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
NZ_CP053541	Vibrio europaeus strain NPI-1 chromosome 1, complete sequence	0 crisprs	csa3,DinG,DEDDh,PD-DExK,cas3,csx1,RT	0	0	3
NZ_CP053543	Vibrio europaeus strain NPI-1 chromosome 2, complete sequence	0 crisprs	DEDDh,csa3,WYL,cas3	0	0	0
NZ_CP053542	Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence	1 crisprs	NA	1	1	0

Results visualization

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

304541 : 313876

Faustovirus(14.29%)

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_069665543.1\|304541_305756_+	IscS subfamily cysteine desulfurase	A0A0H3TPH2	Faustovirus	4.4e-32	31.1
WP_069665544.1\|305807_306191_+	Fe-S cluster assembly scaffold IscU	A0A218MKD1	uncultured_virus	1.2e-52	77.4
WP_069665545.1\|306258_306582_+	iron-sulfur cluster assembly protein IscA	A0A2H4N7N5	Lake_Baikal_phage	6.8e-25	50.5
WP_171801134.1\|306638_307154_+	co-chaperone HscB	NA	NA	NA	NA
WP_171801135.1\|307173_309027_+	Fe-S protein assembly chaperone HscA	A0A0N9QXN8	Chrysochromulina_ericina_virus	2.6e-108	39.9
WP_004747803.1\|309038_309377_+	ISC system 2Fe-2S type ferredoxin	NA	NA	NA	NA
WP_038197960.1\|309433_309628_+	Fe-S cluster assembly protein IscX	NA	NA	NA	NA
WP_069665549.1\|309779_311078_+	aminopeptidase PepB	Q6GYZ8	Mycoplasma_phage	7.7e-35	34.2
WP_069665550.1\|311135_311561_+	nucleoside-diphosphate kinase	L7Y4C4	Megavirus	2.7e-21	40.6
WP_069665551.1\|311788_313876_+	elongation factor G	E4ZFJ7	Streptococcus_phage	9.1e-62	28.2

DBSCAN-SWA_2

1573587 : 1582563

Mycobacterium_phage(28.57%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_069666495.1\|1573587_1574559_-	class 1b ribonucleoside-diphosphate reductase subunit beta	A0A0M4S3B4	Mycobacterium_phage	3.3e-123	69.1
WP_171801708.1\|1574572_1576705_-	class 1b ribonucleoside-diphosphate reductase subunit alpha	A0A0D3MSW9	Lactococcus_phage	1.9e-203	49.8
WP_171801709.1\|1576697_1577096_-	class Ib ribonucleoside-diphosphate reductase assembly flavoprotein NrdI	A0A142F1R4	Bacillus_phage	1.9e-16	41.6
WP_171801710.1\|1577095_1577317_-	glutaredoxin-like protein NrdH	V5UN81	Mycobacterium_phage	6.9e-13	48.6
WP_069666499.1\|1577503_1577872_+	iron-sulfur cluster assembly accessory protein	A0A0P0CQC4	Ostreococcus_lucimarinus_virus	2.0e-09	32.1
WP_171801711.1\|1577874_1579341_+	Fe-S cluster assembly protein SufB	NA	NA	NA	NA
WP_069666501.1\|1579345_1580092_+	Fe-S cluster assembly ATPase SufC	A0A285PWH2	Cedratvirus	2.9e-10	27.0
WP_171801712.1\|1580066_1581338_+	Fe-S cluster assembly protein SufD	NA	NA	NA	NA
WP_171801713.1\|1581330_1582563_+	SufS family cysteine desulfurase	A0A2K9L2Y3	Tupanvirus	6.7e-73	36.1

DBSCAN-SWA_3

2320465 : 2327041

Staphylococcus_phage(66.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_004415274.1\|2320465_2320936_-	6,7-dimethyl-8-ribityllumazine synthase	A0A2H4PQS3	Staphylococcus_phage	3.7e-32	48.7
WP_004744879.1\|2321144_2322254_-	bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II	A0A2H4PQS2	Staphylococcus_phage	5.2e-64	39.0
WP_171802010.1\|2322319_2322970_-	riboflavin synthase	A0A2H4PQS5	Staphylococcus_phage	1.5e-34	38.1
WP_171802011.1\|2322972_2324079_-	bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD	A0A2H4PQS8	Staphylococcus_phage	1.6e-44	35.6
WP_004744882.1\|2324091_2324541_-	transcriptional regulator NrdR	NA	NA	NA	NA
WP_171802012.1\|2324645_2325896_-	glutamate-5-semialdehyde dehydrogenase	A0A1X9I5D4	Streptococcus_phage	2.9e-100	49.7
WP_004744884.1\|2325907_2327041_-	glutamate 5-kinase	A0A1X9I5D0	Streptococcus_phage	4.2e-61	40.8

Anti-CRISPR protein detection

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

2. NZ_CP053542

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Crispr_ID: NZ_CP053542_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP053542_1

48647-48727

Orphan

Consensus_repeat	Method
GCTGACCGTTAACGTGTCGTCACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP053542_1

>merge|NZ_CP053542|1|48647-48727|CRISPRCasFinder
GCTGACCGTTAACGTGTCGTCACCCTCGCCGCCATCCAGCGAGTTTGACCCGCGTCCGCTGACCGTTAACGTGTCGTTACC

>NZ_CP053542|1|1|48647-48727|CRISPRCasFinder
GCTGACCGTTAACGTGTCGTCACC	CTCGCCGCCATCCAGCGAGTTTGACCCGCGTCC
GCTGACCGTTAACGTGTCGTTACC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP053542.1\|WP_171802435.1\|36090_36423_-\|AzlD-domain-containing-protein	unknown	unknown	gnl\|CDD\|377512
NZ_CP053542.1\|WP_069669699.1\|65742_66018_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_CP053542.1\|WP_171802439.1\|40400_40742_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053542.1\|WP_171802442.1\|43324_43813_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|366048
NZ_CP053542.1\|WP_171802441.1\|41194_42493_-\|DUF521-domain-containing-protein	unknown	unknown	gnl\|CDD\|377349
NZ_CP053542.1\|WP_171802444.1\|47304_47910_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053542.1\|WP_171802443.1\|44193_47292_-\|calcium-binding-protein	unknown	unknown	gnl\|CDD\|225483
NZ_CP053542.1\|WP_171802438.1\|38485_40171_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP053542.1\|WP_171802449.1\|57973_60118_-\|type-I-secretion-system-permease/ATPase	unknown	unknown	gnl\|CDD\|273831
NZ_CP053542.1\|WP_171802437.1\|37205_38483_-\|phosphopyruvate-hydratase	unknown	unknown	gnl\|CDD\|234617
NZ_CP053542.1\|WP_171802446.1\|49362_54084_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|380205
NZ_CP053542.1\|WP_171802436.1\|36419_37121_-\|AzlC-family-ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224215
NZ_CP053542.1\|WP_171802451.1\|61324_62209_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_CP053542.1\|WP_171802450.1\|60535_61207_-\|type-1-glutamine-amidotransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|153235
NZ_CP053542.1\|WP_171802447.1\|54558_56616_-\|type-I-secretion-system-permease/ATPase	unknown	unknown	gnl\|CDD\|273831
NZ_CP053542.1\|WP_069669698.1\|64514_65750_-\|type-II-toxin-antitoxin-system-HipA-family-toxin	unknown	unknown	gnl\|CDD\|377920
NZ_CP053542.1\|WP_171802448.1\|56615_57989_-\|HlyD-family-type-I-secretion-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|130902
NZ_CP053542.1\|WP_171802453.1\|63607_64228_+\|NAD(P)H-binding-protein	unknown	unknown	gnl\|CDD\|187555
NZ_CP053542.1\|WP_171802440.1\|40783_41173_-\|DUF126-domain-containing-protein	unknown	unknown	gnl\|CDD\|224700
NZ_CP053542.1\|WP_171802452.1\|62894_63545_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228

Protein	Function_ID	Function_description	E-value
NZ_CP053542.1\|WP_171802435.1\|36090_36423_-\|AzlD-domain-containing-protein	gnl\|CDD\|377512	pfam05437, AzlD, Branched-chain amino acid transport protein (AzlD). This family consists of a number of bacterial and archaeal branched-chain amino acid transport proteins. AzlD is known to be involved in conferring resistance to 4-azaleucine although its exact role is uncertain.	4.09259e-11
NZ_CP053542.1\|WP_069669699.1\|65742_66018_-\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	0.00208993
NZ_CP053542.1\|WP_171802452.1\|62894_63545_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	3.70964e-12
NZ_CP053542.1\|WP_171802442.1\|43324_43813_-\|hypothetical-protein	gnl\|CDD\|366048	pfam00353, HemolysinCabind, Haemolysin-type calcium-binding repeat (2 copies).	2.62761e-06
NZ_CP053542.1\|WP_171802441.1\|41194_42493_-\|DUF521-domain-containing-protein	gnl\|CDD\|377349	pfam04412, DUF521, Protein of unknown function (DUF521). Family of hypothetical proteins.	2.7806e-101
NZ_CP053542.1\|WP_171802448.1\|56615_57989_-\|HlyD-family-type-I-secretion-periplasmic-adaptor-subunit	gnl\|CDD\|130902	TIGR01843, Hemolysin_secretion_protein_D_plasmid, type I secretion membrane fusion protein, HlyD family. Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking].	2.92429e-115
NZ_CP053542.1\|WP_171802451.1\|61324_62209_+\|LysR-family-transcriptional-regulator	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.	3.86663e-72
NZ_CP053542.1\|WP_171802449.1\|57973_60118_-\|type-I-secretion-system-permease/ATPase	gnl\|CDD\|273831	TIGR01846, type_I_sec_HlyB, type I secretion system ABC transporter, HlyB family. Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking].	0
NZ_CP053542.1\|WP_171802437.1\|37205_38483_-\|phosphopyruvate-hydratase	gnl\|CDD\|234617	PRK00077, eno, enolase; Provisional.	0
NZ_CP053542.1\|WP_171802446.1\|49362_54084_-\|hypothetical-protein	gnl\|CDD\|380205	NF033203, entero_EhxA, enterohemolysin EhxA. Members of this family are the RTX toxin called enterohemolysin or EhxA, because it is found in enterohemorrhagic Escherichia coli (EHEC) strains such as O157:H7.	2.64703e-16
NZ_CP053542.1\|WP_171802436.1\|36419_37121_-\|AzlC-family-ABC-transporter-permease	gnl\|CDD\|224215	COG1296, AzlC, Predicted branched-chain amino acid permease (azaleucine resistance) [Amino acid transport and metabolism].	9.27851e-43
NZ_CP053542.1\|WP_171802450.1\|60535_61207_-\|type-1-glutamine-amidotransferase-domain-containing-protein	gnl\|CDD\|153235	cd03141, GATase1_Hsp31_like, Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein. Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers.	5.28661e-84
NZ_CP053542.1\|WP_171802447.1\|54558_56616_-\|type-I-secretion-system-permease/ATPase	gnl\|CDD\|273831	TIGR01846, type_I_sec_HlyB, type I secretion system ABC transporter, HlyB family. Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking].	0
NZ_CP053542.1\|WP_069669698.1\|64514_65750_-\|type-II-toxin-antitoxin-system-HipA-family-toxin	gnl\|CDD\|377920	pfam07804, HipA_C, HipA-like C-terminal domain. The members of this family are similar to a region close to the C-terminus of the HipA protein expressed by various bacterial species. This protein is known to be involved in high-frequency persistence to the lethal effects of inhibition of either DNA or peptidoglycan synthesis. When expressed alone, it is toxic to bacterial cells, but it is usually tightly associated with HipB, and the HipA-HipB complex may be involved in autoregulation of the hip operon. The hip proteins may be involved in cell division control and may interact with cell division genes or their products.	2.70518e-47
NZ_CP053542.1\|WP_171802443.1\|44193_47292_-\|calcium-binding-protein	gnl\|CDD\|225483	COG2931, COG2931, RTX toxins and related Ca2+-binding proteins [Secondary metabolites biosynthesis, transport, and catabolism].	9.68111e-17
NZ_CP053542.1\|WP_171802453.1\|63607_64228_+\|NAD(P)H-binding-protein	gnl\|CDD\|187555	cd05244, BVR-B_like_SDR_a, biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs. Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	4.01337e-45
NZ_CP053542.1\|WP_171802440.1\|40783_41173_-\|DUF126-domain-containing-protein	gnl\|CDD\|224700	COG1786, COG1786, Swiveling domain associated with predicted aconitase [Energy production and conversion].	4.22729e-26

>NZ_CP053542.1|WP_171802444.1|47304_47910_-|hypothetical-protein
MFQGYEQAIKQASTSQQPSSYDFLLLSIKYRYGFGTKINLTKSTAYLQNMAQSDETSITALKYYFLATNKLCDGFDTQSLTYLKQSAQLGNHSARFLYHYLTYYRSDTTSLEQYVAALMALAKDYDKYAIFELIYLAQTYQLKRPEIEIYQRTFAESTVFATCDLYEFARRGSGVNGLVVGWAEKQQLITRYWPDYVKQCQ
>NZ_CP053542.1|WP_171802443.1|44193_47292_-|calcium-binding-protein
MNKKKMEAVDQMLSHLNHSNKLSQEQKDYIQACQTAASDPSAQNLKAVRDKLQTLKETEAGRSLDALGVLGGAQGLIVAEGTKALLSKARPLHDYYKHDAELADLLDEVRGKDKALRQEFSDLCEQEGRQFDRPPMPEREPIKKLPQSPLTLDLQGDGITTTGLSQPIYFDHNGDGKRTRTGFIDASDGLLALDLDQDGTISSGQELFGNNTLLNNGQRARHGFEALAQYDTNRDRRIDDNDAIFQQLRVFQDLNQDGISQSHELFSLSHFDIQALNLNYVNASDVDNNGNVHRQKSSYVLEGGTQRDLVDVWFKTNNRDLDYVEIAIPEEVTSLPNVNGIGSLPSLHYAMASDKTGRLQGLVETYLNSHEPEAKKLALTEVMFAWAGVAGPYKEQYATTIDPRKVDTLAAFYGRDLPRATGSNQYRFYNDKFQQLMDDIALRLNGTKSEFFEQVRWVRHPENHRWYGDFSSVARTLLDLAQSQTPEAFKSIQGFFSQVRDADDPFATNLKSLYASLLDRVDENASELPVGFDQLLHLSMTDKVMMSESDSMHSDAANDFMLGTSSHDRITTGTGTDAVYAGNGNDQITADYSGTKAIYGQQGDDIITVATPERSGYRFANFNEARRYSHTLSGGQGNDILTGGFGKETYLFNLGDGLDTITDFSLYSGDTDRILMGAGITLSDLSLVKDGQDMKIRIKGANSGDEITIKKAYADTKYSIEEVHLSDGTVIPTRAIPIETEGLSVLEGSNYDDTFRTGDKAVTIKAAGGNDTIVTGRGNDVIDAGFGNDDVVYAGAGNDHIKGAETAYGQEGDDVIESWAGGRLEGGCGDDTLSVSYAAAKASLVGGEGNDTLKVTTPTSRGYRNGNYKNAMRATHVLIGGKGNDHLYGGWGSDQYLYAKGDGWDIITDHDSLSTNKDSLVFGPSLRVEDMFWSRKGDDLSISVGSGPKEQGVTIAQFYQDTSYQIEEFRFDDGTVITNETLADVTSEVSTELLIQTMSAFDDSPGVSTENALLPTQSLALAEIVTTSHLLK
>NZ_CP053542.1|WP_171802442.1|43324_43813_-|hypothetical-protein
MNAGSGNDVVRGGEGNDTLHGGTGNDRLVGGLGAERYEFSRGDGHDTIRDRDVYGTSVDQIVLGEGNHMVLLIGGAESGDSITIENAYTASHFRIEEVVLSDGSKVSPLALPDYVDPVIETNLLVQAMSAFDTQESVANNAVIDGVTSSLSPNVVVSGQSQL
>NZ_CP053542.1|WP_171802441.1|41194_42493_-|DUF521-domain-containing-protein
MQLTDTEQAFLMGEAGRGMQKCMQMLVNFSNAFGASRLVKIASAHVIPNIPLGLLEAYTQEVESVSVMTTLHPHMSALCPSNWQSMGIGADYAYDQLADVKRRAALFAEKGFNQTYTCYPPSVGSLAKKGDFVSWIGSGGQVLVNSTIGARCNRDGALLTLACAITGRAPYHGLFLDENRLAQVHVRFSGVDANSLTKSELSAVGYYLGAQAQTHNIVVEGIERGISMDSLRQLMIPLTVTGAVGVCHVPGSTPEADNVNEALGAQRPIKHIVVDRKVVTQSLATYAPKKRTTEVMPIVLTPKDGAITRALPGSVTDMVVLGCPHLSIQEVRLIAQRLSGKVIPSNRHLWIGLAHQQYQLAKEMGYANTIESAGGLMVSACMSTIPDSPIPKSVSTLMTSSMKAAHYITQLNRGRISVAVADIEQCIDALLH
>NZ_CP053542.1|WP_171802440.1|40783_41173_-|DUF126-domain-containing-protein
MKLSARALNIGHVTADAFVVDQAFSFIGDFDPYTGTLLLPEHTFSGQSLAGKVLVCPNGKGGTMAPFLLYEAHQRGNAPAAILCDHADQILFESAMAINIPILDCFDRDVCSLFLHGQTITIAGNDVTV
>NZ_CP053542.1|WP_171802439.1|40400_40742_+|hypothetical-protein
MNRLSTYVLAIHSSHSQVRVVAQSQKQILTDNGECIEETTTTYTFDNGVKIVCHTELDSFQSEDACPECWIQYQVLESGAAAETISPQKKQFYNRCQETFWLKMQSIHDEPNG
>NZ_CP053542.1|WP_171802438.1|38485_40171_-|hypothetical-protein
MTDELTHSLLDPRGQIKRETFQLALRKDTATLTQGKILFFDNTKLAFCNYNEIFVRLEAMLYEWGCHHIEHVCRSVRGTMTEQIRLLADELASADYAAAVVALADMGTSVMTTILSIELEKRGIPTLLIASPPGNQLAEHVAHYRAGQLCICHLDIYQASTVDDIRQQVDAKHDVVFAALTQEGHTQAAAQLVPKMDADLTTLMGKLMPEQDLDDLMTWYETQSIGDGLPVIPPTPARVEAMTQYSPEPLDTVLIPEAGPSGCDITVRDVVVNSVLAGCEPHYLPIVIATFRAMTDPAFNFQQSITTSYNGGNLVLVSGPIAKELGISSGQGCLGPGYRANATIGRAVNLTILNVCRAYPGKADLGCLGSPVEFTYCFAESLTDSPWPTLNEEHYDPLATSVYLMKAEPPTDVVDFLSQTASSLLDVIIDSATHLGRMNAYIPGRILVVLTPDHAQMLHEAGWDKADLRSHLHRQIYNDRQAVQGKGLVPVRPAHFADLEHIPATRSPQDIDLVVAGGRGGHSAILASWGLYCDAVTVPLTLPNGQFALSIHDFNTSKGNK
>NZ_CP053542.1|WP_171802437.1|37205_38483_-|phosphopyruvate-hydratase
MSRIVDVRAREVFDSRADITLEVEVRLDSDKRGRAMIPSGSSMGKHEAVEVRDHDKARFNGKGVLRAIEIVEHTIKPHLYGMSPFDQMAIDRMLIELDGTLNKSKLGANAILGVSLAVARAAAAQRDCSLCDYLSQGREPAIPQPIFSMLSGGMHGDGNCDFQDYQIIALKATDLEAALQVAKNVHCTLKTMLIERGMCTGVSGTGGFLPTLASNEEGLAVLVEAIKRAGYVPGVDVGLSMDIAAEMFFHEGCYQLAAEQRDLTTVEMIDYLVTLCDRYPITLIEDPLGEDDFDGWVALTQRIGERIELVGDDLFTTNQQRFDLGLNLNMANAILVKPNQIGTLSETIQIVDSANQAGYGIVISRRSGETEDTSIADLAVALGCPKVKFGSLARTESMAKYNQLLRLKDAIAMRQLCEEDEVKVA
>NZ_CP053542.1|WP_171802436.1|36419_37121_-|AzlC-family-ABC-transporter-permease
MSMFKRGCLDATPQLISLLPFAILTGVSAIQAGMTPWTAQLSSVLLMSGASQIAAASLMTTGATPLVVIFTHIAINFRYAIYSAGLAQLKLDVTPAKKVAAAQVLIDQTYALTFLRSQEHMMTPRERTYYYFGTALPMWLTWQCGTAIGILGGSNVPDYWELDFAITLCFISLLVPMVKSHTVVVVTGVSGISAAMTYHWPYNLGFLFSIASGVLAGGGLLKWKSQQAQRETV
>NZ_CP053542.1|WP_171802435.1|36090_36423_-|AzlD-domain-containing-protein
MTQSMIWVVLITSAIATFLLRYSFLWLNGKRPFPDVAAKWLTLIPPAAIIALIVPSLMTSVDSANIEGAPKLVAALLAVVIMGRTRSAGSALVVGMLALWLGQWLMGWHL
>NZ_CP053542.1|WP_171802446.1|49362_54084_-|hypothetical-protein
MTVGYEQYLKDLESYSESGGELYGFEGAFKDFNEVIDLVEERGTQVLSDIANDIGSVGGLSAGAAGIAQALGSVLSQSEDSSDLTDVISKITNSRKFEIPHGMSKVISNNYVGAAAISAYALNEFRENGDANAAAKTIVDSAIAAPVGVATGAIVLPLLTAIAGTVASPFALGAIAGLAAALAGAYVVRELNEQGFLDPLYGATENAIAELFGWQPAPPPHRDPLILDLDGNGVSLTESTYFDHNGNGIANRTQWVSSTDGFLVLDRDGNGTIDSGRELFGDNTLDANGNVASDGYAALKAFDSNGDDVINQKDQVFDQLKVWVDANSDGVSQENELKTLKSLGVESIDLTHDNLHSQYHDASGKSHQTQSVNLDVNNFDRRFVESLAVPESFSSLPDMRGTGTVRDLHEAMTLSGQLSGQIAQFSSSSSRDEQVELSEKILFSWAKTSQYYDEHIPVFSGPEIDKVYAIEAFYGDKVPWAVSFGTNGAALALPTGMINNAYDSLVKMIYFELASQTRLKDYYGALTLSSDESGLSLSLEGALELFSSRTLNPTLIADAMDFMSAMSSASNSDLTGFYTFVSDALYGFTDADIGELQAAMDFNGIALTNAEEITKVTFNDGAITFTEGSTSTEITGGSGADVLSGTSLDDVIHTGSGNDEVHGGVGDDTLHGQDGNDQLFGDQGNDTLTVSGRGSNSLDGGEGDDTLTVSNNTDYRYQRDVLSHARNTLAGGKGNDRLEGHAGAETYLFNRGDGQDTIRDYDHRINSSSDGWNKTDRIVLGEGIRLEELSLRRDGNHMVLVIGGLESGDSITIENAYTDKRYRIEEIELADGSRVAPYSLPLFATAGDDVVQGSGYAEKVELQAGDDVVHAGSGNDEVHGGLGDDTLHGQDGNDQLFGDQGNDTLTVSGRGSNSLDGGEGDDTLTVSNNTDYRYQRDVLSHARNTLAGGKGNDRLEGHAGAETYLFNRGDGQDTIRDYDHRINSSSDGWNKTDRIVLGEGIRLEELSLRRDGNHMVLVIGGLESGDSITIENAYTDKRYRIEEIELADGSRVAPYSLPLFATAGDDVVQGSGYAEKVELQAGDDVVHAGSGNDEVHGGLGDDTLHGQDGNDQLFGDQGNDTLTVSGRGSNSLDGGEGDDTLTVSNNTDYRYQRDVLSHARNTLAGGKGNDRLVGHAGAETYLFNRGDGQDTIRDYDHRINSSSEGWNKTDRIVLGEGIRLEELSLRRDGNHMVLVIGGLESGDSITIENAYTDKRYRIEEIELADGSSVAPYSLPLIATAGDDVVQGSGYAETLDLQAGNDTFHAEGGDDRVQAGLGNDVVHAGSGNDEVHGGLGDDTLHGQDGNDQLFGDQGNDTLTVSGRGSNSLDGGEGDDTLTVSNNTDYRYQRDVLSHARNTLAGGKGNDRLEGHAGAETYLFNRGDGQDTIRDYDHRINSSSDGWNKTDRIVLGEGIRLEELSLRRDGNHMVLVIGGLESGDSITIENAYTDKRYRIEEIELADGSRVAPYSLPLFATAGDDVVQGSGYAEKVVCKRVTMWCMRAQAMTKCMGAWATTRCMARMAMISCLVTKVTTR
>NZ_CP053542.1|WP_171802447.1|54558_56616_-|type-I-secretion-system-permease/ATPase
MDKNVASSPSGLRCLAYIAKHFDKSVELTHLQHKLGESIVELDRLHLCRCAQWMGLKAKYVSVQFEQLVSTPLPAIVELNGRYMVLTACSSTHISLYCTAEQTQVTWEAKRFCDQWSGQLYLLADNALSTSDVKFGFSWFIPSLKKHLRQARQVIWLSLLIQMIALVTPLVFENVIDRVLVSRSVSSLHVLGIALLTMAVFEPLFGYLRSWMYANLASKLNAELSARLYAHLMGLPLRYFNQRQTGQITARVREMDQIRQFLAGSALTLILDLVFVGIFIAVLFAYASFLTWLVLGSLVLYFVFWLAIGPTLRAKVTKEYETAADNTAFLTESISGIETVKTNTLEPSFEKRWQHHLAGQLKAGFRARVVSIWAEQGIGLIQKLTAALTLWWGVKLVLAGELSPGELVAFNMLAGQVTQPILRLAQVWQDFQHTLIALRRVGDILDEPQEAGSGGLASIPSMRGEVTFNQVRFRYDTDAPEVLKNLSLTIQAGEFVGITGRSGSGKSTLTKLLQRLYVPTSGQVLVDGMDLAIADPVELRRNMSVVLQESCLFGGTIADNIRQCAPNASDEALVQAAQLAGAHEFILDLPQGYNAQVGESGSRLSGGQRQRIALARALITNPRILILDEATSALDYESEAAIISRLPEISQGRTVISIAHRLSTLAHCDRVINLSLDGQCQAQHI
>NZ_CP053542.1|WP_171802448.1|56615_57989_-|HlyD-family-type-I-secretion-periplasmic-adaptor-subunit
MFPIIAKVIRAKQGQTHRIRRNAHDYEFLPAYLEIIEKPPSPWSRRIAFTIATFLLLVLIWSIVGRLDIHASAQGKVMVSSHSKVIQALEQGEVVEINVRNGQFVRQGDVLIQLNPAGANAESTRLSEQHVRYQLNKARLLALLLPNPMQSFTPPREATPAQITASQQHLQSEYQETQQMLERLNAERDVNRAELEANQQGIQALNKLKQNIVTRLHARRALMESNAIARVDLLEQEKEWLDVERDISNMQAQQAILKAKASSLVEQRETLLAQKQLEYYDELNQIDGQIAEIEQELIKAKERQRIQALRSPVDGVVQQLAIHTLGGVASPAEPLMVIVPQNADLEAEVNILNKDVGFVMAGQPVEIKIDSFPFTKYGTIPGELLYVSKDAVEDERLGAVFPARIRLERDQILVDDTWVTLGAGMSLNAEIKTGSRRIIEYLLSPLQQYQSEAMRER
>NZ_CP053542.1|WP_171802449.1|57973_60118_-|type-I-secretion-system-permease/ATPase
MVRAYPKRDALSHSAVVSSQVLLKLLGVSCQMPTEHPGDDLKGWLKKASGQTDGQLRLKRLTENTLTASHLPLAYQQHDGEFVVLARLSDDQALIQRHHEQTPQVISRTTLEEAWAGQVIQYHESGRQFDIRWFIPEFIRHRGLLGEILFFSLLLQMLALVLPLFFQVIMDKVLVHNALSTLDVLVVALVVVGLFEVILKGLREYLLAHTTTRIDIRLGTKLFKHLLGLPLLYFKNRHVGAIVTRVRELDSIRNLLTGAALTLLVDVSFTFVFLGVMVYLSAPLTALVSATLPLYALLAWATSEPLKRRIEHQFACGAKNTAFLTESLNGVETVKSLALEPRFERRWEGQTQELVAANFSRQSFQAQVSQCVTLLQKVTSVGVLWLGAQMVMSLELTIGQLIAFNMMVNHVSQPLAKLVELWQQFIQTRVAVDNLSEMLNLPAEQEMGEFQPNAPIQGHIEFQQVWFRYQPQLAPVLHGLSLTIKPGESIGLVGPSGSGKSTVTRLIQKLYLAEKGQVLIDGTPLNQWSAAALRQGIGVVLQENYLFHRTVRENIAIRQPTASFEAVVEAAKLAGAHEFIIKMPKGYDTLLAEGGASLSGGQKQRIAIARALMTQPRILIFDEATSALDEESQSIVNQNMAKIARGRTVITVAHRLSAVQGCDRIAVIEQGEVTELGNHQHLLAQQGCYARLWHIQQNKQVESVGEEVLPCSQS
>NZ_CP053542.1|WP_171802450.1|60535_61207_-|type-1-glutamine-amidotransferase-domain-containing-protein
MKKVLIIVTNHATLGETDQANGTFAPELTHALSELLGAGFDYDIASIKGGQAPLYGTDIEGDAVNAKVLADDDFQNRINNTIPVSQVNGDSYDAIFYPGGFGLLSDLASNEDLAKISAKHYEDGGIVAAVCHGPGALLPITLSNGEKLLTSKSVTGFTREEEIDFGTINDIPFLLEESLARGAARYSKVQPWQELVIVDDRVITGQNPTSAYGVGKAIVDLLA
>NZ_CP053542.1|WP_171802451.1|61324_62209_+|LysR-family-transcriptional-regulator
MESFEGINEFVSVAESGGFSAAAKQLGCSTSHVSRQVTRLEERLGVALLARSTRMVSLTESGQAYYQQCKELVIGLQQANEQLTTQQTQLSGTLRVSAAGAFSENYVAPALMQFAKQHPNLTVEINFNTSMVNFIEDGFDFAIRYGRLSDSGLVARKLVDRPMAAAASQSYIDHYGLPAHPEQLKRHSCIVANKDVWQFQKEGKPLDGVKVQGRWKSNNAYSVVQACEEGLGVAYLPKSSFNDAISSGRLVPILETYWGSGNSSWIVYQNRHFLPLRARLAIDFLLDHFAKWQE
>NZ_CP053542.1|WP_171802452.1|62894_63545_+|TetR/AcrR-family-transcriptional-regulator
MVKTNIRNSLSQKRILQVAVKYADKHGIDSLNMRELAKLLNTGPMSIYHYFSNKEELLDEMVEWVAAKIPKPNPRDPWRKAITDIAIAAHHILMKHAWVNSIWSTQKLGPNKLMFMESILRVLREGGFSVPLACDAYHAIVIHIEGFTLHAVGFPVKAKDAQSVASAFLESVEEPELIPYFIEHVQHHVGQQSCGDQFGATLDMLLDGFEARFNHS
>NZ_CP053542.1|WP_171802453.1|63607_64228_+|NAD(P)H-binding-protein
MKILLLGANGRTGREILDRALLAGDSVTALVRSEDKLADIAHSQLSVHVGDVCDSNDLKKIIVGHDLVISTLGPRLPTKAACTVYSESAKAIVDAMQGCGVNRLLVTSTALLFSTNKWLDRILRFVARHNVRNANLMEETIRSSGLEWTIARVGFLNDKASKDYRQAEGSLPEGGGAISRAALANFLLSEAKQSVHVHSVVGISNK
>NZ_CP053542.1|WP_069669698.1|64514_65750_-|type-II-toxin-antitoxin-system-HipA-family-toxin
MLKAALTVKRTLSTGEKVFVGKLVENSKQSFFQFDEAYLSGHSTSLAPFNLKPDTSLQVAPKEPHYGIHGVFGDSLPDGWGLYLMDRVFRQNGHNPKEVTALERLAYLGDRCMGALSYEPELDLLDESKESIDIITLGRAAIEEFEGTESALLEHLMNTGGSGGARPKMNVTRLANGQYSTLDDALGTKLIVKLTSEKFDLKHSESLVEYCYMQMARNVGIEVPDFHLIDAGHGRFWLEQERFDCTEQGGRIHMISACGLLDAPFREPSLDYVDLVKATRIMCSITESQKLIKRCMFNYLTVNQDDHSKNFSFLASDADNWTLSPFYDIVYSPNPYKEHMTAFGGNGRTPKSAMDQLAAQSGLSSKKAIMVMAEEIFETTRSFSHEAKHLGLSPNLIKEIDKGMVEKFKAL
>NZ_CP053542.1|WP_069669699.1|65742_66018_-|helix-turn-helix-transcriptional-regulator
MLSLYTAYDVQMELKEFIKSARKNDKLSVQKMADLSGVPYATIRKFESTGNISLRQFLMLYETVGDLKKVKELTKSSKPEFKSIEDVLRHA

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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
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542.1	51979-52011	0	1.0
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542.1	49322-49354	1	0.97
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542.1	49972-50004	1	0.97
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542.1	50677-50709	1	0.97
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542.1	51328-51360	1	0.97

1. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to position: 51979-52011, mismatch: 0, identity: 1.0

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagtttgacccgcgtcc	Protospacer
*********************************

2. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to position: 49322-49354, mismatch: 1, identity: 0.97

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagttcgacccgcgtcc	Protospacer
*********************.***********

3. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to position: 49972-50004, mismatch: 1, identity: 0.97

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagttcgacccgcgtcc	Protospacer
*********************.***********

4. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to position: 50677-50709, mismatch: 1, identity: 0.97

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagttcgacccgcgtcc	Protospacer
*********************.***********

5. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to position: 51328-51360, mismatch: 1, identity: 0.97

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagttcgacccgcgtcc	Protospacer
*********************.***********

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542	Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence	48671-48703	0	1.0
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542	Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence	51979-52011	0	1.0
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542	Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence	49322-49354	1	0.97
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542	Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence	49972-50004	1	0.97
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542	Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence	50677-50709	1	0.97
NZ_CP053542_1	1.1\|48671\|33\|NZ_CP053542\|CRISPRCasFinder	48671-48703	33	NZ_CP053542	Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence	51328-51360	1	0.97

1. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to NZ_CP053542 (Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence) position: , mismatch: 0, identity: 1.0

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagtttgacccgcgtcc	Protospacer
*********************************

2. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to NZ_CP053542 (Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence) position: , mismatch: 0, identity: 1.0

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagtttgacccgcgtcc	Protospacer
*********************************

3. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to NZ_CP053542 (Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence) position: , mismatch: 1, identity: 0.97

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagttcgacccgcgtcc	Protospacer
*********************.***********

4. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to NZ_CP053542 (Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence) position: , mismatch: 1, identity: 0.97

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagttcgacccgcgtcc	Protospacer
*********************.***********

5. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to NZ_CP053542 (Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence) position: , mismatch: 1, identity: 0.97

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagttcgacccgcgtcc	Protospacer
*********************.***********

6. spacer 1.1|48671|33|NZ_CP053542|CRISPRCasFinder matches to NZ_CP053542 (Vibrio europaeus strain NPI-1 plasmid pVEu, complete sequence) position: , mismatch: 1, identity: 0.97

ctcgccgccatccagcgagtttgacccgcgtcc	CRISPR spacer
ctcgccgccatccagcgagttcgacccgcgtcc	Protospacer
*********************.***********

Prophage detection

Region	Region Position	Protein_number	Hit_taxonomy	Key_proteins	Att_site	Prophage annotation

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP053541

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NZ_CP053542

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Click the colored protein region to show detailed information

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection