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
LS483510	Mycoplasma mycoides subsp. capri strain GM12 genome assembly, chromosome: omosome	2 crisprs	NA	0	1	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: LS483510_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483510_1

140556-140639

Orphan

Consensus_repeat	Method
AAAAAACACTGGAATTCCATATA	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483510_1

>merge|LS483510|1|140556-140639|CRISPRCasFinder
AAAAAACACTGGAATTCCATATATTTTTTTCTAAATTACTAAAAAACAATCTTTTTACGAAAAAAAACACTGGAATTCCATATA

>LS483510|1|1|140556-140639|CRISPRCasFinder
AAAAAACACTGGAATTCCATATA	TTTTTTTCTAAATTACTAAAAAACAATCTTTTTACGAA
AAAAAACACTGGAATTCCATATA

Protein	Signature genes	Signature genes Name	Protein_function
LS483510.1\|SRX66131.1\|144313_144529_-\|exodeoxyribonuclease-VII-small-subunit	unknown	unknown	gnl\|CDD\|273536
LS483510.1\|SRX66117.1\|125537_127628_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|173412
LS483510.1\|SRX66128.1\|142671_142947_+\|hypothetical-protein	unknown	unknown	unknown
LS483510.1\|SRX66118.1\|127857_130347_-\|lipoprotein	unknown	unknown	gnl\|CDD\|224117
LS483510.1\|SRX66132.1\|144518_145928_-\|exodeoxyribonuclease-VII-large-subunit	unknown	unknown	gnl\|CDD\|272979
LS483510.1\|SRX66125.1\|137798_138716_+\|DNA-adenine-methylase	unknown	unknown	gnl\|CDD\|223415
LS483510.1\|SRX66130.1\|143507_144314_-\|TlyA-family-rRNA-(cytidine-2'-O)-methyltransferase	unknown	unknown	gnl\|CDD\|224110
LS483510.1\|SRX66121.1\|132102_134937_-\|preprotein-translocase-subunit-SecA	unknown	unknown	gnl\|CDD\|237258
LS483510.1\|SRX66119.1\|130517_131288_-\|hypothetical-protein	unknown	unknown	unknown
LS483510.1\|SRX66134.1\|146339_147452_-\|hypothetical-protein	unknown	unknown	unknown
LS483510.1\|SRX66124.1\|136792_137809_+\|CCATC--recognizing-type-II-restriction-modification-system-(MmyCVI)-adenine-DNA-methyltransferase-subunit-1	unknown	unknown	gnl\|CDD\|225927
LS483510.1\|SRX66122.1\|135027_135603_+\|Xaa-Pro-dipeptidase	unknown	unknown	gnl\|CDD\|376491
LS483510.1\|SRX66126.1\|138693_140277_+\|AlwI-family-type-II-restriction-endonuclease	unknown	unknown	gnl\|CDD\|312855
LS483510.1\|SRX66136.1\|148339_149092_-\|riboflavin-kinase	unknown	unknown	gnl\|CDD\|214901
LS483510.1\|SRX66129.1\|142936_143506_+\|dephospho-CoA-kinase	unknown	unknown	gnl\|CDD\|238980
LS483510.1\|SRX66123.1\|135677_136589_+\|~5'-3'-exonuclease	unknown	unknown	gnl\|CDD\|214682
LS483510.1\|SRX66135.1\|147477_148347_-\|deoxyribonuclease-IV	unknown	unknown	gnl\|CDD\|179214
LS483510.1\|SRX66127.1\|140716_142012_+\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|224292
LS483510.1\|SRX66133.1\|145929_146328_-\|transcription-antitermination-factor-NusB	unknown	unknown	gnl\|CDD\|273891
LS483510.1\|SRX66120.1\|131271_131988_-\|putative-membrane-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
LS483510.1\|SRX66131.1\|144313_144529_-\|exodeoxyribonuclease-VII-small-subunit	gnl\|CDD\|273536	TIGR01280, xseB, exodeoxyribonuclease VII, small subunit. This protein is the small subunit for exodeoxyribonuclease VII. Exodeoxyribonuclease VII is made of a complex of four small subunits to one large subunit. The complex degrades single-stranded DNA into large acid-insoluble oligonucleotides. These nucleotides are then degraded further into acid-soluble oligonucleotides. [DNA metabolism, Degradation of DNA].	6.53311e-06
LS483510.1\|SRX66117.1\|125537_127628_-\|hypothetical-protein	gnl\|CDD\|173412	PTZ00121, PTZ00121, MAEBL; Provisional.	4.99109e-12
LS483510.1\|SRX66118.1\|127857_130347_-\|lipoprotein	gnl\|CDD\|224117	COG1196, Smc, Chromosome segregation ATPases [Cell division and chromosome partitioning].	2.67534e-14
LS483510.1\|SRX66132.1\|144518_145928_-\|exodeoxyribonuclease-VII-large-subunit	gnl\|CDD\|272979	TIGR00237, exodeoxyribonuclease_VII_large_subunit, exodeoxyribonuclease VII, large subunit. This family consist of exodeoxyribonuclease VII, large subunit XseA which catalyses exonucleolytic cleavage in either the 5'->3' or 3'->5' direction to yield 5'-phosphomononucleotides. Exonuclease VII consists of one large subunit and four small subunits. [DNA metabolism, Degradation of DNA].	5.43204e-150
LS483510.1\|SRX66125.1\|137798_138716_+\|DNA-adenine-methylase	gnl\|CDD\|223415	COG0338, Dam, Site-specific DNA methylase [DNA replication, recombination, and repair].	1.50825e-26
LS483510.1\|SRX66130.1\|143507_144314_-\|TlyA-family-rRNA-(cytidine-2'-O)-methyltransferase	gnl\|CDD\|224110	COG1189, COG1189, Predicted rRNA methylase [Translation, ribosomal structure and biogenesis].	9.92721e-90
LS483510.1\|SRX66121.1\|132102_134937_-\|preprotein-translocase-subunit-SecA	gnl\|CDD\|237258	PRK12903, secA, preprotein translocase subunit SecA; Reviewed.	0
LS483510.1\|SRX66124.1\|136792_137809_+\|CCATC--recognizing-type-II-restriction-modification-system-(MmyCVI)-adenine-DNA-methyltransferase-subunit-1	gnl\|CDD\|225927	COG3392, COG3392, Adenine-specific DNA methylase [DNA replication, recombination, and repair].	1.28918e-66
LS483510.1\|SRX66122.1\|135027_135603_+\|Xaa-Pro-dipeptidase	gnl\|CDD\|376491	pfam01205, UPF0029, Uncharacterized protein family UPF0029.	1.35261e-43
LS483510.1\|SRX66126.1\|138693_140277_+\|AlwI-family-type-II-restriction-endonuclease	gnl\|CDD\|312855	pfam09491, RE_AlwI, AlwI restriction endonuclease. This family includes the AlwI (recognizes GGATC), Bsp6I (recognizes GC^NGC), BstNBI (recognizes GASTC), PleI(recognizes GAGTC) and MlyI (recognizes GAGTC) restriction endonucleases.	2.94452e-32
LS483510.1\|SRX66136.1\|148339_149092_-\|riboflavin-kinase	gnl\|CDD\|214901	smart00904, Flavokinase, Riboflavin kinase. Riboflavin is converted into catalytically active cofactors (FAD and FMN) by the actions of riboflavin kinase, which converts it into FMN, and FAD synthetase, which adenylates FMN to FAD. Eukaryotes usually have two separate enzymes, while most prokaryotes have a single bifunctional protein that can carry out both catalyses, although exceptions occur in both cases. While eukaryotic monofunctional riboflavin kinase is orthologous to the bifunctional prokaryotic enzyme. the monofunctional FAD synthetase differs from its prokaryotic counterpart, and is instead related to the PAPS-reductase family. The bacterial FAD synthetase that is part of the bifunctional enzyme has remote similarity to nucleotidyl transferases and, hence, it may be involved in the adenylylation reaction of FAD synthetases. This entry represents riboflavin kinase, which occurs as part of a bifunctional enzyme or a stand-alone enzyme.	2.89707e-39
LS483510.1\|SRX66129.1\|142936_143506_+\|dephospho-CoA-kinase	gnl\|CDD\|238980	cd02022, DPCK, Dephospho-coenzyme A kinase (DPCK, EC 2.7.1.24) catalyzes the phosphorylation of dephosphocoenzyme A (dCoA) to yield CoA, which is the final step in CoA biosynthesis.	5.1944e-35
LS483510.1\|SRX66123.1\|135677_136589_+\|~5'-3'-exonuclease	gnl\|CDD\|214682	smart00475, 53EXOc, 5'-3' exonuclease.	3.91482e-70
LS483510.1\|SRX66135.1\|147477_148347_-\|deoxyribonuclease-IV	gnl\|CDD\|179214	PRK01060, PRK01060, endonuclease IV; Provisional.	4.01977e-127
LS483510.1\|SRX66127.1\|140716_142012_+\|ATP-binding-protein	gnl\|CDD\|224292	COG1373, COG1373, Predicted ATPase (AAA+ superfamily) [General function prediction only].	4.42008e-57
LS483510.1\|SRX66133.1\|145929_146328_-\|transcription-antitermination-factor-NusB	gnl\|CDD\|273891	TIGR01951, nusB, transcription antitermination factor NusB. A transcription antitermination complex active in many bacteria was designated N-utilization substance (Nus) in E. coli because of its interaction with phage lambda protein N. This model represents NusB. Other components are NusA and NusG. NusE is, in fact, ribosomal protein S10. [Transcription, Transcription factors].	9.6032e-29

>LS483510.1|SRX66126.1|138693_140277_+|AlwI-family-type-II-restriction-endonuclease
MRKVEEHKPISFSTTMRNPERMSQFIACMKDFEGHILTDELIMQIVRKVIKNKLYKPNYIKENCAINNIYNDESSTFSNVQLDDIVNNSPQNHKEAGFAKGWSSRFDTWYKLCKEFGFIYYDMDKKIEISSSGHMLCDAYLLNSKYDDLNNSGKKIQKIFLNALMKYQTNNPFRRNLNQNAPIPLLLNVLNLLALNSYSTGLHRREIPFLMCWENNDYERLYEFIINFRNKYGFKASDEIIYEECLKLLKSSNKKRFKMSQIIKEGVDDFIRKLRITGIFSLRGLGRFVDINKLESESVDYIIKNYTKYNIFSNKYDFYKYMSEIDTKILEFQEIAANHEINNIRIKTLRKISQKYSVEQIHKELRNLQLNKNSEDEYFKLIDSPTRLEFLTSIAIIQKFPQYEIHPNYSIDDEGNPTFTAKGGVADIEIYDTNLNSIVEVTLMKSRQQAANEIPAITRHLKKQRDDYGNNNVFSLFIAPNIHEDTVYMCEFTRYKEKLGIYPYTIVDFVQKIQTTNSLLELEYNLN
>LS483510.1|SRX66125.1|137798_138716_+|DNA-adenine-methylase
MKNNIXSPFFYVGDKYKIMPQIVKFFPEKINNYYEPFLGGGSSAMYTKANKYFLNDINKSIIDLHKYLSSYSKNKNLLLNNLFKLIKKYRLSCSYLSITVPDELKKKYVKTYYSKFNKESYIELRNDYNKKNDSLKLYLLLIYGFNHMIRFNQQGKFNLPVGNVDFNKNVYQALMTYLEFADDNKIEFSNNDYIDFIKEIDFKEGDFIYLDPPYLISNSEYNRNWTIIDEQNLYDLIDNLDRKKVYFGLSNMLTHKGRKNHLLEKRMKKYYIHEIKSNYISRFDNKIKKDSKEVYITNYEKSRRT
>LS483510.1|SRX66124.1|136792_137809_+|CCATC--recognizing-type-II-restriction-modification-system-(MmyCVI)-adenine-DNA-methyltransferase-subunit-1
MRLTSRRYIGSKAKLLDWIFSNIDNNVKGNSFFDIFAGTGCVIEKALTSYDSVIINDILSSNKVVYDAFWGDIVINIDIINKYKLMFNSLDSIIDHNYFSINYGDKYFGVNDSKKIGYIRELIENDFKKNYINRREKNILLASLIYSIDKIANTVGHYEAYRKVEIIDNRFKFDLIDIPNKNINKKVEIYKEDANRLARKIYSDIVFVDPPYNSRQYSRFYHVIENLVEWEKPELFGIALKPAPQKMSEYCRNNAPAVFDDLITNLNCKYIVVTYNNTYNSKSSSSKNKIKLEEILNSLNKRGKTQIFSSDHRFFNAGKTSLPNHKEYLFITEVTCEK
>LS483510.1|SRX66123.1|135677_136589_+|~5'-3'-exonuclease
MITNETKPILLIDGYHLLHKGYYGTLKRTIVSKNKDGIVINAIYSFVANILKFVQSDRYHSVIVAFDFDENCWRKELYSEYKAKRKPTPIDLVPQLQIARDFLTSANISWYEKYNYEGDDVIGSICRIANKLGYDVCILTNDKDIYQLVNNKTSIITNISKKEKTKIIKPQQVYEHFLCQPNQVADIKAILGDQSDNIKGVKYIKRKQAENLINKYENVENILAHINELNEPLKTIISENKQLIIDNKKITKILTNVKLGRINFKPTKITYYGLIRFLKEQEMYAFIKPIRRYLDRTNKNLKK
>LS483510.1|SRX66122.1|135027_135603_+|Xaa-Pro-dipeptidase
MKTIKKEIYKNEFIIKNSKFITIATNINSKDELEEFLNKYSDINATHNCYAYMIYDQKLIGGYNDDHEPKNTAGKPIFNVISKNNLVNIVILVIRYFGGIKLGASVLTRTYSNAASLIIKDLEIIEIKTYYQYLISFDIKNLKLVNQWINQNNIEIISKDFSLNVVFKIRSTSKITSCNFFKIIDFKTIKN
>LS483510.1|SRX66121.1|132102_134937_-|preprotein-translocase-subunit-SecA
MVSDKRLLKKFGKIADKIIALEPQMRQLKDEDFILKTQEFKQMLEDGKSLDDILIEVYAVAREAARRVLGLNAYKVQLIGGIILNSGDIAEMRTGEGKTLTGIFPAYLNALSGKGVHIVTVNEYLSKRDSEINGQVFDLLGISVGLNGSSLTKTEKREAYNKDITYTTNAELGFDYLRDNMVSDYSLKVQRKLNYCIIDEADSVLIDEARTPLIISGGTSTRINLYKAANNFALTLKEHDDLDIDLESKQVYLNEQGMKKANEFFSLKNLFAIENTEIFHLIMNALKAQFAFKEGVEYTVRDNEILLIDQFTGRIMHGRSYSDGLQQALQAKENVDIEEETVTLATITYQNFYRLYSKIAGMTGTAKTEEEEFIKIYNTRVIQTPTNKPVIRKDEPDLTFGTKNAALKKLVEDVLEAHEKGAPILIGTTSVESSEQIARYLKKANLKFETINAKNHDREAEIVSKAGEIGAITLATNMAGRGTDIKLAKGVAELGGLRVFGVERNEARRIDNQLRGRSGRQGDPGLSRFYISMDDDLMMRFTAPKTRQRFKALGDDYIKSKMFTRAVTNAQKKLEGMNFDQRKNVLDYDNILAQQREIIYAQRDDILEANDLSVVIEKMQITAAYELIEKHSTLVHGEKTINKKELLDAIDGTLVPKNKFRVDDFNNKEKMDLAVEIAEGMMQLYKARISDIPDDVIIGMERKIILDSFDKYWTKHLDIAGKLKSGIYLQQYAQNNPLAIYVEQATDLFNKMKINIANEVVENLANVILRVVEDEEQREERIEVTDKDIEEILFETGLQPSDINNKAINQRFDELEEEFKDDKQKLRRLRIQRDVMLGLVLELERRAEMIISPQNDQQAITQLIKELQNDIDIASITIDQIHQNFNNMVEQINDPEKLKHLVIAKDVLLQLVARMDDIKEQEKQTRKKKKKKPHEDESSKTKIG
>LS483510.1|SRX66120.1|131271_131988_-|putative-membrane-protein
MQKRTIKSDTIFYSVILFLNLLTNFIYWITHAFNVVYVDEPTNLDIVLALDSASIAIWGLWISTFYAGICLYHSFIKKQLYQAYLLQLFIISMLISTGLIFIGISIINKTANINNWSALLRVVNVHFLLPTSMLLYLIFFRTNMIISKKSKLVGMWRILAVGLSYISWITYRTVPNVQVNLINKPFLYTSLQPSNIGWAIFMSLSFSSFILYFLTYLIIVLINNKINDKYGGCDAKTI
>LS483510.1|SRX66119.1|130517_131288_-|hypothetical-protein
MLKRFNQFRQQRSFKLELIISSILLFFAISCLVLYFITKSVGLYNKKTLSADVIFLQDITFLSEWYAVFVMIFCSFKISRMLTSKQVYLYKYTEYSFTSWSIFIFLLYIAGFIMGQAIINDDKDFPTLYRALAIHVFIPITWITYFILFPLNDQKTKKQLWLGCLQTFTILCFYSLWLLLRLLPGISLDDKIWINKIPYSFISPYNIGVIKYIFVNIGIFSVFIGGYILTYYSNKFIYKRITTSKNIDKTKEIITK
>LS483510.1|SRX66118.1|127857_130347_-|lipoprotein
MKKLLTILGSIMISTSGAALVVACKTPATKQPTNSNENTNQNEPTRPSEKDKDQTDPKKPVEPVNPSSKPENNQTKPTENYDPKTYKDTTIFNRHFVSGNPSSWVGTIHNSSFIYGSPFKPNNETKPNESTTPIEPKKPVDPTPSTKPNDNNRNDSNSNQSRPLTPLQPSIPTNKPETKPVSPTTTWYSVYNDSATGADINLNPTKEQIEKEEKRLEDWVKEYLDKNKRENQALFDYLIKIEYDRIFRDSPTGADINFYLTKEQIEAENKKQEDQLKAILDKNYKDNFANLMAIKASQTIKELFSDEFSDLVKQAVQRYKHHGDTHARESAKITEEIFSDEFSNKVKEAVERYKKHGDTHARESAKATIELFSXEFSDLVKQAVQRYKHHGDTHARESANAAEKLFNDKYNLVNEYKHNLETKLAKLNEEVNTHILERTRIEKEYNNKEKELEELATNNLVTLKKEYETGKQNLESRKTENETKLDRITLELPKLKDXKEKIKEEIKDSTELLEEAKLLLKENQDKQVEHNKVLNQAKDLEHQIDSINKQIESKNKLVTDNNNKEKELLDIEKELDKELSEEKVIIKQLDDENKLYEKIIDDLKKETYDSDLWFYDYGDWTLWTGFNHNKIARLKNYIYGNKELKKEVPNIIKNLEKELEITKQQNIEKIKQLKEQNTKIQAEISEITKSLEPLNAEKNKIDKQLSDINSEVVKTNKNIELYTNNLRTLEEEITSNSELQKQIIAQIDQYTSDQLSLEKQKEEILNSIKEFENSTNKIILESKQQYEDELLKLEKQAHSLESKEDEKIKEIEKTIAKLKESIKLLNQKY
>LS483510.1|SRX66117.1|125537_127628_-|hypothetical-protein
MKKLLAILGTIAISSTGASLVIACNNPNSKPSVEPDKTTPKNKPKETAKEETDKNSTNKTDKNSKESSDKNNTVLTKRSWNSVFNDSLTGYDIIYKLDETVLQNNKHYKFFVNSSSNLVSDLFDDKFAEEVKEAKNRWDKIQAKKTKLEKERLYKEFTTSSANATEDYFKTLEKIAELEAKAEAXKKELEKWEAKLAEEFKNSASSTTEDYFKTLEKISELEAKAKEKEKEAENRTKAEEKAEKEKVDNLIDAEINAELASDLTEDYFKTLEKIAELEAKAEAKKKELEKWEAKLAEEFKNSASSTTEDYFKTLEKISELEAKAKEKEKEAENRTKAEEKAEKEKVDNLIDAEINAELASDLTEDYFKTLEKIAELEAKAEAKKKELEKWEAKLAEEFKNSASSTTEDYFKTLEKISELEAKAKEKEKEAENRTKAEEKAEKEKVDNLIDAEINAELASDLTEDYFKTLEKIAELEAKAEAKKKELEKWEAKLAEEFKNSASSTTEDYFKTLEKISELEAKAKEKEKEAENRTKAEEKAEKEKVDNLIDAEINAELASDLTEDYFKTLEKIAELEAKAEAKKKELEKWEAKLAEEFKNSASSTTEDYFKTLDTTKEVSEWNSEKEKLIQLISNINKQVEELKESGKDINSVIVTVESNLESYKNNIKEHKNSKDFWRFEMWSHWLEDVLANLKKQN
>LS483510.1|SRX66127.1|140716_142012_+|ATP-binding-protein
MVIKRDQYLDKLISKKHNGRVKIITGIRRCGKSYLLFNLFKDYLLDNGVDQSQIITMNLDDPLNVKYHNPLELYNYFLNKTTNKEIQYYVFIDEIQNCQAIKNPYFKEDSKLIDFTGVLIGLMLHENIDIYVTGSNSKMLSSEIVTEFRDRGDEIKVYPLTFKEIYESKQVKNFDLKTYFIYGGMPFVYKIDSSNERAIYLKNLFKTTYIRDILERYNVNNDQLILETLLNFISSNIGSLTNPLKLANRFLSEQKTKISSNTISKYIRYFEESFIISKAKRYDVKGAKYFTTPLKYYFTDIGLRNAWLNFSELDRSHILENIVYNELKIRGFNVDVGYLLYDQKSSDSRNIHNLEIDFIANLIDLKYYIQVALNIDEADKKEQEIRPLLKVNDNYKKVVIVYDDIFEHYDNNGILYIGLKKFLLDPEALNS
>LS483510.1|SRX66128.1|142671_142947_+|hypothetical-protein
MSYYYRHNFSFSYHGLQRAKERLKLXDKKDYEVKEICLEHIRNSTKSFMSGNEIYISASNTNIFFVVNKTNNLIITVTEISAEKQLRMHGI
>LS483510.1|SRX66129.1|142936_143506_+|dephospho-CoA-kinase
MVYKMIIGIYGKIGSGKTYISNKFINFHPEFKIINADNVSKKLLEDSKIKSKLFEIDNNIIKNDIVDKKYLRKKLFTNKKLKQQVDSLLWPLISKQIQKEIKNNPNTNYIIEAALLFELNLTNLDLIVKVKSSLLKSIFRVLKRDKTNIRDILRIRRNQNKSIKRKKPDLVISNFYQLEFYIQKNRLLI
>LS483510.1|SRX66130.1|143507_144314_-|TlyA-family-rRNA-(cytidine-2'-O)-methyltransferase
MKLRLDEYIYKNNLTQSRNKAKEHILNKEVYVNNIAIIKPSFLVDSNDLIEIRSTKLEYVSRAYEKLKKAINKWNIDLTNKICLDIGASTGGFTQCCLDNNASLVYAVDVGTDQLHSSLLNNLKVINMSQYNFRNAKKQDFLKSIDFVCCDVSFISLEKIFLPLKDILEFNTSGVFLIKPQFELQPKNIKNGRINSKLDHKQAILKVISYANNNSFDVINLDYSPILGNKKQNIEYLAYVIKKENNYKIWKEDQINQLVNIAWKELKK
>LS483510.1|SRX66131.1|144313_144529_-|exodeoxyribonuclease-VII-small-subunit
MSNKSKSYDELISEIKEDTKKLSSNEISVEQAMEIFEQNIEKIKLAKEKLTQYKGQIYKVMQDDELEEFKD
>LS483510.1|SRX66132.1|144518_145928_-|exodeoxyribonuclease-VII-large-subunit
MEKILTVQELNEALKTLIENKQEFKDIYVQGELSNLTFNKSGHIYFSIKEQDAAINCMMWKTNAYKIQSLNLEDGMQIICYGRLTYYIPTGRVSFEVRDIKIHGIGDLQKIFEQRYKELEQKGWFDPNLKKPIPEFVKNVGIITADSGAAIYDLIRTIHRRLPLINIFLFPAQVQGDKAEKDIANKIKQANDFKVQLDVLIVGRGGGSYEDLWAFNELEVLQAIKNSQIPIISAVGHEPDWVLSDYVADIRAATPTAAGELVSKSIIEIKNQLKXYYQNYKTLILNKLDFFDEKLNNYKKEQTKYIKNNFSFKYLQLKQLSIDNTKWTKNKINLVIDKLENYKQSINNSTLHIINSQNKTLKNYLIADEQKILNYLKKQISEFNYTISSFKGHINQILKYEELSFNTLENKLNSLDPLKPLQNGYSIVTNLNHQKIRSYKQVKLNEDLKVILTDSKLTVTIKEVKINEQ
>LS483510.1|SRX66133.1|145929_146328_-|transcription-antitermination-factor-NusB
METKISFSKKRKLLIQTFYKYQLLNASIDYIHQDILDDVQNINNKDVLFEIEQIAKKQTDLINHININVSSSWKWDRIPAVIRAILIVGTYEILYTNTPKPVTINEMVKYVKEIEPDFDYKFVNAVLDKLVK
>LS483510.1|SRX66134.1|146339_147452_-|hypothetical-protein
MKKLLSIITGFSLLITPSLFXISCSSKVQVISKFDDITSIKNTGAFKNNQAFISRNELKEIVNSNNTTNSSTASSTAVMTSTSTTSTGTQPNNNDAKYASERLKALAANNFTKNKKQAWDSLQNTSMTFYKKVEPTAVNVLGYEQITKDNVEKLEKNLKTVFLVFKDNTKETEKLEVELLPEINNGNKVIDNGSLYLDLLEKPENLKLXNQKSIIEVLRPEITKIKVVLQNTKNNNSTNKEDIKNTEVFNLLIKQLSIYLANTVKYFNSESGIITTNPTFSYKTRSNQIYDYIVKNKKDELYKKLETAFTSEFNKINFIDIFKDFQFDENNSNDNKKITTKIIKSSTNSSTSSSNSSTTTTTEPSSTTTR
>LS483510.1|SRX66135.1|147477_148347_-|deoxyribonuclease-IV
MNKVLLGCHVSMNKQNNYLVGSVNEAISYKANTFMIFTGPPQSTLRTNTNHLYINQMHELMNSYKIDAKDLVVHAPYIINIANSVDQNKWKFAVDFLIQEIKRCEEIKIPTLVLHPGSHTTGNYKDSLNQIIKALDIVSNYQVNVKIALETMSGKGTEVCSKLEDFKYILDNVKNKDKVGVCLDTCHLHDAGYDLSKWDEFKEQMKQNFDLNKVLCIHLNDSKNMISSHKDRHANIGYGYVGFDTLVNVVFDKDFSNISKILETPYIDKKPPYKIEIEDLLNKTFTNRL
>LS483510.1|SRX66136.1|148339_149092_-|riboflavin-kinase
MNNQIIALFCDFKYITTKLLNKFNKNQLIIFGYSLNKDDFDYICSDYQLEIFKNQNYKFIDLKNENIDQLVKKYQISKIHITKSFKNYDHFLNFFPNTITEDDLLDINNIKKALINADINTFYKIAGFNYTFSGIVTHCNHLGRTIGFPTANILTNDSLVIKNGVYLVKVIIGDKNIQFGMGDHWINRNNLKVFETYIFNFSNDIYNSKITFELLDYIRDNQKINSLDQLKTLLNNDKKECLKRLEKYNE

