.1\|860299_861301_+	phosphoribosylformylglycinamidine cyclo-ligase	A0A0E3FGG1	Synechococcus_phage	1.5e-70	48.7
WP_087326942.1\|861288_861903_+	phosphoribosylglycinamide formyltransferase	M4QRX9	Synechococcus_phage	4.9e-24	35.6
WP_049039972.1\|861915_863421_+	bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase	Q58MG4	Prochlorococcus_phage	8.8e-67	47.5

DBSCAN-SWA_2

1027865 : 1108695

Clostridium_phage(45.24%)

protease,tail,coat,portal,head,plate,terminase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_111693796.1\|1027865_1028819_+\|protease	serine protease	A0A0E3T7R5	Bacillus_phage	6.9e-17	42.6
WP_111693797.1\|1029144_1030956_+	ABC transporter ATP-binding protein	F2Y302	Organic_Lake_phycodnavirus	5.0e-24	30.4
WP_111693798.1\|1032964_1033462_+	PH domain-containing protein	NA	NA	NA	NA
WP_111693799.1\|1033470_1035153_+	PH domain-containing protein	NA	NA	NA	NA
WP_003449190.1\|1035664_1035949_+	winged helix-turn-helix transcriptional regulator	A0A2H4PQT4	Staphylococcus_phage	2.9e-11	55.4
WP_004457247.1\|1036067_1036466_+	arsenate reductase ArsC	NA	NA	NA	NA
WP_111693800.1\|1036482_1037799_+	MATE family efflux transporter	NA	NA	NA	NA
WP_003449171.1\|1037961_1038630_+	response regulator transcription factor	NA	NA	NA	NA
WP_111693801.1\|1038626_1039637_+	sensor histidine kinase	Q8QNA2	Ectocarpus_siliculosus_virus	3.6e-08	21.0
WP_111693802.1\|1039920_1040631_+	Fic family protein	NA	NA	NA	NA
WP_111693803.1\|1041055_1041667_-	hypothetical protein	NA	NA	NA	NA
WP_111693804.1\|1042057_1043626_+	clostripain	NA	NA	NA	NA
WP_111693805.1\|1044136_1044325_+	hypothetical protein	NA	NA	NA	NA
WP_111693806.1\|1045254_1045662_-	hypothetical protein	NA	NA	NA	NA
WP_111693807.1\|1045666_1046122_-	hypothetical protein	NA	NA	NA	NA
WP_111693808.1\|1046669_1048022_+	hypothetical protein	R9TRQ8	Vibrio_phage	7.3e-28	27.7
WP_003449271.1\|1051118_1051886_+	ABC transporter ATP-binding protein	G9BWD6	Planktothrix_phage	3.4e-38	40.6
WP_111693809.1\|1051875_1053921_+	FtsX-like permease family protein	NA	NA	NA	NA
WP_111693810.1\|1054170_1055709_+	alpha-galactosidase	NA	NA	NA	NA
WP_111693811.1\|1055959_1056262_-	Dabb family protein	NA	NA	NA	NA
WP_111693812.1\|1056524_1057667_+	alanine--glyoxylate aminotransferase family protein	NA	NA	NA	NA
WP_111693813.1\|1057831_1058749_+	hypothetical protein	NA	NA	NA	NA
WP_111693814.1\|1058953_1059493_+	rubrerythrin family protein	NA	NA	NA	NA
WP_111693815.1\|1060018_1063087_+	alpha-mannosidase	NA	NA	NA	NA
WP_111693816.1\|1063343_1063901_-	GNAT family N-acetyltransferase	NA	NA	NA	NA
WP_003449272.1\|1064140_1065313_+	iron-containing alcohol dehydrogenase	NA	NA	NA	NA
WP_003474311.1\|1065626_1066688_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_111693817.1\|1066833_1068003_+	GntP family permease	NA	NA	NA	NA
WP_111693818.1\|1068011_1069523_-	recombinase family protein	M9Q2G2	Clostridium_phage	4.3e-53	31.1
WP_111693819.1\|1069547_1069751_-	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_111693820.1\|1070083_1070443_-	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_111693821.1\|1070718_1070928_+	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_111693822.1\|1070924_1071650_+	ORF6C domain-containing protein	A0A075KJT3	Lactobacillus_phage	7.8e-21	40.8
WP_111693823.1\|1071775_1071967_+	hypothetical protein	NA	NA	NA	NA
WP_111693824.1\|1071960_1072140_+	hypothetical protein	M9Q2G4	Clostridium_phage	2.1e-12	67.8
WP_111693825.1\|1072151_1072700_+	sigma-70 family RNA polymerase sigma factor	M9Q2I8	Clostridium_phage	8.5e-44	54.1
WP_172606775.1\|1072819_1073056_+	hypothetical protein	NA	NA	NA	NA
WP_111693827.1\|1073058_1073301_+	hypothetical protein	NA	NA	NA	NA
WP_172606764.1\|1073314_1073812_+	siphovirus Gp157 family protein	B6CXH7	Clostridium_phage	9.5e-26	41.6
WP_111693829.1\|1073821_1074391_+	ERF family protein	A0A2H4J7J4	uncultured_Caudovirales_phage	2.5e-38	49.7
WP_111693830.1\|1074392_1074581_+	hypothetical protein	NA	NA	NA	NA
WP_111693831.1\|1074598_1075309_+	GntR family transcriptional regulator	A0A0A7RTY6	Clostridium_phage	2.5e-32	59.1
WP_163236374.1\|1075309_1075483_+	hypothetical protein	NA	NA	NA	NA
WP_111693832.1\|1075513_1075984_+	hypothetical protein	F8UBI1	Clostridium_phage	2.2e-16	34.9
WP_111693833.1\|1075984_1076380_+	RusA family crossover junction endodeoxyribonuclease	A0A2K9V3I2	Faecalibacterium_phage	1.2e-18	44.0
WP_111693834.1\|1076391_1076793_+	hypothetical protein	NA	NA	NA	NA
WP_111693835.1\|1076806_1078741_+	PcfJ domain-containing protein	A0A142F1B5	Bacillus_phage	1.1e-16	27.1
WP_172606765.1\|1078760_1078937_+	hypothetical protein	NA	NA	NA	NA
WP_111693836.1\|1078949_1079411_+	hypothetical protein	A0A0A7RUP7	Clostridium_phage	1.7e-13	40.4
WP_003453749.1\|1079410_1079614_+	hypothetical protein	NA	NA	NA	NA
WP_003453684.1\|1079643_1080117_+	DUF722 domain-containing protein	Q0SPJ6	Clostridium_phage	2.3e-21	37.7
WP_003453679.1\|1080626_1080809_+	hypothetical protein	NA	NA	NA	NA
WP_111693837.1\|1080883_1081270_+	hypothetical protein	NA	NA	NA	NA
WP_111693838.1\|1081299_1082166_+\|terminase	terminase small subunit	E5DV49	Deep-sea_thermophilic_phage	2.7e-44	41.6
WP_111693839.1\|1082158_1083415_+\|terminase	PBSX family phage terminase large subunit	B6CXD2	Clostridium_phage	7.3e-99	45.8
WP_111693840.1\|1083426_1084881_+\|portal	phage portal protein	A0A1S5SAF3	Streptococcus_phage	6.4e-139	55.4
WP_111693841.1\|1084873_1085794_+\|head	head protein	D2J057	Enterococcus_phage	3.7e-60	41.4
WP_111693842.1\|1085984_1086230_+	hypothetical protein	A0A1S5SCQ9	Streptococcus_phage	3.0e-09	50.7
WP_111693843.1\|1086345_1086939_+	phage scaffolding protein	A0A0A7S0J5	Clostridium_phage	5.1e-26	45.7
WP_111693844.1\|1086954_1087791_+\|coat	P22 coat protein - protein 5 domain protein	A0A1L2JY55	Aeribacillus_phage	2.3e-72	52.2
WP_111693845.1\|1087834_1088389_+	hypothetical protein	A0A1S5S8X7	Streptococcus_phage	1.4e-30	44.9
WP_003450361.1\|1088388_1088730_+	hypothetical protein	NA	NA	NA	NA
WP_110060434.1\|1088722_1089163_+	HK97 gp10 family phage protein	A0A1S5SAB8	Streptococcus_phage	4.4e-35	58.3
WP_111693846.1\|1089171_1089537_+	hypothetical protein	A0A1S5SAQ0	Streptococcus_phage	1.6e-14	35.7
WP_111693847.1\|1089546_1090182_+	hypothetical protein	A0A1S5S9Y8	Streptococcus_phage	2.5e-63	60.2
WP_111693848.1\|1090234_1090612_+	hypothetical protein	A0A1S5SAG5	Streptococcus_phage	4.4e-15	38.3
WP_111693849.1\|1090677_1090887_+	peptide methionine sulfoxide reductase	NA	NA	NA	NA
WP_111693850.1\|1090899_1094292_+\|tail	phage tail tape measure protein	A0A0A7S163	Clostridium_phage	1.1e-75	51.4
WP_111693851.1\|1094294_1094993_+\|tail	phage tail protein	Q0SPL3	Clostridium_phage	2.7e-42	45.5
WP_111693852.1\|1095020_1095299_+	hypothetical protein	Q0SPL4	Clostridium_phage	2.0e-25	63.9
WP_003453707.1\|1095362_1095587_+	hypothetical protein	NA	NA	NA	NA
WP_111693853.1\|1095605_1099442_+\|tail	phage tail protein	M9Q2I5	Clostridium_phage	3.5e-75	88.1
WP_111693854.1\|1099457_1099754_+	hypothetical protein	NA	NA	NA	NA
WP_111693855.1\|1099767_1102404_+\|plate	BppU family phage baseplate upper protein	I2E8W5	Clostridium_phage	5.9e-167	56.7
WP_111693856.1\|1102422_1102659_+	hypothetical protein	I2E8W6	Clostridium_phage	1.3e-25	79.5
WP_011590771.1\|1102744_1102978_+	hemolysin XhlA family protein	Q0SPG4	Clostridium_phage	5.8e-34	100.0
WP_110003775.1\|1102998_1103481_+	cobalt ABC transporter permease	I2E8W8	Clostridium_phage	1.1e-71	93.1
WP_111693857.1\|1103537_1104566_+	SH3 domain-containing protein	Q0SPG7	Clostridium_phage	2.5e-198	99.7
WP_111693858.1\|1104842_1105355_+	DUF4352 domain-containing protein	A0A0S2MVG4	Bacillus_phage	3.7e-17	34.9
WP_111693859.1\|1105747_1106869_+	glycerate kinase	W6LM47	Streptococcus_phage	2.5e-42	37.8
WP_004459044.1\|1107258_1108695_+	DEAD/DEAH box helicase	Q5GF26	Diachasmimorpha_longicaudata_entomopoxvirus	1.2e-57	33.3

DBSCAN-SWA_3

1955119 : 1968373

Clostridium_phage(22.22%)

tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_003457168.1\|1955119_1956157_-\|tRNA	tRNA 2-thiocytidine(32) synthetase TtcA	A0A0U2S5Z2	Escherichia_phage	5.4e-31	36.0
WP_003454568.1\|1956355_1956625_+	ACT domain-containing protein	NA	NA	NA	NA
WP_004459400.1\|1956641_1957994_+	PFL family protein	NA	NA	NA	NA
WP_004459349.1\|1958205_1958709_-	QueT transporter family protein	E7DN70	Pneumococcus_phage	1.1e-13	37.2
WP_003457231.1\|1959032_1959908_-	MBL fold metallo-hydrolase	Q332C0	Clostridium_botulinum_C_phage	1.1e-64	50.2
WP_004459354.1\|1960078_1961401_-	sensor histidine kinase	X5JAC0	Clostridium_phage	6.1e-72	37.8
WP_003449818.1\|1961394_1962105_-	response regulator transcription factor	A0A2R2ZGH8	Clostridioides_phage	3.3e-32	31.8
WP_004459421.1\|1962243_1963257_-	N-acetylmuramoyl-L-alanine amidase	Q8SBN4	Clostridium_phage	2.5e-121	64.2
WP_111694089.1\|1963353_1963641_-	thiamine-binding protein	NA	NA	NA	NA
WP_003456055.1\|1963864_1964878_-	DUF348 domain-containing protein	A0A143FMI2	Bacillus_phage	3.5e-19	52.0
WP_003451999.1\|1965303_1966602_-	uracil permease	Q9KX94	Enterobacteria_phage	3.6e-69	39.3
WP_003456099.1\|1966789_1968373_+	ATP-binding cassette domain-containing protein	A0A1V0SGN0	Hokovirus	8.5e-44	25.6

DBSCAN-SWA_4

2651778 : 2664676

Streptococcus_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_111694231.1\|2651778_2652669_-	conjugal transfer protein	A0A1S5SF22	Streptococcus_phage	3.3e-77	51.5
WP_111694232.1\|2652682_2653681_-	lysozyme family protein	A0A1S5SEZ8	Streptococcus_phage	7.5e-123	63.4
WP_111694233.1\|2653677_2655897_-	YtxH domain-containing protein	A0A1S5SF30	Streptococcus_phage	3.4e-176	59.7
WP_111694234.1\|2655896_2658344_-	ATP-binding protein	A0A1S5SF64	Streptococcus_phage	0.0e+00	78.8
WP_111694235.1\|2658315_2658720_-	conjugal transfer protein	A0A1S5SEX7	Streptococcus_phage	1.2e-47	70.6
WP_111694236.1\|2658799_2659303_-	antirestriction protein ArdA	A0A1S5SF25	Streptococcus_phage	5.6e-50	59.1
WP_111694237.1\|2659391_2659988_-	hypothetical protein	NA	NA	NA	NA
WP_111694238.1\|2660050_2660272_-	hypothetical protein	A0A1S5SEY0	Streptococcus_phage	1.2e-28	87.7
WP_111694239.1\|2660338_2661523_-	XRE family transcriptional regulator	A0A1S5SEX3	Streptococcus_phage	4.2e-157	67.4
WP_111694240.1\|2661713_2663117_-	DNA translocase FtsK	A0A1S5SFB5	Streptococcus_phage	9.4e-180	69.9
WP_172606778.1\|2663103_2663925_-	hypothetical protein	NA	NA	NA	NA
WP_111694241.1\|2663970_2664348_-	YdcP family protein	A0A1S5SF96	Streptococcus_phage	9.0e-45	81.1
WP_111694242.1\|2664361_2664676_-	YdcP family protein	A0A1S5SF38	Streptococcus_phage	1.9e-40	74.8

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_LS483461

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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

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection