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
LS483395	Achromobacter xylosoxidans strain NCTC10808 genome assembly, chromosome: 1	2 crisprs	csa3,PD-DExK,cas3,DinG,DEDDh,WYL	1	0	6	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: LS483395_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483395_2

2273306-2273422

Orphan

Consensus_repeat	Method
GGGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483395_2

>merge|LS483395|2|2273306-2273422|CRISPRCasFinder
GGGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGGGCCTTTTTTTGCCGCCGGGCCGCCCCAAGGCAAAAACGCCCCCTCGGGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGG

>LS483395|2|2|2273306-2273422|CRISPRCasFinder
GGGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGG	GCCTTTTTTTGCCGCCGGGCCGCCCCAAGGCAAAAACGCCCCCTC
GGGGGGCAGCGACCCGCGCAGCGGCGGAGCGTGGGG

Protein	Signature genes	Signature genes Name	Protein_function
LS483395.1\|SQG71619.1\|2262832_2263747_+\|dTDP-4-dehydrorhamnose-reductase	unknown	unknown	gnl\|CDD\|367904
LS483395.1\|SQG71630.1\|2273805_2275368_+\|Competence-protein-ComM	unknown	unknown	gnl\|CDD\|223679
LS483395.1\|SQG71635.1\|2279945_2280272_+\|Integration-host-factor-subunit-alpha	unknown	unknown	gnl\|CDD\|178961
LS483395.1\|SQG71621.1\|2266113_2266614_+\|Translation-initiation-factor-IF-3	unknown	unknown	gnl\|CDD\|234582
LS483395.1\|SQG71629.1\|2273468_2273720_+\|Uncharacterized-protein-conserved-in-bacteria	unknown	unknown	gnl\|CDD\|377337
LS483395.1\|SQG71637.1\|2281151_2281265_+\|Uncharacterised-protein	unknown	unknown	unknown
LS483395.1\|SQG71627.1\|2271862_2272201_-\|Nitrogen-regulatory-protein-P-II-2	unknown	unknown	gnl\|CDD\|366157
LS483395.1\|SQG71634.1\|2277512_2279930_+\|Phenylalanine--tRNA-ligase-beta-subunit	unknown	unknown	gnl\|CDD\|234804
LS483395.1\|SQG71638.1\|2281222_2281660_-\|Uncharacterised-protein	unknown	unknown	unknown
LS483395.1\|SQG71636.1\|2280329_2280761_+\|HTH-type-transcriptional-repressor-YcgE	unknown	unknown	gnl\|CDD\|133393
LS483395.1\|SQG71620.1\|2264089_2266042_+\|Threonine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234752
LS483395.1\|SQG71628.1\|2272747_2273179_+\|Uncharacterised-protein	unknown	unknown	gnl\|CDD\|237030
LS483395.1\|SQG71625.1\|2268597_2270373_+\|Phosphoenolpyruvate-protein-phosphotransferase	unknown	unknown	gnl\|CDD\|224006
LS483395.1\|SQG71631.1\|2275824_2276022_+\|Ribosomal-protein-A	unknown	unknown	gnl\|CDD\|234676
LS483395.1\|SQG71633.1\|2276476_2277499_+\|Phenylalanine--tRNA-ligase-alpha-subunit	unknown	unknown	gnl\|CDD\|234780
LS483395.1\|SQG71622.1\|2266777_2267755_+\|Glutathione-synthetase	unknown	unknown	gnl\|CDD\|235371
LS483395.1\|SQG71626.1\|2270592_2271831_-\|Ammonia-transporter	unknown	unknown	gnl\|CDD\|182630
LS483395.1\|SQG71623.1\|2267772_2268174_+\|EIIAB-Man	unknown	unknown	gnl\|CDD\|225446
LS483395.1\|SQG71624.1\|2268284_2268554_+\|Phosphocarrier-protein-HPr	unknown	unknown	gnl\|CDD\|376329
LS483395.1\|SQG71632.1\|2276039_2276399_+\|RRP-L20	unknown	unknown	gnl\|CDD\|179959

Protein	Function_ID	Function_description	E-value
LS483395.1\|SQG71619.1\|2262832_2263747_+\|dTDP-4-dehydrorhamnose-reductase	gnl\|CDD\|367904	pfam04321, RmlD_sub_bind, RmlD substrate binding domain. L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesized by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsible for binding a sugar nucleotide.	1.2411e-113
LS483395.1\|SQG71630.1\|2273805_2275368_+\|Competence-protein-ComM	gnl\|CDD\|223679	COG0606, COG0606, Predicted ATPase with chaperone activity [Posttranslational modification, protein turnover, chaperones].	0
LS483395.1\|SQG71635.1\|2279945_2280272_+\|Integration-host-factor-subunit-alpha	gnl\|CDD\|178961	PRK00285, ihfA, integration host factor subunit alpha; Reviewed.	2.3706e-62
LS483395.1\|SQG71621.1\|2266113_2266614_+\|Translation-initiation-factor-IF-3	gnl\|CDD\|234582	PRK00028, infC, translation initiation factor IF-3; Reviewed.	2.36603e-90
LS483395.1\|SQG71629.1\|2273468_2273720_+\|Uncharacterized-protein-conserved-in-bacteria	gnl\|CDD\|377337	pfam04380, BMFP, Membrane fusogenic activity. BMFP consists of two structural domains, a coiled-coil C-terminal domain via which the protein self-associates as a trimer, and an N-terminal domain disordered at neutral pH but adopting an amphipathic alpha-helical structure in the presence of phospholipid vesicles, high ionic strength, acidic pH or SDS. BMFP interacts with phospholipid vesicles though the predicted amphipathic alpha-helix induced in the N-terminal half of the protein and promotes aggregation and fusion of vesicles in vitro.	2.31634e-18
LS483395.1\|SQG71627.1\|2271862_2272201_-\|Nitrogen-regulatory-protein-P-II-2	gnl\|CDD\|366157	pfam00543, P-II, Nitrogen regulatory protein P-II. P-II modulates the activity of glutamine synthetase.	1.56881e-56
LS483395.1\|SQG71634.1\|2277512_2279930_+\|Phenylalanine--tRNA-ligase-beta-subunit	gnl\|CDD\|234804	PRK00629, pheT, phenylalanyl-tRNA synthetase subunit beta; Reviewed.	0
LS483395.1\|SQG71636.1\|2280329_2280761_+\|HTH-type-transcriptional-repressor-YcgE	gnl\|CDD\|133393	cd04765, HTH_MlrA-like_sg2, Helix-Turn-Helix DNA binding domain of putative MlrA-like transcription regulators. Putative helix-turn-helix (HTH) MlrA-like transcription regulators (subgroup 2), N-terminal domain. The MlrA protein, also known as YehV, has been shown to control cell-cell aggregation by co-regulating the expression of curli and extracellular matrix production in Escherichia coli and Salmonella typhimurium. These proteins belong to the MerR superfamily of transcription regulators that promote expression of several stress regulon genes by reconfiguring the spacer between the -35 and -10 promoter elements. Their conserved N-terminal domains contain predicted HTH motifs that mediate DNA binding, while the dissimilar C-terminal domains bind specific coactivator molecules.	9.75016e-41
LS483395.1\|SQG71620.1\|2264089_2266042_+\|Threonine--tRNA-ligase	gnl\|CDD\|234752	PRK00413, thrS, threonyl-tRNA synthetase; Reviewed.	0
LS483395.1\|SQG71628.1\|2272747_2273179_+\|Uncharacterised-protein	gnl\|CDD\|237030	PRK12270, kgd, multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit.	6.49313e-06
LS483395.1\|SQG71625.1\|2268597_2270373_+\|Phosphoenolpyruvate-protein-phosphotransferase	gnl\|CDD\|224006	COG1080, PtsA, Phosphoenolpyruvate-protein kinase (PTS system EI component in bacteria) [Carbohydrate transport and metabolism].	0
LS483395.1\|SQG71631.1\|2275824_2276022_+\|Ribosomal-protein-A	gnl\|CDD\|234676	PRK00172, rpmI, 50S ribosomal protein L35; Reviewed.	5.92937e-23
LS483395.1\|SQG71633.1\|2276476_2277499_+\|Phenylalanine--tRNA-ligase-alpha-subunit	gnl\|CDD\|234780	PRK00488, pheS, phenylalanyl-tRNA synthetase subunit alpha; Validated.	0
LS483395.1\|SQG71622.1\|2266777_2267755_+\|Glutathione-synthetase	gnl\|CDD\|235371	PRK05246, PRK05246, glutathione synthetase; Provisional.	0
LS483395.1\|SQG71626.1\|2270592_2271831_-\|Ammonia-transporter	gnl\|CDD\|182630	PRK10666, PRK10666, ammonium transporter AmtB.	0
LS483395.1\|SQG71623.1\|2267772_2268174_+\|EIIAB-Man	gnl\|CDD\|225446	COG2893, ManX, Phosphotransferase system, mannose/fructose-specific component IIA [Carbohydrate transport and metabolism].	5.57584e-23
LS483395.1\|SQG71624.1\|2268284_2268554_+\|Phosphocarrier-protein-HPr	gnl\|CDD\|376329	pfam00381, PTS-HPr, PTS HPr component phosphorylation site.	1.83273e-32
LS483395.1\|SQG71632.1\|2276039_2276399_+\|RRP-L20	gnl\|CDD\|179959	PRK05185, rplT, 50S ribosomal protein L20; Provisional.	8.30203e-63

>LS483395.1|SQG71628.1|2272747_2273179_+|Uncharacterised-protein
MNTQRKTFAVLALAAALAALAGCNKSDEKAAPPAASTTPAPSTTTPGTPPAATTPPATTAPSGSGAPAGATAGLPAECDAYLTQVSACMDKLGASNPAAASFKQQLDAAKTQWATISDKTQLASQCKQSADLFAQSASQMGCK
>LS483395.1|SQG71627.1|2271862_2272201_-|Nitrogen-regulatory-protein-P-II-2
MKLIIAIIKPFKLDEVRVALSGIGVQGLTVTEVKGFGRQKGHTELYRGAEYAVDFLPKLRVEAAVPDHLVDQVIEAIEQAARTGKIGDGKIFAAPLEQVIRIRTGEAGEAAL
>LS483395.1|SQG71626.1|2270592_2271831_-|Ammonia-transporter
MDKADISWLLVSTLLVLMMAVPGLAMFYGGLVRSKNVLSVLLQVMCTFVLGLVLWFIYGYSLAFTEGNAFFGGLSRAFFSGMFTPADGKYAMSNSLTELLFASFQATFAGITCALIVGSFAERARFSAVLVFTVIWFTFAYIPIAHMVWFASETAPGLLNAKGALDFAGGTVVHINAGVAGLVGAYVVGKRVGYGREAMQPHNLPMTFVGAALLWVGWFGFNAGSALAANENATLAFFNTMIATAGAVLAWLFTEWAIKGKPSMLGAASGAVAGLVGITPAAGLVGPVGALIIGVVAGVVCVWGVNGLKRLLRADDALDVFGVHGVGGIVGALLTGIFNAQALGGPGLAEPGMILGQLWVQLEGVLLTIVWSGVVAWIAYKIANALCGLRVPEDQEREGLDVTSHGESAYHS
>LS483395.1|SQG71625.1|2268597_2270373_+|Phosphoenolpyruvate-protein-phosphotransferase
MSAAGTAVLAHDGDGSASPVICLYGKGVARGYAIGRAVVMGAAALEVAHYRIAPEDVPAESSRLTEALASAQQELRQLADTLPADAPRELGAMLNVHSLLLGDPLLAEQTLALIAERHYNAEWALTTQGQILGQQFDAMEDEYLRERGADVRQVIERVLHVLSGTSAILPDMSHMGGDEALVVVAHDISPADMLRLRGGRFAAFVTDLGGPTSHTAIVARSMGVPAVVAMGNVRELVRDGDMLIIDGAAGAVVVNPSERILQEYRRRQAAYADERAELGLLRDEPSVTLDGIDIVLHANIELPEEAALALASGAHGIGLFRSEFLFMGRPDLPGEEEQYEAYASVVKVMAGRPVTIRTLDIGSDKTLDGEATVATNPALGQRAIRYCLARPEMFATQLRAILRASAHGPVRLLIPMIAHMHEVVATRAAIESARRELDARGQAYAAHMEVGAMVEVPAIAIAIEPFAQALDFLSIGTNDLIQYTLAIDRGDHDVASLYDPLHPAVLRLVAHTINAGERAGKPVAVCGEMAGDSRMTRLLLGLGLTEFSMHPQQLLDVKREVRRAHTNALRVKVASALNRALPVDLDTLDLA
>LS483395.1|SQG71624.1|2268284_2268554_+|Phosphocarrier-protein-HPr
MPNTDIVISNKLGLHARAAAKLTQLASKFSSEIFISRGAQRVNAKSIMGVMMLAAGLGVTVKLEASGSDAEQALSEIETLFDSKFGEQE
>LS483395.1|SQG71623.1|2267772_2268174_+|EIIAB-Man
MTTGIVIVVHAPLGAAMRECASHVMGNLDGMLAIHDIQPEDLPDDLAPAVLKDILEQDHGGGVLVLTDLIGATPANISKRAVADAQAQGIQCCVLAGLNTPMLLRALTYRNLSLAETREKALAGGVQGVLRVD
>LS483395.1|SQG71622.1|2266777_2267755_+|Glutathione-synthetase
MHVLFVLDPLPLLKAYKDSSVAMMRALVARGHTLSVAMQGDLYIETGTVKAVTTPIELVDGADLHGHDWWRESAPQDLPLADFGAVVMRKDPPFDMEYVYSTHLLEYAQAQGAKVFNGGAAIRNHPEKLAITEISEFTAPTLVTRNMARLKAFHDTHHDVIVKPLDGMGGTGVFRLQPKDPNLNAILETLTDNGARTIMAQRYIPEIVKGDKRILLIGGEPVPYSLARIPLAGETRGNLAAGGRGVAQPLSPRDREIAEAVAPRLAARGLLLVGLDVIGDYVTEVNVTSPTCFVEIAEQTGFDVAGMFVEALEKAVATGAVAAAA
>LS483395.1|SQG71621.1|2266113_2266614_+|Translation-initiation-factor-IF-3
MRLIGLDGEQLGIVKIADAFRLSEQNDVDLVEIAPNAEPPVCRLMDYGKFKYQEQKRQAEARSKQKVIQVKEVKFRPATDEGDYQVKLRNLRRFLEEGDKAKVTLRFRGREMAHQELGMRVLERVRDDLLELAQVEAMPKLEGRQMVMVLAPKKKAAPAGKPESAA
>LS483395.1|SQG71620.1|2264089_2266042_+|Threonine--tRNA-ligase
MVQITLPDGSQRQYPGPVTVAEVAQSIGAGLAKAALGGRVTFDGADSTLVDTSYRIEGDARLAIVTAKDADGLDMIRHSTAHLLAYAVKELFPDAQVTIGPVIDNGFYYDFSYKRPFTPEDLAAIEKKMAELAKKDEVVTREVWSRDDAVEFFKGIGEKYKAEIIASIPSNEPLSLYREGEFIDLCRGPHVPSTGKLKVFKLMKVAGAYWRGDSKNEMLQRIYGTAWATKEEQEAYLHMLEEAERRDHRKIGRELDLFHFQDEAPGLIFWHPKGWALWQQVEQYMRSVYRDNGYQEVKAPQILDISLWKKTGHWDNYRENMFTTESENRVYGLKPMNCPGHVQIFNAGLHSYRELPLRYGEFGQCHRNEPSGSLHGMMRVRGFTQDDGHIFCTEEQLQDECADFTALLQKVYRDFGFTEVLYKVATRPEKRIGSDEVWDTAEQALMESLRRTGCEFEISPGEGAFYGPKVEYTLKDAIGRHWQCGTIQVDFSMPVRLGAEYVDQNDQRRPPVMLHRAILGSLERFIGMLIENHAGAMPPWLAPVQAVVCCISEPSADYAAEITQSLKKQGFRVESDLRGEKITRKIREHSLQKVPYILVVGDKEKQNGTVAVRGLGGLDLGAIAFDDFVARLSEDVSTRRDVNQPDGSAA
>LS483395.1|SQG71619.1|2262832_2263747_+|dTDP-4-dehydrorhamnose-reductase
MPKKILVIGRDGQLGFELRRSLAPLGVVTAVGRADCDLTYPLQIARLVRREKPDVIVNAAAFTAVERAQEDGVRAMRINAEAAGELSALAAERGALIVHYSSDYVFDGAKPGAYDERDTPAPLNVYGRSKLAGEQAVRAMNPAHLVFRTSWVYGVFGNSFLKTMLMALRQPETLRVVSDQRGAPTGAAYIADATALVLARYLARPADEAFPFGLYHLAATGDASWHEYACFIAQQARRAGLAVTLTPADIRAVPSDQYPTTARRPLNSRLDSRLLERTFGIRAPHWEDGVTHALAAIADSRNLA
>LS483395.1|SQG71629.1|2273468_2273720_+|Uncharacterized-protein-conserved-in-bacteria
MNNRTQWMEDIQKNISDLIARSPAADVERNVRALMTQAFSKLDLVTREEFDVQADLLARTRARVDQLSATVEQLESRLAALDK
>LS483395.1|SQG71630.1|2273805_2275368_+|Competence-protein-ComM
MTLAVIASRTLSGLHAHAVRVETHLGPGLPSFNVVGLPDTEVRESRERVRAAILNSGFNFPAGRITVNLSPADIPKESGRFDLPIALGLLLAAGQLAPREEGAREEGAREGGAGAADAAAPDPLLAGLVLAGELSLTGALVPVSAALVIALSVARESPGATLILPAGSAEQAAWVEGLRVLSARSLADVAAHVAGVCRLPDAIAASWPAAPPAPCLSDVRGQPGARRALEVAAAGGHSLLMVGPPGAGKSMLAARLPGLLPPLARTQALEVAAIAALAGAPDARMGTPPFRAPHHSASPFALVGGGGRPRPGEISLAHHGVLFLDELPEFSRRTLEALREPLETGRVVIARALHTAQFPARFQLVAAMNPCPCGWRGHPRRACQCTPDQVARYAGKVSGPLLDRIDLYVTLPPPDLESLQGPPGEASAPVRARVARCRERQLARQGKSNAGLAGAELERHCPMDPSAQALLLQAMRRLAGSGRALHRALRVARTIADLDGADTLQASHVAQAVQYRRPGV
>LS483395.1|SQG71631.1|2275824_2276022_+|Ribosomal-protein-A
MPKMKTKKSAAKRFQVRGSGSIKRGQAFKRHILTKKTTKNKRQLRGSAAVHETNVASVKAMMPFA
>LS483395.1|SQG71632.1|2276039_2276399_+|RRP-L20
MPRVKRGVTARARHKKVIAAAKGYRGRRGNVFRIAKQAVMRAGQYAYRDRRNKKRTFRALWITRINAAVREHGVSYSVFIAGLKKAAIELDRKVLADLAVRDKAGFAAIVQQAKAALAA
>LS483395.1|SQG71633.1|2276476_2277499_+|Phenylalanine--tRNA-ligase-alpha-subunit
MTQSVDDLVSQAQERFAAATDAAALENAKARFLGKDGALTVLLKGLGKLDPEQKRDMGARINQAKQKVEELLNLRRAALAQAELDARLASETIDVSLPGRGRVPGGIHPVIRTWERVEEIFRSIGFDVADGPEVENDWTNFTALNNPLDHPARSMQDTFYVDMKDADGLPLLLRTHTSPMQVRYARMHKPPIKVIAPGRTYRVDSDATHSPMFHQVEGLWIAEDISFADLKGVYTDFLRCFFESDDLVVRFRPSFFPFTEPSAEIDMMFTSGPNRGRWLEISGSGQVHPQVVRNFGLDPERYIGFAFGSGLERLTMLRYGVNDLRQFYEGDLRFLRQFNE
>LS483395.1|SQG71634.1|2277512_2279930_+|Phenylalanine--tRNA-ligase-beta-subunit
MQFPESWLRTLVNPPIATDELAHRLTMAGLEVEDTVPAAPAFTGVVVAHIVEIAPHPDADKLRVCQVDDGSGALLQIVCGAPNAAAGLKVPLARVGAELPGGMKIGVAKMRGVQSSGMLCSARELGLSQDHAGLLELPADMAPGQSIREALDLDDTLFTLKMTPNRADCLSILGVAREVAALTGAPLSVPTAKAVPVTLDELRPVRIEAPDLCGRFGGRVIRGVNARAQTPAWMKTRLERAGQRSVSALVDISNYVMLELGRPSHVFDLDKIHGDLSVRWAREGETLELLNGQTVTLDSKVGVVVAGDQVESLAGIMGGEATAVTLDTQNIYLEAAFWWPQSLAGRARRYKFSSEASHRGERGVDFATIPQHIEFITRLIVDICGGQAGPLDDQIVNLPKREPVRMRLARCHRVLGVPVTQAEVAKIFGSLGLEFTLDGDDFVVTPPSYRFDLEIEEDLIEEVARIYGFENIPTVPPLARAKMFSQPEVRRGPHALRRLAAAQDYQEVVNYSFVEAEWERDYAGNDTPVKLVNPIASHLSVMRSSLIAGLVANIRHNANRKQTRVRLFELGRVFARDDAAKDGPLEVAGVRQPLKLAGAAWGPSVEEQWGVPARQVDFYDVKMDVEALFGARGARLRFEAAAHPALHPGRSARITLDGTQVGWLGELHPRWAQQADLAHAPVVFELDVQALSEGELPQVRELSRQPVVVRDLALWVDAPVTVQSMLDTVAATVKADPQLAVVQDVRLFDVWREKPQGDQPVAEKSLAFRFWLQDTEVTLDEARVAACLARIKDALVSAHGARQRA
>LS483395.1|SQG71635.1|2279945_2280272_+|Integration-host-factor-subunit-alpha
MLAEPRTLTKAELAELLFERVGLNKREAKDIVDTFFEEIRDALARGDSVKLSGFGNFQVRDKPPRPGRNPKTGETIPIAARRVVTFHASQKLKSVVEQATPAAPDAEE
>LS483395.1|SQG71636.1|2280329_2280761_+|HTH-type-transcriptional-repressor-YcgE
MTRTESTVTLPPIPAKRYFTIGEVSDLCGVKPHVLRYWEQEFTQLKPVKRRGNRRYYQHHEVLLIRRIRSLLYEQGFTISGARNRLGDARDTPHDQDAAVRLSGAEMQALRNELGNVSTMLGEALGSAATASSGNAVSANATA
>LS483395.1|SQG71637.1|2281151_2281265_+|Uncharacterised-protein
MKITNPLSHFRAHIACDVPMASSAQNLNPLMYSPHEL
>LS483395.1|SQG71638.1|2281222_2281660_-|Uncharacterised-protein
MLKSICRIAPAVILPLTLSACMGLSVYSPTRNKLNAQVGKNINEMLPAWPPETGAKPFVNKVDDQTTSYTYVYGYHPGHYEGRGYSTNGPMGTTYGSYCAYVPEYTDCAVIFYTDKAGTVLRYDMKTNGKISYNSCGEYISGFRF

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Crispr_ID: LS483395_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

LS483395_3

4664866-4664968

Orphan

Consensus_repeat	Method
TTTTCATCGCCGAGCCGCCTCAAGAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of LS483395_3

>merge|LS483395|3|4664866-4664968|CRISPRCasFinder
TTTTCATCGCCGAGCCGCCTCAAGATGAAAAATGCCCCCTCGGGGGGCAGCAAGCCGAAGGCGCGGCGTGGGGGCCCTTTTCATCGCAGAGCCGCCTCAAGAT

>LS483395|3|3|4664866-4664968|CRISPRCasFinder
TTTTCATCGCCGAGCCGCCTCAAGAT	GAAAAATGCCCCCTCGGGGGGCAGCAAGCCGAAGGCGCGGCGTGGGGGCCC
TTTTCATCGCAGAGCCGCCTCAAGAT

Protein	Signature genes	Signature genes Name	Protein_function
LS483395.1\|SQG76415.1\|4672028_4672919_+\|D-malate-degradation-protein-R	unknown	unknown	gnl\|CDD\|176114
LS483395.1\|SQG76416.1\|4672959_4673733_-\|LigB-family-dioxygenase	unknown	unknown	gnl\|CDD\|153375
LS483395.1\|SQG76401.1\|4652822_4655024_-\|Ferrichrome-receptor-FcuA-precursor	unknown	unknown	gnl\|CDD\|238657
LS483395.1\|SQG76411.1\|4667091_4668591_+\|Multidrug-resistance-outer-membrane-protein-MdtP-precursor	unknown	unknown	gnl\|CDD\|273830
LS483395.1\|SQG76410.1\|4666100_4666994_-\|Nodulation-protein-D-2	unknown	unknown	gnl\|CDD\|176149
LS483395.1\|SQG76409.1\|4664985_4666032_-\|Outer-membrane-protein-OmpAb	unknown	unknown	gnl\|CDD\|143586
LS483395.1\|SQG76399.1\|4651001_4651997_+\|Beta-ketoacyl-acyl-carrier-protein-synthase-I	unknown	unknown	gnl\|CDD\|176180
LS483395.1\|SQG76412.1\|4668587_4669724_+\|Inner-membrane-protein-yibH	unknown	unknown	gnl\|CDD\|185090
LS483395.1\|SQG76402.1\|4655308_4656283_-\|Pirin-C-terminal-cupin-domain	unknown	unknown	gnl\|CDD\|224655
LS483395.1\|SQG76417.1\|4673977_4675180_+\|Protein-of-uncharacterised-function-(DUF2863)	unknown	unknown	gnl\|CDD\|371362
LS483395.1\|SQG76414.1\|4671288_4671993_+\|Vibriobactin-utilization-protein-ViuB	unknown	unknown	gnl\|CDD\|99790
LS483395.1\|SQG76400.1\|4651993_4652761_+\|3-oxoacyl-[acyl-carrier-protein]-reductase-FabG	unknown	unknown	gnl\|CDD\|235546
LS483395.1\|SQG76418.1\|4675189_4676305_+\|Uncharacterized-protein-conserved-in-bacteria	unknown	unknown	gnl\|CDD\|378385
LS483395.1\|SQG76403.1\|4656401_4657310_+\|D-malate-degradation-protein-R	unknown	unknown	gnl\|CDD\|184959
LS483395.1\|SQG76405.1\|4658361_4659873_-\|Long-chain-fatty-acid--CoA-ligase	unknown	unknown	gnl\|CDD\|236215
LS483395.1\|SQG76407.1\|4660875_4661805_+\|D-malate-degradation-protein-R	unknown	unknown	gnl\|CDD\|176114
LS483395.1\|SQG76408.1\|4662109_4664815_+\|Aconitate-hydratase	unknown	unknown	gnl\|CDD\|236445
LS483395.1\|SQG76406.1\|4659869_4660769_-\|Gluconate-5-dehydrogenase	unknown	unknown	gnl\|CDD\|187627
LS483395.1\|SQG76413.1\|4669723_4671253_+\|Multidrug-resistance-protein-B	unknown	unknown	gnl\|CDD\|129794
LS483395.1\|SQG76404.1\|4657320_4658304_-\|Argininosuccinate-lyase	unknown	unknown	gnl\|CDD\|270296

Protein	Function_ID	Function_description	E-value
LS483395.1\|SQG76415.1\|4672028_4672919_+\|D-malate-degradation-protein-R	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain 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.	2.94943e-47
LS483395.1\|SQG76416.1\|4672959_4673733_-\|LigB-family-dioxygenase	gnl\|CDD\|153375	cd07363, 45_DOPA_Dioxygenase, The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine. This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.	1.79369e-120
LS483395.1\|SQG76401.1\|4652822_4655024_-\|Ferrichrome-receptor-FcuA-precursor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	5.36338e-108
LS483395.1\|SQG76411.1\|4667091_4668591_+\|Multidrug-resistance-outer-membrane-protein-MdtP-precursor	gnl\|CDD\|273830	TIGR01845, Outer_membrane_protein_OprM, efflux transporter, outer membrane factor (OMF) lipoprotein, NodT family. Members of this model comprise a subfamily of the Outer Membrane Factor (TCDB 1.B.17) porins. OMF proteins operate in conjunction with a primary transporter of the RND, MFS, ABC, or PET systems, and a MFP (membrane fusion protein) to tranport substrates across membranes. The complex thus formed allows transport (export) of various solutes (heavy metal cations; drugs, oligosaccharides, proteins, etc.) across the two envelopes of the Gram-negative bacterial cell envelope in a single energy-coupled step. Current data suggest that the OMF (and not the MFP) is largely responsible for the formation of both the trans-outer membrane and trans-periplasmic channels. The roles played by the MFP have yet to be determined. [Cellular processes, Detoxification, Transport and binding proteins, Porins].	3.77231e-66
LS483395.1\|SQG76410.1\|4666100_4666994_-\|Nodulation-protein-D-2	gnl\|CDD\|176149	cd08460, PBP2_DntR_like_1, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold. This CD includes an uncharacterized LysR-type transcriptional regulator similar to DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. This substrate-binding domain shows significant homology to 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.	2.38816e-69
LS483395.1\|SQG76409.1\|4664985_4666032_-\|Outer-membrane-protein-OmpAb	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	6.09839e-40
LS483395.1\|SQG76399.1\|4651001_4651997_+\|Beta-ketoacyl-acyl-carrier-protein-synthase-I	gnl\|CDD\|176180	cd05276, p53_inducible_oxidoreductase, PIG3 p53-inducible quinone oxidoreductase. PIG3 p53-inducible quinone oxidoreductase, a medium chain dehydrogenase/reductase family member, acts in the apoptotic pathway. PIG3 reduces ortho-quinones, but its apoptotic activity has been attributed to oxidative stress generation, since overexpression of PIG3 accumulates reactive oxygen species. PIG3 resembles the MDR family member quinone reductases, which catalyze the reduction of quinone to hydroxyquinone. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	0
LS483395.1\|SQG76412.1\|4668587_4669724_+\|Inner-membrane-protein-yibH	gnl\|CDD\|185090	PRK15136, PRK15136, multidrug efflux MFS transporter periplasmic adaptor subunit EmrA.	7.60854e-108
LS483395.1\|SQG76402.1\|4655308_4656283_-\|Pirin-C-terminal-cupin-domain	gnl\|CDD\|224655	COG1741, COG1741, Pirin-related protein [General function prediction only].	1.35864e-36
LS483395.1\|SQG76417.1\|4673977_4675180_+\|Protein-of-uncharacterised-function-(DUF2863)	gnl\|CDD\|371362	pfam11062, DUF2863, Protein of unknown function (DUF2863). This bacterial family of proteins have no known function.	0
LS483395.1\|SQG76414.1\|4671288_4671993_+\|Vibriobactin-utilization-protein-ViuB	gnl\|CDD\|99790	cd06193, siderophore_interacting, Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).	7.80577e-39
LS483395.1\|SQG76400.1\|4651993_4652761_+\|3-oxoacyl-[acyl-carrier-protein]-reductase-FabG	gnl\|CDD\|235546	PRK05653, fabG, 3-oxoacyl-ACP reductase FabG.	4.98682e-91
LS483395.1\|SQG76418.1\|4675189_4676305_+\|Uncharacterized-protein-conserved-in-bacteria	gnl\|CDD\|378385	pfam10093, EarP, Elongation-Factor P (EF-P) rhamnosyltransferase EarP. This entry includes family members such as EarP enzymes which are essential for post-translational activation of elongation factor P(EF-P). It was identified as EF-P arginine R32 specific rhamnosyl transferase in Shewanella oneidensis using dTDP-beta-L-rhamnose as donor substrate. This was further confirmed for Pseudomonas aeruginosa, Pseudomonas putida, and Neisseria meningitidis. As for S. oneidensis and P. aeruginosa, EarP enzyme acts as an inverting glycosyltransferase, thus mediating the formation of an alpha-L-rhamnosidic linkage. Structural analysis show that EarP is composed of two opposing domains with Rossmann folds, thus constituting a B pattern-type glycosyltransferase (GT-B) and provide basis for arginine glycosylation by EarP. Mutational analysis of efp and earP genes, resulted in a substantial decrease in the production of rhamnolipids and pyocyanin (important factors for colonization and invasion during infection) of P. aeruginosa. Collectively this indicates that EarP and EF-P are essential for P. aeruginosa pathogenicity.The protein family is also annotated in the CaZy Database as GT104.	4.19896e-175
LS483395.1\|SQG76403.1\|4656401_4657310_+\|D-malate-degradation-protein-R	gnl\|CDD\|184959	PRK14997, PRK14997, LysR family transcriptional regulator; Provisional.	1.1118e-62
LS483395.1\|SQG76405.1\|4658361_4659873_-\|Long-chain-fatty-acid--CoA-ligase	gnl\|CDD\|236215	PRK08276, PRK08276, long-chain-fatty-acid--CoA ligase; Validated.	0
LS483395.1\|SQG76407.1\|4660875_4661805_+\|D-malate-degradation-protein-R	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain 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.	8.34323e-56
LS483395.1\|SQG76408.1\|4662109_4664815_+\|Aconitate-hydratase	gnl\|CDD\|236445	PRK09277, PRK09277, aconitate hydratase AcnA.	0
LS483395.1\|SQG76406.1\|4659869_4660769_-\|Gluconate-5-dehydrogenase	gnl\|CDD\|187627	cd05369, TER_DECR_SDR_a, Trans-2-enoyl-CoA reductase (TER) and 2,4-dienoyl-CoA reductase (DECR), atypical (a) SDR. TTER is a peroxisomal protein with a proposed role in fatty acid elongation. Fatty acid synthesis is known to occur in the both endoplasmic reticulum and mitochondria; peroxisomal TER has been proposed as an additional fatty acid elongation system, it reduces the double bond at C-2 as the last step of elongation. This system resembles the mitochondrial system in that acetyl-CoA is used as a carbon donor. TER may also function in phytol metabolism, reducting phytenoyl-CoA to phytanoyl-CoA in peroxisomes. DECR processes double bonds in fatty acids to increase their utility in fatty acid metabolism; it reduces 2,4-dienoyl-CoA to an enoyl-CoA. DECR is active in mitochondria and peroxisomes. This subgroup has the Gly-rich NAD-binding motif of the classical SDR family, but does not display strong identity to the canonical active site tetrad, and lacks the characteristic Tyr at the usual position. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRS are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes have a 3-glycine N-terminal NAD(P)(H)-binding pattern (typically, TGxxxGxG in classical SDRs and TGxxGxxG in extended SDRs), while substrate binding is in the C-terminal region. A critical catalytic Tyr residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering), is often found in a conserved YXXXK pattern. In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) or additional Ser, contributing to the active site. Substrates for these enzymes include sugars, steroids, alcohols, and aromatic compounds. The standard reaction mechanism is a proton relay involving the conserved Tyr and Lys, as well as Asn (or Ser). Some SDR family members, including 17 beta-hydroxysteroid dehydrogenase contain an additional helix-turn-helix motif that is not generally found among SDRs.	9.23447e-111
LS483395.1\|SQG76413.1\|4669723_4671253_+\|Multidrug-resistance-protein-B	gnl\|CDD\|129794	TIGR00711, Uncharacterized_MFS-type_transporter_YhcA, drug resistance transporter, EmrB/QacA subfamily. This subfamily of drug efflux proteins, a part of the major faciliator family, is predicted to have 14 potential membrane-spanning regions. Members with known activities include EmrB (multiple drug resistance efflux pump) in E. coli, FarB (antibacterial fatty acid resistance) in Neisseria gonorrhoeae, TcmA (tetracenomycin C resistance) in Streptomyces glaucescens, etc. In most cases, the efflux pump is described as having a second component encoded in the same operon, such as EmrA of E. coli. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Other].	2.39588e-126
LS483395.1\|SQG76404.1\|4657320_4658304_-\|Argininosuccinate-lyase	gnl\|CDD\|270296	cd13578, PBP2_Bug27, Aromatic solutes transporter of Bug (Bordetella uptake gene) protein family; contains the type 2 periplasmic binding fold. Bug27 binds non-carboxylated solute nicotinamide, in contrast to BugD (aspartic acid transporter) and BugE (glutamate transporter) which both bind aliphatic carboxylated ligands. The Bug (Bordetella uptake gene) protein family is a large family of periplasmic solute-binding (PBP) receptors present in a number of bacterial species, but mainly in proteobacteria. Bug proteins are the PBP components of the tripartite carboxylate transporters (TTT). Their expansive expansion in proteobacteria indicates a large functional diversity.	1.81934e-127

>LS483395.1|SQG76408.1|4662109_4664815_+|Aconitate-hydratase
MPHNTLDTLKNFKIGNKSCQYYSLPALGKALGIDVQRLPVSIRIVLESVLRNCDGKKVTEEHVRQLANWQANAKREDEIPFVVARVVLQDFTGVPLLADIAAMRSVADKMGKSPKSIEPLVPVDLVVDHSVMIDYFGTKNALDLNMKLEFKRNQERYQFMKWGMQAFDTFGVVPPGFGIVHQVNLEYLARGVHQDKKNNVYYPDSLVGTDSHTTMINGIGVVGWGVGGIEAEAGMLGQPVYFLTPDVVGVELKGKLRGGVTATDLVLTITEMLRREKVVGKFVEFCGEGTASLSVAERATIGNMAPEYGATMGFFPVDGRTIDYFRGTGRTEDEIAAFEAYFKAQDMFGVPAAQDINYTKLLTLDLSTVAPSLAGPKRPQDRIEIGNVKSTFIDLFSKPVAENGFNQPAEKLQQTFTTSTGTKVKNGDILIAAITSCTNTSNPSVLLAAGLLAKKAVEAGLKVPKHIKTSLAPGSRVVTEYLTKTGLLPYLEKLGFDVAAYGCTTCIGNAGDLTPDLNEVITSNDLVCSAVLSGNRNFEARIHPNIKANFLASPPLVVAYALAGTVTRDLMTEPVGRGKNGDIWLGDIWPTTEEVEALLKYALDPKAFEANYGQVKSNPGKLWENIKGVTGETYNWPDSTYIAEPPFFEGFGMTPGAMPTVKNARALGVFGDSVTTDHISPAGSIKETSPAGKWLKENGVMKADFNSYGSRRGNHEIMMRGTFANVRIKNLMIPARPDGSRFEGGETLFQPTGEQMSIYDAAMKYVAAGTPTVVFGGEEYGTGSSRDWAAKGTQLLGVKAVITRSFERIHRSNLVGMGVLPLQFKGSDSVQSLGITGEETYDISGLENGIKPMQDVTLTITRKDGSKQDVTLLLRIDTPIEVDYYQHGGILPFVLRQLLAA
>LS483395.1|SQG76407.1|4660875_4661805_+|D-malate-degradation-protein-R
MTTPPVLDLNLIQLFVTIVEAGTLSEAALRQGVTRSHVSRNLQKLERAFGAQLIRRTTRRLELTHEGSVLYDHGARMAREVESARHALQKLGAEPTGHVRLSLPTGLGELDMLRPLLVRFALEHPSLSLRVLFSNRVSDLISSEIDVALRAISVPPQDYVARELGRIKWHLCAAPEYLARMGMPAHPRDLGRFDFLGPPGARPQATLRLRGKGQPHEVKLATRLQSEYFPFLAQAAREGAGVALLPAYIVRPDLEAGRLLQVLPAYQAEGPGDKLYILTSPTPYPSSAQRALVDFLKRELEPLLRTFLA
>LS483395.1|SQG76406.1|4659869_4660769_-|Gluconate-5-dehydrogenase
MRQTMFRADLFQGQRILITGGGTGLGYAMARQLAALGATVHLCGRRLAVLEQAAQALRGESGGQVHVHPVDIRDAGAVDAMVARIWDQHGGLDALVNNAAGNFISPTEKLSERGFNAIADTVFRGTFYMTQAVGKRWIGSGASGAVVSIVVTWVWTGSPFVVPSAMSKAGIDAMTKSLAVEWGRRGIRLNAIAPGVIPTEGASARLRPNDSGTDALVKQNPMQRLGQGQDIGELAAFLLAPGNDWINGQTIALDGGDYLANGAYFKQYFDWSDDDWAAARAAIEARTAADKAQRPAGQA
>LS483395.1|SQG76405.1|4658361_4659873_-|Long-chain-fatty-acid--CoA-ligase
MSASVTQGAGRIIAGDCQLDRAALMRRGEQVAAGLAAMGIGQGDVVAVLLRNGMPYLEIIQACKRLGCYYCPINWHYTPDEVAYLVRDSGARLLIAEEDLWQAARAALPADLPSRRVGAAAVSEDYASWREAQAPYDGPVVAPRGHMAYTSGTTGRPKGVVRAPFPLDQLAQRLAAVEAVVEQAYGLRPGCRALLPAPVYHSAPSVFAQVALRVCETLVLAPRFDPLEVLRLIERHRIDTVYLVPIMYVRLLKLDPAQRAAFDLSSLRFVASTGAPCAPALKRAMIDWLGPVIHETYASSEAGMVTVIDSHEALARPGSAGRPIGGAQIRIYGDDGALCAPGQIGRIHVRQPAYADFTYRNNPEARSRIERDGLIGLGDLGYLDDDGYLFVCDRESDMVISGGVNIYPAEIEHHLTQYPGVADCAVFGVPDDEFGERLLALVQPAADTALAPEEVLRWLSTRVARYKVPRELRLRQSLPRDDNGKIAKRRLRDAFWAERDRKV
>LS483395.1|SQG76404.1|4657320_4658304_-|Argininosuccinate-lyase
MFMKNSGIGRAAAALLLCMAAVSPAQAAFPERPVKLVVPYTPGGAADLLSRVLAERLSQELAQPVVVENKPGANTMIAATQVARAQPDGYTLFLASNASMVLNPMLYRKISYDAQRDFRVLSVVAELPLVVVANNSVPASTLAQFVDYARARPGKLNYASVGIGNPLQLATELLKSRTGIDVAHVPYNGSAPALSSLMANDTQLMVDVISTSLPLVRENKIKALAVTGAQRLPVLPDVPTVAESGFAGFRAATWFGVAVPRGTPPAEADRLREAVAAVMRQADFRDRFQAQGLVIQAPRGQAEVDAYLAEDRERWNGVIQANHIRLD
>LS483395.1|SQG76403.1|4656401_4657310_+|D-malate-degradation-protein-R
MHSYIHHLDDLLLFTEVVEKGGFSAAARVLNMQRSKLSRRVAELEARLGLRLLQRNTRRVSLTPMGEQIYVHALAMAREARSAFDLAAAMGDTPSGLLRMTAPSALAVTLLGELVARFCLQHPGVRVLLDTRDQVIDLVGEGYDLAFRAQGASLTDSRLVARELAPVPLILVAAPAMARAAPRHPRDLNALPLLAHATQDSPQSWHFVGPAGEAESIEFRPRCLSSNLAALREMARAGLGVALLPHYLCAGSLAKGDLAQLLPAWRAAPARIYAVMPARRGAPLALRRFLDFAAAEMPALLA
>LS483395.1|SQG76402.1|4655308_4656283_-|Pirin-C-terminal-cupin-domain
MTIRLSPPVARPFEPEGDICSYRHFRHSDFPQGMSPLVLVDHFIMTGPAVAPHPHAGISTVTLLLEDTQGGLRIRDSLDNEHEARAGDLHWTVAGRGIVHGHELVGAARLNGLRLYVNLPARLKSMPPSATLVRGWEMPVLQSDAGRVRVVSGRYDGWDAPLATPEPLLILDGWLRPGASRLVPLPAGWNAWLYAAQGEVGVRARHETTPPPRPPVEAAPVIPAARFRPAGRAATTGRRAADPDFAVLPPGAALTATADRDGFLQLLAAGAPAHFILVAGAAIDEPVIQRGPFVMTDARALAQAVAAYEAGDFGQLRQESGVPG
>LS483395.1|SQG76401.1|4652822_4655024_-|Ferrichrome-receptor-FcuA-precursor
MKIRTLACVVAALPYTAIVHAQSAAPAADGSVVSMEAIKVEASADASAGGLAQPYAGGQVARGGRVGVLGTQDIMSTPFSVTSYTNELIQDKQARSVGDVLQNDAGVRVARGFGNFQESYFIRGFILSSDDVAYNGLYSLLPRQYIATELFERVEVLRGASAFLTGAAPSGGGIGGVINLVPKRAPNEPLTRFTTGVSSGGQFSVSTDIARRFGPDDSTGIRLNVANRSGDTGIDDEHSRTSLVSLGLDWRSADTRLSADIGWQENKLKRARPNVTLRGVTSVPDAPDASSNYAQPWSYSNERDVFGTVRAEHDFSDKLTGWAAFGMRRSDEANSLGNVTVTNGSTGDGNFYRFDNTREDSVNTGELGLRAKVRTGPVGHEFVASASFFDLKKKNAYVMDYLNTFPTNIYDPVSYDRPAYGSKALFGNDLDDPALQGRTRLSSYAFGDTMSFLDDKVLLTLGIRHQRLSQRDYAYNTGKEQSAYDASRNSPAAGIVFKVAPSVSLYANYIEALVAGDTAPQTANGKPVPNAGQSLQPYVSKQKEIGVKYDGGGLGAGLALFSTDKPRAAYDASNRFTASGKDRHQGIELTVFGEPVNRVRVLGGMTFLDAKQRSTGNSAIDGNRVIGVPRFQANLGAEWDIPGVQGLTVDGRVVYTGASYADDANTLKVPGWTRFDAGLRYMMDVDGHVVTLRARVENIANRNYWSSVGGYPGNGYLVLGGPRTFSLSASMDF
>LS483395.1|SQG76400.1|4651993_4652761_+|3-oxoacyl-[acyl-carrier-protein]-reductase-FabG
MSARFQDQVIIVTGAVGGIGSAIVEGFLAEGGKVGLIDFNSQGGQAYEKELKKRGHAVSFVHADVSHFDQCQAAYERITRDLGPATILVNNVGISPKTDGRALKVWEMTPGEWDKVVAVNLNSVFYMTHLATPHMVRQRQGRVINMSSVAGKAYCDIVAAHYAATKAALLGLTRHWAAELGEHDVTVNGLAPGRISTPLLKSVPKEINDAVAEVTALRRLGTPEEVADACLFFASDQARFVTGQVLDVAGGWLMT
>LS483395.1|SQG76399.1|4651001_4651997_+|Beta-ketoacyl-acyl-carrier-protein-synthase-I
MSLRCTFIDHGTGGAPDCLRLAEREMAAPAGRQVLIEVAYAGVNRPDVLQRSGSYPPPPGASPYLGLEVAGTVIAVGPDATRWQVGDRVCALTPGGGYAQYCLADERHCLPVPRGLDLLSAAAIPENYFTVWTNVFERARLAAGEKFLVHGGSSGIGLTAIQLARAFGAEVWTTVGNQEKAEACLKAGAQHALIYRDTDFEADIRQATGGQGVDVILDMVGGAYINKNIRLLAVNGRLVQIAFLEGSKAEIDALPIMTKRLSFTGSTLRPRSDEDKGAIAQALADKVLPLMEQGRCLPLIHQVFPLEQAAQAHALMESSRHIGKIMLKVRA
>LS483395.1|SQG76409.1|4664985_4666032_-|Outer-membrane-protein-OmpAb
MHNGCRPHRGRFLVLDACRRLPAGSVEIVKAHIVKVASLAIVAATLTASPAWAEDVEGSRDHPALTRFEGAEIRAYEHKDYDEALMPDRPVARESEAKGLTLEGKLTRIAYRIDGKKSALEVYRNYQGALQAGGFKTVFECKGDEQCGGDFQSFVLNSGKVSQPGQGDAAFGGKYYVVLAKKEAPTGDIYVFLDVMEDSSNNITPVFQQVIETKPMQTGQVKVLDMAAMQKSLAESGRVAVYGVYFDTDKAEVKAESKAALDEMGKLLNANPKLKVYVVGHTDNQGTLAGNLELSQKRADAVVKALEAGYKIPAARLSARGVASLAPVAANDAEAGRAKNRRVELVAQ
>LS483395.1|SQG76410.1|4666100_4666994_-|Nodulation-protein-D-2
MDLNLLVALDALLAEGSVTGAAERLQLSVPAMSRTLERIRRMMGDPLFVRAGRGLVPTPRAEALREPVRTLVAQARELLAQDAAFDLKTLRRVFTIRADDGAVSTLGPALLDTLAKEAPRVTVRFISQGKQDVLSLREGAIDLDIGVIEDMGPEIVRQRLFPDRFVAVFRPANPLARHRKLTPERFARARHATVSRRGVLSGPVDIELGKVGLARHISAVTHSFAEALAITRKSDLVATVPDLLTLHLRDDLQMRALPFDTPAVTISQAWHPRFNEDPAHRAIRQMVHRISLAISGR
>LS483395.1|SQG76411.1|4667091_4668591_+|Multidrug-resistance-outer-membrane-protein-MdtP-precursor
MIHSTRYRPDARPARRMRLRHAPLAAALAALVAVAGCASHDGLRPAGKPLDLAALDAGQDIAAAVRDTADDAAPWWRAWGDDQLDRLMADALRQAPGVRAAQARLGQAEAVFGSVDANRQPTLDGSATITADRYPGHYTYGAPYADNTGGSGSLLASLRLRLDIWGKWRALADAARLDAEGAALAHADAQLALQQGIAAAYLRLDAAFRLHELARQQRERQRQALELHQTRRQAGLGSDAPVADARGRLARMDAEVERLDREIARQRHALAALAGQAPGYGDVLRRPRLALRADPALPAALPARLLGLRPDVLAQRKRLDAADRRIEAAKAEFYPDIDLKAFAGLQSLGLSHLLQGNSLAAGIGPALTLPIFDGGRLRAGLRDRIAGYDLAVADYDATVVRALQEVADGLAGMAQARARRDAARVSLREAGTLARLQAVRASRGLSARQDEIDTDLARLRADSELAAADLDLGLARTALAGALGGRWSPSQSSDNEALK
>LS483395.1|SQG76412.1|4668587_4669724_+|Inner-membrane-protein-yibH
MTATQTPDSRTSTRKSRLMLAGGATLLAGAGWAAWTFLAGAATQTTDNAYVNGHVVAITPQVGGAVSAIWADNADRIRAGQTLVEVDPADTQIALAGARADLARARRRVQALFASRDQAGAEVARRQAELDRAQADVSARRGIAAQGAITSEEARHAADALNAARAALAVAQAAERAAQAQVDGVTPDTHPDVTLAQARLRAAALDAQRTTIRAPVGGMVAQRSVQLGKHVAIGDKLMAVVPLDQMWIDANFKEIQLAGICPGQPAVVTVDAHGAKVRYRGRVGDVMAGSGSAFALLPSQNATGNWIKVVQRVPVRINLDPKELADHPLRIGLSAEVTVDTARCDPAQAGAARGETTDIYRQQRQAADTLAQAGQGLQ
>LS483395.1|SQG76413.1|4669723_4671253_+|Multidrug-resistance-protein-B
MSAAPRPIEPMTGLPRVVAAVAISLASFMAVVDITIANVSVPTISGNLGVSPEIGEWAITFFAIANSICIPLTGWLSRRLGQVRLFVLSVAAFTLASVLCGVAQNFESLLAFRVLQGMVSGPIVPLSQALLVAIFPPDKRTLALSMWAMTNMAGPVAGPVLGGWLTDDFSWPWIFLVNAPVGIAVVAVTATMFRGRDTPSTRLPVDLRGLILLAVAIGCLQLTLDRGRTLDWFASPFIVTTALLSALGFVFLVIWELGEAHPIVDLSLFRHRNFAMGTLAVAVGFGLYFAALVLIPLWLQTDMRYTATWAGLATAPMGVFGILLAPLLGRWVQRGDARVFASLAFVAWSLVAWWRASMTTDVGVGLISLACLLQGIGIGLFLTPLVSLSLAGLPPERIAAASGLQTAIRMMAGSLVASLASTYWDERSRYYQNVLVDSATPARPAVQDTLNALAGAGLDEPQSWGVIWNGLKTQADMLALNDFFLWSSLAFALSIALVWLARHPRAAKA
>LS483395.1|SQG76414.1|4671288_4671993_+|Vibriobactin-utilization-protein-ViuB
MQPFSLPRRDVPCIVLRARDVARDMRRLTLGGPELSAWLARPGVDQPGAWVKVFPPGVPGRAYTLRGIDFEASSVEIDFVVHGDAPGTVSEWARRARPGDAVSIAGPRDGGFSLLADTRWVWLGADASAWPAASRIIESLPGGIQVLGVRHPAGDDDWPAIASARAPQWAARSLPPGGDEPSAPAPDGPGQVWLAGQAAWVKAWRAHWLQRLRFDPARLSAKGYWKAGEQDYKE
>LS483395.1|SQG76415.1|4672028_4672919_+|D-malate-degradation-protein-R
MKKELDRMRDMALFVQVAALGSLTRAAESTGVPASTLSRRISEFESQIGVKLLHRSTRRLALTDIGQRYLERITDVVDRARAISGELEEEMGRPTGHLRVCAPVDFNAYFPEAALADYCASHPGVRFELHCSAQLPDLATEPYDICIATTEPPQASRMVRRRIGMAEYQLYAAPAYLRAYGVPAHPAELARHRCVVMPDSESGLALTDGNASAQVALAPLLVLNNQLAVENLLRDGLGIGPLTRGRADALVREGALAPVLPGWTLPPRPILALTASRALPARVRGFIDLLVARVVT
>LS483395.1|SQG76416.1|4672959_4673733_-|LigB-family-dioxygenase
MRWPTLFVSHGSPMLAVEPGATGPALAAWSRSLGRKPGAILVVSPHWMGHGLALSTRDRQVAWHDFGGFPPELYTLQYAAPGSPELAARVQALLAEGGIAADRDPRRPLDHGAWVPLRYLYPEVDVPVVQLSLDMGRDAAGQLELGRALAPLRDEDVLIIGSGSLTHNLRDVRMPQDAPPAPYVPAFQAWYADRLAAHDVPALLDWQARAPGAAQAHPHDDHLMPLYVALGAGGARATRLTDEISYGALAMDAYAFD
>LS483395.1|SQG76417.1|4673977_4675180_+|Protein-of-uncharacterised-function-(DUF2863)
MARSRSQSAPRLTRDATRLITLAQSLNRSGSRVEDVYWENQLGEAIPKLLKAGQDAPLEAALDHLAQGDVGAYEVLIEQAETLSESMKIDKNGVRYDILLIVAPVVAWTRYAIPTGPVPASAQQALLAQLHGHVLSSQARSALMPHLVSVDQMPRTFSETWQWLQRLGSQALGAETTKPALNTEVETANMLADTRYIVAAVAVPEFAPVFRWQEQIGEADASRDACLAQWAAQAQPTLAGLLPGCGFEALLPDAYYVSNREADRRVRPLSLRAAISWLEGAVSLDASQLRAVIAGCGESRVDEYRVSFTARNSNDVYYGCVWPLYGREEDLPADEGQPDVVDEIAALLKEYGVSDVRRIPGVLPPEYCEDCGAPYFPNPLGELVHAELPEDAEAAPAKFH
>LS483395.1|SQG76418.1|4675189_4676305_+|Uncharacterized-protein-conserved-in-bacteria
MQADIFCRVVDNYGDIGVCWRLARRLAHGHGWEVRLWVDDLASFARIQPGIDAGLARQAFNGVDIVRWSDAPDPALGARDVVIEAFACDPPEPFLDSMRQRHPAWINLEYLSAEAWVESCHGLPSQRPDGLVKHFYFPGFTPATGGLLREPGLSAERDAFQADTAAQDTFLRGLGVAEAHLSLRHNGARTMSLFCYPDAPVDGLARALAADPRPALLLAPEGVAPGLEAACAMPGGPAVARLPFVAQPDFDRVLWCADLNFVRGEDSFVRAAWAARPLVWQIYPQDENIHLEKLDAWLARYPAPETATALMRAWNQPGAGAATAAALAAALAPPAWQAWARAARDWDAAQAARPDLAENLAGFCAELAKKR

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
LS483395_2	2.1\|2273342\|45\|LS483395\|CRISPRCasFinder	2273342-2273386	45	LS483395.1	2041534-2041578	1	0.978

1. spacer 2.1|2273342|45|LS483395|CRISPRCasFinder matches to position: 2041534-2041578, mismatch: 1, identity: 0.978

gcctttttttgccgccgggccgccccaaggcaaaaacgccccctc	CRISPR spacer
gcttttttttgccgccgggccgccccaaggcaaaaacgccccctc	Protospacer
**.******************************************

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

1970427 : 1981873

Burkholderia_phage(50.0%)

plate

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
SQG71374.1\|1970427_1970877_+	Uncharacterised protein	A0A0N7IRF3	Acinetobacter_phage	1.1e-17	36.5
SQG71375.1\|1971054_1972728_+	Uncharacterised protein	NA	NA	NA	NA
SQG71376.1\|1972720_1973320_+	Uncharacterised protein	NA	NA	NA	NA
SQG71377.1\|1973329_1973629_+	Uncharacterised protein	NA	NA	NA	NA
SQG71378.1\|1973630_1974659_+	Uncharacterised protein	A9YX04	Burkholderia_phage	1.9e-76	50.3
SQG71379.1\|1974693_1975437_+\|plate	phage baseplate assembly protein V	A9YX06	Burkholderia_phage	2.5e-83	63.5
SQG71380.1\|1975445_1975799_+	Uncharacterised protein	A9YX11	Burkholderia_phage	6.1e-35	66.7
SQG71381.1\|1975795_1976977_+	Uncharacterized homolog of phage Mu protein gp47	A9YX12	Burkholderia_phage	5.8e-130	62.6
SQG71382.1\|1976978_1977644_+	Protein of uncharacterised function (DUF2612)	A9YX13	Burkholderia_phage	9.6e-74	60.6
SQG71383.1\|1977658_1978600_+	Uncharacterised protein	A0A0M3ULD8	Salmonella_phage	5.8e-16	54.1
SQG71384.1\|1979330_1979681_+	Uncharacterised protein	NA	NA	NA	NA
SQG71385.1\|1979683_1980706_-	Site-specific recombinase XerD	A0A2H4JE37	uncultured_Caudovirales_phage	2.8e-24	32.3
SQG71386.1\|1980891_1981353_+	Uncharacterised protein	A0A0U5LBV3	unidentified_phage	7.7e-14	37.2
SQG71387.1\|1981342_1981873_+	Uncharacterised protein	A0A2H4JFP9	uncultured_Caudovirales_phage	7.0e-43	57.4

DBSCAN-SWA_2

2843432 : 2851366

Moraxella_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SQG72165.1\|2843432_2844020_+	IMPACT family member yigZ	A0A1X9I5T8	Streptococcus_phage	1.2e-19	36.8
SQG72166.1\|2844053_2844428_-	Thioredoxin-1	V9SJ74	Achromobacter_phage	1.1e-10	27.8
SQG72167.1\|2844624_2845647_-	Limonene 1,2-monooxygenase	NA	NA	NA	NA
SQG72168.1\|2846025_2846382_+	Predicted enzyme related to lactoylglutathione lyase	NA	NA	NA	NA
SQG72169.1\|2846466_2847759_-	Probable adenine permease PurP	A0A0R6PHV4	Moraxella_phage	5.4e-65	36.3
SQG72170.1\|2847867_2848899_+	t(6)A37 threonylcarbamoyladenosine biosynthesis protein	A0A0R6PI74	Moraxella_phage	1.4e-92	51.6
SQG72171.1\|2848968_2849610_-	G3P acyltransferase	NA	NA	NA	NA
SQG72172.1\|2849798_2850557_+	5'-nucleotidase surE	A0A1B1ITZ2	uncultured_Mediterranean_phage	1.5e-67	51.6
SQG72173.1\|2850541_2851366_+	Protein-L-isoaspartate O-methyltransferase	A0A1B1IU40	uncultured_Mediterranean_phage	2.5e-31	45.2

DBSCAN-SWA_3

4054713 : 4089011

Xylella_phage(20.0%)

protease,terminase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SQG75553.1\|4054713_4057164_-\|protease	Lon protease	A0A0R6PGP8	Moraxella_phage	7.8e-222	52.2
SQG75556.1\|4057414_4058713_-\|protease	ATP-dependent Clp protease ATP-binding subunit ClpX	G3M9Z9	Bacillus_virus	1.7e-130	54.1
SQG75559.1\|4058814_4059468_-\|protease	ATP-dependent Clp protease proteolytic subunit	A0A223W000	Agrobacterium_phage	2.2e-54	55.7
SQG75561.1\|4059472_4060783_-	Trigger factor	NA	NA	NA	NA
SQG75563.1\|4060951_4061707_-\|protease	Uncharacterized metalloprotease yggG	NA	NA	NA	NA
SQG75566.1\|4061969_4062515_+	Predicted membrane protein	K4K6D8	Caulobacter_phage	1.3e-20	32.7
SQG75568.1\|4062615_4062822_-	CS7.4	A0A1W6JNX5	Morganella_phage	1.4e-15	59.7
SQG75571.1\|4063114_4063678_-	Uncharacterized protein conserved in bacteria	A0A1V0SIY0	Klosneuvirus	1.2e-16	41.2
SQG75573.1\|4064475_4064796_-	Uncharacterised protein	NA	NA	NA	NA
SQG75576.1\|4064886_4065285_-	Uncharacterised protein	NA	NA	NA	NA
SQG75577.1\|4065407_4065695_+	Uncharacterised protein	NA	NA	NA	NA
SQG75578.1\|4065788_4066061_-	Uncharacterised protein	NA	NA	NA	NA
SQG75579.1\|4066162_4066558_-	Enamine/imine deaminase	NA	NA	NA	NA
SQG75580.1\|4066584_4067733_-	D-threonine aldolase	NA	NA	NA	NA
SQG75581.1\|4067879_4068797_+	D-malate degradation protein R	NA	NA	NA	NA
SQG75583.1\|4068979_4069378_-	putative endoribonuclease L-PSP	NA	NA	NA	NA
SQG75585.1\|4069445_4070636_-	Major Facilitator Superfamily	NA	NA	NA	NA
SQG75587.1\|4070769_4071351_+	DNA-binding transcriptional repressor AcrR	NA	NA	NA	NA
SQG75588.1\|4071474_4072002_+	Uncharacterised protein	NA	NA	NA	NA
SQG75590.1\|4072072_4072378_+	Uncharacterised protein	NA	NA	NA	NA
SQG75592.1\|4072401_4072710_-	Uncharacterised protein	NA	NA	NA	NA
SQG75594.1\|4072776_4073634_-	2-dehydro-3-deoxyphosphooctonate aldolase	E3T537	Cafeteria_roenbergensis_virus	1.1e-50	41.7
SQG75596.1\|4073870_4074830_+	Uncharacterized conserved protein	NA	NA	NA	NA
SQG75597.1\|4074853_4076071_+	Uncharacterized protein conserved in bacteria	NA	NA	NA	NA
SQG75600.1\|4076114_4076825_-	Bacterial nodulin-like intrinsic protein	A0A1B1ISL4	uncultured_Mediterranean_phage	1.2e-05	50.0
SQG75602.1\|4076967_4077549_-	Glycerol-3-phosphate responsive antiterminator	NA	NA	NA	NA
SQG75604.1\|4077550_4079107_-	Uncharacterized FAD-linked oxidoreductase Rv2280	NA	NA	NA	NA
SQG75606.1\|4079103_4080783_-	Aerobic glycerol-3-phosphate dehydrogenase	NA	NA	NA	NA
SQG75608.1\|4080779_4082318_-	Glycerol kinase	NA	NA	NA	NA
SQG75610.1\|4082332_4083790_-	Probable metabolite transport protein CsbC	NA	NA	NA	NA
SQG75612.1\|4084012_4084402_+	Uncharacterized protein conserved in bacteria	NA	NA	NA	NA
SQG75614.1\|4084506_4084866_+	Uncharacterised protein	NA	NA	NA	NA
SQG75616.1\|4084876_4085389_+	Uncharacterised protein	NA	NA	NA	NA
SQG75618.1\|4085490_4085766_-	Uncharacterised protein	NA	NA	NA	NA
SQG75619.1\|4086035_4086851_+	Uncharacterised protein	NA	NA	NA	NA
SQG75621.1\|4087136_4087868_-	Uncharacterised protein	NA	NA	NA	NA
SQG75623.1\|4087956_4088646_-\|terminase	Bacteriophage terminase large (ATPase) subunit and inactivated derivatives	C8CLI4	Xylella_phage	1.2e-18	56.5
SQG75625.1\|4088741_4089011_-\|terminase	Bacteriophage terminase large (ATPase) subunit and inactivated derivatives	C8CLI4	Xylella_phage	4.2e-20	58.5

DBSCAN-SWA_4

4093293 : 4119834

uncultured_Caudovirales_phage(23.81%)

protease,portal,tail

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SQG75640.1\|4093293_4093833_-	Site-specific recombinase XerD	A0A1B1P9F9	Acinetobacter_phage	5.4e-35	43.8
SQG75642.1\|4093835_4094288_-	Uncharacterised protein	A0A0A1I5U0	Burkholderia_phage	1.4e-07	33.6
SQG75644.1\|4094626_4095319_+	Uncharacterised ACR, COG2135	Q5QF62	Pseudomonas_virus	2.4e-35	37.9
SQG75646.1\|4095302_4095497_-	Uncharacterised protein	NA	NA	NA	NA
SQG75658.1\|4095683_4095929_+	Uncharacterised protein	NA	NA	NA	NA
SQG75660.1\|4096456_4096723_-	Uncharacterised protein	NA	NA	NA	NA
SQG75662.1\|4096725_4097217_-	Uncharacterised protein	I6NSS1	Burkholderia_phage	1.2e-44	59.3
SQG75664.1\|4097220_4097664_-	Uncharacterised protein	A0A0A1IVG1	Pseudomonas_phage	3.8e-10	35.3
SQG75666.1\|4097752_4098481_-	Uncharacterised protein	A0A0B5A5A1	Achromobacter_phage	1.5e-64	51.5
SQG75668.1\|4098776_4101950_-	Domain of uncharacterised function (DUF1983)	A4JX16	Burkholderia_virus	3.8e-277	47.3
SQG75670.1\|4101946_4102555_-\|tail	Phage-related protein, tail component	Q6JIL3	Burkholderia_virus	2.9e-53	56.2
SQG75672.1\|4102558_4103332_-	NlpC/P60 family	A4JX14	Burkholderia_virus	7.7e-67	51.7
SQG75674.1\|4103334_4104063_-\|tail	phage minor tail protein L	Q6JIL5	Burkholderia_virus	1.1e-65	55.3
SQG75676.1\|4104071_4104482_-	Uncharacterised protein	NA	NA	NA	NA
SQG75678.1\|4104478_4105990_-	Uncharacterised protein	A0A0B5A596	Achromobacter_phage	2.1e-52	54.0
SQG75680.1\|4105995_4106337_-	Phage-related protein	Q6UAW6	Klebsiella_phage	5.7e-30	54.5
SQG75682.1\|4106333_4109309_-\|tail	Phage-related minor tail protein	A0A2H4J9A1	uncultured_Caudovirales_phage	1.2e-94	32.9
SQG75684.1\|4109342_4109432_-	Uncharacterised protein	NA	NA	NA	NA
SQG75686.1\|4109719_4110139_-	Uncharacterised protein	NA	NA	NA	NA
SQG75687.1\|4110211_4111147_-	Uncharacterised protein	G8CLB2	Synechococcus_phage	2.9e-60	40.9
SQG75689.1\|4111179_4111383_-	Uncharacterised protein	NA	NA	NA	NA
SQG75691.1\|4111409_4111832_-	Uncharacterised protein	NA	NA	NA	NA
SQG75693.1\|4111828_4112131_-	Uncharacterised protein	NA	NA	NA	NA
SQG75695.1\|4112136_4113141_-	Uncharacterised protein	A0A2H4J890	uncultured_Caudovirales_phage	4.1e-68	42.2
SQG75697.1\|4113221_4113572_-	Uncharacterised protein	A0A2H4JF15	uncultured_Caudovirales_phage	8.7e-18	49.6
SQG75699.1\|4113599_4114706_-\|protease	ATP-dependent Clp protease proteolytic subunit	A0A2H4JDI2	uncultured_Caudovirales_phage	3.3e-47	36.8
SQG75701.1\|4114734_4116234_-\|portal	phage portal protein, lambda family	A0A2H4JFL5	uncultured_Caudovirales_phage	4.1e-125	50.1
SQG75702.1\|4116230_4116437_-	Uncharacterised protein	A0A2H4EUL1	Aeromonas_phage	4.5e-06	42.6
SQG75703.1\|4116482_4118555_-\|tail	Bacteriophage tail assembly protein	R9TMM4	Vibrio_phage	2.3e-118	37.3
SQG75704.1\|4118554_4119052_-	Phage DNA packaging protein Nu1	NA	NA	NA	NA
SQG75705.1\|4119048_4119834_-	Uncharacterised protein	A0A1B0Z000	Pseudomonas_phage	5.7e-33	39.3

DBSCAN-SWA_5

4137333 : 4146353

Klebsiella_phage(16.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SQG75734.1\|4137333_4137864_+	Uncharacterised protein	A0A248SL53	Klebsiella_phage	5.9e-18	44.0
SQG75735.1\|4137860_4138241_+	Uncharacterised protein	NA	NA	NA	NA
SQG75736.1\|4138237_4138453_+	Uncharacterised protein	NA	NA	NA	NA
SQG75737.1\|4138449_4138677_+	Uncharacterised protein	Q6V7Q9	Burkholderia_virus	3.2e-05	46.2
SQG75738.1\|4138707_4139499_-	Uncharacterised protein	NA	NA	NA	NA
SQG75739.1\|4140117_4142133_+	DNA (cytosine-5-)-methyltransferase	Q5QF27	Pseudomonas_virus	1.2e-159	47.7
SQG75740.1\|4142129_4142303_+	Uncharacterised protein	NA	NA	NA	NA
SQG75741.1\|4142588_4143506_+	Domain of Uncharacterised Function with PDB structure	A0A0K2FIF7	Achromobacter_phage	4.6e-18	66.2
SQG75742.1\|4143502_4144969_+	Uncharacterised protein	A0A291L9X3	Bordetella_phage	1.9e-13	65.6
SQG75743.1\|4145111_4146353_+	Integrase	A0A1W6JTA0	Pseudomonas_phage	1.4e-118	57.8

DBSCAN-SWA_6

6026337 : 6043348

Burkholderia_virus(25.0%)

tail

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
SQG77645.1\|6026337_6027156_+	D-beta-hydroxybutyrate dehydrogenase	W8CYX9	Bacillus_phage	1.4e-10	49.3
SQG77646.1\|6027174_6028104_-	Cyn operon transcriptional activator	NA	NA	NA	NA
SQG77647.1\|6028245_6028842_-\|tail	Phage-related protein, tail component	C7BGD3	Burkholderia_phage	1.9e-49	53.0
SQG77648.1\|6028838_6029075_-	Uncharacterised protein	NA	NA	NA	NA
SQG77649.1\|6029055_6029427_-	Uncharacterised protein	NA	NA	NA	NA
SQG77650.1\|6029423_6033035_-	Domain of uncharacterised function (DUF1983)	A0A2R3UA88	Siphoviridae_environmental_samples	2.2e-265	44.6
SQG77651.1\|6033031_6033637_-\|tail	Phage-related protein, tail component	Q6JIL3	Burkholderia_virus	1.0e-50	55.7
SQG77652.1\|6033633_6034413_-	NlpC/P60 family	Q3HQU3	Burkholderia_phage	1.5e-65	47.3
SQG77653.1\|6034415_6035144_-\|tail	phage minor tail protein L	Q6JIL5	Burkholderia_virus	2.2e-71	58.3
SQG77654.1\|6035146_6037108_-	Uncharacterised protein	A0A0K0KVF1	Prochlorococcus_phage	1.9e-13	36.2
SQG77655.1\|6037104_6037449_-	Phage-related protein	A0A0S2SYI2	Pseudomonas_phage	4.8e-21	38.4
SQG77656.1\|6037445_6038732_-	Uncharacterised protein	A0A1W6JP49	Morganella_phage	1.4e-12	27.2
SQG77657.1\|6038789_6039080_-	Uncharacterised protein	S4TND7	Salmonella_phage	9.1e-13	50.0
SQG77658.1\|6039079_6039553_-\|tail	Phage tail assembly chaperone	A4JX08	Burkholderia_virus	4.8e-27	45.1
SQG77659.1\|6039558_6040026_-	Uncharacterised protein	NA	NA	NA	NA
SQG77660.1\|6040276_6040870_-	Uncharacterised protein	NA	NA	NA	NA
SQG77661.1\|6041142_6041838_+	Uncharacterised protein	NA	NA	NA	NA
SQG77662.1\|6041890_6043348_-	Uncharacterized conserved protein	M1IA53	Paramecium_bursaria_Chlorella_virus	2.3e-64	35.6

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. LS483395

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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