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Crispr_ID: LS483510_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483510_2

228792-228882

Orphan

Consensus_repeat	Method
AATAATTAAGGTGTATTTCCACCTTTTTT	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483510_2

>merge|LS483510|2|228792-228882|CRISPRCasFinder
AATAATTAAGGTGTATTTCCACCTTTTTTGTTCATTATAATTTTATCATAAAAATACCTACGAATAATTAAGGTGTATTTCCACCTTTTTT

>LS483510|2|2|228792-228882|CRISPRCasFinder
AATAATTAAGGTGTATTTCCACCTTTTTT	GTTCATTATAATTTTATCATAAAAATACCTACG
AATAATTAAGGTGTATTTCCACCTTTTTT

Protein	Signature genes	Signature genes Name	Protein_function
LS483510.1\|SRX66201.1\|234437_235418_-\|alpha-glycosidase	unknown	unknown	gnl\|CDD\|200477
LS483510.1\|SRX66198.1\|231833_231980_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|319818
LS483510.1\|SRX66187.1\|213477_216168_-\|alanine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234701
LS483510.1\|SRX66197.1\|229919_231617_-\|LppA-family-lipoprotein	unknown	unknown	gnl\|CDD\|274602
LS483510.1\|SRX66195.1\|227468_228773_-\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|224292
LS483510.1\|SRX66188.1\|216195_216471_-\|hypothetical-protein	unknown	unknown	unknown
LS483510.1\|SRX66193.1\|222559_225661_+\|lipoprotein	unknown	unknown	gnl\|CDD\|173869
LS483510.1\|SRX66200.1\|233808_234438_-\|beta-phosphoglucomutase	unknown	unknown	gnl\|CDD\|213672
LS483510.1\|SRX66196.1\|229004_229886_+\|Cof-type-HAD-IIB-family-hydrolase	unknown	unknown	gnl\|CDD\|319818
LS483510.1\|SRX66199.1\|232016_233699_-\|LppA-family-lipoprotein	unknown	unknown	gnl\|CDD\|274602
LS483510.1\|SRX66189.1\|216688_217933_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223674
LS483510.1\|SRX66194.1\|226078_227374_-\|ATP-binding-protein	unknown	unknown	gnl\|CDD\|224292
LS483510.1\|SRX66190.1\|217948_218959_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224094
LS483510.1\|SRX66205.1\|240444_242235_+\|lipoprotein	unknown	unknown	gnl\|CDD\|270450
LS483510.1\|SRX66203.1\|236296_238093_-\|alpha-glycosidase	unknown	unknown	gnl\|CDD\|200477
LS483510.1\|SRX66191.1\|218972_220673_+\|peptide-ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|223521
LS483510.1\|SRX66192.1\|220674_222543_+\|ABC-transporter	unknown	unknown	gnl\|CDD\|185037
LS483510.1\|SRX66204.1\|238350_240150_+\|lipoprotein	unknown	unknown	gnl\|CDD\|270303
LS483510.1\|SRX66186.1\|212184_213126_-\|BspA-family-leucine-rich-repeat-surface-protein	unknown	unknown	gnl\|CDD\|308794
LS483510.1\|SRX66202.1\|235398_236178_-\|alpha-glycosidase	unknown	unknown	gnl\|CDD\|200477

Protein	Function_ID	Function_description	E-value
LS483510.1\|SRX66201.1\|234437_235418_-\|alpha-glycosidase	gnl\|CDD\|200477	cd11338, AmyAc_CMD, Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	1.22451e-111
LS483510.1\|SRX66198.1\|231833_231980_+\|hypothetical-protein	gnl\|CDD\|319818	cd07516, HAD_Pase, phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily. Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	8.14322e-10
LS483510.1\|SRX66187.1\|213477_216168_-\|alanine--tRNA-ligase	gnl\|CDD\|234701	PRK00252, alaS, alanyl-tRNA synthetase; Reviewed.	0
LS483510.1\|SRX66197.1\|229919_231617_-\|LppA-family-lipoprotein	gnl\|CDD\|274602	TIGR03490, Uncharacterized_lipoprotein_lpp, mycoides cluster lipoprotein, LppA/P72 family. Members of this protein family occur in Mycoplasma mycoides, Mycoplasma hyopneumoniae, and related Mycoplasmas in small paralogous families that may also include truncated forms and/or pseudogenes. Members are predicted lipoproteins with a conserved signal peptidase II processing and lipid attachment site. Note that the name for certain characterized members, p72, reflects an anomalous apparent molecular weight, given a theoretical MW of about 61 kDa.	2.18256e-174
LS483510.1\|SRX66195.1\|227468_228773_-\|ATP-binding-protein	gnl\|CDD\|224292	COG1373, COG1373, Predicted ATPase (AAA+ superfamily) [General function prediction only].	2.18584e-56
LS483510.1\|SRX66193.1\|222559_225661_+\|lipoprotein	gnl\|CDD\|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	6.25286e-11
LS483510.1\|SRX66200.1\|233808_234438_-\|beta-phosphoglucomutase	gnl\|CDD\|213672	TIGR01990, bPGM, beta-phosphoglucomutase. This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides].	4.37984e-71
LS483510.1\|SRX66196.1\|229004_229886_+\|Cof-type-HAD-IIB-family-hydrolase	gnl\|CDD\|319818	cd07516, HAD_Pase, phosphatase, similar to Escherichia coli Cof and Thermotoga maritima TM0651; belongs to the haloacid dehalogenase-like superfamily. Escherichia coli Cof is involved in the hydrolysis of HMP-PP (4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate, an intermediate in thiamin biosynthesis), Cof also has phosphatase activity against the coenzymes pyridoxal phosphate (PLP) and FMN. Thermotoga maritima TM0651 acts as a phosphatase with a phosphorylated carbohydrate molecule as a possible substrate. Escherichia coli YbhA is also a member of this family and catalyzes the dephosphorylation of PLP, YbhA can also hydrolyze erythrose-4-phosphate and fructose-1,6-bis-phosphate. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	9.2288e-59
LS483510.1\|SRX66199.1\|232016_233699_-\|LppA-family-lipoprotein	gnl\|CDD\|274602	TIGR03490, Uncharacterized_lipoprotein_lpp, mycoides cluster lipoprotein, LppA/P72 family. Members of this protein family occur in Mycoplasma mycoides, Mycoplasma hyopneumoniae, and related Mycoplasmas in small paralogous families that may also include truncated forms and/or pseudogenes. Members are predicted lipoproteins with a conserved signal peptidase II processing and lipid attachment site. Note that the name for certain characterized members, p72, reflects an anomalous apparent molecular weight, given a theoretical MW of about 61 kDa.	3.0076e-131
LS483510.1\|SRX66189.1\|216688_217933_+\|ABC-transporter-permease	gnl\|CDD\|223674	COG0601, DppB, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	2.14716e-44
LS483510.1\|SRX66194.1\|226078_227374_-\|ATP-binding-protein	gnl\|CDD\|224292	COG1373, COG1373, Predicted ATPase (AAA+ superfamily) [General function prediction only].	1.48069e-50
LS483510.1\|SRX66190.1\|217948_218959_+\|ABC-transporter-permease	gnl\|CDD\|224094	COG1173, DppC, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	5.06323e-47
LS483510.1\|SRX66205.1\|240444_242235_+\|lipoprotein	gnl\|CDD\|270450	cd14747, PBP2_MalE, Maltose-binding protein MalE; possesses type 2 periplasmic binding fold. This group includes the periplasmic maltose-binding component of an ABC transport system from the phytopathogen Xanthomonas citri and its related bacterial proteins. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 proteins are comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	0.00253297
LS483510.1\|SRX66203.1\|236296_238093_-\|alpha-glycosidase	gnl\|CDD\|200477	cd11338, AmyAc_CMD, Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	0
LS483510.1\|SRX66191.1\|218972_220673_+\|peptide-ABC-transporter-ATP-binding-protein	gnl\|CDD\|223521	COG0444, DppD, ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	6.5072e-118
LS483510.1\|SRX66192.1\|220674_222543_+\|ABC-transporter	gnl\|CDD\|185037	PRK15079, PRK15079, oligopeptide ABC transporter ATP-binding protein OppF; Provisional.	9.0578e-78
LS483510.1\|SRX66204.1\|238350_240150_+\|lipoprotein	gnl\|CDD\|270303	cd13585, PBP2_TMBP_like, The periplasmic-binding component of ABC transport systems specific for trehalose/maltose and similar oligosaccharides; possess type 2 periplasmic binding fold. This family includes the periplasmic trehalose/maltose-binding component of an ABC transport system and related proteins from archaea and bacteria. Members of this group belong to the type 2 periplasmic-binding fold superfamily. PBP2 is comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The majority of PBP2 proteins function in the uptake of small soluble substrates in eubacteria and archaea. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	0.00453094
LS483510.1\|SRX66186.1\|212184_213126_-\|BspA-family-leucine-rich-repeat-surface-protein	gnl\|CDD\|308794	pfam03382, DUF285, Mycoplasma protein of unknown function, DUF285. This region appears distantly related to leucine rich repeats.	1.58044e-54
LS483510.1\|SRX66202.1\|235398_236178_-\|alpha-glycosidase	gnl\|CDD\|200477	cd11338, AmyAc_CMD, Alpha amylase catalytic domain found in cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	9.14423e-64

>LS483510.1|SRX66195.1|227468_228773_-|ATP-binding-protein
MENMIIPRDFYLNQLLDKKDNGRVKVITGIRRCGKSELLFTLYKDYLLSTGVKKKQIIALQLDGDENIKYRDPLALGSYIRKQIKSKSKRYYVFIDEIQFCYAVFNPYVKEKEPSITFVDTVLGLMKIPNIDLYITGSNSKMLSSEILTQFSDRGDQIHVQPFSFSEIYHLFENSQDALAHYLNYGGMPEIYKLKTEEQKVQHLKQLFKTTYIRDVLLKYDIKNEEQILDKLLDFVSSVVGSLVSFNNLSKQLAANDQIKISPNTIQKYLSYFEESFVLSNARRYDIKGSEYFRSPSKYYFADIGLRNARLNFRQIEDNHLTENVIYNELIKRGYNVDVGMVEYEVNKANTRQKRQAEVDFVANLGHKRYYIQYADNINTKEKREQETNSLLRIKDNFKKIVVVKDNIIAKHDDNGILYLGLKQFLLEPNAIDI
>LS483510.1|SRX66194.1|226078_227374_-|ATP-binding-protein
MQINRDYYLNKLISKKNNNKIKVITGIKNVGKSYLLFNIYKNYLLSIGINEDQIITLKLDKWENANYRKLDSLYNYIKQRTSNPNKTYYVFIDEIQYCETIKQTNQSGYEQILTFVDVILSFYDNPNIDLYITGSNSKMLSSDILTNFRGRSSQIKVYPLVFSEVNYLFKNDDEALDHYINYGGLPEVYLNQTIEEKKXYLTNQFEEIYLKDIKERYNIQKEITILETLLKFVSSAIGSFTNPTKLQNRFKSEMKTDISSNTIANYLSYFENSFILSHIKKYDVKGNKHFSTINKYYFTDIGLRNACINYRQIESNHIIENIIYNELVKRNYSVYVSSVEYQTNSENKRTTKQLEVDFVIQKASKKYYIQFAMNVYTKQKKEQEINSLLRIKDNFKKIVIVYDDIEPRYDENGILYIGLKQFLLDENIIDF
>LS483510.1|SRX66193.1|222559_225661_+|lipoprotein
MKKVLGMTLLGSIIATAVASAVSCSVGISLDKILNRKNSNTRVLRELTNYSLANLNSATNNTSNDADIIANLQDVLLAVNNHDHYEGALAEYWDHNKDSDYWKFRLRKNAYWTKIENSKQVKGDLITGQDLFNTFXYVLNKNNLALTTEHFLTNFKYVPQLMDFIDKLSDPKYDKSNGQAKPDKLYDSRFNKDLPGDLRTNELRSSYWIDRAILAFNIEPTNEEKAKNLALDLSMSTKQLAKKSFEEGKIVDNGKSKEKNDNSNGLDSSXFDIGFHLSKKISYFESVISYLAFAPIPEVALLYAEDSGQKSNIYAGTNYGKPLARKSGYNGLWYSGPYVIQDYFPGSNLNLTKNEFYYNKENVHIEKILYSYVNKADAATRRFLFETGDVSSTRINANDLAGYKKYVGSDESNPVFEGTNVLKQKPTTTWAFGFNFNTKETSIYDDIKLDQEGSLVPTKRRVRTPEEDSILNRAIALKSLRIMTRFVLNRSLYAKFFSEAKDGNNHPVSSQLRNTFTSKYVSTYNDKEHKVLDKKSQNTVADYADFLAKDYYDITKYDDNNKKLNNTNSVSSTPVRTRRATPSGTSESSSASTEQQSWSDWMIKVLQKHSLYDESRLTSWANRFGKVKDKKDLKNTEKVSVYSEGNDAFLENDLLAFTAFLKEDQLQSKNGGQDGTFDLKRDPNKVEFKNPELAKEFGKLIGVYDKDFDPKKDYQNQDSKLSTLYKKINLLKQQVKEDLKNTSGITSNKPITIPFLLDPTGADDFKIKIQRLFGAFNYLVRNKGNGDIDSPFVFDIDKPIDQSAYLKQRRDSKFGLGAFGWSPDYDDPTNYLATLKYGGVYEHIQGWKKLFNGSELKTTNGSNKKGIKLTLKKSDGTSEKAFKELKDALQFFTNELTEIDENEVDIYKRYTRLAQLENFYTLSSAIIIPTHTHQADTLPIISYLDEFSKPTWPTGSHARRLVGVRMFDKIVTKEQFKKQKENFDKETLNGYRSVYPKTFDSKSNKNIYFDQFKGNWREEWKKEYESKNKKLNK
>LS483510.1|SRX66192.1|220674_222543_+|ABC-transporter
MIKKKNEAILKVRDLLIEFGNGRNKLKAVKGVTFDVYKGETFGLVGESGSGKTTIGRAIIGIQPISDGAIYFENKLLRGKSPDVYKINQKIARHLYIMQQNQLTTSLSLNDYSNEFKRVYYKYVQSKFFDFKTQELKDYEDGKSRIIKEGVNLNTTKLVSVKKNANLSIVIQAITDNXKRLLKIIRLQEKASRITKNISKHTSVKVELQDAINKYQDFVHDSILKVKDLENTIYNTLQEMLAIRNDVNEGKYTSVTKFFDQMGSRLKLVIKSQKLITPQLEDASHDQLMNLALTCPKYKNNYYLKKLKQRIEYLNLNNKTKLAQEYESVIQTVENSDFYDNLKTAEIFKSPNKKELKENKKDMQMIFQDPSSSLNERMAVEEIIKEGLDNFPELYSNDEVKKAYQQWFNQKNPENKIVEISEIDKKDIKRFLIXQLLETVGLLPEHLSRYPHEFSGGQRQRIGIARALIMKPKFVVADEPISALDVSIRAQIMNLLAKFQKQFDLTYIFIAHDLSVVRFATDRIAVIYRGDIVELAESNELFDLPLHPYTRSLLSAIPLPDPVQESKKVHFVYQPEVEHHDYLVDFPKWVEVSKNHFVYANEREIKAYKKQIKAYKEQLKNK
>LS483510.1|SRX66191.1|218972_220673_+|peptide-ABC-transporter-ATP-binding-protein
MKNVILSIKDLVVKFRVRSKVLTSIRNISFDIYDGETVAIVGESGSGKSVLTKTLTNMLESNGYIANGSIMYYPNKATRENESAVFKKDTDLVEFHKNSLESESRKGIKKYNNKKIKDALLTIKELEESTIESLNLKIDELQQKADLLKKYEFTNSTKKLVKRNEYLEQIKQLKEQIEWKKDPKKLDFEIQQLEKTIQTAKKEIYNFKTVNIYKKFRYFQIINLINKVNNNQLEDINKLEPHIKWLDEIEYKNNFESLALEILYDIRSNQTKKLDQEKLETLKELWDFIKRFNFWIKRSTDKNLQHLRGGTIATIFQDPMTSLNPLLSVGYQISEVLRNHSKLNRAEAKVEAINLMKRVGIPNAEKRYKDLPGKYSGGMRQRVVIAIALACRPKVLICDEPTTALDVTIQAQILDLIKELKEEYKFTVIFITHDLGVVANIADRVAVMYAGQIIEYGTTQDVFFNSKHPYTWALLSSLPQLGTKGEELYSISGTPPSLFKEIKADAFAPRNTFALAVDYKYEPPMFKISDTHYAKTWLLDPRAPKIKRPKQLNNLKKAVSDSKVGE
>LS483510.1|SRX66190.1|217948_218959_+|ABC-transporter-permease
MKTKQLEQPDFSALLDSEREAFFKRHGLDIYQIDHSLFELVGSQAQTSETIITKPYSYWKAVGKILITSKVFIICSIILLALLLTSIIVPYGKEAIPLKTPGVTQEHPSAQHWFGLGRNGEDYWIEIWLGLRSSLSFAFVMTFLQLSIGIIMGLIWGYYRKLDILFYQLTSLILVIPQLILIIVIMSVFGIGYWPMILGIVIQAWIGPAFSIRILVLSIRDADYNIASITLGTRSDKIIRKNVLPKILPVLIQVSTFSIPTAIAIESTLAYFDRGFVDGKVNTSLGKILQSIMQSSEWQVYPHLIVLPILFICIISTLFFLVLKVFADSLDPKNHR
>LS483510.1|SRX66189.1|216688_217933_+|ABC-transporter-permease
MKSTLKTKQEVLNLNSELLLDDFSLLNETNQQHKVSKWTTFKYWYYDTSANIYKYFLRHPLYGYSFKRILYGLITLLLSIIILYVVIRLITPDTKYLPPDIEKTGLSRAQQDKLLEDRMKRFGVYGPLIPQILTYLKNITPFIPKQIVLGSEVTILQNGNAIIDSSKLITETRWVYLGVTTATTIAEEGSDALSIFLKAMPYSFAIGSVSVLISYALAILIGVRAAKKKGKLFDNVFNGISALLLAIPSIVIIIGTFIFSVAVLGNSGIYNTGSFATRFWPIFAIVVINLPGIATFVRRYIVDEMTVDYAKFALAKGTSSNKTYYVHIFRNAGVRIIRSIPSEIILTVFGSSMIVETQWAIPGMGRLIKESAGGNDFFVFLGFTVLSSFVSIFAKLLADLVHVLLDPRVSLTKD
>LS483510.1|SRX66188.1|216195_216471_-|hypothetical-protein
MKKSKVFKELKDIDKFTKEQHEKQVNKSIXQVYDSDDFKMNFYDYQQAKKLRLIGWLIVFLIFIIGSLIGVLVGYLTLNVSSLDKLIYISI
>LS483510.1|SRX66187.1|213477_216168_-|alanine--tRNA-ligase
MKKLSTNQIRKIWLDFFISKNHYFLETVSLIPVDDPSLLWINSGVATLKPYFDGRKTPPSPRLTNSQKAIRTNDIENVGVTARHHTMFEMLGNFSIGDYFKKEAIELAWELLTDKNYFDIDKDKLYITVFNEDTEAYNIWKDVIKIDEDHIFRLSRKTNFWDVGQGPCGPNTEIFYDRGEIWDPNKIGPRLISDDIENDRYIEVWNIVFSQFNNDGNDNYTELPRKNIDTGAGLERFASIFQNTPTNFETDIFYPTIKKVEQLTNDQFKYSIDNYFNPNKKQTRINTAFKVIADHIRATVFAISDGVFPXNKDRGYIIRRLIRRSCVFGKELGIKQAFLYKLVDSVIESMKEFYPYLIDKKTLVEQTIKDEEEKFLKTLSKGYDLLENIIKTKNTVSDKDALLLFESYGFPIEQTIEISELSNVTVDIEGFKKLLEQTKQATRNARKDLKAWDKQNELFTKLKVESEFTGWSETSRDNAKVIYMFTDQKQVESITDQEAFVILDKTPFYAEKGGQAADSGIIFNDQMKGFVIDVQQGPMHQNIHRIKVQGTLKVNDLVNCRVDEEKRIYTMKNHSGTHMIHYALREVLGTSVMQSGSYNDENGLRMDFTYHRLPTNQELLKAQNLVLEKIKNKIDRQTYFCSLEESVKKHQALAFFTEKYDEIVRVIKFGDFSSELCGGTHVNNTSEIEDFIITGIESKGSGLYRIKCLTSFKTVNEYLNEQFKIYKDQAEIIIDKYNQNKDLLKNDQLENIYLQIKNITINKDNLLVIKDLLDKLKEINKDYDKKVNDLITANKLLKYKDLTPSLNKDNINEIRLETTDLNIKDXKQLADDLRNKYDDLIVILLSSTSENNFVVVAVSQSLQNXYKAIDIFNNLEGYETKGGGNANLAQGKFVKK
>LS483510.1|SRX66186.1|212184_213126_-|BspA-family-leucine-rich-repeat-surface-protein
MLLVHQLLVYANEKGLKDITLVDGLNENEHLKEDKEGKWQNIVKLKLYGSDFTFKPKKVLKDEVETIYSEDKKIVKQIGYKKVFNKDIKIKKITELIEEVPVHLPLKITSLSKAFSESKIKTVRNLDKWNTKNIKSMLSVFENAKTFNQDISNWDTSNVTNMSGMFKDAAQFNQSLNEWKVHNVVEMEDMFAGASSFNQNLNKWKTTSLENMKQMFWDASKFNGDISTWDVSKVKTLYNTFADATSFNQDISNWITSNVTIMEGTFSRANKFSYSLIKWNVGKVTTTKDFNKGIQSILGEDKLPKFTVPITYS
>LS483510.1|SRX66196.1|229004_229886_+|Cof-type-HAD-IIB-family-hydrolase
MKLKDLNLKRLILIDLDGTTLTNQNDQIHKITKKAILDAQKKGHVVCIVTGRPYRAVEHIYKELKLTTLLANFDGAHIHDPNNKLMKRVVLPINCEIIKQIINEPVIKGNVENILIEYYDKSLLWKTDKELEDFFHLNKAKNSKDFQFIKASPYTDWKSPSNNLVLKLKSDKHKDEVIRVLTKYQDAIKIQSDILYGITTSKTKPVITLTNKNADKGFASIFLAQYYNKDIRDVIAFGDQLNDLEMLKTVGCSVAMKNGVNSLKFVAKGITHYTNDEGGLGHYLNLLLAGKEV
>LS483510.1|SRX66197.1|229919_231617_-|LppA-family-lipoprotein
MRKFNKLFLTILPISSISAFSVVSCTTNTKNNNQIPTIPNNKKPENQTQPEQPSDKKPESTEEHTNKKPNENTNDQKQPNNSEKSDAEPNPGKPENKPNNSHNPKQPEQPKKPEHNDSNSNNNTNNNSNADQPQGDEPQDEPWNKVDFSDINKLDKEVKFEFFTTYSRMDAKSAWVQIQGRQPAIFKEIIFKGKNEILNRYEIEFDSQKVPNIVDEKGTIDNVGIKFSKNGKSKTREFVFTGFRKLENKVDKGKNKDEYIKPKTNIDKSLSGIFPSLVAYMLLYSEETQSNNKYDRNIKQSGNVINFDELKNKNLELFGEYFVGFSVGTKELLFDYKNEYNKIYKDKIVAARYDDINGILELEVQVSNTDEYENRNDPTKSYKFTFKGFRSIDFDNPNKNVLSISLQQRFLKKLVDDKILKTIIDQLVQHNHFNHKAPVSNINNSNLKGELFEKLTVDIIDDENHLYKSSQTLKIDLFKKENNNKSILGLKNQMSIYPFHSRITKDSIKNIYITINNKNSTKELELEAEIEIPIYSSTLTDLTDHTYAAEKPLKITVKQSVKLNQ
>LS483510.1|SRX66198.1|231833_231980_+|hypothetical-protein
MLKTVGCSVAMKNAVNSLKFVAKGITHYTNDEGGLGHYLNLLLDGKEV
>LS483510.1|SRX66199.1|232016_233699_-|LppA-family-lipoprotein
MRKFNKLFLTILPISSISAFSVVSCTTNTKNNNQIPTIPNNKKPENQKQPNDKKPGSTEEHTNKKPNENTNDQKQPNNSEKSDAESNPGKPENKPNNSHNPKQPEQPEHNDPNSNNTTDNNNSTNNDEPQADQPQHNQEDDSSNNTEEIFSEIDALKKEIEFNFYTTYKNKDALTSWIEIKSRKQAIFKEVIFSRNIDILEKYQIEFDSQNDPEIIKENGIISNVKIKFTKNGKSKVYEFTFTGFKEEDKIDSKNNKDIYIKQKDKIDVKLAGLYPSLLAYMLLYVEQSGTNIYDRDIKQSGNVINFDDLINNNQDLFDYNFSGFSVGTKDLLFDYNRKDEKLYKDKIVEAKYDDINGTLGLKVEISNRDDNHSNESTITKEFNFNGFRKIDIDNYKNNPFTFSLLPKNLSEIIKNDKIRKTLEESGVDIHKNQVDEFGGFYSKDNIWETLIFKNLLVDLTDNDHHTYRSNKTLKVDFSGSDRNYKSILGLKSNQSLYPFHTIITKDSIKNILVTIKDKKFTLDFELHIPIYSTSFSNLLSHAGSDKTLLVRVSQTTKID
>LS483510.1|SRX66200.1|233808_234438_-|beta-phosphoglucomutase
MKFKGVIFDLDGVITDTAPLHYLAWSQAVKTIGITNLDKSFLDKLRGISRKESLQVILDFYNLKLDQSQFNNLLEQKNLLYKKALQNIDKTWILPGIIDFIKDLKKHNIKICLGSSSFNAKDILTKLELINEFDYLVDPSEIKHSKPASDIFIKASQLLGLDVKECVVIEDAIAGVQASLNANIFCIGINVEANIKLKSTADLSINLLK
>LS483510.1|SRX66201.1|234437_235418_-|alpha-glycosidase
MLFLKYKDWFYINKFPLQEKIIDKNNQEKTVNNYYTFAFHEVMPKINTTNKDAKKYLLKVANYWIKEFDIDAWRLDAANEVDHEFWRDFRKTVNKNKPIYILGEIWGYAHPWLKGDQFDGVTNYMITSPICELVTKWIKPSKFNDKTTEVLNNYPRNVFKGMLNCLTSHDTTRLLTLCNNDVRKFKLAYSLVFMLAGAPSIYYGDEIGLDGAHDPLNRKCMNWNKDQWNHEIFNYLKKLIQIRKQNPVLGSYGTLKYTLIDDDKNYLEFIKYDDNNTYLILVNNSDEKLEVKKEELVNKIDLISDQIQTNNIVSLEPISMKVFKIK
>LS483510.1|SRX66202.1|235398_236178_-|alpha-glycosidase
MKVIDRVAIHHQQRSNMAYCYDKDYIHIILRTKKDDLKKVVIHHGDPFLRGHYLLGSDYIDLKPKEMTKSGSXKLYDYWFVEVKPEFKRLTYFFELFGIEDDHCYFGEKGFYETDDFKMINTGGWGFNYAWMNPNDVYQAPDWINDTIWYQIFPERFANGNKNNDPKNTLAWNSTDPSYNSFFGGDLQGIIDHLDHLVELGVNGLYLCPIFKAKSNHKYDTIDYLQIDPNFGDKKTFKKLVEECHKRNIKVMLDAVFKI
>LS483510.1|SRX66203.1|236296_238093_-|alpha-glycosidase
MVNIERAAILHIPKSNMAYCYDKDRIHIVLRAKKNNLKEVIFHCSEPFEPKVVVETNNYDLNLEKTAMRKVGSTEIYDYWFISVKPPFKRLSYYFELASENERIYYSQKGFYPLEKIKSVQTSQFSFPWMNEIDIFDVPTWVKDTIWYQIFPERFANGNPEISPKNVLAWNSEAPAANNFFGGDLQGIIDHLDHLVELGVNGLYLCPIFKARTNHKYDTIDYFEIDPHFGDKKTFKKLVEECHKRNIKIMLDAVFNHFGYWHPYXQDVLKNQEKSKYKDWFYINKFPVEKLDENLTENTSLDLNYYTFAFTGYMPKVNTSNPEVKKYLLEVARYWVEEFDIDAWRLDVANEIDHHFWREFRQVVNQKKRTYILGEVWSDSNPWLKGDQFDGVMNYVLTRQIIDFVATREIDVRRFKNRVTNVIFLYQKNIWPGMFNCLASHDTARLLTLCENDPNRLKLAYSILFTLSGSPSIYYGDEIGINGEHDPDCRKCMIWDKSQWNLDIFNHLKNLIKVRKENPTIGSYGFLEFKSYDEEKQYLEYIKTDTKTNYLILVNNSDNQIEVEHADLINNTELLTNEKQTNSKVVLKPFSMKIFKLN
>LS483510.1|SRX66204.1|238350_240150_+|lipoprotein
MKKILTMLTSLVVVGGSALTVLACKTTNNTDIVVQANDKWVPIYQQAANKVNKRFEEQGYKWRVKLKEIGLFDEKKLIDGRGVRDKGISDIFAIPLDRYPQYINQNTLKDLTEYIKKDLIKTKEDEDRFGIKIDNSKSGVDAIKLEKNVNTWKTVLGSDLKGNRLYGMIPMSIENMIWLFDEDRLGIKKEKGDDNKLYAYLVGSELEKVKNQLEKYEEKDGVGKKLIGKPKASIENLIILNKAQTNDYKFENLNEIEDKENVNKGAPLAFVDAGASFQGGMFLNSILNKRADDISKLKADNSSLGMVWVNKNKSLNSTNINDFDSIWENDMFKEDFNQTTQTIVDYVKSLGGHITEIYGGAAGQINQILDDALRDGTIAMTLVGPWEVSSKLETMRKAPKNKGHKFGFASIGDISFNKGKNKLTGFAGGYGWGIKSSISNTKLKNNKGEEMDKTSAAIEFIKEISKKDYATEMAFVDGKISAYSDVADFLIEELKQGNNIPXLNEKGKKKTNEELKAEKENRQIIGEAXRSIIDGYEKTGKDADVAPRADNELFGIYWEAYTTAFGSTFNKKQNKGMKEKFADIFRTTYKKQKSQYKFH
>LS483510.1|SRX66205.1|240444_242235_+|lipoprotein
MKKILTMLASIVVVGGSALTVLACKTRNNTDIVVQANDKWMPIYQKAADKVNKRFEEQGYKWRVKLKQIDIFAEKGLIDLRGVRDKGVSDVFAVPLDRFPQYLNQNTLKDLTEYIKTGIAGDSEAKERFGLDIVEGKTGVDAIKLTKNQNSWKTALGSDIKGKRQYGMIPMSIENMVWIFNENRLGIKKEKVGDKEYSYLVGTEVDKIKDKLDKYDDKSQANGRLKDKPKASIENLIKLNESQTNAYKFEDSKEIDTSKVNKGAPLAYIDAGGSFHGGMFLNSILNKRAEDIAAEKSESSSLGMVWVKKGKAINSTNKEDFDSIWENEKFKNDFDNTTKTIIDYVKSLGGHINEIYGGAAGQIGQILDDALRDGTTVMSLVGPWEVSSKLETMKKAPKNKDGKFGFASIGDITFNGDSKLTGFAGGYGWGIKSSISNLKLKNNKGEEMDKTAAAIEFIKEISKKDYATEMAFVDGKISAYKDVADNLIKELKEGTNIPELNDKGVKKTTEEIKAEKENRKIIGEAYESIVKGYEKTGKDADVAPRADNEMFGIYWGVYGTALGSTFNKKQNPGMKKQFSEIFRTTYESEKLKYKFH

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
LS483510_2	2.1\|228821\|33\|LS483510\|CRISPRCasFinder	228821-228853	33	NZ_CP013682	Clostridium botulinum strain 1169 plasmid pRSJ8_1, complete sequence	13914-13946	8	0.758
LS483510_2	2.1\|228821\|33\|LS483510\|CRISPRCasFinder	228821-228853	33	NZ_CP013295	Clostridium botulinum strain CDC_54064 plasmid pNPD1_1, complete sequence	24630-24662	8	0.758
LS483510_2	2.1\|228821\|33\|LS483510\|CRISPRCasFinder	228821-228853	33	MN812211	Flavobacterium phage vB_FspS_laban6-1, complete genome	22169-22201	9	0.727
LS483510_2	2.1\|228821\|33\|LS483510\|CRISPRCasFinder	228821-228853	33	CP019152	Acinetobacter lwoffii strain ZS207 plasmid pZS-2, complete sequence	8788-8820	9	0.727
LS483510_2	2.1\|228821\|33\|LS483510\|CRISPRCasFinder	228821-228853	33	MN693975	Marine virus AFVG_250M1117, complete genome	8793-8825	9	0.727

1. spacer 2.1|228821|33|LS483510|CRISPRCasFinder matches to NZ_CP013682 (Clostridium botulinum strain 1169 plasmid pRSJ8_1, complete sequence) position: , mismatch: 8, identity: 0.758

gttcattataattttatcataaaaatacctacg	CRISPR spacer
atctgctataatttcatcataaaaataccaacc	Protospacer
.*....********.************** **

2. spacer 2.1|228821|33|LS483510|CRISPRCasFinder matches to NZ_CP013295 (Clostridium botulinum strain CDC_54064 plasmid pNPD1_1, complete sequence) position: , mismatch: 8, identity: 0.758

gttcattataattttatcataaaaatacctacg	CRISPR spacer
atctgctataatttcatcataaaaataccaacc	Protospacer
.*....********.************** **

3. spacer 2.1|228821|33|LS483510|CRISPRCasFinder matches to MN812211 (Flavobacterium phage vB_FspS_laban6-1, complete genome) position: , mismatch: 9, identity: 0.727

gttcattataattttatcataaaaatacctacg	CRISPR spacer
ttttattataattttataataaaaatcaacaat	Protospacer
 **.************* ********   .*

4. spacer 2.1|228821|33|LS483510|CRISPRCasFinder matches to CP019152 (Acinetobacter lwoffii strain ZS207 plasmid pZS-2, complete sequence) position: , mismatch: 9, identity: 0.727

gttcattataattttatcataaaaatacctacg	CRISPR spacer
gagcattataattttaacataaatatatgaatt	Protospacer
*  ************* ****** ***.  *.

5. spacer 2.1|228821|33|LS483510|CRISPRCasFinder matches to MN693975 (Marine virus AFVG_250M1117, complete genome) position: , mismatch: 9, identity: 0.727

gttcattataattttatcataaa-----aatacctacg	CRISPR spacer
tttcattataatttgatcatcaaaaagtaatat-----	Protospacer
 ************* ***** **     ****.

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

551922 : 608746

Bacillus_phage(28.57%)

protease,transposase

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
SRX66487.1\|551922_552216_+\|transposase	IS3 family transposase	A0A1B1P773	Bacillus_phage	1.9e-10	43.2
SRX66488.1\|552241_552595_+\|transposase	IS3 family transposase	A0A1B1P773	Bacillus_phage	3.3e-25	54.2
SRX66489.1\|552756_554172_+	NADP-dependent glyceraldehyde-3-phosphate dehydrogenase	NA	NA	NA	NA
SRX66490.1\|554358_556290_+	DNA topoisomerase IV subunit B	G3M9Z3	Bacillus_virus	4.7e-121	40.8
SRX66491.1\|556291_558988_+	DNA topoisomerase IV subunit A	A0A172JHV7	Bacillus_phage	4.6e-98	33.1
SRX66492.1\|559095_560487_+	exodeoxyribonuclease V subunit alpha	A0A0K2FLP8	Brevibacillus_phage	3.3e-15	26.5
SRX66493.1\|560542_561229_+	exodeoxyribonuclease V subunit alpha	A0A167R0P7	Powai_lake_megavirus	3.0e-14	29.9
SRX66494.1\|561490_562711_+	ABC transporter ATP-binding protein	Q6GZ03	Mycoplasma_phage	1.7e-12	39.0
SRX66495.1\|562703_563717_+	glycerol ABC transporter	NA	NA	NA	NA
SRX66496.1\|563694_564504_+	carbohydrate ABC transporter permease	NA	NA	NA	NA
SRX66497.1\|564643_566512_+	glycerol ABC transporter glycerol-binding protein	NA	NA	NA	NA
SRX66498.1\|566710_570667_+	hypothetical protein	NA	NA	NA	NA
SRX66499.1\|570717_571449_-\|transposase	IS1296 transposase protein B	A0A1B1P773	Bacillus_phage	7.1e-62	50.9
SRX66500.1\|571586_572129_-	helix-turn-helix domain-containing protein	NA	NA	NA	NA
SRX66501.1\|572193_573372_-	NADH dependent flavin oxidoreductase	NA	NA	NA	NA
SRX66502.1\|573371_574409_-	lipoate--protein ligase A	A0A2H4UVX5	Bodo_saltans_virus	3.9e-13	29.9
SRX66503.1\|574386_575082_-	hypothetical protein	NA	NA	NA	NA
SRX66504.1\|575083_575428_-	glycine cleavage system H protein	NA	NA	NA	NA
SRX66505.1\|575614_576409_+	alpha/beta hydrolase	NA	NA	NA	NA
SRX66506.1\|576410_577205_+	alpha/beta hydrolase	NA	NA	NA	NA
SRX66507.1\|577198_578008_+	lipase-esterase	NA	NA	NA	NA
SRX66508.1\|578026_579160_-	BspA family leucine-rich repeat surface protein	NA	NA	NA	NA
SRX66509.1\|579422_580823_+	putative lipoprotein	NA	NA	NA	NA
SRX66510.1\|580969_581689_+	ABC transporter ATP-binding protein	A0A2H4PQG7	Staphylococcus_phage	2.6e-16	28.8
SRX66511.1\|581688_582444_+	ABC transporter permease	NA	NA	NA	NA
SRX66512.1\|582572_583154_-	L-lactate dehydrogenase	NA	NA	NA	NA
SRX66513.1\|583431_584589_-	N-acetylglucosamine-6-phosphate deacetylase	NA	NA	NA	NA
SRX66514.1\|584757_585492_+	hypothetical protein	NA	NA	NA	NA
SRX66515.1\|585503_586088_-	hypothetical protein	NA	NA	NA	NA
SRX66516.1\|586092_587739_-	hypothetical protein	NA	NA	NA	NA
SRX66517.1\|587890_588103_+	hypothetical protein	NA	NA	NA	NA
SRX66518.1\|588194_589586_+	hypothetical protein	NA	NA	NA	NA
SRX66519.1\|589657_590095_-	lipoprotein (VlcE)	NA	NA	NA	NA
SRX66520.1\|590410_590575_+	~30S ribosomal protein S21	NA	NA	NA	NA
SRX66521.1\|590683_591244_+	Holliday junction DNA helicase RuvA	NA	NA	NA	NA
SRX66522.1\|591260_592184_+	Holliday junction branch migration DNA helicase RuvB	G3MBE0	Bacillus_virus	3.0e-09	34.4
SRX66523.1\|592261_593620_+	dihydrolipoyl dehydrogenase	A0A2K5B2C5	Erysipelothrix_phage	5.9e-46	31.3
SRX66524.1\|593635_594445_-	hypothetical protein	NA	NA	NA	NA
SRX66525.1\|594520_595441_+	hypothetical protein	NA	NA	NA	NA
SRX66526.1\|595449_596553_+	ribosome biogenesis GTPase YqeH	NA	NA	NA	NA
SRX66527.1\|596561_597785_-	DNA polymerase IV	A0A290GHP0	Caldibacillus_phage	1.2e-08	26.2
SRX66528.1\|597928_600187_+\|protease	cysteine protease	NA	NA	NA	NA
SRX66529.1\|600326_600584_+\|protease	cysteine protease	NA	NA	NA	NA
SRX66530.1\|600661_601285_-	uridine kinase	A0A1V0SD85	Indivirus	4.7e-22	32.4
SRX66531.1\|601308_601746_-	hypothetical protein	NA	NA	NA	NA
SRX66532.1\|601821_603171_-	Xaa-His dipeptidase	NA	NA	NA	NA
SRX66533.1\|603326_604007_-	N-acetylmannosamine-6-phosphate 2-epimerase	NA	NA	NA	NA
SRX66534.1\|604065_604941_-	ROK family protein	NA	NA	NA	NA
SRX66535.1\|604933_605383_-	YhcH/YjgK/YiaL family protein	NA	NA	NA	NA
SRX66536.1\|605391_607095_-	sodium:solute symporter family protein	NA	NA	NA	NA
SRX66537.1\|607096_607984_-	N-acetylneuraminate lyase	NA	NA	NA	NA
SRX66538.1\|608148_608430_-	~50S ribosomal protein L27	NA	NA	NA	NA
SRX66539.1\|608431_608746_-\|protease	ribosomal-processing cysteine protease Prp	NA	NA	NA	NA

DBSCAN-SWA_2

901755 : 915799

Lactococcus_phage(25.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SRX66786.1\|901755_903054_-	adenylosuccinate synthase	L7Y4J5	Megavirus	1.6e-56	34.4
SRX66787.1\|903407_904085_-	hypothetical protein	NA	NA	NA	NA
SRX66788.1\|904084_904831_-	site-specific DNA-methyltransferase	A0A0C5AFG8	Paenibacillus_phage	8.6e-15	26.6
SRX66789.1\|904864_905710_-	BspA family leucine-rich repeat surface protein	NA	NA	NA	NA
SRX66790.1\|905815_907978_-	class 1b ribonucleoside-diphosphate reductase subunit alpha	V9VI16	Lactococcus_phage	9.4e-163	44.3
SRX66791.1\|907964_908438_-	class Ib ribonucleoside-diphosphate reductase assembly flavoprotein NrdI	R4JF54	Bacillus_phage	1.0e-13	35.0
SRX66792.1\|908446_909466_-	class 1b ribonucleoside-diphosphate reductase subunit beta	B5LJM6	Mycobacterium_phage	2.5e-97	53.7
SRX66793.1\|909764_910049_+	preprotein translocase subunit SecG	NA	NA	NA	NA
SRX66794.1\|910084_912199_+	ribonuclease R	Q0GXV6	Lactococcus_phage	1.6e-61	32.8
SRX66795.1\|912208_912655_+	SsrA-binding protein	W5RAM5	Staphylococcus_phage	1.1e-20	38.5
SRX66796.1\|912654_913140_+	hypothetical protein	NA	NA	NA	NA
SRX66797.1\|913259_913511_+	hypothetical protein	NA	NA	NA	NA
SRX66798.1\|913561_915799_+	PTS eiic domain protein	A0A2I7SAJ6	Vibrio_phage	9.6e-09	45.5

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. LS483510

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CRISPR-Cas detection and classification

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Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection