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
NC_014230	Croceibacter atlanticus HTCC2559, complete sequence	1 crisprs	DEDDh,cas3	0	1	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NC_014230_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_014230_1

2812061-2812142

Orphan

Consensus_repeat	Method
GGGATTAGGGATTTGGGATTAGTTG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_014230_1

>merge|NC_014230|1|2812061-2812142|CRISPRCasFinder
GTAAGTGGGGATTGGGGATTAGGGATTTGGGATTAGTTGGTTGTTGGTTGTTGGTTGGGGGTTGGGGATTTGGGATTGGGGA

>NC_014230|1|1|2812061-2812142|CRISPRCasFinder
GTAAGTGGGGATTGGGGATTAGGGA	TTTGGGATTAGTTGGTTGTTGGTTGTTGGTTG
GGGGTTGGGGATTTGGGATTGGGGA

Protein	Signature genes	Signature genes Name	Protein_function
NC_014230.1\|WP_013188335.1\|2811837_2812050_+\|hypothetical-protein	unknown	unknown	unknown
NC_014230.1\|WP_013188341.1\|2816747_2818139_-\|phenylacetate--CoA-ligase-family-protein	unknown	unknown	gnl\|CDD\|224458
NC_014230.1\|WP_013188342.1\|2818132_2819098_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340839
NC_014230.1\|WP_041241034.1\|2819783_2821601_-\|asparagine-synthase-(glutamine-hydrolyzing)	unknown	unknown	gnl\|CDD\|132152
NC_014230.1\|WP_013188327.1\|2803744_2804140_+\|PUR-family-DNA/RNA-binding-protein	unknown	unknown	gnl\|CDD\|378691
NC_014230.1\|WP_013188328.1\|2804223_2806734_+\|zinc-carboxypeptidase	unknown	unknown	gnl\|CDD\|349457
NC_014230.1\|WP_013188332.1\|2809923_2810115_+\|cold-shock-domain-containing-protein	unknown	unknown	gnl\|CDD\|239905
NC_014230.1\|WP_013188326.1\|2801920_2803678_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224055
NC_014230.1\|WP_013188339.1\|2814237_2815539_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379441
NC_014230.1\|WP_013188340.1\|2815593_2816745_-\|glycosyltransferase-family-4-protein	unknown	unknown	gnl\|CDD\|340837
NC_014230.1\|WP_013188345.1\|2821602_2822700_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340839
NC_014230.1\|WP_013188333.1\|2810248_2811001_-\|hypothetical-protein	unknown	unknown	unknown
NC_014230.1\|WP_013188346.1\|2822686_2823859_-\|O-antigen-polymerase-(wzy)	unknown	unknown	unknown
NC_014230.1\|WP_013188331.1\|2808862_2809693_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223669
NC_014230.1\|WP_013188329.1\|2806743_2807178_+\|SRPBCC-domain-containing-protein	unknown	unknown	gnl\|CDD\|176856
NC_014230.1\|WP_013188343.1\|2819274_2819787_-\|acyltransferase	unknown	unknown	gnl\|CDD\|100053
NC_014230.1\|WP_013188330.1\|2807183_2808713_-\|SulP-family-inorganic-anion-transporter	unknown	unknown	gnl\|CDD\|223732
NC_014230.1\|WP_013188338.1\|2813559_2814174_-\|acetyltransferase	unknown	unknown	gnl\|CDD\|100050
NC_014230.1\|WP_041241032.1\|2811630_2811828_+\|hypothetical-protein	unknown	unknown	unknown
NC_014230.1\|WP_013188337.1\|2812228_2813380_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NC_014230.1\|WP_041241034.1\|2819783_2821601_-\|asparagine-synthase-(glutamine-hydrolyzing)	gnl\|CDD\|132152	TIGR03108, eps_aminotran_1, exosortase A system-associated amidotransferase 1. The predicted protein-sorting transpeptidase that we call exosortase (see TIGR02602) has distinct subclasses that associated with different types of exopolysaccharide production loci. This model represents a distinct clade among a set of amidotransferases largely annotated (not necessarily accurately) as glutatime-hydrolyzing asparagine synthases. Members of this clade are essentially restricted to the characteristic exopolysaccharide (EPS) regions that contain the exosortase 1 genome (xrtA), in genomes that also have numbers of PEP-CTERM domain (TIGR02595) proteins.	3.52334e-146
NC_014230.1\|WP_013188341.1\|2816747_2818139_-\|phenylacetate--CoA-ligase-family-protein	gnl\|CDD\|224458	COG1541, PaaK, Coenzyme F390 synthetase [Coenzyme metabolism].	4.18988e-45
NC_014230.1\|WP_013188327.1\|2803744_2804140_+\|PUR-family-DNA/RNA-binding-protein	gnl\|CDD\|378691	pfam11680, DUF3276, Protein of unknown function (DUF3276). This bacterial family of proteins has no known function.	1.39356e-58
NC_014230.1\|WP_013188343.1\|2819274_2819787_-\|acyltransferase	gnl\|CDD\|100053	cd04647, LbH_MAT_like, Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.	2.08932e-32
NC_014230.1\|WP_013188342.1\|2818132_2819098_-\|glycosyltransferase	gnl\|CDD\|340839	cd03811, GT4_GT28_WabH-like, family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.	2.33772e-49
NC_014230.1\|WP_013188326.1\|2801920_2803678_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	1.40614e-167
NC_014230.1\|WP_013188339.1\|2814237_2815539_-\|hypothetical-protein	gnl\|CDD\|379441	pfam14052, Caps_assemb_Wzi, Capsule assembly protein Wzi. Many bacteria are covered in a layer of surface-associated polysaccharide called the capsule. These capsules can be divided into four groups depending upon the organisation of genes responsible for capsule assembly, the assembly pathway and regulation. This family plays a role in group 1 capsule biosynthesis. It is likely to be involved in the later stages of capsule assembly. It is likely to consist of a beta-barrel structure.	1.37123e-18
NC_014230.1\|WP_013188345.1\|2821602_2822700_-\|glycosyltransferase	gnl\|CDD\|340839	cd03811, GT4_GT28_WabH-like, family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.	1.20681e-71
NC_014230.1\|WP_013188331.1\|2808862_2809693_-\|alpha/beta-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	2.0216e-41
NC_014230.1\|WP_013188330.1\|2807183_2808713_-\|SulP-family-inorganic-anion-transporter	gnl\|CDD\|223732	COG0659, SUL1, Sulfate permease and related transporters (MFS superfamily) [Inorganic ion transport and metabolism].	2.209e-126
NC_014230.1\|WP_013188328.1\|2804223_2806734_+\|zinc-carboxypeptidase	gnl\|CDD\|349457	cd06238, M14-like, Peptidase M14-like domain; uncharacterized subgroup. Peptidase M14-like domain of a functionally uncharacterized subgroup of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding carboxypeptidases (CPs) which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Two major subfamilies of the M14 family, defined based on sequence and structural homology, are the A/B and N/E subfamilies. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by an N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. The A forms have slightly different specificities, with Carboxypeptidase A1 (CPA1) preferring aliphatic and small aromatic residues, and CPA2 preferring the bulky aromatic side chains. Enzymes belonging to the N/E subfamily enzymes are not produced as inactive precursors and instead rely on their substrate specificity and subcellular compartmentalization to prevent inappropriate cleavage. They contain an extra C-terminal transthyretin-like domain, thought to be involved in folding or formation of oligomers. MCPs can also be classified based on their involvement in specific physiological processes; the pancreatic MCPs participate only in alimentary digestion and include carboxypeptidase A and B (A/B subfamily), while others, namely regulatory MCPs or the N/E subfamily, are involved in more selective reactions, mainly in non-digestive tissues and fluids, acting on blood coagulation/fibrinolysis, inflammation and local anaphylaxis, pro-hormone and neuropeptide processing, cellular response and others. Another MCP subfamily, is that of succinylglutamate desuccinylase /aspartoacylase, which hydrolyzes N-acetyl-L-aspartate (NAA), and deficiency in which is the established cause of Canavan disease. Another subfamily (referred to as subfamily C) includes an exceptional type of activity in the MCP family, that of dipeptidyl-peptidase activity of gamma-glutamyl-(L)-meso-diaminopimelate peptidase I which is involved in bacterial cell wall metabolism.	2.19715e-103
NC_014230.1\|WP_013188329.1\|2806743_2807178_+\|SRPBCC-domain-containing-protein	gnl\|CDD\|176856	cd07814, SRPBCC_CalC_Aha1-like, Putative hydrophobic ligand-binding SRPBCC domain of Micromonospora echinospora CalC, human Aha1, and related proteins. This family includes the SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of Micromonospora echinospora CalC, human Aha1, and related proteins. Proteins in this group belong to the SRPBCC domain superfamily of proteins, which bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket. MeCalC confers resistance to the enediyne, calicheamicin gamma 1 (CLM), by a self sacrificing mechanism which results in inactivation of both CalC and the highly reactive diradical enediyne species. MeCalC can also inactivate two other enediynes, shishijimicin and namenamicin. A crucial Gly of the MeCalC CLM resistance mechanism is not conserved in this subgroup. This family also includes the C-terminal, Bet v1-like domain of Aha1, one of several co-chaperones, which regulate the dimeric chaperone Hsp90. Aha1 promotes dimerization of the N-terminal domains of Hsp90, and stimulates its low intrinsic ATPase activity, and may regulate the dwell time of Hsp90 with client proteins. Aha1 can act as either a positive or negative regulator of chaperone-dependent activation, depending on the client protein, but the mechanisms by which these opposing functions are achieved are unclear. Aha1 is upregulated in a number of tumor lines co-incident with the activation of several signaling kinases.	2.98144e-22
NC_014230.1\|WP_013188340.1\|2815593_2816745_-\|glycosyltransferase-family-4-protein	gnl\|CDD\|340837	cd03808, GT4_CapM-like, capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.	2.44269e-99
NC_014230.1\|WP_013188332.1\|2809923_2810115_+\|cold-shock-domain-containing-protein	gnl\|CDD\|239905	cd04458, CSP_CDS, Cold-Shock Protein (CSP) contains an S1-like cold-shock domain (CSD) that is found in eukaryotes, prokaryotes, and archaea. CSP's include the major cold-shock proteins CspA and CspB in bacteria and the eukaryotic gene regulatory factor Y-box protein. CSP expression is up-regulated by an abrupt drop in growth temperature. CSP's are also expressed under normal condition at lower level. The function of cold-shock proteins is not fully understood. They preferentially bind poly-pyrimidine region of single-stranded RNA and DNA. CSP's are thought to bind mRNA and regulate ribosomal translation, mRNA degradation, and the rate of transcription termination. The human Y-box protein, which contains a CSD, regulates transcription and translation of genes that contain the Y-box sequence in their promoters. This specific ssDNA-binding properties of CSD are required for the binding of Y-box protein to the promoter's Y-box sequence, thereby regulating transcription.	7.4563e-19
NC_014230.1\|WP_013188338.1\|2813559_2814174_-\|acetyltransferase	gnl\|CDD\|100050	cd03360, LbH_AT_putative, Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.	1.40207e-71

>NC_014230.1|WP_013188335.1|2811837_2812050_+|hypothetical-protein
MATTTDIALRIIDARDLADLTKSSMSTAYTLLKSIRKHYGKESHQLVLNTEAAAYLGIEVRAFERILNGV
>NC_014230.1|WP_041241032.1|2811630_2811828_+|hypothetical-protein
MASKLRLITTHDLCLYKHVKLRAAQKEMVRIKDFHNKLKHQQVTNLDAADYYGIPLSLFESSLDH
>NC_014230.1|WP_013188333.1|2810248_2811001_-|hypothetical-protein
MAKLKSLLKIEGTLDGMTFYKGPDGSYLVKTKSGVSKNRIANDPAFIRTRENGQEFGHVATSGKWFRRAIATLLFDVKDRYKSSRLTQVLAKVKNLDTTSVRGERKVNIGLQTTEGKELLKFFDFNKNAKLNSILRTNYSLDTATSEVQIPEFNPLQHLGVPQGATHVEISAAHLKFNFEDGVGDVVVSNVENLQIENIETSLVFTFPNTPGGTGNDFYFLKVAFFQTINATQYPLNNGVYNAVQLIEIV
>NC_014230.1|WP_013188332.1|2809923_2810115_+|cold-shock-domain-containing-protein
MKNGRVKFFNDTKGFGFITDSETSEEYFVHVSGLIDRISEGDHVAFDLKDGKKGLNAIDVRVV
>NC_014230.1|WP_013188331.1|2808862_2809693_-|alpha/beta-hydrolase
MPYITNKREKETVDIFYEDYGEGQPVILIHGWPLSSKAWEQQRWKIIEEGYRCISYDRRGFGRSSAPWDSYDYSTLASDLAELINQLDLKDAVLVGFSMGGGEVVRYLTDFGSDKIAKAALISSIIPLVKQKDDNPDGVPEEDIQGILDALQSNRVAFLNDFHKNFYNYEDNKDTVKIQNLGYDFNIASSASPRATIQAAIAWADTDFRSELKNVTVPTLIVHGDADNIVPIETAGNQAAKGIKDNTFKVVKDGPHGLNLTHANELNTYLIDFLKS
>NC_014230.1|WP_013188330.1|2807183_2808713_-|SulP-family-inorganic-anion-transporter
MKKIINLFDFSQKVNYKTEILSGLTVAMALVPEAIAFALIAGLSPLTGLYAAFVLGLITSIFGGRPGMISGATGAVAVVIVSLVQSHGVEYVFATVVLAGLIQVLAGVFKLGKLMRLVPHPVIFGFVNGLAIIIFMSQLTQFKDASGDWLTGTSLYVLLGLVLLTMLIIWGLPKLSKAIPAALVAILVVFGLVVVFGLDTRTIGDIASIEGGFPPFHLPAVPFNIETLAIIFPYAAVVAGVGLIESLLTLNIVDEITETRGSGNKEAVAQGAANILSGVFSGMGGCAMIGQSLINISNGARARLSGIVASVMLLIFIMFGAGLIERLPMAALTGLMIMVSIGTFEWASLRTFRRMPKSDIFVMVLVTLVTVFLHNLALAVVIGVIISALVFAWDNAKRIRARKHIANDGTKHYEIYGPLFFGSVQAFNDKFDILNDPEQIVIDFAESRVVDMSAIEALNKITERYQKVGKKVHLKHLSEDCRTLLANAEDLIEVNVLEDPTYKVLTDKV
>NC_014230.1|WP_013188329.1|2806743_2807178_+|SRPBCC-domain-containing-protein
MTTQDPPIITTQEFNIPTEKLWEIITTPKLMRSWFFEQIQDFKAEKGFSTTFLIEHENRRFTHQWTIILVDKPNTIVYQWNYKEHQGDSTVTFNITPTITGCKLTVTAKTLEDFPQDIPEFKRESCIGGWQYFINERLKAYVSQ
>NC_014230.1|WP_013188328.1|2804223_2806734_+|zinc-carboxypeptidase
MRSILLLVLFTSITLQAQKNQLSLDYYLPEDVTYNTAIPTPEDVLGYVPGTWHVSHDKLVSYMKVLAKASDRIHIEQQGLTYEDRPLLLLTITSPENHNRLETIRQDHLALTETASERLNTNELPVVVYQGFSIHGNEPSGSNAALVAAYYLAAAQGPKINELLKHTVILFDPSLNPDGLQRFAYWANTNKSKHINTDPQDREYDEVWPGGRTNHYWFDMNRDWLPVQLPESRARIATFHKWHPNILTDHHEMGSNSSFFFQPGIPSRTHPLTPALNQELTKNIGNYHAKALDNIGSLYYTEEDYDDFYYGKGSTFPDINGSIGILFEQASSRGHAQETDNGVLTFPFTIRNQFTAALSTLDAAVGMRTELLDYQRDFYKTARSKSTKGSYVFGNEKDAASGYHLAEILKRHNIDVYELKENFSKNGKTFKKAHSYVVPKNQRQQRLLEAMFETRTTFQDSLFYDISAWTFPLAFNLDFIEEASTSHLGPKIDSLEMPKGVVTKSNYGYLMQWHHYYAPKALQQLLDKDLRAKVAMKPFSLNGKDYDYGTIFIPVQNQELNSTELFTFLSDVSKKSHLTLTGVPTGLTEGIDLGSRQFKPISKTKVALLVGEGITPYDAGEIWHLFDTRYAMNITKLDVKNFNRYDLSSYTDIILPNSWGRALTPKDAQHLKDWVKDGGTLIGFKNAARFYNSEKFMSLKFKRVEDTASNISFEDRNNYFGAKGIGGAIFEAKQDRSHPINFGYKNTTIPLFRNSTIFIEADKDSYNNPLQYTKSPLLSGYINDKNLDALAETVPFKHNRLGSGHVILFTDNTNFRAFWYGTNKLLMNAIFFGNHM
>NC_014230.1|WP_013188327.1|2803744_2804140_+|PUR-family-DNA/RNA-binding-protein
MSDFGKNDHEDIYSKVLRAGRRTYFFDVRSTKADDYYLTITESKKFTNDDGSFHYKKHKIYLYKEDFDGFRENLEDMTDYIVREKGEEVISERHQSDFKKDYEEDTEVVETTSNSESTVKNFTDVSFDDIA
>NC_014230.1|WP_013188326.1|2801920_2803678_+|ABC-transporter-ATP-binding-protein
MKELQHLNKYFYKYKWQLILGLIITLVAKVFAVLVPRFIGNISNVIEQRINGGFSSDSTYYDALLTNILLVIGVALLSALFTFFMRQTIIVVSRHIEYDLKNEVFRQYQNLSLNFYKKNRTGDLMNRISEDVSKVRMYAGPAYMYSVSTFGMFLVAIPYMIYLSPTLTLYTIIPLPVLSFAIYKLSKAIHKRSTVVQQYLSKLNTFTQESFSGISVIKSYGLEAQTNTGFTTLANDSKEKNINLVKVQAFFFPLMVLLIGVSNILVIYIGGRMLINGTIENFGILVQFLLYVNMLTWPVAVIGWVTSMIQQAEASQKRINEFLVEEPEIKNLNEAPSKITGAIAFKNVSFVYDDTGIEALKNISFKVSPNETLAIIGKTGSGKSTLLELIGRLYDVTSGVLTIDGTDIRQLNLNSLRKSIGYVPQDAFLFSESIKENIKFGKAEATDKEVMQAAKNASVHKNIVGFSNGYDTVLGERGITLSGGQKQRVSIARAIIQDPKILLFDDCLSAVDTETEEAILSNLYDISKDKTTIIVSHRVSSAKNADQIIVLEDGKIQQQGSHSELINKDGYYKELYEKQLSEKEI
>NC_014230.1|WP_013188337.1|2812228_2813380_-|hypothetical-protein
MEIKYIEETTLEDRLKYLPENSNEFWSFYMIAFVNKAYKQNDFEKYFKDYKDIGRFGLEDNKIVQQLFDSVMQRRNVEYFRYYRDDEGASFKFWDVFYEDEKKQAELLKEKSDQLYSYFNFLVMSDVKIKNISFFFYNNSYKNKKSNIDFKNYATPKIGSDFINIDTYQKTFYTVFIDIDKLYYESLLQNKIPNSVEVIEIINKSLDLQELASPIIFIEYPKELVVYKKLIKNWLLMEVEKRKRQFMWEEGYIPMPYLEITKFANRLLDPAERDYLIKDSPEYFQYPKHIFSGYKGYKLFKYYSKGIYNQTMLTFIYRNMRSNEREEYKILADPAPFLEWYNSQREHDNIFQINQPLSKVNSKERQQNYKIIKSLIEELYPTT
>NC_014230.1|WP_013188338.1|2813559_2814174_-|acetyltransferase
MGNQKLNIYGASGHAKVIIDIIKSIDNKTIGYIFDDNEKLIELLGWQIKRSVNTKLLTKHSAIIAIGNNKIRKEIVENKQVQVAEAISHISAIISKLTSIGKGTVIMPNAVINADATIGTHCIINTAAVVEHDVVIENYTHISPNATVTGGVKIGEGTHVGAGAVILPNLNIGKWVTIGAGAVVTKNVPDYSTVIGNPAKPLQK
>NC_014230.1|WP_013188339.1|2814237_2815539_-|hypothetical-protein
MCGTLQSFGQTGEHAVISQIKSFYSNTEELPYWFTHNQRGRISDSTNVLVSTDYKFNYDTATKHNFSGGANVQYVNQAASKFQIDQLYINYSNRWLNATLGAKHPNIKYNGLSSSNGNILWSGNTRAIPGLLLKANTPIKITKAIALNWGIGHYELGNDRYAKGAKIHYKSLGAFIKFNKKSQLQLGIKHYVQWAGDTEAFGKAPSGVSDFIDIFFAKKAGDENAIDGEKVNALGNHLGLYDIKYSYKFKNSKLELYHQHLFEDGSGSAFKNFPDGIWGVNLTNKASWLSSILYEYVYTLNQSGSTGISGRDNYFSNSFYRTGWRYKNRVIGIPFITPNTIENGSGNNRVKAHHIGAKLDFRKLEITIKGSILERLGTYSSPINPKQKSLYSYINGSYLISNKFLMSLSVGVDYNSYKKNVYSIGGALKYNIF
>NC_014230.1|WP_013188340.1|2815593_2816745_-|glycosyltransferase-family-4-protein
MHKLIRITTVPISLEKLLEDQLNFMSDYFEVTAISSDKNRLKKYGENQNVKTFSINLTRKITPVRDLLAVWKLIKFLKKNKPYIVHTHTPKAGIVGMLAAYIARVPHRLHTVAGLPLMEATGIKRKVLNVVEKLTYACATKVYPNSKGLQDVILKENFTKPSKLKIIGNGSSNGIDTTYFDPDRYTKTFKNELKLKLGISETDKVFIFVGRLVSDKGINELITAFNKLQQNHQNIKLLLVGPLESDLDPLHKQTLNIIKSNQHIISLGFQKDVRPWFAISDMLTFPSYREGFPNVVLQASAMGLPCIVTNINGCNEIITDNLNGIIVPKKNTDALADAMIVLIKNPILFNKLRVNARKLIQEKYERKVFWKALLQEYKSLDKQ
>NC_014230.1|WP_013188341.1|2816747_2818139_-|phenylacetate--CoA-ligase-family-protein
MLDKIYDCSPHFIQNLFVSGYNILAYKKRYGGKYKAFRDLYKLNRSLSREDLLRSQKSRYKNFIEQAIANSEFYRKLYSDIENPQDLDNIQRLPIIDKELFRTNINDITIKSRKKLVSSKTGGTTGKSLEVHYKEVNLQERFALLDDFRSRFGYKLGKKTAWFSGKKILTIKDVNEKKFWKYDYFNKTKYYSTFHLKNNFLQYYVENLIKFKPKYLVGFPSTIAEIARYGLDNNYLFPDNTVKAVFPTAENLTKQMRELIEKFFHTAVYNQYASSEGAPFIFECKNGNLHLELQSGVFEVLDECNNPSTTGRLVVTSFTTEGTPLIRYDIGDSITLKNQNLICSCGNNNPIVKSINGRVADYVYSPENGKINIVNIANAIKDVKGIISYQIIQNEINCLNFNIIIDKSIYNNEEEKLFKKNWRDRVGDNMEFNINYVNSINVESSGKHRVVLNNIKDLIEKTV
>NC_014230.1|WP_013188342.1|2818132_2819098_-|glycosyltransferase
MNSNTNLNLISKIFLFPKLVFLYNRFLQQNNIEISLSLLTRPNLLNGLIKLFNKNVKVIISERCYPSIAYSSKSYRLKLYKFLIPKLYNKADVLFSNSYEINKDLNENFGVKLPMNVIYNPVIKKTFKTSHSTEAPSDYTLINVGSLYAIKNQSLLINALANIKFNCKLYFVGNGVDMEKLKFKSKTSNLDSKINFVGKVKNVDDYLLKSDCFILTSNSEGFPNVLLEAMSVGLPVISTNCKSGPLEILNENETIVIKKGEFYLAKYGILININDSIALAKAIEYFYDNKSERDYYAKLAYDRSKDFNLERIYPQLKDILC
>NC_014230.1|WP_013188343.1|2819274_2819787_-|acyltransferase
MIKIINFLKKKILSHENYAKSLGVKIGANCNIQNVSFGSEPYLIEIGNHVQITNGTKIFTHGGAWPLRKKYPDLDFFGKVTLKNNIYVGNNCLIMPGVTIESNVIIASGSVVTKSVKENSIVAGNPAKVIGNLKEFEIKVLPYNLKSKQLDYNSKKKHLLEQNENRFIKK
>NC_014230.1|WP_041241034.1|2819783_2821601_-|asparagine-synthase-(glutamine-hydrolyzing)
MCGIYATNMNFKNSEIQAKLKSIEFRGPDNYEMKTFNKVKLAHLRLSILDLDSRSNQPFSYKNLSISYNGEIYNFNDLKKELANIGYTFYTESDTEVLLIGYYEWGERVLDKLNGMFAFVIYDSIKDTIFCARDRLGVKPFYYKYLDNKFEICSQIQPLLDSNNKLSEIAISVYLDCGYVPSPFSIFENIFKLEPGSKMIIDLTKKAILIDKYWDIKKTETLKISYNDAKNKLHELLVDATRIRMQSDVPLGTFLSGGIDSALVTSIAASISERKVSSYTIGFNEKRFDESSTSTAFAKALKTKHKVKHLVTNDLLDLIPKLIEVYDEPFADSSALPSLLLCKNTKEDVTVALSGDGGDESFMGYRNFDYLSNKIQVNKLPKWCRAAMARLPLDYIFRYNKARLKSLFKSSTDGFTENIFISFKTLQKKDLKTKWFSHYENYKLKSNNPYQKMADLNIKLWLENDSNVKVDRASMAYSMEVRSPFLDYRVIEFARSLPVGYRYYKGNKKKILKDILSEYLPKHLFDLPKKGFGIPLFNWLQGDLKENVLKELNDEFLLRVPNLNVKLFKHQLNQFYQNKIDHSSNIWKLYILALWFKRYYKQEDL
>NC_014230.1|WP_013188345.1|2821602_2822700_-|glycosyltransferase
MKNSKHIAIFVPSFLGGGVEKMMVYLANNFVGKNYTVDYIVINNSGPYKKLLSSQVNIVDLRKKRILNTIFPLTKYLNNNKPDALLTAMNYVNIIAIVSCILSYNKINIIISERAITSLNIIQSRYSFLMKILIKLFYKYPKKIVAISTDVKTDLENNFNVKSKKIKVIYNMVNINKINKVIPDESIRKQLGIKTTNNLLIAIGRLDKYKNFQYLISSLVHLKNLNNTHLILLGDGEEKESLVNQINLLNLNKNVSLLGFVDNPESYLKVSNLFISTSTQEGFGNVIIEAMAAGVPVVVTNCLGGPREILCNGKFGELVPLNKPQILAKAIEKSLSRKKHPDIKKRSKDFSINIISQQYLNFLFQ
>NC_014230.1|WP_013188346.1|2822686_2823859_-|O-antigen-polymerase-(wzy)
MGFINLTIKWNVIKYTLYFLLIPIGYLNASLNWLVILLGPFLLYRIPKSLKVFRLEKNFLIALLFFLSIVIFSGIISIDPLYPVKNALNIISIILACYFVALRLKTKSELFDFLNSIFYTCVVFASILYFISFDGFTFNFIESDSFGKNSSAVILFIGLVVNLLRDQLIKSHLISIVFTLYFYVSIFFTASIKSIVVSTILILSFYVLKSSISLKKIFLNSFFTVLFIIVCIYFLKDTEYLNNYSVLRITSRLSVLFGGSSEIGYIDSEYMTGYRSYLISKGLSIFYENPIIGIGLENTRAYLGTYTHNNFVEILAGTGILGFGFFLYAILTIFWSTLKIYNIQLKVILIISLFCFMLIANAQRIYDNRFLMIFMFSFISIQNVINNEKQ

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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
NC_014230_1	1.1\|2812086\|32\|NC_014230\|CRISPRCasFinder	2812086-2812117	32	AP014482	Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S24-C109, * SEQUENCING IN PROGRESS *, 2 ordered pieces	6659-6690	11	0.656
NC_014230_1	1.1\|2812086\|32\|NC_014230\|CRISPRCasFinder	2812086-2812117	32	AP014054	Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S33-C14, * SEQUENCING IN PROGRESS *	20031-20062	11	0.656
NC_014230_1	1.1\|2812086\|32\|NC_014230\|CRISPRCasFinder	2812086-2812117	32	AP014055	Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S41-C174, * SEQUENCING IN PROGRESS *	9721-9752	11	0.656
NC_014230_1	1.1\|2812086\|32\|NC_014230\|CRISPRCasFinder	2812086-2812117	32	AP014483	Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S39-C115, * SEQUENCING IN PROGRESS *, 2 ordered pieces	6538-6569	11	0.656
NC_014230_1	1.1\|2812086\|32\|NC_014230\|CRISPRCasFinder	2812086-2812117	32	AP014052	Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S27-C13, * SEQUENCING IN PROGRESS *	19629-19660	11	0.656
NC_014230_1	1.1\|2812086\|32\|NC_014230\|CRISPRCasFinder	2812086-2812117	32	AP014053	Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S29-C16, * SEQUENCING IN PROGRESS *	20044-20075	11	0.656
NC_014230_1	1.1\|2812086\|32\|NC_014230\|CRISPRCasFinder	2812086-2812117	32	AP014058	Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S42-C22, * SEQUENCING IN PROGRESS *	19621-19652	11	0.656
NC_014230_1	1.1\|2812086\|32\|NC_014230\|CRISPRCasFinder	2812086-2812117	32	AP014060	Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S45-C20, * SEQUENCING IN PROGRESS *	20031-20062	11	0.656

1. spacer 1.1|2812086|32|NC_014230|CRISPRCasFinder matches to AP014482 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S24-C109, *** SEQUENCING IN PROGRESS ***, 2 ordered pieces) position: , mismatch: 11, identity: 0.656

tttgggattagttggttgttggttgttggttg	CRISPR spacer
ccattagttagttggttgttgtttgtaggtat	Protospacer
..   ..************** **** ***

2. spacer 1.1|2812086|32|NC_014230|CRISPRCasFinder matches to AP014054 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S33-C14, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 11, identity: 0.656

tttgggattagttggttgttggttgttggttg	CRISPR spacer
ccattagttagttggttgttgtttgtaggtat	Protospacer
..   ..************** **** ***

3. spacer 1.1|2812086|32|NC_014230|CRISPRCasFinder matches to AP014055 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S41-C174, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 11, identity: 0.656

tttgggattagttggttgttggttgttggttg	CRISPR spacer
ccattagttagttggttgttgtttgtaggtat	Protospacer
..   ..************** **** ***

4. spacer 1.1|2812086|32|NC_014230|CRISPRCasFinder matches to AP014483 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S39-C115, *** SEQUENCING IN PROGRESS ***, 2 ordered pieces) position: , mismatch: 11, identity: 0.656

tttgggattagttggttgttggttgttggttg	CRISPR spacer
ccattagttagttggttgttgtttgtaggtat	Protospacer
..   ..************** **** ***

5. spacer 1.1|2812086|32|NC_014230|CRISPRCasFinder matches to AP014052 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S27-C13, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 11, identity: 0.656

tttgggattagttggttgttggttgttggttg	CRISPR spacer
ccattagttagttggttgttgtttgtaggtat	Protospacer
..   ..************** **** ***

6. spacer 1.1|2812086|32|NC_014230|CRISPRCasFinder matches to AP014053 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S29-C16, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 11, identity: 0.656

tttgggattagttggttgttggttgttggttg	CRISPR spacer
ccattagttagttggttgttgtttgtaggtat	Protospacer
..   ..************** **** ***

7. spacer 1.1|2812086|32|NC_014230|CRISPRCasFinder matches to AP014058 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S42-C22, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 11, identity: 0.656

tttgggattagttggttgttggttgttggttg	CRISPR spacer
ccattagttagttggttgttgtttgtaggtat	Protospacer
..   ..************** **** ***

8. spacer 1.1|2812086|32|NC_014230|CRISPRCasFinder matches to AP014060 (Uncultured Mediterranean phage uvMED isolate uvMED-GF-C12B-MedDCM-OCT-S45-C20, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 11, identity: 0.656

tttgggattagttggttgttggttgttggttg	CRISPR spacer
ccattagttagttggttgttgtttgtaggtat	Protospacer
..   ..************** **** ***

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

720662 : 729359

Prochlorococcus_phage(16.67%)

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_013186395.1\|720662_720896_-	acyl carrier protein	M4QDG5	Prochlorococcus_phage	3.0e-06	51.7
WP_041240887.1\|721046_721655_+	phosphoribosylglycinamide formyltransferase	M4QRX9	Synechococcus_phage	1.4e-15	31.7
WP_013186397.1\|721644_722283_+	ribonuclease H family protein	H8ZJH4	Ostreococcus_tauri_virus	1.8e-05	50.0
WP_013186398.1\|722369_723293_+	bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase	NA	NA	NA	NA
WP_013186399.1\|723347_725246_+	hypothetical protein	A0A0M3SGR2	Mollivirus	2.2e-14	25.0
WP_013186400.1\|725474_726083_-	superoxide dismutase	Q56AR7	Bacillus_thuringiensis_phage	5.5e-60	56.7
WP_013186401.1\|726194_729359_+	UvrD-helicase domain-containing protein	A0A068EQC7	Bacillus_phage	1.3e-14	27.7

DBSCAN-SWA_2

2829639 : 2840333

Escherichia_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_013188354.1\|2829639_2830650_-	UDP-N-acetylglucosamine 4,6-dehydratase (inverting)	A0A1V0SAI8	Catovirus	4.0e-39	35.3
WP_148232823.1\|2830656_2832114_-	oligosaccharide flippase family protein	NA	NA	NA	NA
WP_013188356.1\|2832220_2833522_-	nucleotide sugar dehydrogenase	M1H5A7	Paramecium_bursaria_Chlorella_virus	9.8e-22	26.2
WP_013188357.1\|2833524_2834532_-	SDR family oxidoreductase	A0A2K9L0I7	Tupanvirus	6.1e-88	49.8
WP_013188358.1\|2834531_2835749_-	UDP-N-acetyl-D-mannosamine dehydrogenase	M1H4V0	Acanthocystis_turfacea_Chlorella_virus	4.2e-19	25.2
WP_013188359.1\|2835745_2836873_-	UDP-N-acetylglucosamine 2-epimerase (non-hydrolyzing)	A0A1V0SAG5	Catovirus	1.3e-30	30.6
WP_013188360.1\|2836874_2837735_-	glucose-1-phosphate thymidylyltransferase RfbA	I7I009	Enterobacteria_phage	2.2e-94	60.8
WP_013188361.1\|2837856_2838723_-	dTDP-4-dehydrorhamnose reductase	A0A291LA50	Escherichia_phage	1.7e-38	36.1
WP_013188362.1\|2838722_2839271_-	dTDP-4-dehydrorhamnose 3,5-epimerase	A0A1D7XFA9	Escherichia_phage	8.2e-31	43.3
WP_013188363.1\|2839280_2840333_-	dTDP-glucose 4,6-dehydratase	A0A1D7XFE8	Escherichia_phage	4.9e-88	52.4

Anti-CRISPR protein detection

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