CRISPRimmunity

Please click to download your results

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_CP053346	Sphingomonas sp. AP4-R1 chromosome, complete genome	2 crisprs	DinG,DEDDh,csa3,WYL,RT	0	0	2	0
NZ_CP053347	Sphingomonas sp. AP4-R1 plasmid unnamed1, complete sequence	0 crisprs	csa3,RT	0	0	2	0

Results visualization

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP053346_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053346_1

1841680-1841769

Orphan

Consensus_repeat	Method
GCCCCTCCCGCAGGCGGGGGGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053346_1

>merge|NZ_CP053346|1|1841680-1841769|CRISPRCasFinder
GCCCCTCCCGCAGGCGGGGGGGGCAGGAGGGGGAAGGCAAGGCTCGCTGTGCTCGCGCCCACCCCCGGCCCCTCCCGCAGGCGGGAGGGG

>NZ_CP053346|1|1|1841680-1841769|CRISPRCasFinder
GCCCCTCCCGCAGGCGGGGGGGG	CAGGAGGGGGAAGGCAAGGCTCGCTGTGCTCGCGCCCACCCCCG
GCCCCTCCCGCAGGCGGGAGGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053346.1\|WP_171744186.1\|1845008_1846070_-\|NAD(P)-dependent-alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|176186
NZ_CP053346.1\|WP_171744191.1\|1852379_1853357_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350130
NZ_CP053346.1\|WP_171744176.1\|1832908_1833790_-\|NAD(+)-diphosphatase	unknown	unknown	gnl\|CDD\|225373
NZ_CP053346.1\|WP_171744177.1\|1833789_1834869_-\|A/G-specific-adenine-glycosylase	unknown	unknown	gnl\|CDD\|224115
NZ_CP053346.1\|WP_171744182.1\|1840407_1840641_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053346.1\|WP_171744185.1\|1843391_1844888_+\|glycosyltransferase-family-39-protein	unknown	unknown	gnl\|CDD\|224720
NZ_CP053346.1\|WP_171746862.1\|1841782_1843201_-\|UdgX-family-uracil-DNA-binding-protein	unknown	unknown	gnl\|CDD\|274850
NZ_CP053346.1\|WP_171744184.1\|1840840_1841671_+\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381357
NZ_CP053346.1\|WP_171744188.1\|1847419_1848427_+\|LLM-class-flavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|274646
NZ_CP053346.1\|WP_171744175.1\|1831874_1832765_+\|prephenate-dehydratase	unknown	unknown	gnl\|CDD\|237014
NZ_CP053346.1\|WP_171744179.1\|1835443_1836151_+\|thioredoxin-domain-containing-protein	unknown	unknown	gnl\|CDD\|372611
NZ_CP053346.1\|WP_171744183.1\|1840642_1840792_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053346.1\|WP_171744192.1\|1853475_1854483_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053346.1\|WP_171744181.1\|1836984_1840401_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|274008
NZ_CP053346.1\|WP_171744190.1\|1851474_1852122_+\|GDSL-family-lipase	unknown	unknown	gnl\|CDD\|239945
NZ_CP053346.1\|WP_171744193.1\|1854518_1855457_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053346.1\|WP_171744189.1\|1848779_1851422_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|224544
NZ_CP053346.1\|WP_171744180.1\|1836200_1836962_+\|thioredoxin-domain-containing-protein	unknown	unknown	gnl\|CDD\|372611
NZ_CP053346.1\|WP_171744187.1\|1846149_1847256_-\|NADH:flavin-oxidoreductase/NADH-oxidase	unknown	unknown	gnl\|CDD\|239242
NZ_CP053346.1\|WP_171744178.1\|1834883_1835447_+\|DUF721-domain-containing-protein	unknown	unknown	gnl\|CDD\|227679

Protein	Function_ID	Function_description	E-value
NZ_CP053346.1\|WP_171744191.1\|1852379_1853357_+\|family-43-glycosylhydrolase	gnl\|CDD\|350130	cd18618, GH43_Xsa43E-like, Glycosyl hydrolase family 43, including Butyrivibrio proteoclasticus arabinofuranosidase Xsa43E. This glycosyl hydrolase family 43 (GH43) subgroup belongs to the GH43_AXH-like subgroup which includes enzymes that have been characterized with beta-xylosidase (EC 3.2.1.37), alpha-L-arabinofuranosidase (EC 3.2.1.55), alpha-1,2-L-arabinofuranosidase 43A (arabinan-specific; EC 3.2.1.-), endo-alpha-L-arabinanase as well as arabinoxylan arabinofuranohydrolase (AXH) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. AXHs specifically hydrolyze the glycosidic bond between arabinofuranosyl substituents and xylopyranosyl backbone residues of arabinoxylan. This subgroup includes Cellvibrio japonicus arabinan-specific alpha-1,2-arabinofuranosidase, CjAbf43A, which confers its specificity by a surface cleft that is complementary to the helical backbone of the polysaccharide, and Butyrivibrio proteoclasticus GH43 enzyme Xsa43E, also an arabinofuranosidase, which has been shown to cleave arabinose side chains from short segments of xylan. Several of these enzymes also contain carbohydrate binding modules (CBMs) that bind cellulose or xylan. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	1.48896e-146
NZ_CP053346.1\|WP_171744176.1\|1832908_1833790_-\|NAD(+)-diphosphatase	gnl\|CDD\|225373	COG2816, NPY1, NTP pyrophosphohydrolases containing a Zn-finger, probably nucleic-acid-binding [DNA replication, recombination, and repair].	3.11398e-73
NZ_CP053346.1\|WP_171744177.1\|1833789_1834869_-\|A/G-specific-adenine-glycosylase	gnl\|CDD\|224115	COG1194, MutY, A/G-specific DNA glycosylase [DNA replication, recombination, and repair].	5.28325e-129
NZ_CP053346.1\|WP_171744185.1\|1843391_1844888_+\|glycosyltransferase-family-39-protein	gnl\|CDD\|224720	COG1807, ArnT, 4-amino-4-deoxy-L-arabinose transferase and related glycosyltransferases of PMT family [Cell envelope biogenesis, outer membrane].	1.59009e-08
NZ_CP053346.1\|WP_171746862.1\|1841782_1843201_-\|UdgX-family-uracil-DNA-binding-protein	gnl\|CDD\|274850	TIGR03914, SPO1_DNA_polymerase-related_protein, uracil-DNA glycosylase family domain. This model represents a clade within the uracil-DNA glycosylase superfamily. Among characterized proteins, it most closely resembles the Thermus thermophilus uracil-DNA glycosylase TTUDGA, which acts uracil (deamidated cytosine) in both single-stranded DNA and U/G pairs of double-stranded DNA. This domain may occur either as a stand-alone protein or as the C-terminal domain of a fusion with another domain that always pairs with a particular radical-SAM family protein.	1.68807e-122
NZ_CP053346.1\|WP_171744184.1\|1840840_1841671_+\|aldo/keto-reductase	gnl\|CDD\|381357	cd19131, AKR_AKR5C2, Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins. Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.	8.47112e-150
NZ_CP053346.1\|WP_171744188.1\|1847419_1848427_+\|LLM-class-flavin-dependent-oxidoreductase	gnl\|CDD\|274646	TIGR03558, oxido_grp_1, luciferase family oxidoreductase, group 1. The Pfam domain family pfam00296 is named for luciferase-like monooxygenases, but the family also contains several coenzyme F420-dependent enzymes. This protein family represents a well-resolved clade within family pfam00296 and shows no restriction to coenzyme F420-positive species, unlike some other clades within pfam00296. [Unknown function, Enzymes of unknown specificity].	5.64596e-176
NZ_CP053346.1\|WP_171744186.1\|1845008_1846070_-\|NAD(P)-dependent-alcohol-dehydrogenase	gnl\|CDD\|176186	cd05283, CAD1, Cinnamyl alcohol dehydrogenases (CAD). Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.	0
NZ_CP053346.1\|WP_171744175.1\|1831874_1832765_+\|prephenate-dehydratase	gnl\|CDD\|237014	PRK11899, PRK11899, prephenate dehydratase; Provisional.	8.25329e-161
NZ_CP053346.1\|WP_171744179.1\|1835443_1836151_+\|thioredoxin-domain-containing-protein	gnl\|CDD\|372611	pfam13462, Thioredoxin_4, Thioredoxin.	1.50831e-20
NZ_CP053346.1\|WP_171744181.1\|1836984_1840401_+\|AAA-family-ATPase	gnl\|CDD\|274008	TIGR02168, Chromosome_partition_protein_Smc, chromosome segregation protein SMC, common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].	0
NZ_CP053346.1\|WP_171744190.1\|1851474_1852122_+\|GDSL-family-lipase	gnl\|CDD\|239945	cd04501, SGNH_hydrolase_like_4, Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.	7.6911e-38
NZ_CP053346.1\|WP_171744189.1\|1848779_1851422_+\|TonB-dependent-receptor	gnl\|CDD\|224544	COG1629, CirA, Outer membrane receptor proteins, mostly Fe transport [Inorganic ion transport and metabolism].	1.20345e-34
NZ_CP053346.1\|WP_171744178.1\|1834883_1835447_+\|DUF721-domain-containing-protein	gnl\|CDD\|227679	COG5389, COG5389, Uncharacterized protein conserved in bacteria [Function unknown].	8.02851e-16
NZ_CP053346.1\|WP_171744187.1\|1846149_1847256_-\|NADH:flavin-oxidoreductase/NADH-oxidase	gnl\|CDD\|239242	cd02932, OYE_YqiM_FMN, Old yellow enzyme (OYE) YqjM-like FMN binding domain. YqjM is involved in the oxidative stress response of Bacillus subtilis. Like the other OYE members, each monomer of YqjM contains FMN as a non-covalently bound cofactor and uses NADPH as a reducing agent. The YqjM enzyme exists as a homotetramer that is assembled as a dimer of catalytically dependent dimers, while other OYE members exist only as monomers or dimers. Moreover, the protein displays a shared active site architecture where an arginine finger at the COOH terminus of one monomer extends into the active site of the adjacent monomer and is directly involved in substrate recognition. Another remarkable difference in the binding of the ligand in YqjM is represented by the contribution of the NH2-terminal tyrosine instead of a COOH-terminal tyrosine in OYE and its homologs.	0
NZ_CP053346.1\|WP_171744180.1\|1836200_1836962_+\|thioredoxin-domain-containing-protein	gnl\|CDD\|372611	pfam13462, Thioredoxin_4, Thioredoxin.	5.86827e-28

>NZ_CP053346.1|WP_171744184.1|1840840_1841671_+|aldo/keto-reductase
MTQVPQQLLNDGRTIPQLGLGVYQTPPAETETIVRAALDAGYRYVDTAMFYRNEEGVGAAVRDCPDWVFVTTKLWNADQGYDRTLAAFDESMQRLGLDELDLFLIHWPVPKIDRFVESWKAMIRLREEGRVRSIGVSNFRVEDLQRIIDETGVTPATNQIVLHPGFQQRELRAFHERHGIVTTCWAPLGQGEALRDPVIGRIAEKHGKTPAQTIIRWHIDSGFNVIPKTASVGRLPENIDVFDFQLDHEDMRTIEALDRSDGRIGSDPATMAMGVE
>NZ_CP053346.1|WP_171744183.1|1840642_1840792_+|hypothetical-protein
MVGLTLAIGDFMMLLISAVLWTGGGFVLLALLGVGAIGGIAMLAKKLMR
>NZ_CP053346.1|WP_171744182.1|1840407_1840641_+|hypothetical-protein
MAKRYRVVHQRKSIWEALVSGRGSRDWYLAQAGYWFGWRTIATCLSTEEAEAACRDHAGGTLLRGGHRVVSEFERPD
>NZ_CP053346.1|WP_171744181.1|1836984_1840401_+|AAA-family-ATPase
MRIRKLRLAGFKSFVEPAELLIEPGLTGIVGPNGCGKSNLLEAIRWVMGEGSPKSLRGGGMEDVIFAGTASRPSRDFAEVSLLVELRGDDANWAEQEVVRRIERGAGSAYRLNGRDVRQRDVALLFADAATGAHSPALVSQGRIAAVIAAKPQQRREMLEEAAGIAGLHVRRREAEIRLRATEANLEKLDEMLGEMEVRANALRRQARAAERYRTLSTEIGLAEARALFARWREAAAAAEQARSKAALSEQAVAQAAEAQRAAAAYVGGATTALAEARAAADAAREAASTTRHRLDEVRAEAGRVGRRIEELARQVAMLKADREREDALAIDAAAALKALEEEDKALGVAITQATAERAGSDQAQAEAERKVRDAEVAVAQALAAAAAEEAEARVAEAALVAARQRFARADAEAQRVARDVAALGEAAPLLAAVEDAKTQVAAAEAAVATASAAIGEAEAARDRAALAREEAETRSGLATAALARAESEAKALTAGLARDAGDRALTKLTVAAGYERALAAALGDDLDAPIGGEGARAWTGADPQAGDPALPAGVVSLAEHVGGGEALARRLAQIGVVESDEGWPLAVGQRIVTFAGRLRRWDGYVARDVGAAAAERLVRANRLREIEAGLPGLREEAGAARAALDGATTMQRAAREQAEAARRALATAEEQVRASRRREDQAQAAAERHAASLTALADRRARADSELAEAQAAVGTAEAAVQALPDRATSRAALDQLNTAADLVRSELATARGRAAALGETIARDQRRRDAARGEAKGWRSRAGDAAKRIDEMAKRLAAAEAEHASLAAKPEALARDIEQAEGRATEAEAAAKAARETEAMRETELRRIEAAAAQAGEALANAREARATLTAHAEHQESRRGELSRAAGDRFQCPAATLPEKIGFDSGALLPAEEEGARHDRLVADRERLGPVNLVADTELAELDATRTTNAAEREELGQAVHRLRGSIGSLNREGRQRLLAAFEAVDGHFRRLFATLFGGGEAHLALIDSDDPLEAGLEIMAQPPGKRLGSLTLLSGGEQALTAVALIFALFLTNPAPICVLDEVDAPLDDANIERFCDLLVVMTKETDTRYLVVTHNAVTMSRMHRLFGVTMIERGVSRLVSVDLGGAESLLAAE
>NZ_CP053346.1|WP_171744180.1|1836200_1836962_+|thioredoxin-domain-containing-protein
MMSRRPAVAVLIALSLGACSKKAADGNAASLPGGPVAAVAPPAGKDWTEIASMTPEGGVRMGNPDAPVKLVEYASLTCPHCAEFTKEGAEPIQAQFVKTGKVSWEYRPFVLNSFDIPAFMLTRCRGAEPFFKLAEQAYAQQQEWVGKAMALTPAQQAELQSTEQAQLFKKMASFMGLDAFFRARGISQADQDKCLGDVAAAEKLAQGTTTATNDKNVTGTPTFFINDEQWSVPVTTQPVAPQLIARLKSVTGG
>NZ_CP053346.1|WP_171744179.1|1835443_1836151_+|thioredoxin-domain-containing-protein
MTQMIRRLLPLLSLAFAFAIPATAPAATPTVAAKDWSKVAARTPAGTFIQGNPDAKVKLVEYLSFTCPHCALFESQAAVPLTQRYIRTGLVSYEVRLALRDPFDLAAAVLARCSGPAAFFAVKPALFAAQPQWEAQGQKWGATAPKLDQMTEADAGKAIAAGAGLDTFFLKHGLPRARIDACLANTEEQHDLSAAAQKIWTPDFPGTPMFEINGKRAEDVHEWPQLEAKLKAALG
>NZ_CP053346.1|WP_171744178.1|1834883_1835447_+|DUF721-domain-containing-protein
MAMPMTERKTRKAALAGADAPRANGVRTVAEMVPQVGAMAFKRFGFVQSSIVSRWAEIVGERYAEVSTPESIRFPQGKKQDGVLNLNVQGSHATMMQHVAPAIIERVNRFFGYPAVVKLAIRQGAVVAPKPRRAPPSLKPVPIELGESLRAIADPELRETLSALAGAVAASTGIPKLSAGRPRGSND
>NZ_CP053346.1|WP_171744177.1|1833789_1834869_-|A/G-specific-adenine-glycosylase
MLVDSMAPRSAASPAEQSPAGRLLAWYDVHRRTLPWRAAPGAPAPDPYAVWLSEVMLQQTTVAAVKPYFARFLDRWPTVTALAAADDADVMAAWAGLGYYARARNLIACARAVAGEHDGTFPDTEEGLRALPGLGAYTAAAVAAIAFGRRAVVVDANVERVVSRLFAVEQPLPAARPELRRLADSITPEARAGDFAQAMMDLGATICTPRGPACALCPLSPDCAARAACTQEDYPRKAAKRDKPVRRGTIFWLEAEGHVLLRRREPKGMLGGMRALPSGSWEASDPSLADAPLAADWRPLGGGRHVFTHFALDYAVVGTVVADRSAEGEWWPIDRLDEAGLPTLFARAAAIAISQRESA
>NZ_CP053346.1|WP_171744176.1|1832908_1833790_-|NAD(+)-diphosphatase
MPFTPGFTGSVLDRVEIERLAPDIVPRLLAEGDALFLDMPDYLPAADESGLLWTAVPGDIPPEQLVLLGRIAGRPRFTRIAPDLLGGRRTPAVSALIEALSAGDATTYAVARSLLDWHARHRFCAFCGHASDLARAGWGRLCPNCGTEHFPRTDPVVIMLAEHERGPQARVLVGRQPTFPPGRYSALAGFLEVGESIEGAVARELAEEAGVRAGAIRYVASQPWPFPSQLMIACIAEVADPTVTLDMNELEDARWVDRDEVFAALAGDESAPFQAPPPYAIANTLLRAWAEGA
>NZ_CP053346.1|WP_171744175.1|1831874_1832765_+|prephenate-dehydratase
MESYPAPARALVAELTQAAAQAPERAVAFQGAPGCNSHIAAMNVVPDGLPLPCFHFEDALDAVRDGRAAKALIPIENSLHGRVADIHFLLPESGLSIVGEHFMPIRYGLMGFGEGITEAMSHPQALGQCRRWLRERGIKPVPYPDTAGAAAAAAELGRPEVGAIAPPLAADLYSLKILAEGLEDSDDNTTRFVQLSREPLATSFEGVAMTTFIFEVKNIPAALYKALGGFATNGVNMTKLESYQRGASFAATEFYCDVEGRPEDATLGRALEELEFHTKWMRVLGTYPQERARTLT
>NZ_CP053346.1|WP_171746862.1|1841782_1843201_-|UdgX-family-uracil-DNA-binding-protein
MVPLDAEDDFDGWRDAARALVRADVSPDRVIWQVGEGVTDLFGGAAGPLPAATAPAFSVPRAFLDLARSVIGHRDPERFALLHTALARLREAPGLMQDQADPLIRRLEQLAKEVRRDIHKMRAFLRFREVADGGGARFVAWFEPDHHIVRANADFFLNRFAAMRWTILTPELSLDWDGETLREGPGAARADAPDGDPLEETWKTYYASIFNPARVKVGAMLKEMPRKYWKNMPETALVPALIAGAQAREAGMVAASHTAMTKGEAGTRRGASRETSWEALREEAAGCTRCPLFKPATQTVFGEGRIDAPLMFVGEQPGDQEDLAGRPFVGPAGQMFDKALAEAGLDRAAAYVTNAVKHFKYEQRGKRRIHAKPNGPEIDACRWWIDQERTLIQPRLIVALGATAARSVLGKAVTIAATRGTPHPLADGSEAWVTVHPSYLLRLPDAQAAEAEYARFVEDLARMKARLGELAG
>NZ_CP053346.1|WP_171744185.1|1843391_1844888_+|glycosyltransferase-family-39-protein
MASRALPYSPGLTGRLSLAGRGWRDALAMLVVAFALRCWWFGNPAIQVDEQFYLLVGDRMLHGALPYVDIWDRKPIGLFLLYAGVRLLGGAGIVQYQVVATVFAAATAFLVVRIAARIASPTAARLAGAASLIFTVVFDGAGGQSPVFYNPFVAGAAWMVLQALDVPPAGERRFVAWGAGAMALIGLAMQIKYTALFEGVTMGFVLLWAARRRGIDAALPGVALLWILLAILPTAAAFAAYAAAGHGEAFFYANFVSIGDRPGTAALQLAKRTIVAAGMGLPLILAAIAGVRVRQHGEEAKRARAFLIVWLAGAVIGFFAIGSLFKHYFLPVVTPLAVFTAPAFDVGRRDRWRAVAVLAIGLVLAAGMSLHRGSTRGGERHMDELVAAIRPHLKDDLFVFDGEPILYLLTGAKLVSPYAFPNHLNQMKEAPAIGVDPVAEVRRVMAARPSVVVVTDRPGADRNPVTWEIVRAGLMRDYAQVGAVRFHKKWRLVYARKA
>NZ_CP053346.1|WP_171744186.1|1845008_1846070_-|NAD(P)-dependent-alcohol-dehydrogenase
MTSQAKAFAAQSATTPLAPFTFERRDPLPTDVAIDIAYCGVCHSDLHTARSEWDGTIFPCVPGHEIVGHVTAVGSDVTKFAVGDIVGVGCMVGSCGTCPSCSDGEEQYCTGTGMVGTYNGPDAHLGGHTFGGYSDKIVVDQDFVLKVAHAEADLAAVAPLLCAGITTYSPLKHWGAGPGKKVGVVGLGGLGHMGVKIAAAMGAHVVAFTTSASKIEDAKKLGAHEVVVSKNEDEMAAHAGSFDMILNTVAASHNLDAFTALLKRDGTLVLVGVPEHAHPSPNVGTLIFGRKAIAGSLIGGIAETQEMLDFCAKHGLTADIEMIPAQGINDAYERMLKSDVKYRFVIDMATLAA
>NZ_CP053346.1|WP_171744187.1|1846149_1847256_-|NADH:flavin-oxidoreductase/NADH-oxidase
MASKLFAPYAVGGLDLANRIVIAPMCQYSAEDGAMTDWHAQHLGQLAQSGAGLLTIEATAVVPEGRITYADVGLYDDRTEAAMGTVIQGIRRWSDMPIAIQLAHAGRKASTDLPWLGGAQIAPDAEHGWQVVSASPAPFTEGTAPSMALDRAGMGRVRDAFVEAARRADRLGIDMIQLHGAHGYLIHQFLSPLSNTRTDEYGGSLENRMRFPLEIFDAVRAAFPADKPVTVRVSGTDWVEGGWDVAQTIAFAKELEARGCAGIHVSSGGLDARQQIPVGPGYQVPLGRAVKDAVTMPVTTVGLITDFDHAEAIVATGDADFVALARTILYDPRWPWHAAAHLRAQVKAAPQYLRCQPSRYRDLFTTGR
>NZ_CP053346.1|WP_171744188.1|1847419_1848427_+|LLM-class-flavin-dependent-oxidoreductase
MVAISILDLVRIREGGSARTALDDARDLAAHAETLGYTRFWMAEHHNMPGIASAATSIAIAHVAAGSKTIRVGAGGVMLPNHSPVVIAEQFGTLEALFPGRIDLGLGRAPGTDQITLRALRRDPSASEHFPQDVQELQQLLGPLQPGQRVQAVPGTDSNVPLWILGSSLFGAQLAAHLGLPYGFASHFAPQSLLPALQIYRDRFQPSAQLARPYATVGVNIVAAPSDEEARFLATTQQMAIANLFRGARGLSLPPIDDIDSYWTPQEKAQAHGFLARSIVGGPETVAKGIAALVAETKADELIIVSDVFDHALRKRSYSLIAEAAGVARLAEAAE
>NZ_CP053346.1|WP_171744189.1|1848779_1851422_+|TonB-dependent-receptor
MFAIALLAASASGAVEAAPAAAEPEILVTATQRPTPAGDVPVAITSIGREALRDGAVVDLRTLNVLAPSLLVSSSSNEAGGGGARIRGIGTVGDNAGLESSVATFVDGVYRARAATALTELGPLERVDVLRGPQGTLFGRNASAGLINVVTAQPSRTLGGYAEASVGNYDYWRLGAGITGPLTETLSGRIDGVYIKRQGFFQDVVSGRHLNGRDRGLVRGKLKWEPDASFAATLTVDYAKRDEECCAGGYSVVRDLRSSTPGAGGGSLVTAPSSIAALIRAMPGGQVLDDPGVRKVALSPGQSFRQDVTDGGVALNMTKTLGGITIDSITAWRSNKFIKGQDADFSSLDLIRRPSDGSGFIRFRNFSQELRARGEAFGGKLDWLVGGYWGEERLTLQDNMAYGADYDRFASARIGALGGAFAAFPTYGFANLKGFAQNYGGAALAAAVQNVPIAGTGELDRFRQHDSNQALFTHDIVHVTDRLSLTLGARYTRDRKTLDANLASTSSCGIYLDTIARLRALGTASATALANSVLAPLAGYPCNINSVNGAIDQRRTEHRWSGTAALDYRIARGANVYASWSRGYKAGGFNLDRGGLFNTGRLQQLPASSLAFAPETVEAWELGAKLHRRLFDLDVALFRQAFRNFQLNSYTGTNFVVSNVQGCSTSLGNRDSDNIAGNSACSDTKAGVISKGVELDATLRPAADWVLTGGFTYADTRYAKDIVGSPDALTGDNSLPPVLFLLPGARLSNAPAYTATGSVRWTPAIREGLRALAYVGTRYQSKINTGSDLLTEKAQKGFGLVDARVGVSTASGWSLELWAQNVFNVTYTQVAFSEPLQGGGSGGMPGTAAAVTAFGTTSSQLFGAFLGDPRTWGLTARKRF
>NZ_CP053346.1|WP_171744190.1|1851474_1852122_+|GDSL-family-lipase
MAAIIQTALRKAGRARVQAMWMAHRAGGKRRRPIAIFLGDSITRQWLEHDPGFFRGKKRRNAGLGGDTSAGMLARFDAEVLAVGPRVVHIMAGTNDLWHGDPGPDATKTIANIAEMAARARAAGIAVILAAPPPIGRNAVPLFNRPGLAPMLREGVARLCGGEDGPIHVDYAASLGDGIGGIRFDLTTDGVHLTRAGYYAIRAQAERALALALGD
>NZ_CP053346.1|WP_171744191.1|1852379_1853357_+|family-43-glycosylhydrolase
MKRLVLGGMLALASGMAAQAQPAAPGSNPILRDQFTADPAALVVGDTVYLYVGHDVSDDERYRMPDWLLYSSKDMKHWTPHGTILRPTDFAWSKGDAYASQVVEKGGKFYFYANAKEAATGSMAIGVAVSDKPTGPFVDARGSVLITNAMTPQGQHGWSDIDPTVLIDDDGTPWLMWGNGNCFRAKLKPNMIELDGPIEEVKLTRYEEGPWLHKHGKTYYVTYASRERGPKEPETISYATAPAVTGPWTYRGELTGPAENSGTIHPAIIAFKGKDYFFYHDGTLTIGDKKGGSYRRAVRVERLFYNADGTMKPVAQTAAGVSGRP
>NZ_CP053346.1|WP_171744192.1|1853475_1854483_+|hypothetical-protein
MRWKIAPCIALIAAPLWAASAAAPPPPADPEIVVNGKRIILEGGEWEFDRSTGITQSAGLSNMPASNWRACLPTGSQVSILRRLLGAMPAVQTTATGGTICGQMGFRIRGNRVVGHQNCSILFAGVLPARTYHRSQRMIATVGEDQVAVEFDQTDDMPPPSRSIGIPSEGLGLRRFNWRLAARRVGACPLPNMAASRSRVTPPLLANAEPAPTAIPPRVFLEPLNVSLTITEDMLASPLTAARDALPASEDDIVVIGRRLRRAKLHFANEGRLLTWCHTDVSTGDARVDRIACAIVQACVREGVTDLLPVRACYARKVAYFDDAVHAARSRAPSS
>NZ_CP053346.1|WP_171744193.1|1854518_1855457_+|hypothetical-protein
MIAAPIWGAGAAAPPPPADPEIIVNGKRIILEGGEWEFDRSVGIGATHVSRPMKWKACIPAGDQIVMLRQLLGAMPAVQVAAGSGTLCGKMSFRFRGNRVTGRQGCRVVVVGEQLTASYDRSQWLEAIVTEDRIAVESEIATDGGARGPSRTSWRMTARRVGICRMPQTFASKSAAPGMLTRAAEPAPAAIPPRLFLEPLDVSLSITRDMLASPLMEEGRDTLPAREDDIVVIGRRLRRAKLHFANEGRLLVWCHTDVSTGDARVDRIACAIVQACVREGVSELLPVRACYARKVALLDDDIRAARGRKPTS

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

Click the colored protein region to show detailed information

Crispr_ID: NZ_CP053346_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053346_2

1932576-1932671

Orphan

Consensus_repeat	Method
TCCCCTCCCGCATGCGGGAGGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053346_2

>merge|NZ_CP053346|2|1932576-1932671|CRISPRCasFinder
TCCCCTCCCGCATGCGGGAGGGGTTGGGGGTGGGCAGGCGCCGGAGCTCGCTCCGTTCGCGCCCACCCCTCGATCCCCTCCCGCAGGCGGGAGGGG

>NZ_CP053346|2|2|1932576-1932671|CRISPRCasFinder
TCCCCTCCCGCATGCGGGAGGGG	TTGGGGGTGGGCAGGCGCCGGAGCTCGCTCCGTTCGCGCCCACCCCTCGA
TCCCCTCCCGCAGGCGGGAGGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053346.1\|WP_171744252.1\|1939415_1939940_+\|acyloxyacyl-hydrolase	unknown	unknown	gnl\|CDD\|378181
NZ_CP053346.1\|WP_171744251.1\|1938578_1939109_+\|N-acetyltransferase-family-protein	unknown	unknown	gnl\|CDD\|224168
NZ_CP053346.1\|WP_171744241.1\|1922302_1923400_+\|dihydropteroate-synthase	unknown	unknown	gnl\|CDD\|238380
NZ_CP053346.1\|WP_171744257.1\|1946597_1947188_+\|CspA-family-cold-shock-protein	unknown	unknown	gnl\|CDD\|239905
NZ_CP053346.1\|WP_171744255.1\|1944054_1945830_-\|fatty-acyl-AMP-ligase	unknown	unknown	gnl\|CDD\|236403
NZ_CP053346.1\|WP_171744256.1\|1945945_1946482_+\|RecX-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|225048
NZ_CP053346.1\|WP_171744249.1\|1932682_1936852_-\|DNA-directed-RNA-polymerase-subunit-beta	unknown	unknown	gnl\|CDD\|181983
NZ_CP053346.1\|WP_171744240.1\|1922115_1922295_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053346.1\|WP_171746869.1\|1920866_1921949_+\|site-specific-DNA-methyltransferase	unknown	unknown	gnl\|CDD\|334588
NZ_CP053346.1\|WP_171744247.1\|1927680_1928037_-\|PilZ-domain-containing-protein	unknown	unknown	gnl\|CDD\|377796
NZ_CP053346.1\|WP_171744250.1\|1937149_1938475_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|223910
NZ_CP053346.1\|WP_171744244.1\|1925317_1926496_-\|glycosyltransferase-family-1-protein	unknown	unknown	gnl\|CDD\|340842
NZ_CP053346.1\|WP_171744258.1\|1947184_1947676_+\|DUF192-domain-containing-protein	unknown	unknown	gnl\|CDD\|376876
NZ_CP053346.1\|WP_171744245.1\|1926542_1927076_-\|CHAP-domain-containing-protein	unknown	unknown	gnl\|CDD\|226451
NZ_CP053346.1\|WP_171744246.1\|1927260_1927506_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053346.1\|WP_171744254.1\|1942397_1943798_-\|M20/M25/M40-family-metallo-hydrolase	unknown	unknown	gnl\|CDD\|236388
NZ_CP053346.1\|WP_171744248.1\|1928277_1932558_-\|DNA-directed-RNA-polymerase-subunit-beta'	unknown	unknown	gnl\|CDD\|234794
NZ_CP053346.1\|WP_171744242.1\|1923582_1924239_-\|ribonuclease-HII	unknown	unknown	gnl\|CDD\|260003
NZ_CP053346.1\|WP_171744253.1\|1940077_1942174_+\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|224423
NZ_CP053346.1\|WP_171744243.1\|1924389_1925334_+\|glucokinase	unknown	unknown	gnl\|CDD\|367143

Protein	Function_ID	Function_description	E-value
NZ_CP053346.1\|WP_171744252.1\|1939415_1939940_+\|acyloxyacyl-hydrolase	gnl\|CDD\|378181	pfam09411, PagL, Lipid A 3-O-deacylase (PagL). PagL is an outer membrane protein with lipid A 3-O-deacylase activity. It forms an 8 stranded beta barrel structure.	9.89313e-10
NZ_CP053346.1\|WP_171744256.1\|1945945_1946482_+\|RecX-family-transcriptional-regulator	gnl\|CDD\|225048	COG2137, OraA, Uncharacterized protein conserved in bacteria [General function prediction only].	2.01132e-13
NZ_CP053346.1\|WP_171744241.1\|1922302_1923400_+\|dihydropteroate-synthase	gnl\|CDD\|238380	cd00739, DHPS, DHPS subgroup of Pterin binding enzymes. DHPS (dihydropteroate synthase), a functional homodimer, catalyzes the condensation of p-aminobenzoic acid (pABA) in the de novo biosynthesis of folate, which is an essential cofactor in both nucleic acid and protein biosynthesis. Prokaryotes (and some lower eukaryotes) must synthesize folate de novo, while higher eukaryotes are able to utilize dietary folate and therefore lack DHPS. Sulfonamide drugs, which are substrate analogs of pABA, target DHPS.	7.44314e-104
NZ_CP053346.1\|WP_171744257.1\|1946597_1947188_+\|CspA-family-cold-shock-protein	gnl\|CDD\|239905	cd04458, CSP_CDS, Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in eukaryotes, prokaryotes, and archaea. CSP's include the major cold-shock proteins CspA and CspB in bacteria and the eukaryotic gene regulatory factor Y-box protein. CSP expression is up-regulated by an abrupt drop in growth temperature. CSP's are also expressed under normal condition at lower level. The function of cold-shock proteins is not fully understood. They preferentially bind poly-pyrimidine region of single-stranded RNA and DNA. CSP's are thought to bind mRNA and regulate ribosomal translation, mRNA degradation, and the rate of transcription termination. The human Y-box protein, which contains a CSD, regulates transcription and translation of genes that contain the Y-box sequence in their promoters. This specific ssDNA-binding properties of CSD are required for the binding of Y-box protein to the promoter's Y-box sequence, thereby regulating transcription.	9.12617e-19
NZ_CP053346.1\|WP_171744255.1\|1944054_1945830_-\|fatty-acyl-AMP-ligase	gnl\|CDD\|236403	PRK09192, PRK09192, fatty acyl-AMP ligase.	0
NZ_CP053346.1\|WP_171744249.1\|1932682_1936852_-\|DNA-directed-RNA-polymerase-subunit-beta	gnl\|CDD\|181983	PRK09603, PRK09603, DNA-directed RNA polymerase subunit beta/beta'.	0
NZ_CP053346.1\|WP_171744251.1\|1938578_1939109_+\|N-acetyltransferase-family-protein	gnl\|CDD\|224168	COG1247, COG1247, Sortase and related acyltransferases [Cell envelope biogenesis, outer membrane].	5.46867e-54
NZ_CP053346.1\|WP_171744247.1\|1927680_1928037_-\|PilZ-domain-containing-protein	gnl\|CDD\|377796	pfam07238, PilZ, PilZ domain. PilZ is a c-di-GMP binding domain which is found C terminal to pfam07317. Proteins which contain PilZ are known to interact with the flagellar switch-complex proteins FliG and FliM. This interaction results in a reduction of torque generation and induces CCW motor bias. This domain forms a beta barrel structure.	1.18266e-05
NZ_CP053346.1\|WP_171744250.1\|1937149_1938475_-\|hypothetical-protein	gnl\|CDD\|223910	COG0840, Tar, Methyl-accepting chemotaxis protein [Cell motility and secretion / Signal transduction mechanisms].	1.71685e-20
NZ_CP053346.1\|WP_171744244.1\|1925317_1926496_-\|glycosyltransferase-family-1-protein	gnl\|CDD\|340842	cd03814, GT4-like, glycosyltransferase family 4 proteins. This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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. The members of this family are found mainly in bacteria and eukaryotes.	1.95186e-126
NZ_CP053346.1\|WP_171744258.1\|1947184_1947676_+\|DUF192-domain-containing-protein	gnl\|CDD\|376876	pfam02643, DUF192, Uncharacterized ACR, COG1430. Two structures have been solved for members of this large (>500 members) family of bacterial proteins present mostly in environmental bacteria and metagenomes (distant homologs are also present in several Plasmodium species). TOPSAN analysis for Structure 3pjy shows that there is much similarity with the other solved structure, Structure 3m7a, solved for UniProt:Q2GA55 (Saro_0823), a homolog of Thermotoga maritima TM1668, UniProt:Q9X1Z6., The homolog in Caulobacter crescentus (CC1388), UniProt:Q9A8G6, is associated with CspD, a cold shock protein (CC1387), UniProt:Q9A8G7. However, the genomic context of UniProt:Q2GA55 is most conserved with a putative xylose isomerase, suggesting a possible role in extracellular sugar processing. Saro_0821, UniProt:Q2GA57, is annotated as an AMP-dependent synthetase and ligase. Structure 3m7a structure corresponds to the C-terminal (27-165) fragment of the YP_496102 (Saro_0823) protein and it is structurally unique, as the best hits from Dali have a Z-score of 3.8 (1nt0, 2j1t, 3kq4) and it is thus a likely candidate for a new fold. Interestingly, many of the top Dali hits are involved in sugar metabolism. There are no obvious active site-like cavities on the protein surface of 3m7a (http://www.topsan.org/Proteins/JCSG/).	4.59849e-50
NZ_CP053346.1\|WP_171744245.1\|1926542_1927076_-\|CHAP-domain-containing-protein	gnl\|CDD\|226451	COG3942, COG3942, Surface antigen [General function prediction only].	6.14539e-10
NZ_CP053346.1\|WP_171746869.1\|1920866_1921949_+\|site-specific-DNA-methyltransferase	gnl\|CDD\|334588	pfam01555, N6_N4_Mtase, DNA methylase. Members of this family are DNA methylases. The family contains both N-4 cytosine-specific DNA methylases and N-6 Adenine-specific DNA methylases.	4.56829e-78
NZ_CP053346.1\|WP_171744254.1\|1942397_1943798_-\|M20/M25/M40-family-metallo-hydrolase	gnl\|CDD\|236388	PRK09133, PRK09133, hypothetical protein; Provisional.	0
NZ_CP053346.1\|WP_171744248.1\|1928277_1932558_-\|DNA-directed-RNA-polymerase-subunit-beta'	gnl\|CDD\|234794	PRK00566, PRK00566, DNA-directed RNA polymerase subunit beta'; Provisional.	0
NZ_CP053346.1\|WP_171744242.1\|1923582_1924239_-\|ribonuclease-HII	gnl\|CDD\|260003	cd07182, RNase_HII_bacteria_HII_like, Bacterial Ribonuclease HII-like. This family includes mostly bacterial type 2 RNases H, with some eukaryotic members. Bacterial RNase HII has a role in primer removal based on its involvement in ribonucleotide-specific catalytic activity in the presence of RNA/DNA hybrid substrates. Several bacteria, such as Bacillus subtilis, have two different type II RNases H, RNases HII and HIII; double deletion of these leads to cellular lethality. It appears that type I and type II RNases H also have overlapping functions in cells, as over-expression of Escherichia coli RNase HII can complement an RNase HI deletion phenotype. In Leishmania mitochondria, of the four distinct RNase H genes (H1, HIIA, HIIB, HIIC), HIIC is essential for the survival of the parasite and thus can be a potential target for anti-leishmanial chemotherapy. Ribonuclease H (RNase H) is classified into two families, type I (prokaryotic RNase HI, eukaryotic RNase H1 and viral RNase H) and type II (prokaryotic RNase HII and HIII, and eukaryotic RNase H2). RNase H endonucleolytically hydrolyzes an RNA strand when it is annealed to a complementary DNA strand in the presence of divalent cations, in DNA replication and repair.	4.81473e-76
NZ_CP053346.1\|WP_171744253.1\|1940077_1942174_+\|S9-family-peptidase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	1.73771e-48
NZ_CP053346.1\|WP_171744243.1\|1924389_1925334_+\|glucokinase	gnl\|CDD\|367143	pfam02685, Glucokinase, Glucokinase. This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes phosphorylate glucose using ATP as a donor to give glucose-6-phosphate and ADP.	1.50668e-27

>NZ_CP053346.1|WP_171744248.1|1928277_1932558_-|DNA-directed-RNA-polymerase-subunit-beta'
MNELTNFANPIAKPETFDQIKIGIASPDRIRSWSFGEIKKPETINYRTFKPERDGLFCARIFGPIKDYECLCGKYKRMKYKGIVCEKCGVEVTVSKVRRERMGHIELAAPVAHIWFLKSLPSRIGLLLDMQLKQLERVLYFEAYIVTEPGLTPLEKFQLLTEDELLDAQDEYGEDAFSAGIGAEAVKTMLMDLDLEGEKKALLEELAVTKSELKPKKIIKRLKVVESFLDSGNRPEWMILDVVPVIPPELRPLVPLDGGRFATSDLNDLYRRVINRNNRLKRLMELRAPDIIVRNEKRMLQEAVDALFDNGRRGRTITGANKRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVTGPELKLHQCGLPKKMALELFKPFIYARLDAKGLSMTLKQAKKWVEKERKEVWDILDEVIREHPVLLNRAPTLHRLGIQAFEPVLIEGKAIQLHPLVCSAFNADFDGDQMAVHVPLSLEAQLEARVLMMSTNNILSPANGKPIIVPSQDMVLGLYYLSMMKEGEPGEGMLLANMTEVHQALNAKAVTLHTKITSRVPQTDENGQPYMKRVETTPGRMLLGETLPKSHKVPFETINRLLTKKEIGDVIDIVYRHTGQKETVLFADGIMSLGFRHAFQAGISFGKDDMVIPAAKEELVDETKLLVKDYEQQYQDGLITQQEKYNKVIDAWSRCGDRVAAEMMKEIQTVRRYEDGENAGREKPINAIYMMAHSGARGSAAQIKQLAGMRGLMAKPSGEIIETPIISNFKEGLTVLEYFNSTHGARKGLADTALKTANSGYLTRRLVDVSQDCVIVELDCGTERALEMRAIVQGGATIASLGERILGRTTAEDIVDSKTGEVVAPEGTLLDEALIAKIEAVSPQAVKIRSPLVCESKGGVCAACYGRDLARGTPVNIGEAVGVIAAQSIGEPGTQLTMRTFHIGGAAQLNEQSNLEAVSDGKLELRGLPTILNPRGQRISLARNGEIAIVDMDGRERATHRLPYGAQVLFEEGHLVSKGDRIAQWDPAFMPVITEKKGTVRYQDLIENRTVREESDETTGLTQRVVIEDVGRGKKDDLRPRLTLLDDSSGEAGVSRLIVGAVIAVDDGQSVEAGEVLARVPREAAKTRDITGGLPRVAELFEARKPKENAIIAKVSGRVEFGKDYKAKRKILIRPEDGGEPVEYLIPKSKTIDAQEGDYVKRGDNLIGGSPDPHDILEVLGIEPLAEYLVSEIQEVYRLQGVKINDKHIETIVRQMLQKVEITFAGDTTLLPGEQVDREEMDELNAKAAEHGGQPAQGKPILLGITKASLQTRSFISAASFQETTRVLTEASVQGKVDTLTGLKENVIVGRLIPAGTGAGMNRLRVTASSRDAALRAQQKSWQASLIAPQTAAEEHAAELRQPVQADTGSDALAEVVGESHGTDADAGDYLDK
>NZ_CP053346.1|WP_171744247.1|1927680_1928037_-|PilZ-domain-containing-protein
MVFITPTGERLAQDRRRTRRWPTHATCGVRGPDGVPSSVTLWNISEGGFGAQCAAAVAGGDRLTFRLGRTGYADARVVWRIGDVVGCEFLRPVSPAEVALALATATPVAIDDKDEPRR
>NZ_CP053346.1|WP_171744246.1|1927260_1927506_-|hypothetical-protein
MKKALALPALAVCALALSGCVRTVGTIVTAPVKAASWTVDKATTSQSEADRNAGRKMRKDEEKRAREERKRQKEAARNQDS
>NZ_CP053346.1|WP_171744245.1|1926542_1927076_-|CHAP-domain-containing-protein
MFKSARAAVAALIFITAISAPTAANAQSTYWQCAPFARVFSGIQLFGAAASWWHQAIGKYAQGGAPKMGSVLVFKAIGAMRSGHVATVTKIVSDRIIKVTHANWGGAKGRVENDVTVVDASPNGDWSQVKVWYSPIHDIGQRAYPTYGFIYGGAKAVAAEAAAAGQALEGKNAGIGG
>NZ_CP053346.1|WP_171744244.1|1925317_1926496_-|glycosyltransferase-family-1-protein
MDVTDLRVALFSGNYNYVRDGANQALNRLVGYLMREGAKVRIYSPKVAKPAFASTGRVVNVPSLPLPGRGEYRAPLGIPGKVRRNLREFGANIFHVASPEILGHRAVTLARYWGKPVVASVHTRFETYPRYYGFAFLEPAVEAYLRRFYRRCDAIFAPSESMAQVLREQRMSYDVGIWTRGVDNAIFTPQRRDMEWRRSIGLADDEPAIGYVGRLVMEKGLDVFAETIDLMRQRGTKGRIVVVGEGPAREWFEKRLPEDTIFAGFQRGEDLGRAMASCDMLFNPSVTETFGNVTLEAMASGLPVVAAKATGSESLVEDGITGRLIRPGANEAFAQALRLYCEDAGAREAAGRAGLAASERYTWDRVNQALVEGYLRVIRLREMGGRPISKAR
>NZ_CP053346.1|WP_171744243.1|1924389_1925334_+|glucokinase
MSDDWLLIDIDGGNARFALACGADHAELRQQRHYSSRDFVTATDCILHYGREAGITLRGLPTAVVISGPVIGDTVRVARSPWIISVRGLAYVMDRMPAVMNDSAAKLWSDLAPSSNRHSPLGGLAEPRQLPDGSKGGYLAVNFRSGLGAALLIHSPHGIAHAETEIGHIAFSPFGDVERTVWTALSGARGPVGWERALLVGRDDPIWAGTSLRGNAIGIARARAAMLGAFCGDAVLATGAWNGLLLHGAGNDLLAGDQLAAAFNERFEARAGYASMLRRVPRWRVEAREENLVGAANFLRARMKAGEGSLSAPC
>NZ_CP053346.1|WP_171744242.1|1923582_1924239_-|ribonuclease-HII
MPSKSSPSSKSSVRPFARRRASLFPPVIGCDEVGRGALCGPVVVCAVWFEPEALPKGLLARLDDSKKIAQAEREALYPLIARCARVSFAARSARYIDVYNIRNATLQAMTQAVTRLDLDAPVRIDGIDVPRGLSGDALAVIKGDAIVPQIAAASIMAKVMRDRLMARLAQRHIYYRWEQNAGYGTKAHRDAILTHGSTRHHRRSFGDLLAGLEPVVAR
>NZ_CP053346.1|WP_171744241.1|1922302_1923400_+|dihydropteroate-synthase
MTGSRLYLRPTAFVDAPFGHDGKVLRLAGGLCFFSAVEVIEVEAGRRIAQTLVAVEALDAFLGGLPGALAEQGRAFLARLIAPRAPLQLGARTIRLDQPQVMAILNMTPDSFSDGGRNADPASAALSATRMLEAGAALIDVGGESTRPGAAAVWEQDEIARVVPVIQLLAGAGAAISIDTRKAAVMAAALDAGAGLINDVSGLTYDKEAEALVAARGAPVVIMHHRGDPATMQQDPHYGDALIEVYDWLEDRVASAVAAGIDRTRIMVDPGVGFGKTLRHNLAVMNGLSLFHGLGCAILLGASRKRFIGALSNEAPAQERLGGSVAVVLTGAAQGVQMVRVHDAYETVQALRVWRGLRDEALSPV
>NZ_CP053346.1|WP_171744240.1|1922115_1922295_+|hypothetical-protein
MAERFERHRQPWKQDEIQKLHTLAKKGMALKAIAKALTRSEDSVKERAKLDGLSIAKLH
>NZ_CP053346.1|WP_171746869.1|1920866_1921949_+|site-specific-DNA-methyltransferase
MSLLPLDTILIGDCIAEMAKLPDKCIDMIFADPPYNLQLGGDLFRPDGSQVDAVDDEWDKFDSLAAYDRFTRRWLAEARRILKDDGSIWVIGSYHNIFRVGTALQDEGFWILNDIVWRKANPMPNFKGTRFTNAHETMIWASKGQKARYTFNYRAMKTLNDDVQMRSDWELPICGGAERLKDEHGHKTHPTQKPEALLYRVLLSASKPGDIVLDPFFGTGTTGAVARRLRRRWIGIDRETTYVKAARARIDSTLPLDESAMLVVAERKTEKRVAFGLLVESGAVAPGTKLMDSRRRWTAEVMADGGLVCADGAGGSIHKLGATLQNAPSCNGWTFWHFEEAGALMPIDVLRQRHLAAAKG
>NZ_CP053346.1|WP_171744249.1|1932682_1936852_-|DNA-directed-RNA-polymerase-subunit-beta
MATQSVPARAPTHMSAAKKRIRKVFGNIHEVVQMPNLIEVQRESYEQFLRSDASIGYVSGLEKTLRSVFPIRDFAGTAELDFVTYELEEPKYDIEECRQRGITFAAPMRVTLRLIVFEVDPDTETRSVLDIKEQDVYMGDMPLMTENGTFIINGTERVIVSQMHRSPGVLFDHDRGKTHASGKYLFAARVIPYRGSWLDFEFDAKDIVNVRIDRKRKLPVTTLLYALGLNGEQILNEFYKTQRYVRGEGGWKVPFLPENWRGQKPSFDVVNGESGEVVFPAGTKISPRAANKAAKDGLQNLLIPTEEIYGRYSAFDLIDEATGRIYIEAGDEVTPENLEKLDNAGFDHVDLLDIDHISTGAWMRNTLAADKVEERDHALSEIYRVMRPGEPPTKETAEALFAGLFFDPERYDLSAVGRVKLNMRLDLDVEDTVTTLRAEDILEVVKTLVNLKDGKGEIDDIDNLGNRRVRSVGELLENQYRVGLLRMERAVKERMSSVDVSTVMPNDLINAKPAVAAVREFFGSSQLSQFMDQTNPLSEVTHKRRVSALGPGGLTRERAGFEVRDVHPTHYGRICPIETPEGPNIGLINSLASFSRVNKYGFIETPYRKVIDHKVTDEVVYLSAMEEAKHTIAQANAEVLTDGTFVEDLISAREAGEFLMAPRDHITLMDVSPKQLVSVAASLIPFLENDDANRALMGSNMQRQAVPLVRAEAPFVGTGMEETVARDSGAAIAAKRPGIVDQVDAGRIVIRASGEVDAGRSGVDIYTLMKFQRSNQSTCINQRPLVKVGDVVKAGDILADGPSTEFGELALGRNTLVAFMPWNGYNYEDSILISERIVKDDVFTSIHIEEFEVMARDTKLGPEDITRDIPNVGEEALHNLDEAGIVYVGAEVEPGDILCGKITPKGESPMTPEEKLLRAIFGEKASDVRDTSLRLPPGVAGTIVDVRVFNRHGIDKDERALAIEREEIDRLTKDREDERAILNRASWSRLKEMLLGHTIASGPKGTKKGAVIDETILEEVERRDWWKFAVADDARQSDLEAVKAQYDEAVAAIVAKFDDRVEKLQRGDELPPGVLKMVKVFVAVKRKLQPGDKMAGRHGNKGVISRILPIEDMPFLEDGTHVDIVLNPLGVPSRMNVGQIFETHLGWAARGLGQQVTQALEEWRDANPDPKAGAAPSAVSESLKRVYGAQYHDEIDALSSDQVVEMAKLLKNGVPMATPVFDGARESDVSDMLTLAGYDTSGQSTLYDGRTGDAFDRKVTVGYIYMLKLHHLVDDKIHARSIGPYSLVTQQPLGGKAQFGGQRFGEMEVWALQAYGAAYTLQEMLTVKSDDVVGRTKVYEAIVKGDDTFEAGIPESFNVLVKEMRSLGLNVDLNSAEDADDDGLAEAAE
>NZ_CP053346.1|WP_171744250.1|1937149_1938475_-|hypothetical-protein
MTALLPRAEPAADTADLLTLCEPGGAALKVEADAPLRAAIDLFRDQPTLRLLAIVDAADRPVGAMLEQDIRAILYNPFGHSLLMNPGFARTAASRRRDCPTAEIGTPLGELLDIYARNGGGEGMLLTEKGRFCGLLANRTLLKLAGERETRLAAAQAERWERSAQASARFLGDVDLIADDLTDAATAIDGAADGTRSRVEAFQRQSAIVAAACQRTTDDMTGLADQGSRLATTIQHLRDAAASARTSAGEAIELTEAGSRRGAALATAAQSIDENLALIRSVATQAHLLSVNAAIEAARLGEAGGGFSIVARELRQFAGRTREAVGTIGGQMGEIRDIAVDIAASQAAVEQIARIVDGVSLSVEQAVEAEADSARLLASNVHRARQASAAIQAGASETERLVTTASGHTEALRARADDLGRDARRLRERVDAFLAELGTAG
>NZ_CP053346.1|WP_171744251.1|1938578_1939109_+|N-acetyltransferase-family-protein
MSHPILIRPVRQDDAAALATIYAAHVRHGTATFEVEAPDAEEMRLRVATVVSRGWPWIVAERAGEVIGYAYCGLFRTRHAYRFTCEDSIYVDADQVGTGAGRALLAGLIEAARAAGFREMIAVIGDADNRASIGLHEALGFDHAGVMRRVGYKFDRWIDVIYMQKCLVEPGDPMLR
>NZ_CP053346.1|WP_171744252.1|1939415_1939940_+|acyloxyacyl-hydrolase
MVRRVAWWGGMMLAGAMPAQATDLFGGLYKHDVNIFAKKLHEGGADIEAGIRGDAISALGFVGGPAPYAFVSVNTDGGTNFAAAGLSWTFGGPIYVRPGIGIAVHDGPLRRYRGTDRIDLGSRVLFKPELAIGWQVAPRWSVEASLTHLSHAQIFSHQNPGVDMAGIRVNFHLP
>NZ_CP053346.1|WP_171744253.1|1940077_1942174_+|S9-family-peptidase
MRAKYWLATLGGFGLAITAVQAASPPDLETFLAYPFLSGLTAPAQGGRLAWIENRQGKRSVWLAKGADLAATRLAGTGLDDGMELGELTFSPDGRILAWVRGGGEHNGWAASLPPPNPASAVVQPTQSVWVSVDGAAPIEVAEGAEPALSSTGRLAFIKGNQAWTVALTPGAKPEKLFYDRGHVGELVWSPDGSKLAFVSRRGDHSFVGIYAGPDVPIRWLAPATAYDGDFAWSPDGTRIAFVRREGEPDGLASPLAETPNPFSLWVAEVTANRARKIWESPKTLDGSYPEVPDGMFVQWMAGDRIVFRAEMDGWPHLYALPAAGGTPKLLTPGAFMVEHVTATPDGKSLIYDANTGATPGDVDRRHLYRVSVDGGAPVALTRGVEGEFTAAAVSDDRLAYVGAPATGAMRVMLAGAKGAAHPIGEAGAPYAPSGMVVPQPVTFTAADGTTIHGQLFAAKGGSAHKPGLVFVHGGPPRQMLAGWAYREYYAHSYAMNQYYAAHGYVVLSVNYRLGIGYGRAFQHPAKGGIAGNSEYQDVQAGARFLAATNGVDPARIGIWGGSYGGLLTAHALAHDSATFKAGVDFHGVHDWSLFPSLISKPDRYEQGDYEAAMKSAFESSPEAALKGWTSPVLLIAGDDDRNVRFDQTVDLARRLRAQGTPYETFILPNEIHGFLRYESWLRADEVSVEFLGRTLKP
>NZ_CP053346.1|WP_171744254.1|1942397_1943798_-|M20/M25/M40-family-metallo-hydrolase
MTRSALATFGAFLLATTAHAQAPGQLAFRDLYKEFIETDTSVATGSCTALAEKIAGHLKSAGYSDSQITLFTDPKFPLDGGLVAMLPGSDAKAKPMLLLGHLDVVNAKREDWERDPFKFIEENGYFYGRGTSDMKVMDAIWVDMFMRFKKEGYRPKRTIKLALTCGEESGARMNGAEWLSKNKPDLIAAEFAINEGGGGDTDGHGKIITQSMQVGEKSNRSYELTATNPGGHSSIPIDDNAIYELSDALEKVRAYKFPIRFNATTKAFFAKAGAARGDDLGKAMTALSANPSDKAAEATVIADRTYNSMLRTTCVATMLAAGHAVNALPQRAVATINCRIAPGEDGDTTKAALEKAIGDPKLQVAMVGRLRPVAVVPPLTPQIMGPAEKLVARYFPGVPLIPTMSTGATDATYLAPVGIPTYGVPGPWGDPDGNGAHGLNERHAVKSAYVSRDFLTDLVKAYADGK
>NZ_CP053346.1|WP_171744255.1|1944054_1945830_-|fatty-acyl-AMP-ligase
MSSGKTFDQDGGADDAAILRSTPSDDGLPRRYADFPTLGASLDYAAGGTRGLNFHDPRGTLVRPYPFAELRADAIVSARGLLAAGIKPGDRIALLAETGTEFAAAFFGAIYAGAWPVPLPLPTSFGGREAYIDQLAVQLGSSDPILLLYPAELEAMAEAAALLKGVTARSYAAQSALPAPDIALPQASPDDIAYLQYSSGSTRFPHGVAITHRALMSNLAAHSIGMSVQDGDRCVSWLPWYHDMGLVGCLLSPVANQVSTDYLKTEDFARRPLAWLDLISRNPGTTLSYSPTFGYDICARRMSSQTKASDRFDLSRWRVAGNGADMIRPDVMQAFVDAFAEAGFKSTAFLPSYGLAEATLAVSIMPPGEGIVVELVEETELSGSRDEALDRPQRYRAIVNCGKPVRDIVIQIRDEDGGTLPERAIGKVWCSGAPVMVGYFRDQEATDACLVDGWLDTGDMGYISDGYIYIVGRAKDMIIINGKNHWPQDIEWAVEQLPGFKAGDIAAFAITTPGGEETPAVLVQCRTSDPQERSRLRDEIRERVRAITGMNCVVELVPPKTLPRTSSGKLSRAKARNLYLSGEIQPYDLAA
>NZ_CP053346.1|WP_171744256.1|1945945_1946482_+|RecX-family-transcriptional-regulator
MRQSTASRQRRGTRSLDAKGLEALALRYVGRYATSRAKLRDYLLRKIGEADWAGEAAPDPDALVARIAELGYVDDRAFAEQRAAALGRRGYGARRIGMAFRAAGIEAEDGEEALASAREGALDAALALARRRRVGPYAAEPLDRPARERAIAMLVRGGHDPGLARRIAMSEPGEIPET
>NZ_CP053346.1|WP_171744257.1|1946597_1947188_+|CspA-family-cold-shock-protein
MSDDEAGRGLATGVDLDEASPAMATGETVLCVSGSVKWFDGTRGFGFMVGDDGEGDVLIHFSVLREHDRRTLPEGTRVVCEAVERQRGMQARRILKIDLSTAIGPDADMIAKKNADRVDPMALLAIAGPFEPVIVKWFNQIKGYGFVLRPGTTQDIFIHMETVRRAGLGEIEPDQPLRARIADGRKGPLAVIVEGA
>NZ_CP053346.1|WP_171744258.1|1947184_1947676_+|DUF192-domain-containing-protein
MIRNLRAVGAALLIAPVCAAFVPIAPVVFAPAAAEPAASAQSLRTVPLKIGGQGKVRTFTVEVATTFEQQETGLMYRKTMPADHGMIFPMSPPRPATFWMKNTYLPLDLIFIGPDHRIVRIAENAVPLSLDLIDCPEPAAAVLELNGGAVKAQGIAVGDQVRW

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

677508 : 754124

Acinetobacter_phage(25.0%)

transposase,coat,integrase

attL 665574:665590|attR 768058:768092

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
665574:665590	attL	NA	NA	NA	NA
WP_171743252.1\|677508_677742_+\|transposase	transposase	NA	NA	NA	NA
665574:665590	attL	NA	NA	NA	NA
WP_171743253.1\|677799_678114_+	DUF1153 domain-containing protein	NA	NA	NA	NA
WP_171743254.1\|681257_681635_+\|transposase	transposase	NA	NA	NA	NA
WP_171743255.1\|681989_683330_-	hypothetical protein	A0A0P0IY73	Acinetobacter_phage	4.8e-32	28.7
WP_171743256.1\|683359_684538_-	M24 family metallopeptidase	NA	NA	NA	NA
WP_171743257.1\|684540_685605_-	succinylglutamate desuccinylase/aspartoacylase family protein	NA	NA	NA	NA
WP_171743258.1\|685601_686990_-	aldehyde dehydrogenase family protein	NA	NA	NA	NA
WP_171743259.1\|686993_688382_-	aminotransferase class III-fold pyridoxal phosphate-dependent enzyme	NA	NA	NA	NA
WP_171743260.1\|688478_688955_+	Lrp/AsnC family transcriptional regulator	NA	NA	NA	NA
WP_171743261.1\|688979_691313_-	hypothetical protein	NA	NA	NA	NA
WP_171743262.1\|691429_694360_-	TonB-dependent receptor	NA	NA	NA	NA
WP_171743263.1\|694728_695211_+	Lrp/AsnC family transcriptional regulator	NA	NA	NA	NA
WP_171746751.1\|695363_695570_+	DUF2306 domain-containing protein	NA	NA	NA	NA
WP_171743264.1\|696238_697479_-\|transposase	IS3 family transposase	A0A1B0Z042	Pseudomonas_phage	5.9e-77	54.1
WP_171746752.1\|699110_700463_+\|transposase	IS1380 family transposase	NA	NA	NA	NA
WP_171743265.1\|700643_701396_-	hypothetical protein	NA	NA	NA	NA
WP_171743266.1\|701413_704428_-	Ti-type conjugative transfer relaxase TraA	V5UQN3	Mycobacterium_phage	4.4e-09	25.9
WP_171743267.1\|704601_704859_+	conjugal transfer protein TraD	NA	NA	NA	NA
WP_171743268.1\|704944_705169_+	conjugal transfer protein TraD	NA	NA	NA	NA
WP_171743269.1\|705190_706153_-	nucleotidyltransferase	NA	NA	NA	NA
WP_171743270.1\|707763_708408_-	hypothetical protein	NA	NA	NA	NA
WP_171746753.1\|708564_708750_+	hypothetical protein	NA	NA	NA	NA
WP_171743271.1\|709118_709907_+	methyltransferase domain-containing protein	NA	NA	NA	NA
WP_171743272.1\|710149_711502_+	hypothetical protein	NA	NA	NA	NA
WP_171743273.1\|711581_712508_+	phosphotransferase	NA	NA	NA	NA
WP_171743274.1\|712599_713070_+	GFA family protein	NA	NA	NA	NA
WP_171743275.1\|713132_714149_-	hypothetical protein	NA	NA	NA	NA
WP_171743276.1\|714846_715152_-	type II toxin-antitoxin system RelE/ParE family toxin	NA	NA	NA	NA
WP_171743277.1\|715148_715454_-	type II toxin-antitoxin system RelB/DinJ family antitoxin	NA	NA	NA	NA
WP_021316615.1\|716001_716217_+	AlpA family phage regulatory protein	NA	NA	NA	NA
WP_171743278.1\|716213_716408_+	helix-turn-helix domain-containing protein	NA	NA	NA	NA
WP_171746754.1\|716382_717621_-\|integrase	integrase arm-type DNA-binding domain-containing protein	A0A077KET4	Ralstonia_phage	4.7e-66	39.3
WP_171743279.1\|718131_719148_+	zinc-dependent alcohol dehydrogenase family protein	NA	NA	NA	NA
WP_171743280.1\|719258_720089_+	SDR family oxidoreductase	NA	NA	NA	NA
WP_171743281.1\|720210_721236_+	aldo/keto reductase	NA	NA	NA	NA
WP_171743282.1\|721324_721942_-	cysteine hydrolase	NA	NA	NA	NA
WP_171743283.1\|721956_724152_-	xanthine dehydrogenase family protein molybdopterin-binding subunit	NA	NA	NA	NA
WP_171743284.1\|724174_726388_-	xanthine dehydrogenase family protein molybdopterin-binding subunit	A0A0P0I429	Acinetobacter_phage	4.4e-30	25.2
WP_171743285.1\|726392_727343_-	xanthine dehydrogenase family protein subunit M	NA	NA	NA	NA
WP_171743286.1\|727339_727990_-	aldehyde dehydrogenase iron-sulfur subunit	NA	NA	NA	NA
WP_171743287.1\|728320_729214_+	LysR family transcriptional regulator	NA	NA	NA	NA
WP_171743288.1\|729339_732441_-	efflux RND transporter permease subunit	NA	NA	NA	NA
WP_171743289.1\|732437_733535_-	efflux RND transporter periplasmic adaptor subunit	NA	NA	NA	NA
WP_171743290.1\|733611_734232_-	TetR/AcrR family transcriptional regulator	NA	NA	NA	NA
WP_171743291.1\|734333_735788_+	efflux transporter outer membrane subunit	NA	NA	NA	NA
WP_171746755.1\|735813_736428_-\|integrase	site-specific integrase	A0A0K2CP59	Brevibacillus_phage	9.3e-07	26.2
WP_171743292.1\|737109_737622_-\|coat	spore coat protein U domain-containing protein	NA	NA	NA	NA
WP_171743293.1\|737672_737831_+	hypothetical protein	NA	NA	NA	NA
WP_171743294.1\|737824_738334_-\|coat	spore coat protein U domain-containing protein	NA	NA	NA	NA
738185:738201	attR	NA	NA	NA	NA
WP_171743295.1\|738506_739070_-\|coat	spore coat protein U domain-containing protein	NA	NA	NA	NA
738185:738201	attR	NA	NA	NA	NA
WP_171743296.1\|739069_740131_-\|coat	spore coat protein U domain-containing protein	NA	NA	NA	NA
WP_171743297.1\|740133_740553_-	hypothetical protein	NA	NA	NA	NA
WP_171743298.1\|740543_743045_-	fimbrial biogenesis outer membrane usher protein	NA	NA	NA	NA
WP_171743299.1\|743073_743835_-	molecular chaperone	NA	NA	NA	NA
WP_171743300.1\|743848_744415_-\|coat	spore coat protein U domain-containing protein	NA	NA	NA	NA
WP_171743301.1\|744592_745939_-	EAL domain-containing protein	NA	NA	NA	NA
WP_171743302.1\|746043_746643_+\|integrase	site-specific integrase	NA	NA	NA	NA
WP_171746756.1\|747498_748278_-	HNH endonuclease	A0A1S6KZY3	Salmonella_phage	8.2e-16	41.9
WP_171743303.1\|748927_749734_+	matrix metalloproteinase-11	NA	NA	NA	NA
WP_171743304.1\|749794_751228_+	hypothetical protein	NA	NA	NA	NA
WP_171743305.1\|751369_751561_+	hypothetical protein	NA	NA	NA	NA
WP_171743306.1\|751573_751726_+	hypothetical protein	NA	NA	NA	NA
WP_171746757.1\|751792_752410_-	hypothetical protein	NA	NA	NA	NA
WP_171743307.1\|752894_754124_-\|integrase	tyrosine-type recombinase/integrase	B7SYF8	Stenotrophomonas_phage	2.2e-87	43.7
768058:768092	attR	NA	NA	NA	NA

DBSCAN-SWA_2

5065638 : 5087443

Leptospira_phage(22.22%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_171746538.1\|5065638_5066809_+\|transposase	IS3 family transposase	S5WIU1	Leptospira_phage	6.3e-36	36.4
WP_171746539.1\|5066864_5067164_-\|transposase	transposase	NA	NA	NA	NA
WP_171746540.1\|5067295_5067574_-\|transposase	transposase	NA	NA	NA	NA
WP_171746541.1\|5067837_5068167_+	hypothetical protein	NA	NA	NA	NA
WP_171746542.1\|5068314_5068506_+	hypothetical protein	NA	NA	NA	NA
WP_171747221.1\|5069897_5070170_-	PEPxxWA-CTERM sorting domain-containing protein	NA	NA	NA	NA
WP_171746543.1\|5070314_5070536_-	hypothetical protein	NA	NA	NA	NA
WP_171746544.1\|5070758_5071975_-\|transposase	IS3 family transposase	Q8W6R2	Burkholderia_virus	7.6e-101	66.4
WP_171746545.1\|5072025_5073351_-	hypothetical protein	NA	NA	NA	NA
WP_171746546.1\|5073353_5073734_-	hypothetical protein	NA	NA	NA	NA
WP_171746547.1\|5074028_5075154_+\|transposase	IS3 family transposase	S5WIU1	Leptospira_phage	5.6e-50	42.1
WP_171746548.1\|5076234_5076612_-	hypothetical protein	NA	NA	NA	NA
WP_171746549.1\|5076745_5077114_-	hypothetical protein	NA	NA	NA	NA
WP_171746550.1\|5077177_5077837_-	hypothetical protein	NA	NA	NA	NA
WP_171746551.1\|5078185_5079805_-	chaperonin GroEL	A0A240F779	uncultured_virus	1.2e-175	59.1
WP_171746552.1\|5079860_5080175_-	co-chaperone GroES	A0A221S4G8	uncultured_virus	6.4e-20	57.6
WP_171746553.1\|5080446_5080683_+	hypothetical protein	NA	NA	NA	NA
WP_171746554.1\|5080679_5080949_+	protein usg	NA	NA	NA	NA
WP_171747222.1\|5081136_5081658_-	Hsp20/alpha crystallin family protein	A0A1B2LRT2	Wolbachia_phage	2.1e-12	29.8
WP_171747223.1\|5081740_5082217_-	Hsp20 family protein	R9S5E2	Prochlorococcus_phage	1.1e-23	48.8
WP_171746555.1\|5082662_5083358_-	MgtC/SapB family protein	G3MA03	Bacillus_virus	5.0e-17	48.1
WP_171746556.1\|5083485_5083935_+	NUDIX hydrolase	A0A1C3NEZ8	Phage_NCTB	1.4e-07	33.3
WP_171746557.1\|5084022_5084859_-	EamA family transporter	NA	NA	NA	NA
WP_171746558.1\|5084889_5085327_-	GFA family protein	NA	NA	NA	NA
WP_171746559.1\|5086705_5087443_+\|transposase	IS110 family transposase	NA	NA	NA	NA

Anti-CRISPR protein detection

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

2. NZ_CP053347

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

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

0 : 8703

uncultured_Caudovirales_phage(71.43%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_171747242.1\|23_1487_+	N-6 DNA methylase	NA	NA	NA	NA
WP_171747243.1\|1476_2391_+	hypothetical protein	NA	NA	NA	NA
WP_171747244.1\|2387_2876_+	hypothetical protein	NA	NA	NA	NA
WP_171747245.1\|2956_4243_-	arsenic transporter	A0A2H4J144	uncultured_Caudovirales_phage	1.7e-172	73.9
WP_171747246.1\|4319_5075_-	arsenical resistance protein ArsH	A0A2H4J5V6	uncultured_Caudovirales_phage	1.8e-76	63.6
WP_171747267.1\|5074_5551_-	GNAT family N-acetyltransferase	A0A2H4J155	uncultured_Caudovirales_phage	9.7e-20	41.5
WP_171747247.1\|5531_5963_-	arsenate reductase (glutaredoxin)	A0A2H4J8T1	uncultured_Caudovirales_phage	2.4e-49	70.1
WP_171747248.1\|5959_6487_-	arsenate reductase ArsC	A0A2H4J8A6	uncultured_Caudovirales_phage	2.2e-25	44.5
WP_171747249.1\|6498_6828_-	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_171747250.1\|7325_7955_+	transcription elongation protein SprT	A0A088FRV0	Escherichia_phage	2.5e-39	41.6
WP_171747251.1\|8019_8703_+	ParA family protein	B0ZSI1	Halomonas_phage	1.7e-17	34.7

DBSCAN-SWA_2

13660 : 21320

Mycobacterium_phage(50.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_171747259.1\|13660_16708_+	Ti-type conjugative transfer relaxase TraA	V5UQN3	Mycobacterium_phage	1.3e-11	25.9
WP_171747260.1\|16718_17426_+	hypothetical protein	NA	NA	NA	NA
WP_171747261.1\|17428_17785_+	hypothetical protein	NA	NA	NA	NA
WP_171747262.1\|17960_18104_+	hypothetical protein	NA	NA	NA	NA
WP_171747263.1\|18128_18716_+	hypothetical protein	NA	NA	NA	NA
WP_171747264.1\|18791_19085_-	hypothetical protein	NA	NA	NA	NA
WP_171747265.1\|19604_21320_+	RNA-directed DNA polymerase	Q7M2A9	Enterobacteria_phage	1.2e-08	29.1

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_CP053346

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NZ_CP053347

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection