CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP015731	Exiguobacterium sp. U13-1, complete genome	1 crisprs	DEDDh,cas3,casR,csa3,DinG,Cas14u_CAS-V,WYL	1	0	3	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP015731_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP015731_1

2796319-2796426

Orphan

Consensus_repeat	Method
GCAAAAGCCGAAGCAGAGGCAAAA	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP015731_1

>merge|NZ_CP015731|1|2796319-2796426|CRISPRCasFinder
GAAAAAGCTGAAGCTGATGCCAAGAAAAAAGCAGCCGACGACGCAAAACGTGCTGCCGACGCAAAAGCAAAAGCCGAAGCAGAGGCAAAAGCCGAAGCAGAGGCAAAA

>NZ_CP015731|1|1|2796319-2796426|CRISPRCasFinder
GAAAAAGCTGAAGCTGATGCCAAG	AAAAAAGCAGCCGACGAC
GCAAAACGTGCTGCCGACGCAAAA	GCAAAAGCCGAAGCAGAG
GCAAAAGCCGAAGCAGAGGCAAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP015731.1\|WP_047393518.1\|2796636_2798340_-\|acetate--CoA-ligase	unknown	unknown	gnl\|CDD\|235279
NZ_CP015731.1\|WP_029342360.1\|2805570_2806683_+\|aminopeptidase	unknown	unknown	gnl\|CDD\|225191
NZ_CP015731.1\|WP_023469069.1\|2803043_2804129_-\|3-deoxy-7-phosphoheptulonate-synthase	unknown	unknown	gnl\|CDD\|183614
NZ_CP015731.1\|WP_023469064.1\|2798486_2799119_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP015731.1\|WP_047393521.1\|2788146_2789853_-\|septation-ring-formation-regulator-EzrA	unknown	unknown	gnl\|CDD\|179877
NZ_CP015731.1\|WP_029342359.1\|2804861_2805431_-\|DUF948-domain-containing-protein	unknown	unknown	gnl\|CDD\|227109
NZ_CP015731.1\|WP_023469059.1\|2790795_2791395_+\|30S-ribosomal-protein-S4	unknown	unknown	gnl\|CDD\|235411
NZ_CP015731.1\|WP_069940884.1\|2799137_2799770_+\|CBS-domain-containing-protein	unknown	unknown	gnl\|CDD\|341361
NZ_CP015731.1\|WP_029342348.1\|2786519_2788079_-\|amidohydrolase	unknown	unknown	gnl\|CDD\|224490
NZ_CP015731.1\|WP_029342350.1\|2792337_2793585_-\|tyrosine--tRNA-ligase	unknown	unknown	gnl\|CDD\|235645
NZ_CP015731.1\|WP_023469060.1\|2791548_2792076_+\|biotin-transporter-BioY	unknown	unknown	gnl\|CDD\|376871
NZ_CP015731.1\|WP_156772517.1\|2801065_2801821_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379037
NZ_CP015731.1\|WP_047393526.1\|2783182_2784091_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|223897
NZ_CP015731.1\|WP_029342358.1\|2804328_2804865_-\|YtxH-domain-containing-protein	unknown	unknown	gnl\|CDD\|378938
NZ_CP015731.1\|WP_023469068.1\|2801874_2802885_-\|catabolite-control-protein-A	unknown	unknown	gnl\|CDD\|130546
NZ_CP015731.1\|WP_023469054.1\|2784854_2785670_+\|NAD-kinase	unknown	unknown	gnl\|CDD\|179584
NZ_CP015731.1\|WP_023469058.1\|2790076_2790562_+\|GAF-domain-containing-protein	unknown	unknown	gnl\|CDD\|224867
NZ_CP015731.1\|WP_047393524.1\|2785763_2786528_+\|MerR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|133381
NZ_CP015731.1\|WP_047393512.1\|2799766_2800960_+\|acetoin-utilization-protein-AcuC	unknown	unknown	gnl\|CDD\|212520
NZ_CP015731.1\|WP_148662037.1\|2784191_2784689_-\|thiol-peroxidase	unknown	unknown	gnl\|CDD\|179055

Protein	Function_ID	Function_description	E-value
NZ_CP015731.1\|WP_047393518.1\|2796636_2798340_-\|acetate--CoA-ligase	gnl\|CDD\|235279	PRK04319, PRK04319, acetyl-CoA synthetase; Provisional.	0
NZ_CP015731.1\|WP_029342360.1\|2805570_2806683_+\|aminopeptidase	gnl\|CDD\|225191	COG2309, AmpS, Leucyl aminopeptidase (aminopeptidase T) [Amino acid transport and metabolism].	1.84223e-121
NZ_CP015731.1\|WP_023469069.1\|2803043_2804129_-\|3-deoxy-7-phosphoheptulonate-synthase	gnl\|CDD\|183614	PRK12595, PRK12595, bifunctional 3-deoxy-7-phosphoheptulonate synthase/chorismate mutase; Reviewed.	0
NZ_CP015731.1\|WP_023469064.1\|2798486_2799119_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	1.95965e-05
NZ_CP015731.1\|WP_047393521.1\|2788146_2789853_-\|septation-ring-formation-regulator-EzrA	gnl\|CDD\|179877	PRK04778, PRK04778, septation ring formation regulator EzrA; Provisional.	2.13336e-143
NZ_CP015731.1\|WP_029342359.1\|2804861_2805431_-\|DUF948-domain-containing-protein	gnl\|CDD\|227109	COG4768, COG4768, Uncharacterized protein containing a divergent version of the methyl-accepting chemotaxis-like domain [General function prediction only].	1.66057e-29
NZ_CP015731.1\|WP_023469059.1\|2790795_2791395_+\|30S-ribosomal-protein-S4	gnl\|CDD\|235411	PRK05327, rpsD, 30S ribosomal protein S4; Validated.	2.33991e-122
NZ_CP015731.1\|WP_069940884.1\|2799137_2799770_+\|CBS-domain-containing-protein	gnl\|CDD\|341361	cd04584, CBS_pair_AcuB_like, Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain. The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).	1.09305e-43
NZ_CP015731.1\|WP_029342348.1\|2786519_2788079_-\|amidohydrolase	gnl\|CDD\|224490	COG1574, COG1574, Predicted metal-dependent hydrolase with the TIM-barrel fold [General function prediction only].	1.19088e-116
NZ_CP015731.1\|WP_029342350.1\|2792337_2793585_-\|tyrosine--tRNA-ligase	gnl\|CDD\|235645	PRK05912, PRK05912, tyrosyl-tRNA synthetase; Validated.	0
NZ_CP015731.1\|WP_023469060.1\|2791548_2792076_+\|biotin-transporter-BioY	gnl\|CDD\|376871	pfam02632, BioY, BioY family. A number of bacterial genes are involved in bioconversion of pimelate into dethiobiotin. BioY is a component of the BioMNY transport system involved in biotin uptake in prokaryotes.	1.18999e-31
NZ_CP015731.1\|WP_156772517.1\|2801065_2801821_+\|hypothetical-protein	gnl\|CDD\|379037	pfam13115, YtkA, YtkA-like.	2.11533e-05
NZ_CP015731.1\|WP_047393526.1\|2783182_2784091_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|223897	COG0827, COG0827, Adenine-specific DNA methylase [DNA replication, recombination, and repair].	3.06348e-22
NZ_CP015731.1\|WP_029342358.1\|2804328_2804865_-\|YtxH-domain-containing-protein	gnl\|CDD\|378938	pfam12732, YtxH, YtxH-like protein. This family of proteins is found in bacteria. Proteins in this family are typically between 100 and 143 amino acids in length. The N-terminal region is the most conserved. Proteins is this family are functionally uncharacterized.	7.16528e-11
NZ_CP015731.1\|WP_023469068.1\|2801874_2802885_-\|catabolite-control-protein-A	gnl\|CDD\|130546	TIGR01481, catabolite_control_protein_A, catabolite control protein A. Catabolite control protein A is a LacI family global transcriptional regulator found in Gram-positive bacteria. CcpA is involved in repressing carbohydrate utilization genes [ex: alpha-amylase (amyE), acetyl-coenzyme A synthase (acsA)] and in activating genes involved in transporting excess carbon from the cell [ex: acetate kinase (ackA), alpha-acetolactate synthase (alsS)]. Additionally, disruption of CcpA in Bacillus megaterium, Staphylococcus xylosus, Lactobacillus casei and Lactocacillus pentosus also decreases growth rate, which suggests CcpA is involved in the regulation of other metabolic pathways. [Regulatory functions, DNA interactions].	5.5118e-175
NZ_CP015731.1\|WP_023469054.1\|2784854_2785670_+\|NAD-kinase	gnl\|CDD\|179584	PRK03501, ppnK, NAD kinase.	8.6276e-167
NZ_CP015731.1\|WP_023469058.1\|2790076_2790562_+\|GAF-domain-containing-protein	gnl\|CDD\|224867	COG1956, COG1956, GAF domain-containing protein [Signal transduction mechanisms].	9.79095e-86
NZ_CP015731.1\|WP_047393524.1\|2785763_2786528_+\|MerR-family-transcriptional-regulator	gnl\|CDD\|133381	cd01106, HTH_TipAL-Mta, Helix-Turn-Helix DNA binding domain of the transcription regulators TipAL, Mta, and SkgA. Helix-turn-helix (HTH) TipAL, Mta, and SkgA transcription regulators, and related proteins, N-terminal domain. TipAL regulates resistance to and activation by numerous cyclic thiopeptide antibiotics, such as thiostrepton. Mta is a global transcriptional regulator; the N-terminal DNA-binding domain of Mta interacts directly with the promoters of mta, bmr, blt, and ydfK, and induces transcription of these multidrug-efflux transport genes. SkgA has been shown to control stationary-phase expression of catalase-peroxidase in Caulobacter crescentus. These proteins are comprised of distinct domains that harbor an N-terminal active (DNA-binding) site and a regulatory (effector-binding) site. The conserved N-terminal domain of these transcription regulators contains winged HTH motifs that mediate DNA binding. These proteins share the N-terminal DNA binding domain with other transcription regulators of the MerR superfamily that promote transcription by reconfiguring the spacer between the -35 and -10 promoter elements. Unique to this family, is a TipAL-like, lineage specific Bacilli subgroup, which has five conserved cysteines in the C-terminus of the protein.	1.92888e-34
NZ_CP015731.1\|WP_047393512.1\|2799766_2800960_+\|acetoin-utilization-protein-AcuC	gnl\|CDD\|212520	cd09994, HDAC_AcuC_like, Class I histone deacetylase AcuC (Acetoin utilization protein)-like enzymes. AcuC (Acetoin utilization protein) is a class I deacetylase found only in bacteria and is involved in post-translational control of the acetyl-coenzyme A synthetase (AcsA). Deacetylase AcuC works in coordination with deacetylase SrtN (class III), possibly to maintain AcsA in active (deacetylated) form and let the cell grow under low concentration of acetate. B. subtilis AcuC is a member of operon acuABC; this operon is repressed by the presence of glucose and does not show induction by acetoin; acetoin is a bacterial fermentation product that can be converted to acetate via the butanediol cycle in absence of other carbon sources. Inactivation of AcuC leads to slower growth and lower cell yield under low-acetate conditions in Bacillus subtilis. In general, Class I histone deacetylases (HDACs) are Zn-dependent enzymes that catalyze hydrolysis of N(6)-acetyl-lysine residues in histone amino termini to yield a deacetylated histone (EC 3.5.1.98). Enzymes belonging to this group participate in regulation of a number of processes through protein (mostly different histones) modification (deacetylation). Class I histone deacetylases in general act via the formation of large multiprotein complexes. Members of this class are involved in cell cycle regulation, DNA damage response, embryonic development, cytokine signaling important for immune response and in posttranslational control of the acetyl coenzyme A synthetase.	5.40152e-158
NZ_CP015731.1\|WP_148662037.1\|2784191_2784689_-\|thiol-peroxidase	gnl\|CDD\|179055	PRK00522, tpx, thiol peroxidase.	2.09967e-86

>NZ_CP015731.1|WP_029342350.1|2792337_2793585_-|tyrosine--tRNA-ligase
MTLLEDLEFRGLINQMTDEEGLKTLLETPTTLYTGFDPTADSLHIGHLLPILVLKRFQQAGHHVVGLVGGATGMIGDPSGRATERSLNTSDIVEEFANRIKDQLSRFLPLEGENPVTIANNLDWTKDLTIIDFLRDIGKHFPVSYMLAKDSVDSRLQNGISFTEFSYMLLQSFDFLKLYEDKGCRLQVGGSDQWGNITAGMELIRRAGHEEKAFGLTVPLVTKADGQKFGKTAGGAVWLDADKTSPYEFYQFWFNVDDLDVIKFLKYFTFLTHEELDALAEEVKAAPEKRVAQRRLAEEMTVLVHGEEGLTQAQRITTALFSGDIKSLQVEDIEDAFKGMPRFTLGEATNLVDVLVEAKISPSKRQAREDVTNGAIYLNGEREQDLTKEITEADAIGRFTIVRRGKKKYFVVEHA
>NZ_CP015731.1|WP_023469060.1|2791548_2792076_+|biotin-transporter-BioY
MKTRDLTFIALGAAIIAAVSSLPQIQLVGAVPITLQMLAIMTVSAILGGKRGGLAVLIFLLLAAAGLPVLGGKGGLAPFVGPTVGYLIAFPIAGFFIGLVAEKTRRFVPLFIGMIVFGLGLVYLLGTFGLMAVLDLSFKDAFAINYPFVLWDTIKAVIATTIAVRLLPLRLFRTA
>NZ_CP015731.1|WP_023469059.1|2790795_2791395_+|30S-ribosomal-protein-S4
MARYTGPAWKLSRRLGISLTETGKEIAKRPYAPGQHGNSRRKVSEYGLQLQAKQTLRHMYGVNERQFNRIFNDAGKMPGIHGENFMFLLEARLDNVVYRMGMARTRRAARQLVNHGHIQVDGQRVDIPSFRVKPGQTISVREKSKNFVVIKEALEVAPATKDFVTFDAEKLEGTFVRLPERSELNDQIQEQLVVEYYSR
>NZ_CP015731.1|WP_023469058.1|2790076_2790562_+|GAF-domain-containing-protein
MFETKTYEGDRTKQYDMLSKQLDALLMGEDNQVANLSNASALLNQFLDRINWVGFYLTDTEQNQLVLGPFQGLPACVRIPFGRGVCGTSAAEQTTQRIEDVHQFPGHIACDAASNSEIVIPLVKDGQTIGVLDIDSPEFNRFDEVDQAGLEAFCTTLLRHL
>NZ_CP015731.1|WP_047393521.1|2788146_2789853_-|septation-ring-formation-regulator-EzrA
MWAWVIGVIVIVLLVMLFSMISRKKYYAKIDELDMRKQGIVSASIPKELQDLKQLPMAGETETKFSSWHQAWEELLTVHVAQIDETLYRAEEALDKYRFIAVKNDLEVTEQLIAELEGLIDEMLVEMSTFKTNQSVLAELKAQGEADSGQVRKSLLIQANSFGPALARLEERSEQIDAHWNEMCQYEASGEVTKAYETSLLLEQEVATTRQLVELVPKQWKILAHELRQRIDQLGAGYKEMSLDGYPLEPLGLQSEIKRFEEQRLSLSEKIEMLEVDGLEEAIQQLSADVDQMYDTFRREVDARHQVKKENQFLKQKALRMRERIHQLAQEFSILREKYEISADLGIHYETIQRDEELLFEAAKDLDESIAGKIIPFSMLEDQMRDAIRLEEQLMIQYERFTVELQALRKEETEVRERIVEWRHQLSQTRLRLKRLGLPNLPAEVEEALRNANRSLQTLETRLEELPFNVRSIVAQSQDVQETFKHVQERLDTLVFEVTYAERLVQYANRYRRHDNEIHMSLTIAETKFLAGDYERTIVLAERVLNEYDPAAIERIKRSCAPEETLHV
>NZ_CP015731.1|WP_029342348.1|2786519_2788079_-|amidohydrolase
MGTLYVNGLIRTMAHEEDVHSAMFVEKTRIIAMGEEGKLRRRFGRRIDQIHDLNGKAVYPAFTDAHIHLIGYGEAINRVDASRYTTLEALGQAFLKAEPVNGIHVAEGYDETKLDRAPTKAWLNQLFPDAPALLKRTDRHTALVNDVLFQQLGYKASTVIEGGKVGISDNGEADGFLYDAALEPLYALQAGNLERNKSSLRSAIKNLYQYGIIAAHTEDLSYHGDVADILQAYKEVTQETGFHTHLLVHHLVIDEFVQQQPTLPSTMSIGAMKLFVDGALGGRTALLGRGYSDDPTTRGIEVHTPEQLEQLVKRARSYGFTVAAHVIGDLAIERFVQVLEKYPAPKGKRDRIIHATVVRPETLARIRKLPVLIDVQPVFLLDDADFIVDRLGLNRLDWSYRLRSLAETGALLCGGADAPISDPDVRRSLYAATEGTAGRVNKTNETLSMFEALLLFTKNPHLATETHGRKGLLLPGYDADFVIFEEDFYRLRGEAILNNRLVETVQAGKTVYQAEAALV
>NZ_CP015731.1|WP_047393524.1|2785763_2786528_+|MerR-family-transcriptional-regulator
MYSTQKIAKLTGVTKRTLYHYETIGLLVPKRTDAGHRSYSKEDLLRLQQILLYRSLDFPLSEIRRLLTQPDSNHHTTLKKQIALLQEKASHYQMLAQLAEQTLLTLKGGLPMKDEQLFRGLRHDEIVTHEKQHADEVQKHYGDTDAYRISAKRQQQRTPNEKEQLSTMHKQLDQRLTVLYRDGRMTTDPDVQQVVKDQHDFIDTYYYPCALSLFASLGQMYVSDERFRAYYDAYAPGLSTFYSEAISHYAQTSH
>NZ_CP015731.1|WP_023469054.1|2784854_2785670_+|NAD-kinase
MARNNVYLYYRNTQRHETQVRKLIDVGTRYGLNVVQDHRQANIIVSIGGDGAFLQAARFTGFRDDAIYVGFAEGPNSFYCDFDINDLSAVEAIFKETGNRVSDGEIEVRRYPLLEASINGGPPMLCLNECSVKSSIIKSLAIEVYIDDFLFETFRGDGMVISTPTGSTAYNKSLSGAIVDPLIHCLQVSEIASVNNNRYRTLGSAFLLNRGRKLSLRIIEDGNDYPIIGMDNEALSLTRTDSVDIQLSEKELKTVKLTNNTFWHKIQRSFL
>NZ_CP015731.1|WP_148662037.1|2784191_2784689_-|thiol-peroxidase
MHMATFKGNPITLQGTAVQVGQTAPDFQVLANDLSPVTRDTYQGVRIISVVPSIDTGVCDAQTRKFNEEAATIEGVTVMTISNDLPFAQRRWCASSGLDQVVTLSDHRDLSFGTQYGVAIEELRLLARSVFVLDSNNEITYVEYLEESTDEVNFEAALAAAREAK
>NZ_CP015731.1|WP_047393526.1|2783182_2784091_-|class-I-SAM-dependent-methyltransferase
MEPLEKLYKELTRQTKQIERDLDMPYLEALTTVIDRLNDRHTENVDKEVIRKAVSLAILEGMKQAQPNHLPTPDSVALFAGYLIGKLVGKEDIRLLELGSGTGGMLHAVLSQLSTGTAAEAVEVDETLIRLSAAVTELLDYPVTYTHQDALRPLLLDPVDLAMADLPVGYYPDEEAAASYILKRDEGMSYSHFLLIEQAMQYVKPGGFGVFVIPNGLFQHDTEGKLKQYFESKAHVIGILQLPLTMFKQEQAAKSYLIVRNHLAGMKMPKQALLAELPSFTDARAFGGMVKQIDEWINTELK
>NZ_CP015731.1|WP_047393518.1|2796636_2798340_-|acetate--CoA-ligase
MKVLKALPGKHWLAEYDEANTYDWKDAEQYFSWATTGKVNMAHEAIDRHAEGERANKDALIYFDGTTEQRFTYADMKRLTNKAANVLVDAGVKTGDRIFIFMPRSPELYFALLGALKVGAIVGPLFEAFMEQAVRDRLLDSEAKLLVTTKALLPRVPVGELESLEKVVLVDEDVEESDTLLDFRKAFEQASDVFEPVWLDREDGLILHYTSGSTGKPKGVLHVQNAMIQHLMTGRWVLDLQEDDVYWCTADPGWVTGTSYGIFAPFLNGATNIVVGGRFNPDFWYSVIEKYKVTVWYSAPTAFRMLMGAGADVANHHDLSSLRHVLSVGEPLNPEVIRWGKEAFDQRIHDTWWMTETGAMMICNYKSMDIKPGSMGKPIPGTQAAIIDDQGNELPPFRMGNLALKTPWPSMMRQIWNNPQKYESYFFKGWYVSGDSAYMDDEGYFWFQGRVDDVIMTAGERVGPFEVESRLVEHPAVAEAGVIGKPDPVRGEIIKAFIALRDGYEPTDELKQEIQAFVKEGLAAHAAPREIDFRDKLPKTRSGKIMRRVLKAWELNLETGDLSTMED
>NZ_CP015731.1|WP_023469064.1|2798486_2799119_+|GNAT-family-N-acetyltransferase
MFEKQFNHRTHETSLGPVDIEGPVPSQTLATYTLDSGLTAFRPPAEQHQALVEIADLEEGRIIVARQGTEIIGYVTYLYPDPYETWSEGNNPYILELGAIEVSSRFRGQQIGKKLLEISMLDPAMEHYLILTTEYYWHWDLKGSGLSVWDYRKIMEKMMNHGGLVFFPTDDPEIASHPANCLMARIGKHVSPEVVAHFDALRLRRRFMYD
>NZ_CP015731.1|WP_069940884.1|2799137_2799770_+|CBS-domain-containing-protein
MLIEQIMNTTCITMQPTNSIAHAVELMQRHQIRHILVVNARHELVGLVGLKEIQSASSIFHPDTAKQDLQYPVSSIMIESPVTAHPLDFLEDAAVLFYEYRLTCLPIVRGQRLVGVVTETDLLRTFVQLTGALEPSSQIEIRVENTAGTLAKIAALLAKTNINILNVLVYPTDDPYVRIVAFRVQTMNPIRIIDKLRKEGFDVLGPDVSR
>NZ_CP015731.1|WP_047393512.1|2799766_2800960_+|acetoin-utilization-protein-AcuC
MKDFAYLYSPEEATYRFSETHPFNPIRLELTVSLLEAMHQLDDIPCIAPRHATDEELALIHDQDYIAAVKAAGTGALTPLKAQMYGLGTEDTPLFQGMHSGASLLVGGTIEACDLVLSGQYKRTFHIGGGLHHGFRGRASGFCVYNDTAVAMAAMIEKYHCKILYVDTDAHHGDGVQWAFYNRKDVMTLSLHETGRYLFPGTGMVTERGSEEGYGFSWNVPLDAFTEDDSFLLAYETALFEACELFQPDLIITQNGADAHTLDPLTHLSLTMKSYEQIPQIAVAAANKYTNGKIVALGGGGYDWYRVVPRAWSQVFAAMTGQAPFHGEIPISWQERWSGEETPPPTHWHDPTPLYPAIPRRPEIEEKNWETVKRLIWPFVSDERKRQLTTTSPYSVD
>NZ_CP015731.1|WP_156772517.1|2801065_2801821_+|hypothetical-protein
MKKAWLYSGLILSTGIVLAGCGNEKQAMDHDNMQGSGKPTVEVNVNVPAKTMEEDKVVFKASAVEQKKPVNLEDVTFEVWEAGKQDGAHQKFKATLKKTGSYQAEAKLVEGEYEGLYHINDKKGLHHMDKISFVVMDHSHEKEEASHEHGHDHETVDGLSVHYMGATKAKAGAELPVSFHVFLDGKPLKANVQVEVIETGIEKHTYVPLEKKGDAYSGKVTLTAPGQTTVRLHVENDQLHHHQDELITVAK
>NZ_CP015731.1|WP_023469068.1|2801874_2802885_-|catabolite-control-protein-A
MNSNITIYDVAREAAVSMATVSRVVNGNPNVKPSTRKKVQDAIEQLGYRPNAVARGLASKKTTTVGVIVPDISNIFFADLARGIEDVATMYKYNIILCNSDQNREKEIHLLNTLLGKQVDGIIFMGGRLHEDLVREFKTSPVPIVLAATLNQDYDLPAVNIDYESAAHDAVKSLIDRGHERIGFITGPLEQQINGEKKFAGYRRALEEANLPFNEQNVVLGNYTYDSGMKAMNQLLELGEDCPRAIFAGTDEMALGVIHALQDAGHRVPEDFEVIGHDNTRLATMIRPKLTTVVQPMYDIGAVSMRLLTKILNKEEIETNDVTLPHRIEQRDSTRP
>NZ_CP015731.1|WP_023469069.1|2803043_2804129_-|3-deoxy-7-phosphoheptulonate-synthase
MDQHAELKRLRDELDLVNAELLELMNRRGQIAVEIGKVKRAQGLDRYDPVRERQMLESIAANNHGPFETGRLQHVFKEIFKASLELQGEDRTRKLLVSRKQKPTNTIIRIGDAVIGDGSQQLIAGPCAVESEEQVFEVAEQLAKHGVKFMRGGAYKPRTSPYDFQGLGLEGLKMLKKAADAHGLHVITEIMTPSAVESALPYVDIIQVGARNMQNFDLLKEVGRTNKPVLLKRGLSATLEEFMYAAEYIMASGNDQVILCERGIRTYERATRNTLDISAVPILKQETHLPVMVDVTHSTGRKDLLLPTAKAAYAIGADAVMVEVHPFPALALSDANQQLDFQEFDTFIENLTTTFPALNVQ
>NZ_CP015731.1|WP_029342358.1|2804328_2804865_-|YtxH-domain-containing-protein
MTKQHPYQAQDSSKGGGFLAGIIVGGLIGAAAALLSSPKSGREMRDMIDERTAPARQRLTEQTQVVREKAEPLVGEWIQLAKDKAAPVIEKAKNNPTVQEAAQYAGFEKDQASIDAALAEAEQLVRDIEREIGDEVDGASVAEEIDTETVVELSELREQLADEQDEDNDPQSDVNHKK
>NZ_CP015731.1|WP_029342359.1|2804861_2805431_-|DUF948-domain-containing-protein
MEITLGGIAGLVAAIAFVVLVIFLARVLGAASKTLNNVANTTAGLERQLDGIMMETTALLHKTNRLVDTIEEKTELLAPVANSIEELGTSLNKVTDSVRTVSDTVAGAADTNKEQIAQAVRWGSVAVELFKKNKPAETTVQNHSTATTTVEKKPRRRFRKKAEAPVTPEVVSVPDVESIPDELKGDRKS
>NZ_CP015731.1|WP_029342360.1|2805570_2806683_+|aminopeptidase
MRDPRLTQLATNLINYSVALEPGEKVLIENFGIERELVEALVEAAYAAGGHPFVLLKDNRILRKLYRNASEEQLQLMADIERKQMQAMDAYIGLRAGDNINELSDVPAEQMKLYGQTIGKMHTQDRVKGTKWVVLRFPTASMAQLANQSTEAFEDFYFDVCTLDYEKMGQAMEPLVDLMNRTDRVRLVGPGTDLTFSIKDIPAIKCAGNANIPDGEVFTAPVKDSVNGVISYNTPSPYQGFTFENVKLTFKDGKIVEATANDTDRINQVFDTDAGSRFVGEFAIGVNPFIQHPMKDILFDEKIDGSFHFTPGQAYEEAYNGNDSSVHWDLVNIQRPDYGGGEIWFDDVLIRKDGRFVLPELEVLNPENLK

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_CP015731_1	1.2\|2796385\|18\|NZ_CP015731\|CRISPRCasFinder	2796385-2796402	18	NZ_CP015731.1	2796421-2796438	0	1.0
NZ_CP015731_1	1.2\|2796385\|18\|NZ_CP015731\|CRISPRCasFinder	2796385-2796402	18	NZ_CP015731.1	2796439-2796456	1	0.944
NZ_CP015731_1	1.2\|2796385\|18\|NZ_CP015731\|CRISPRCasFinder	2796385-2796402	18	NZ_CP015731.1	331849-331866	2	0.889

1. spacer 1.2|2796385|18|NZ_CP015731|CRISPRCasFinder matches to position: 2796421-2796438, mismatch: 0, identity: 1.0

gcaaaagccgaagcagag	CRISPR spacer
gcaaaagccgaagcagag	Protospacer
******************

2. spacer 1.2|2796385|18|NZ_CP015731|CRISPRCasFinder matches to position: 2796439-2796456, mismatch: 1, identity: 0.944

gcaaaagccgaagcagag	CRISPR spacer
gcaaaagctgaagcagag	Protospacer
********.*********

3. spacer 1.2|2796385|18|NZ_CP015731|CRISPRCasFinder matches to position: 331849-331866, mismatch: 2, identity: 0.889

gcaaaagccgaagcagag	CRISPR spacer
gctaaagcagaagcagag	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

447401 : 455335

Stx2-converting_phage(16.67%)

tRNA

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_047390798.1\|447401_448637_+	D-alanyl-D-alanine carboxypeptidase	B6DZZ7	Stx2-converting_phage	1.2e-21	29.1
WP_069940133.1\|448918_450196_+\|tRNA	serine--tRNA ligase	A0A1B1IVT2	uncultured_Mediterranean_phage	1.6e-93	44.7
WP_083254760.1\|450685_451246_+	DinB family protein	NA	NA	NA	NA
WP_029343036.1\|451320_451998_-	deoxynucleoside kinase	A0A0M3UL55	Enterococcus_phage	8.7e-22	33.2
WP_050679045.1\|451994_452624_-	AAA family ATPase	M1I7A1	Acanthocystis_turfacea_Chlorella_virus	3.7e-11	30.2
WP_029343038.1\|452732_453239_+	nucleoside deaminase	A0A0N9QQ67	Chrysochromulina_ericina_virus	1.4e-05	31.4
WP_069940135.1\|453649_455335_+	DNA polymerase III subunit gamma/tau	D9ZNI9	Clostridium_phage	5.1e-47	35.3

DBSCAN-SWA_2

1964928 : 1976768

Streptococcus_phage(62.5%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_058266059.1\|1964928_1965198_-	type II toxin-antitoxin system RelE/ParE family toxin	A0A1S5S8E8	Streptococcus_phage	2.5e-20	48.8
WP_026829710.1\|1965194_1965419_-	ribbon-helix-helix protein, CopG family	A0A1X9I609	Streptococcus_phage	1.1e-05	37.0
WP_069940630.1\|1965616_1966708_-	hypothetical protein	NA	NA	NA	NA
WP_083254798.1\|1966829_1967195_-	copper resistance protein CopC	NA	NA	NA	NA
WP_069941043.1\|1967395_1967716_+	winged helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_083254800.1\|1967718_1969257_+	hypothetical protein	E4ZFI9	Streptococcus_phage	3.7e-60	37.6
WP_069940633.1\|1969457_1971587_-	cadmium-translocating P-type ATPase	E4ZFI9	Streptococcus_phage	0.0e+00	97.9
WP_017474136.1\|1971579_1971948_-	helix-turn-helix transcriptional regulator	E4ZFI8	Streptococcus_phage	6.1e-62	97.5
WP_069940634.1\|1972148_1972724_-	recombinase family protein	A0A1V0E035	Clostridioides_phage	3.3e-22	35.4
WP_069940635.1\|1972907_1973627_-	peptidoglycan DD-metalloendopeptidase family protein	A0A2D0ZM66	Rhodococcus_phage	9.2e-14	34.3
WP_034786404.1\|1973856_1974555_+	cytochrome C biogenesis protein CcdA	NA	NA	NA	NA
WP_069940636.1\|1974592_1975399_+	hypothetical protein	NA	NA	NA	NA
WP_069940637.1\|1975451_1976768_+	HAMP domain-containing histidine kinase	W8CYF6	Bacillus_phage	2.4e-28	29.7

DBSCAN-SWA_3

2968283 : 2976898

Moraxella_phage(16.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_069940931.1\|2968283_2969708_-	PDZ domain-containing protein	A0A0R6PIZ1	Moraxella_phage	1.2e-25	31.0
WP_029342493.1\|2969802_2971203_-	M23 family metallopeptidase	W8ED04	Mycobacterium_phage	5.4e-18	43.9
WP_069940932.1\|2971243_2972143_-	ABC transporter permease	NA	NA	NA	NA
WP_029342495.1\|2972132_2972819_-	cell division ATP-binding protein FtsE	G9BWD6	Planktothrix_phage	2.2e-28	34.6
WP_034786307.1\|2973012_2973378_-	cytochrome c	NA	NA	NA	NA
WP_023469242.1\|2973499_2974369_-	YitT family protein	M1Q1P6	Streptococcus_phage	9.4e-29	30.7
WP_069940933.1\|2974466_2974970_-	N-acetyltransferase	A0A1P8CWJ6	Bacillus_phage	8.7e-27	46.3
WP_051656296.1\|2974969_2975737_-	class I SAM-dependent methyltransferase	NA	NA	NA	NA
WP_023469245.1\|2975797_2976898_-	peptide chain release factor 2	A0A0S4KWG0	Pseudomonas_phage	7.0e-05	39.0

Anti-CRISPR protein detection

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