CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Prophage number
NC_014333	Bacillus cereus biovar anthracis str. CI plasmid pBAslCI14, complete sequence	0 crisprs	NA	0
NC_014331	Bacillus cereus biovar anthracis str. CI plasmid pCI-XO1, complete sequence	0 crisprs	RT,c2c4_V-U1,csa3	12
NC_014335	Bacillus cereus biovar anthracis str. CI, complete sequence	1 crisprs	cas3,csa3,WYL,c2c9_V-U4,cas14k,DinG,DEDDh,PD-DExK,RT	4
NC_014332	Bacillus cereus biovar anthracis str. CI plasmid pCI-XO2, complete sequence	0 crisprs	NA	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

0 : 1814

Clostridioides_phage(100.0%)

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_000453400.1\|1175_1814_-	NERD domain-containing protein	A0A2R2ZH57	Clostridioides_phage	5.3e-21	34.0

DBSCAN-SWA_2

6727 : 8536

Pseudomonas_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_001099011.1\|6727_8536_-	group II intron reverse transcriptase/maturase	A0A0U4J920	Pseudomonas_phage	4.3e-92	38.8

DBSCAN-SWA_3

25251 : 33135

Bacillus_phage(33.33%)

integrase

attL 21002:21018|attR 41261:41277

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
21002:21018	attL	NA	NA	NA	NA
WP_001006036.1\|25251_26199_+\|integrase	site-specific integrase	A0A1B1P793	Bacillus_phage	7.8e-37	31.0
WP_001118290.1\|26793_28290_+	hypothetical protein	A0A0H3UZK2	Geobacillus_virus	1.7e-118	46.6
WP_002194490.1\|28770_30144_-	hypothetical protein	NA	NA	NA	NA
WP_002194491.1\|30215_30521_-	hypothetical protein	NA	NA	NA	NA
WP_000401613.1\|30614_31058_-	HEPN domain-containing protein	NA	NA	NA	NA
WP_001014144.1\|31203_33135_-	group II intron reverse transcriptase/maturase	A0A0U4J920	Pseudomonas_phage	2.8e-33	28.2
41261:41277	attR	NA	NA	NA	NA

DBSCAN-SWA_4

99566 : 99854

Bacillus_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000678363.1\|99566_99854_+	hypothetical protein	A0A1B1P7B4	Bacillus_phage	1.4e-34	72.6

DBSCAN-SWA_5

112814 : 115060

Bacillus_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000702222.1\|112814_113702_+	UTP--glucose-1-phosphate uridylyltransferase GalU	A0A127AW70	Bacillus_phage	9.1e-80	53.3
WP_001027043.1\|113728_115060_+	UDP-glucose/GDP-mannose dehydrogenase family protein	A0A127AXI2	Bacillus_phage	1.6e-88	41.3

DBSCAN-SWA_6

136496 : 137078

Aeromonas_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000639133.1\|136496_137078_+	recombinase family protein	A0A219Y9V9	Aeromonas_phage	1.2e-27	39.1

DBSCAN-SWA_7

144033 : 146328

Clostridioides_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000746484.1\|144033_146328_+	anthrax toxin protective antigen	A0A1V0E026	Clostridioides_phage	1.8e-74	33.5

DBSCAN-SWA_8

155509 : 156553

Bacillus_phage(100.0%)

integrase

attL 147856:147870|attR 158454:158468

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
147856:147870	attL	NA	NA	NA	NA
WP_001021546.1\|155509_156553_-\|integrase	tyrosine-type recombinase/integrase	A0A0E3T6D9	Bacillus_phage	2.9e-08	24.0
WP_001021546.1\|155509_156553_-\|integrase	tyrosine-type recombinase/integrase	A0A0E3T6D9	Bacillus_phage	2.9e-08	24.0
158454:158468	attR	NA	NA	NA	NA

DBSCAN-SWA_9

160522 : 163492

uncultured_Caudovirales_phage(50.0%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000107154.1\|160522_161743_+	WXG100 family type VII secretion target	A0A2H4J389	uncultured_Caudovirales_phage	8.2e-63	57.5
WP_000073366.1\|161755_162205_+	SMI1/KNR4 family protein	NA	NA	NA	NA
WP_087943629.1\|162326_163492_-\|transposase	IS3 family transposase	A0A1B1P773	Bacillus_phage	4.5e-42	40.6

DBSCAN-SWA_10

168221 : 169307

Brevibacillus_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000070475.1\|168221_169307_+	tyrosine recombinase XerS	A0A0K2CP59	Brevibacillus_phage	2.1e-09	28.8

DBSCAN-SWA_11

172538 : 173633

uncultured_Caudovirales_phage(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000637338.1\|172538_173633_+	tetratricopeptide repeat protein	A0A2H4J8G3	uncultured_Caudovirales_phage	2.5e-95	49.6

DBSCAN-SWA_12

176989 : 179653

Klosneuvirus(100.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000520728.1\|176989_179653_-	type IA DNA topoisomerase	A0A1V0SIB2	Klosneuvirus	2.2e-12	20.7

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. NC_014335

Click the left colored region to show detailed information

CRISPR-Cas detection and classification

Crispr_ID: NC_014335_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NC_014335_1

1171230-1171338

Orphan

Consensus_repeat	Method
TGTATGATTACCTTCCGCATGAGAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NC_014335_1

>merge|NC_014335|1|1171230-1171338|CRISPRCasFinder
TGTATGATTACCTTCCGCATGAGAAGAGAATCCGTTAGCGATAGTCGCAGTTCCTTCTGCATGTGCTGCTTCGCCTAAAGCGATTGTATGTTTACCTTCCGCATGAGAA

>NC_014335|1|1|1171230-1171338|CRISPRCasFinder
TGTATGATTACCTTCCGCATGAGAA	GAGAATCCGTTAGCGATAGTCGCAGTTCCTTCTGCATGTGCTGCTTCGCCTAAAGCGAT
TGTATGTTTACCTTCCGCATGAGAA

Protein	Signature genes	Signature genes Name	Protein_function
NC_014335.1\|WP_001292832.1\|1175143_1175896_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|379312
NC_014335.1\|WP_001079111.1\|1169639_1170533_+\|RluA-family-pseudouridine-synthase	unknown	unknown	gnl\|CDD\|223638
NC_014335.1\|WP_000872687.1\|1172110_1172851_-\|bis(5'-nucleosyl)-tetraphosphatase-PrpE	unknown	unknown	gnl\|CDD\|184187
NC_014335.1\|WP_000654694.1\|1172925_1174086_-\|rod-shape-determining-protein-RodA	unknown	unknown	gnl\|CDD\|274033
NC_014335.1\|WP_000191105.1\|1167042_1167621_-\|CYTH-domain-containing-protein	unknown	unknown	gnl\|CDD\|143627
NC_014335.1\|WP_001081482.1\|1168169_1168808_+\|GTP-pyrophosphokinase-family-protein	unknown	unknown	gnl\|CDD\|225232
NC_014335.1\|WP_000043381.1\|1166463_1166862_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|381281
NC_014335.1\|WP_000069703.1\|1177078_1177678_-\|exosporium-leader-peptide-containing-protein	unknown	unknown	gnl\|CDD\|375999
NC_014335.1\|WP_000360638.1\|1165570_1166464_-\|DsbA-family-protein	unknown	unknown	gnl\|CDD\|372699
NC_014335.1\|WP_000754593.1\|1165167_1165341_-\|hypothetical-protein	unknown	unknown	unknown
NC_014335.1\|WP_000651527.1\|1180538_1181219_+\|streptomycin-biosynthesis-protein-StrF	unknown	unknown	gnl\|CDD\|379345
NC_014335.1\|WP_001271183.1\|1179837_1180524_+\|streptomycin-biosynthesis-protein-StrF	unknown	unknown	gnl\|CDD\|379345
NC_014335.1\|WP_002157369.1\|1174203_1175130_-\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|366154
NC_014335.1\|WP_000932920.1\|1177843_1178941_+\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|133005
NC_014335.1\|WP_001078427.1\|1179151_1179841_+\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|369778
NC_014335.1\|WP_000003400.1\|1163221_1165048_+\|oligoendopeptidase-F	unknown	unknown	gnl\|CDD\|341071
NC_014335.1\|WP_000444380.1\|1176110_1176956_-\|class-I-SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|377550
NC_014335.1\|WP_000673194.1\|1168826_1169624_+\|NAD-kinase	unknown	unknown	gnl\|CDD\|235317
NC_014335.1\|WP_001180009.1\|1167767_1168139_+\|hypothetical-protein	unknown	unknown	unknown
NC_014335.1\|WP_000612269.1\|1161926_1163171_+\|competence-protein	unknown	unknown	gnl\|CDD\|226875

Protein	Function_ID	Function_description	E-value
NC_014335.1\|WP_001292832.1\|1175143_1175896_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|379312	pfam13649, Methyltransf_25, Methyltransferase domain. This family appears to be a methyltransferase domain.	7.79414e-19
NC_014335.1\|WP_001079111.1\|1169639_1170533_+\|RluA-family-pseudouridine-synthase	gnl\|CDD\|223638	COG0564, RluA, Pseudouridylate synthases, 23S RNA-specific [Translation, ribosomal structure and biogenesis].	1.51034e-100
NC_014335.1\|WP_000872687.1\|1172110_1172851_-\|bis(5'-nucleosyl)-tetraphosphatase-PrpE	gnl\|CDD\|184187	PRK13625, PRK13625, bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional.	0
NC_014335.1\|WP_000932920.1\|1177843_1178941_+\|glycosyltransferase-family-2-protein	gnl\|CDD\|133005	cd02511, Beta4Glucosyltransferase, UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide. UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.	9.08688e-55
NC_014335.1\|WP_000191105.1\|1167042_1167621_-\|CYTH-domain-containing-protein	gnl\|CDD\|143627	cd07762, CYTH-like_Pase_1, Uncharacterized subgroup 1 of the CYTH-like superfamily. Enzymes belonging to the CYTH-like (also known as triphosphate tunnel metalloenzyme (TTM)-like) superfamily hydrolyze triphosphate-containing substrates, require metal cations as cofactors, and have a unique active site located at the center of an eight-stranded antiparallel beta barrel tunnel (the triphosphate tunnel). The name CYTH originated from the gene designation for bacterial class IV adenylyl cyclases (CyaB) and from thiamine triphosphatase. Class IV adenylate cyclases catalyze the conversion of ATP to 3',5'-cyclic AMP (cAMP) and PPi. Thiamine triphosphatase is a soluble cytosolic enzyme which converts thiamine triphosphate to thiamine diphosphate. This domain superfamily also contains RNA triphosphatases, membrane-associated polyphosphate polymerases, tripolyphosphatases, nucleoside triphosphatases, nucleoside tetraphosphatases and other proteins with unknown functions. Proteins of this subgroup are of bacterial origin and have not been characterized.	1.94434e-83
NC_014335.1\|WP_001081482.1\|1168169_1168808_+\|GTP-pyrophosphokinase-family-protein	gnl\|CDD\|225232	COG2357, COG2357, PpGpp synthetase catalytic domain [General function prediction only].	1.66713e-95
NC_014335.1\|WP_002157369.1\|1174203_1175130_-\|glycosyltransferase-family-2-protein	gnl\|CDD\|366154	pfam00535, Glycos_transf_2, Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.	1.08223e-25
NC_014335.1\|WP_000069703.1\|1177078_1177678_-\|exosporium-leader-peptide-containing-protein	gnl\|CDD\|375999	pfam18573, BclA_C, BclA C-terminal domain. This is the C-terminal domain of BclA (Bacillus collagen-like protein of anthracis) which is expressed on spores of Bacillus species. Trimers of the C-terminal domain (CTD) form the tips of the spore's hair-like nap and are the immunodominant target of vertebrate antibodies and drive trimerization. Structure analysis indicate the C-terminal region of the peptide folding into an all-beta structure with a jelly-fold topology, similar to the first human complement C1q, a member of the tumor necrosis factor (TNF)-like family. The C-terminal globular domain has been shown to be located on the exterior of the exosporium, and therefore is critical in determining the immunogenicity of the spore in a mammalian host.	1.79217e-21
NC_014335.1\|WP_000360638.1\|1165570_1166464_-\|DsbA-family-protein	gnl\|CDD\|372699	pfam13743, Thioredoxin_5, Thioredoxin.	5.36453e-93
NC_014335.1\|WP_000654694.1\|1172925_1174086_-\|rod-shape-determining-protein-RodA	gnl\|CDD\|274033	TIGR02210, Rod_shape-determining_protein_RodA, rod shape-determining protein RodA. This protein is a member of the FtsW/RodA/SpoVE family (pfam01098). It is found only in species with rod (or spiral) shapes. In many species, mutation of rodA has been shown to correlate with loss of the normal rod shape. Note that RodA homologs are found, scoring below the cutoffs for this model, in a number of both rod-shaped and coccoid bacteria, including four proteins in Bacillus anthracis, for example. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division].	1.52707e-99
NC_014335.1\|WP_001271183.1\|1179837_1180524_+\|streptomycin-biosynthesis-protein-StrF	gnl\|CDD\|379345	pfam13712, Glyco_tranf_2_5, Glycosyltransferase like family. Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.	4.25249e-108
NC_014335.1\|WP_000043381.1\|1166463_1166862_-\|hypothetical-protein	gnl\|CDD\|381281	cd14772, TrHb2_Bs-trHb-like_O, Truncated hemoglobins, group 2 (O); Bacillus subtilis TrHb like. The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. TrHbs are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb2's belonging to this group include monomeric Bacillus subtilis trHb (Bs-trHb), which exhibits an extremely high oxygen affinity, and a dimeric TrHb2 from the thermophilic aerobic spore forming bacterium Geobacillus stearothermophilus(Gs-trHb).	1.17037e-69
NC_014335.1\|WP_001078427.1\|1179151_1179841_+\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|369778	pfam08242, Methyltransf_12, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	3.57676e-18
NC_014335.1\|WP_000003400.1\|1163221_1165048_+\|oligoendopeptidase-F	gnl\|CDD\|341071	cd09608, M3B_PepF, Peptidase family M3B, oligopeptidase F (PepF). Peptidase family M3B oligopeptidase F (PepF; Pz-peptidase B; EC 3.4.24.-) is mostly bacterial and includes oligoendopeptidase F from Lactococcus lactis. This enzyme hydrolyzes peptides containing between 7 and 17 amino acids with fairly broad specificity. The PepF gene is duplicated in L. lactis on the plasmid that bears it, while a shortened second copy is found in Bacillus subtilis. Most bacterial PepFs are cytoplasmic endopeptidases; however, the Bacillus amyloliquefaciens PepF oligopeptidase is a secreted protein and may facilitate the process of sporulation. Specifically, the yjbG gene encoding the homolog of the PepF1 and PepF2 oligoendopeptidases of Lactococcus lactis has been identified in Bacillus subtilis as an inhibitor of sporulation initiation when over-expressed from a multicopy plasmid. This PepF family includes Streptococcus agalactiae PepB, a group B streptococcal oligopeptidase which has been shown to degrade a variety of bioactive peptides as well as the synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly- Pro-Ala in vitro.	0
NC_014335.1\|WP_000444380.1\|1176110_1176956_-\|class-I-SAM-dependent-methyltransferase	gnl\|CDD\|377550	pfam05711, TylF, Macrocin-O-methyltransferase (TylF). This family consists of bacterial macrocin O-methyltransferase (TylF) proteins. TylF is responsible for the methylation of macrocin to produce tylosin. Tylosin is a macrolide antibiotic used in veterinary medicine to treat infections caused by Gram-positive bacteria and as an animal growth promoter in the swine industry. It is produced by several Streptomyces species. As with other macrolides, the antibiotic activity of tylosin is due to the inhibition of protein biosynthesis by a mechanism that involves the binding of tylosin to the ribosome, preventing the formation of the mRNA-aminoacyl-tRNA-ribosome complex. The structure of one representative sequence from this family, NovP, shows it to be an S-adenosyl-l-methionine-dependent O-methyltransferase that catalyzes the penultimate step in the biosynthesis of the aminocoumarin antibiotic novobiocin. Specifically, it methylates at 4-OH of the noviose moiety, and the resultant methoxy group is important for the potency of the mature antibiotic. It is likely that the key structural features of NovP are common to the rest of the family and include: a helical 'lid' region that gates access to the co-substrate binding pocket and an active centre that contains a 3-Asp putative metal binding site. A further conserved Asp probably acts as the general base that initiates the reaction by de-protonating the 4-OH group of the noviose unit.	1.59865e-154
NC_014335.1\|WP_000673194.1\|1168826_1169624_+\|NAD-kinase	gnl\|CDD\|235317	PRK04885, ppnK, inorganic polyphosphate/ATP-NAD kinase; Provisional.	0
NC_014335.1\|WP_000651527.1\|1180538_1181219_+\|streptomycin-biosynthesis-protein-StrF	gnl\|CDD\|379345	pfam13712, Glyco_tranf_2_5, Glycosyltransferase like family. Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.	7.1131e-109
NC_014335.1\|WP_000612269.1\|1161926_1163171_+\|competence-protein	gnl\|CDD\|226875	COG4469, CoiA, Competence protein CoiA-like family, contains a predicted nuclease domain [General function prediction only].	3.62485e-58

>NC_014335.1|WP_001079111.1|1169639_1170533_+|RluA-family-pseudouridine-synthase
MNRFTLKWDIESAEEGTLVREFLKTKGISKAALTDIKFHGGAIEVNGQHASVRHQLQVGEELRIFFPVEERSEGMIAEDIPLCIVYEDDAVLVINKEANMSTIPSREHPSGSVANALLSHYDKQYLPSTVHIVTRLDRDTSGLMLIAKNRFVHHLLSKQHQQKAVKRTYEAIVHGEMVEREGTIDAPIGRKSDSIIERTVCEEGQRAVTHFRVIDSANHKTHVSLELDTGRTHQIRVHMAHIGHPLLGDNLYGGKRDEMKRQALHSTSLTFYHPILEKEMSFAAMIPSDMQEVLRQT
>NC_014335.1|WP_000673194.1|1168826_1169624_+|NAD-kinase
MKFTIMSKGDQSSDTLASTMKEYLLDFGFIMDEQEPDIVISVGGDGTLLYAFHRYYNRLDETAFVGVHTGHLGFYADWLPTEVEKLVIAIAKTPFQVVEYPLLEVIIRYMNGSKESQYLAMNEATVKSAEGTLVTEVEIRGEYFETFRGDGLCISTPSGSTAYNKALGGAIIHPSIEAIQIAEMASINNRVFRTVGSPLVLPKHHTCVLKPTAGMNLQITVDHLTMVHQDVKSIQYRVANEKVRFVRFRPFPFWKRVRDSFVADK
>NC_014335.1|WP_001081482.1|1168169_1168808_+|GTP-pyrophosphokinase-family-protein
MNRNWEEFLAPYHQAVAELKVKLKGMRTQFAMLTEHSPIEFVTGRVKSVASIIDKAEKRNVPLDRLREDMQDIAGLRMMCQFVDEIKPVVEYLRKRNDFEIVEERDYVTQKKDSGYRSYHVVISYPVQTIQGEQKVLVEIQIRTLAMNFWATIEHSLNYKYSGRFPEDIKIRLQRAAEAAFLLDEEMSSIRLEIQEAQKAFSRKQETKDSES
>NC_014335.1|WP_001180009.1|1167767_1168139_+|hypothetical-protein
MQNKIQVKSVEKRENALIFCAENSEIEVKGLSARNHVLVDSDNLSFLYILENESSFIYVSIPHTCWEAMHEAMNNDVVMFVRVNDIEMELEGLKEEVEYLVENIEGNANYGEELVTAVEKVFL
>NC_014335.1|WP_000191105.1|1167042_1167621_-|CYTH-domain-containing-protein
MTQEIEIEFKNIVTEEEFHALCKSFSIEVFTKQVNHYFETPNFSLKEAGSALRIRHKGETYTLTLKQPAEVGLLETHQVVTENEAKMMMETNVIISGAVMNQLCKLQIPVSALTYMGSLTTERAETLFEGGTLVFDHSFYYNHDDYEIEFEVQDEETGKAAFIHLLKQHNIPIRHTNNKVKRFFLAKQNKAR
>NC_014335.1|WP_000043381.1|1166463_1166862_-|hypothetical-protein
MSKQPMTPFEAIGGEQCIAILVDTFYSYVSKHPDLSPIFPDDLTETARKQKQFLTQYLGGPNLYTEEHGHPMLRARHLPFEITPKRAEAWLSCMEQAMDDTGVHGHIREFVFERLALTAQHMVNTPNETGEI
>NC_014335.1|WP_000360638.1|1165570_1166464_-|DsbA-family-protein
MDKQEAKHINMPSPSACEHKSVEAYLFIDPLCKDCWEIEPFIIKLWLEYGKYFSIRHIVTGKVDGTNASSHKWNKPANIRFVWEKTTSLHGFSCDGKVHMQEASSTPYLVSMAIKAAELQGRKAGSKFLRKLQEYIFLENVSNPDCELLLACAKDSDIDVEEFKKDLYSASAKKAFQCDLKFTNEMHITEIPSLVFFHANSDEEGIKIAGTYSYDVYVQLLKELVKCEIEPEPLPPLEVLLEATQFISSKEVAFIYDCSKQEIERELKKLQLKRKVQMIDVKCERYWKWIAKEKDLV
>NC_014335.1|WP_000754593.1|1165167_1165341_-|hypothetical-protein
MKKTYILLIILAVIVSFFLYILSLLQAFPKMIAFPLLFGVIVIALSYFNHKKRFKGF
>NC_014335.1|WP_000003400.1|1163221_1165048_+|oligoendopeptidase-F
MSEQNTAKTLPDRNEIEESSTWRLEDIFQTDTEWEKEFQGIKELLPKLTEFKGKLGDSANNLLEALQYEDEISMRLGKLYTYAHMRYDQDTTNSVYQALNDRATNLYSQVSSSTAYIVPEILSISEDTLQTFLKENRDLSVYEHALEEITRQRPHVLSEAEEALLAEASEVMSASSNTFGMLNNADLKFPSIKGEDGEEVEITHGRYIQFLESDDRRVREDAFKAVYETYGKYKNTFASTLSGAVKRNNFNARVRKYDSARQAALSNNNIPEAVYDQLIESVNDNLHLLHRYIDIRKRALGLDELHMYDLYTPLVPEVKMNVKYEEAQDMLLKSLHVLGDEYVGILKEAYENRWVDVYENKGKRSGAYSSGAYGTNPYILMNWHDNVNNLFTLAHEFGHSVHSYYTRKTQPHVYGDYSIFVAEVASTCNEALLNDYLLKTTEDKKERLYLLNHYLEGFRGTVFRQTMFAEFEHIIHKKVQEGHAVTPDMLTEIYYDLNKKYFGNALVIDEEIGLEWSRIPHFYYNYYVYQYATGFSAATALSKQILEEGQPAVERYINEFLKAGSSDYPIEVLKKAGVDMASPEPVKEALQVFEEKLNELEALLFEEK
>NC_014335.1|WP_000612269.1|1161926_1163171_+|competence-protein
MIPIFIAKRENGEKIHLLDHHDEELLHHMRKRESFFCIACGKEVLMRLGKQKRWHFAHKKVDSCLAFYEAESTYHMYGKELLYRWFKRQNVHVEIEHYLPEIQQRPDIFIERAGRKIAIEYQCANLSIEQLCKRTYSYWQAGIQVIWIIGGNQLKKHSAYWMKFSSIMAFSLQSYPQPLLIFFCSKQKSFMKCTFITSFSTSIAFSHIIYLPIETTTFEMLFSPVPFQREVLNREWKRRKDYFRQNALPIWNYNHKSLLRLLYQCKCNPANFPSEIGVPLPSSFAFQTNSFIWQAFLYMKCIGELAVGDCISLKYVCSYIKKYTKRRMLPYFSQHIWKVAVTEYMTFLCYAGVLYKVGMYTYRKIRDAVPLKTGGEIIKHDEICLAHALSLFEAKFNMRGGKGDIIKTDREGIT
>NC_014335.1|WP_000872687.1|1172110_1172851_-|bis(5'-nucleosyl)-tetraphosphatase-PrpE
MKYDIIGDIHGCFQEFQDLTTKLGYNWNNDLPTHPDQRKLAFVGDITDRGPHSLRMIEIVWELVMHKKVAYYAPGNHCNKLYRFFLGRNVTVAHGLETTVAEYEALPSHKQNMIKEKFITLYEQSPLYHVLDEKRLLVCHAGIRQDYIGRQDKKVQTFVLYGDITGEKHADGSPVRRDWAKEYKGTTWIVYGHTPVKEPRFVNHTVNIDTGAVFGGRLTALRYPEMETVSVPSSLPFVPEKFRPIS
>NC_014335.1|WP_000654694.1|1172925_1174086_-|rod-shape-determining-protein-RodA
MKDPNSQYQIDYVLLCILFAIGTVSCFAIASAQASLPPFLQNVNFVLKQIQWYFIGFIAIGVIMIIDFDRYQKIAWYLYSFALVLLIGLELQVPGAITIKGATAWYRLPGIGNFQPSEIMKLFLIIVTGRIIANHNEKYFYRTIHDDFLLLGKICATSLPPLLLIAKEPDLGNTMVISAMLAAMILVSGIRWRFIFGLVSGIFVTAVTLTYIFFTHTKFFKTHILQEYQLNRFYGWLAPYKYDAQGYQLRQAFLATGSGEMQGKGWENGQVYFPEPHTDFIFTNVAEQFGFLGASVIIAIFFLLIFRMIHIAIESNDPFGSYICAGTIGMFTFQVFQNIGMTIGLLPITGITLPLMSYGGSSLLTYMIAIGFVLNVRSRTKIFMFN
>NC_014335.1|WP_002157369.1|1174203_1175130_-|glycosyltransferase-family-2-protein
MTSEKDLPLVSILIPTYNRPHYFKIALESALAQTYSNIEIIIGDDSTNDETETLIHEQYLPHYKNVTYIRNTPPLGQFHNDLMLLEKSNGEYINFLMDDDVFYKHKIQKMMAYFEQDTNKALALVTSYRVRIDDHGDLIGDAHPTQRLYSEDTPLNGMFLGDWMLKEGHNIIGEPTTTLFRKELLTEPFGTLKERQYSCSVDMASWISLLSKGDAVYISEPLSQFRYHAGQQIHNKLLQGCEDFTHLVITAKEYGFLQNTTDYRTALLSAYKWCKSSLKYYLHQLDIFPDAHVRLSHCLVIIIKELNN
>NC_014335.1|WP_001292832.1|1175143_1175896_-|class-I-SAM-dependent-methyltransferase
MSELNKEITLLPPPELVQYVGGDFKEVGKEFLTHFIQIGALKSNEKVLDVGCGVGRMAVPLMNYLTDDGAYYGFDLFKDGITWCQNNIATIRNNFHFEHVDIYNQFYNPEGKEDASQYRFPYEDETFDFIFLTSVFTHLLPKELEHYLSEIVRVLKKDGRCFITFFLINPESSYYLNAGLSTLGFYHQIENCYVVNKDIPNFAVAYPETNIYSLLNKYGLEAINKPYYGLWCGRHEYTSYQDIVITKKRV
>NC_014335.1|WP_000444380.1|1176110_1176956_-|class-I-SAM-dependent-methyltransferase
MESKSAVQLYLELLKKTILFEIWLEYEAYLPASLHISKELEFEPVTVPLPLFIKQYAENHNLKIVKPNVSKSERHDGMDWPRAAHSMIGRERMNQLQEAMETVVRENIEGDFIETGVWRGGSCIFMNGFLQANNITDRNVWVADSFEGLPAPNLEQYPKDYGDYLHTFDYLRVSLEQVQENFKKYDLLNDQVKFLKGWFKDTLPTAPIEKIAIARLDGDMYESTMDGLVNLYDKVSKGGYIIIDDYGLPPCAEAVTDFRNHRNLKAPITKIDVFGVYWRKE
>NC_014335.1|WP_000069703.1|1177078_1177678_-|exosporium-leader-peptide-containing-protein
MSNNNYSNGLNPDESLSASAFDPNLVGPTLPPIPPFTLPTGPTGPTGPTGATGLTGPTGPTGPSGLGLPAGLYAFNSGGISLDLGINDPVPFNTVGSQFGTAISQLDADTFVISETGFYKITVIANTATASLLGGLTIQVNGVPVPGTGSSLISLGAPIVIQAITQITTTPSLVEVIVTGLGLSLALGTSASIIIEKVA
>NC_014335.1|WP_000932920.1|1177843_1178941_+|glycosyltransferase-family-2-protein
MLNKQGITISLCMIVRDEEKTIARCLDSVEKIVDEIIVVDTGSIDRTKEIVEKYTSNIYDFQWIDDFAAARNFSFSKATQEYILWLDADDVLLEDAQEALKLLKREIDPKIDAVSMPYHLAMDSNGKPLYCTKRNRLVKREKQFQWFGKVHEYLAISGEVFSSNVAITHKKEKKVTDRNLKIFQNTVAAGEELSPRDLFYYANESTDNQKYDDAVLLYETFLNQDEGWYEEKIYACGKLGDCYAKLGMWEKAIESCVKSFRYDVPRGENCTRIGYIYMEQEKYNEAIFWFKLATEVPMATESPFHSPASYTWLPYLQMCICYSRLGEQDKAYYYNELAASYVPNNAAIEYNRKYFRGVFDKPYKV
>NC_014335.1|WP_001078427.1|1179151_1179841_+|class-I-SAM-dependent-methyltransferase
MNREKSSLYEEKSEHYYNAANPNLLKHIKKEWKEVLDIGCSGGALGAAIKENGTRVSGIEAFPEAAEKAKERLDHVILGDIEKIDLPYEEGQFDCVIFGDVLEHLFDPWAVIEKVKPYIKQNGVILASIPNVAHISVLAPLLAGNWTYTEYGLLDKTHIRFFTFNEMLRMFLKAGYVISKVDRVYVDHKMYEPLIEELYGICKKYRLGSGFMAETVVFQYIIEAEKSQL
>NC_014335.1|WP_001271183.1|1179837_1180524_+|streptomycin-biosynthesis-protein-StrF
MSAADKTILFVTCINDRKLYANCVRHILQLLVPPGYIVQFMPIRNAKSMTSGYNQAISHPAKYKVYLHQDVFIINRAFLYGLLQLFEEHEHLGMIGMVGAQYVPPTGVWNEGRGIVGKVIGYMNDLFYMASLEQPYHESKTFIPVECIDGLLMATQYDVPWREDLFDGFDFYDVSQSFEFKKAGYTVGVPVQRDAWCIHYHFDVNMTNYEKYRKIFVEHYMSDVNKEE
>NC_014335.1|WP_000651527.1|1180538_1181219_+|streptomycin-biosynthesis-protein-StrF
MKDHTILVVVCVNNEELFKQCESQIRNIFVPPGYVVQIFPIRDAQSMASAYNRALSYPAKYKVYIHQDTYLINRDMFSTLISLFKENEKLGLIGVAGAQFLPNNGIWWEGKNLVGKVIEYRRRNYQLLNLDQVFYGNQPFLSVQAIDGLFMATQYDIPWREDLFQGFHFYDVSQSLEFQRAGYLIGIPNQANLWCIHYNGDEFDADTYEKYRKVFVEHYKDILSPS

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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

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

293719 : 302096

Synechococcus_phage(33.33%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000625680.1\|293719_295027_+	adenylosuccinate lyase	A0A2H4UUU6	Bodo_saltans_virus	1.1e-20	25.3
WP_001170540.1\|295115_295835_+	phosphoribosylaminoimidazolesuccinocarboxamide synthase	G8EYA2	Synechococcus_phage	2.0e-48	43.9
WP_000278823.1\|295827_296082_+	phosphoribosylformylglycinamidine synthase subunit PurS	NA	NA	NA	NA
WP_000666777.1\|296078_296762_+	phosphoribosylformylglycinamidine synthase subunit PurQ	NA	NA	NA	NA
WP_000055578.1\|296745_298965_+	phosphoribosylformylglycinamidine synthase II	A6N228	Microbacterium_phage	1.3e-162	41.2
WP_000879029.1\|298949_300365_+	amidophosphoribosyltransferase	A0A0M3SGR2	Mollivirus	7.3e-55	35.4
WP_001262436.1\|300471_301512_+	phosphoribosylformylglycinamidine cyclo-ligase	Q58MH8	Prochlorococcus_phage	9.4e-68	46.4
WP_000088592.1\|301508_302096_+	phosphoribosylglycinamide formyltransferase	M4QRX9	Synechococcus_phage	1.2e-27	37.1

DBSCAN-SWA_2

780489 : 789046

Bacillus_phage(66.67%)

holin

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_041183853.1\|780489_781845_-	SH3 domain-containing protein	A0A0S2SXZ8	Bacillus_phage	1.3e-32	73.1
WP_000402993.1\|782945_783299_-	helix-turn-helix transcriptional regulator	A0A2I7SDF8	Paenibacillus_phage	1.0e-05	36.5
WP_000930102.1\|784818_785244_+\|holin	phage holin family protein	A0A0S2MVC4	Bacillus_phage	1.1e-46	72.1
WP_000509861.1\|785248_786232_+	N-acetylmuramoyl-L-alanine amidase	A9QTG1	Bacillus_phage	5.9e-88	74.6
WP_013246210.1\|786335_787619_+	C40 family peptidase	A0A2I7SDE4	Paenibacillus_phage	5.3e-20	31.1
WP_000912173.1\|787822_789046_+	3D domain-containing protein	A0A173GB44	Bacillus_phage	5.9e-21	44.1

DBSCAN-SWA_3

1809190 : 1817848

Bacillus_phage(66.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_000755537.1\|1809190_1810390_+	C40 family peptidase	A0A1V0DZX6	Clostridioides_phage	6.5e-12	32.0
WP_001194297.1\|1810488_1811253_-	alpha/beta hydrolase	NA	NA	NA	NA
WP_000453761.1\|1811482_1814008_+	ATP-binding cassette domain-containing protein	W8CYL7	Bacillus_phage	4.1e-266	95.7
WP_001231487.1\|1814004_1815078_+	sensor histidine kinase	W8CYF6	Bacillus_phage	3.2e-172	88.8
WP_000823543.1\|1815101_1815689_-	DUF3139 domain-containing protein	NA	NA	NA	NA
WP_000818985.1\|1815884_1816604_+	3-ketoacyl-ACP reductase	W8CYX9	Bacillus_phage	5.9e-61	100.0
WP_003158174.1\|1816720_1816834_+	hypothetical protein	W8CYT3	Bacillus_phage	1.6e-05	95.8
WP_001258497.1\|1816975_1817848_+	aminoglycoside 6-adenylyltransferase	A0A1X9I6F2	Streptococcus_phage	1.5e-66	45.5

DBSCAN-SWA_4

2591934 : 2600595

Geobacillus_phage(28.57%)

transposase

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_001065253.1\|2591934_2593302_-	lytic polysaccharide monooxygenase	A0A0K1Y848	Apis_mellifera_filamentous_virus	9.6e-20	38.1
WP_000720566.1\|2593738_2594257_-	DNA topology modulation protein	A0A097BYE2	Leuconostoc_phage	5.6e-45	47.9
WP_001093440.1\|2594484_2594871_-	DUF2809 domain-containing protein	NA	NA	NA	NA
WP_000655490.1\|2594936_2595644_-	class I SAM-dependent methyltransferase	A0A1X9I6N4	Streptococcus_phage	6.7e-17	27.0
WP_000288949.1\|2596033_2596438_-	GNAT family N-acetyltransferase	NA	NA	NA	NA
WP_000714661.1\|2596685_2598071_+	S-layer homology domain-containing protein	Q0H255	Geobacillus_phage	2.1e-78	60.3
WP_000820167.1\|2598073_2598286_+	DUF3006 domain-containing protein	Q0H256	Geobacillus_phage	7.3e-12	54.4
WP_087943621.1\|2598342_2599688_-\|transposase	IS3 family transposase	A0A1B1P773	Bacillus_phage	2.1e-112	74.4
WP_000540635.1\|2599788_2600595_-	N-acetylmuramoyl-L-alanine amidase	D2XR33	Bacillus_phage	1.9e-108	69.3

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. NC_014331

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CRISPR-Cas detection and classification

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. NC_014335

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection