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
CP023472	Vibrio parahaemolyticus strain FORC_072 chromosome 1, complete sequence	0 crisprs	DEDDh,DinG,WYL,cas3,csx1,csa3	0	0	3	0
CP023473	Vibrio parahaemolyticus strain FORC_072 chromosome 2, complete sequence	1 crisprs	DEDDh,WYL,csa3,cas3	0	0	0	0

Results visualization

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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

552678 : 569850

uncultured_Mediterranean_phage(18.18%)

tRNA

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

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
AYF14193.1\|552678_554319_+	CTP synthase	A0A1J0FA14	Only_Syngen_Nebraska_virus	4.2e-155	52.4
AYF14194.1\|554397_555699_+	Enolase	A0A1X9I5Z8	Streptococcus_phage	4.2e-134	59.2
AYF14195.1\|556101_556383_+	cell division protein FtsB	NA	NA	NA	NA
AYF14196.1\|556384_557089_+	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase	A0A2H4UTB4	Bodo_saltans_virus	2.6e-05	23.6
AYF14197.1\|557106_557583_+	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase	NA	NA	NA	NA
AYF14198.1\|557629_558673_+\|tRNA	tRNA pseudouridine 13 synthase	NA	NA	NA	NA
AYF14199.1\|558672_559449_+	5-nucleotidase SurE	A0A1B1ITZ2	uncultured_Mediterranean_phage	6.6e-66	52.4
AYF14200.1\|559448_560075_+	Protein-L-isoaspartate O-methyltransferase	A0A1B1IU40	uncultured_Mediterranean_phage	1.3e-35	52.1
AYF14201.1\|560089_561013_+	Lipoprotein NlpD	D7RWE0	Brochothrix_phage	4.1e-06	35.2
AYF14202.1\|561093_562083_+	RNA polymerase sigma factor RpoS	F4YCU2	Synechococcus_phage	6.9e-36	35.2
AYF14203.1\|562161_564723_-	DNA mismatch repair protein MutS	A0A1V0SC35	Catovirus	3.4e-34	23.5
AYF14204.1\|564807_565290_+	hypothetical protein	B5TK85	Pseudomonas_phage	2.9e-27	48.7
AYF14205.1\|565490_566534_+	RecA protein	A0A2D1GPX2	Mycobacterium_phage	8.1e-112	60.7
AYF14206.1\|566657_567125_+	Regulatory protein RecX	NA	NA	NA	NA
AYF14207.1\|567267_569850_+\|tRNA	Alanyl-tRNA synthetase	A0A1V0SK38	Klosneuvirus	7.7e-79	37.9

DBSCAN-SWA_2

681806 : 688508

Staphylococcus_phage(50.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
AYF14295.1\|681806_682946_+	Glutamate 5-kinase	A0A1X9I5D0	Streptococcus_phage	1.3e-62	41.7
AYF14296.1\|682978_684214_+	gamma-glutamyl phosphate reductase	A0A1X9I5D4	Streptococcus_phage	2.1e-98	47.9
AYF14297.1\|684341_684791_+	Ribonucleotide reductase transcriptional regulator NrdR	NA	NA	NA	NA
AYF14298.1\|684798_685923_+	Diaminohydroxyphosphoribosylaminopyrimidine deaminase	A0A1V0SE20	Indivirus	5.8e-47	35.6
AYF14299.1\|685935_686589_+	Riboflavin synthase eubacterial/eukaryotic	A0A2H4PQS5	Staphylococcus_phage	1.6e-33	37.5
AYF14300.1\|686758_687868_+	3,4-dihydroxy-2-butanone 4-phosphate synthase	A0A2H4PQS2	Staphylococcus_phage	1.5e-63	39.6
AYF14301.1\|688037_688508_+	6,7-dimethyl-8-ribityllumazine synthase	A0A2H4PQS3	Staphylococcus_phage	1.7e-32	49.3

DBSCAN-SWA_3

1440052 : 1454068

Vibrio_phage(30.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
AYF14983.1\|1440052_1440241_-	hypothetical protein	F6LQB8	Bdellovibrio_phage	8.8e-09	52.8
AYF14984.1\|1440338_1440563_-	hypothetical protein	NA	NA	NA	NA
AYF14985.1\|1440565_1441093_-	hypothetical protein	NA	NA	NA	NA
AYF14986.1\|1441085_1444250_-	hypothetical protein	I3PUZ3	Vibrio_phage	8.7e-24	33.6
AYF14987.1\|1444262_1444481_-	hypothetical protein	NA	NA	NA	NA
AYF14988.1\|1445230_1445947_-	hypothetical protein	G9L676	Escherichia_phage	1.4e-22	37.2
AYF14989.1\|1445998_1446250_+	hypothetical protein	A0A1I9KFF6	Aeromonas_phage	2.9e-07	41.9
AYF14990.1\|1446269_1446734_+	hypothetical protein	K7PJS5	Enterobacterial_phage	3.0e-18	48.0
AYF14991.1\|1446730_1446949_+	hypothetical protein	NA	NA	NA	NA
AYF14992.1\|1447014_1447968_+	hypothetical protein	A0A1V0E831	Vibrio_phage	1.3e-39	35.7
AYF14993.1\|1447964_1448345_+	hypothetical protein	NA	NA	NA	NA
AYF14994.1\|1448337_1448988_+	hypothetical protein	K7PKS6	Enterobacteria_phage	4.1e-21	36.5
AYF14995.1\|1448984_1449167_+	hypothetical protein	NA	NA	NA	NA
AYF14996.1\|1449156_1449558_+	hypothetical protein	A0A2I7S3K0	Vibrio_phage	3.7e-20	45.0
AYF14997.1\|1449594_1450002_+	APSE-2 prophage(Q protein)	NA	NA	NA	NA
AYF14998.1\|1450225_1450429_-	hypothetical protein	NA	NA	NA	NA
AYF14999.1\|1451335_1451548_+	Cold shock protein CspG	A0A1W6JNX5	Morganella_phage	2.9e-16	61.2
AYF15000.1\|1451842_1454068_+	3'-to-5' exoribonuclease RNase R	Q0GXV6	Lactococcus_phage	8.2e-61	31.7

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. CP023473

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CRISPR-Cas detection and classification

Crispr_ID: CP023473_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP023473_1

68626-68723

Orphan

Consensus_repeat	Method
TATTTTTAAAATGCCTTTTCAAAAA	CRISPRCasFinder

1 spacers

DEDDh

The CRISPR arrays of CP023473_1

>merge|CP023473|1|68626-68723|CRISPRCasFinder
TATTTTTAAAATGCCTTTTCAAAAATTTGAAACCGCGCAATTAAAGAATCCAGAAAAACTAGATCGCAATCAATATTTTTAAAACGCCTTTTCAAAAA

>CP023473|1|1|68626-68723|CRISPRCasFinder
TATTTTTAAAATGCCTTTTCAAAAA	TTTGAAACCGCGCAATTAAAGAATCCAGAAAAACTAGATCGCAATCAA
TATTTTTAAAACGCCTTTTCAAAAA

Protein	Signature genes	Signature genes Name	Protein_function
CP023473.1\|AYF16870.1\|61920_63069_-\|S-(hydroxymethyl)glutathione-dehydrogenase	unknown	unknown	gnl\|CDD\|176260
CP023473.1\|AYF16874.1\|65832_67701_-\|putative-signal-transduction-protein-containing-cAMP-binding-and-CBS-domains	unknown	unknown	gnl\|CDD\|225457
CP023473.1\|AYF16880.1\|71208_72120_+\|Xylanase	unknown	unknown	gnl\|CDD\|223730
CP023473.1\|AYF16872.1\|64249_65119_+\|Transcriptional-regulator-in-formaldehyde-detoxification-operon	unknown	unknown	gnl\|CDD\|176159
CP023473.1\|AYF16876.1\|68822_69584_+\|2-deoxy-D-gluconate-3-dehydrogenase	unknown	unknown	gnl\|CDD\|181605
CP023473.1\|AYF16868.1\|60112_60574_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226429
CP023473.1\|AYF16883.1\|73963_75589_-\|solute-symporter-family-protein	unknown	unknown	gnl\|CDD\|271371
CP023473.1\|AYF16879.1\|70495_71131_+\|putative-4-deoxy-L-threo-5-hexosulose-uronate-ketol-isomerase	unknown	unknown	gnl\|CDD\|181746
CP023473.1\|AYF16871.1\|63362_64169_+\|N-hydroxyarylamine-O-acetyltransferase	unknown	unknown	gnl\|CDD\|366312
CP023473.1\|AYF16884.1\|75835_76513_+\|Oligogalacturonate-specific-porin-protein-KdgM	unknown	unknown	gnl\|CDD\|368776
CP023473.1\|AYF16873.1\|65119_65830_-\|DNA-polymerase-III-epsilon-subunit	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|236392
CP023473.1\|AYF16867.1\|59021_60113_-\|Transcriptional-regulator-CdgA	unknown	unknown	gnl\|CDD\|143635
CP023473.1\|AYF16878.1\|70134_70455_+\|Pectin-degradation-protein-KdgF	unknown	unknown	gnl\|CDD\|380366
CP023473.1\|AYF16869.1\|61019_61859_-\|S-formylglutathione-hydrolase	unknown	unknown	gnl\|CDD\|178061
CP023473.1\|AYF16881.1\|72218_73148_+\|2-dehydro-3-deoxygluconate-kinase	unknown	unknown	gnl\|CDD\|238571
CP023473.1\|AYF16877.1\|69602_70127_+\|permease	unknown	unknown	gnl\|CDD\|378474
CP023473.1\|AYF16885.1\|76528_78757_+\|Exopolygalacturonate-lyase	unknown	unknown	unknown
CP023473.1\|AYF16866.1\|58607_58997_-\|hypothetical-protein	unknown	unknown	unknown
CP023473.1\|AYF16875.1\|67784_68567_-\|Transcriptional-regulator-KdgR,-KDG-operon-repressor	unknown	unknown	gnl\|CDD\|185046
CP023473.1\|AYF16882.1\|73159_73783_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235577

Protein	Function_ID	Function_description	E-value
CP023473.1\|AYF16870.1\|61920_63069_-\|S-(hydroxymethyl)glutathione-dehydrogenase	gnl\|CDD\|176260	cd08300, alcohol_DH_class_III, class III alcohol dehydrogenases. Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.	0
CP023473.1\|AYF16874.1\|65832_67701_-\|putative-signal-transduction-protein-containing-cAMP-binding-and-CBS-domains	gnl\|CDD\|225457	COG2905, COG2905, Predicted signal-transduction protein containing cAMP-binding and CBS domains [Signal transduction mechanisms].	3.4549e-139
CP023473.1\|AYF16880.1\|71208_72120_+\|Xylanase	gnl\|CDD\|223730	COG0657, Aes, Esterase/lipase [Lipid metabolism].	4.66367e-19
CP023473.1\|AYF16872.1\|64249_65119_+\|Transcriptional-regulator-in-formaldehyde-detoxification-operon	gnl\|CDD\|176159	cd08470, PBP2_CrgA_like_1, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator CrgA-like, contains the type 2 periplasmic binding domain. This CD represents the substrate binding domain of an uncharacterized LysR-type transcriptional regulator (LTTR) CrgA-like 1. 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 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.	1.14139e-108
CP023473.1\|AYF16876.1\|68822_69584_+\|2-deoxy-D-gluconate-3-dehydrogenase	gnl\|CDD\|181605	PRK08993, PRK08993, 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD.	0
CP023473.1\|AYF16868.1\|60112_60574_-\|hypothetical-protein	gnl\|CDD\|226429	COG3915, COG3915, Uncharacterized protein conserved in bacteria [Function unknown].	3.9997e-40
CP023473.1\|AYF16883.1\|73963_75589_-\|solute-symporter-family-protein	gnl\|CDD\|271371	cd11477, SLC5sbd_u1, Uncharacterized bacterial solute carrier 5 subfamily; putative solute-binding domain. SLC5 (also called the sodium/glucose cotransporter family or solute sodium symporter family) is a family of proteins that co-transports Na+ with sugars, amino acids, inorganic ions or vitamins. Prokaryotic members of this family include Vibrio parahaemolyticus glucose/galactose (vSGLT), and Escherichia coli proline (PutP) and pantothenate (PutF) cotransporters. One member of the SLC5 family, human SGLT3, has been characterized as a glucose sensor and not a transporter. This subfamily belongs to the solute carrier 5 (SLC5) transporter family.	2.45075e-100
CP023473.1\|AYF16879.1\|70495_71131_+\|putative-4-deoxy-L-threo-5-hexosulose-uronate-ketol-isomerase	gnl\|CDD\|181746	PRK09273, PRK09273, hypothetical protein; Provisional.	2.15977e-144
CP023473.1\|AYF16871.1\|63362_64169_+\|N-hydroxyarylamine-O-acetyltransferase	gnl\|CDD\|366312	pfam00797, Acetyltransf_2, N-acetyltransferase. Arylamine N-acetyltransferase (NAT) is a cytosolic enzyme of approximately 30kDa. It facilitates the transfer of an acetyl group from Acetyl Coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (M. tuberculosis, M. smegmatis etc) to man. It was the first enzyme to be observed to have polymorphic activity amongst human individuals. NAT is responsible for the inactivation of Isoniazid (a drug used to treat Tuberculosis) in humans. The NAT protein has also been shown to be involved in the breakdown of folic acid.	1.33095e-97
CP023473.1\|AYF16884.1\|75835_76513_+\|Oligogalacturonate-specific-porin-protein-KdgM	gnl\|CDD\|368776	pfam06178, KdgM, Oligogalacturonate-specific porin protein (KdgM). This family consists of several bacterial proteins which are homologous to the oligogalacturonate-specific porin protein KdgM from Erwinia chrysanthemi. The phytopathogenic Gram-negative bacteria Erwinia chrysanthemi secretes pectinases, which are able to degrade the pectic polymers of plant cell walls, and uses the degradation products as a carbon source for growth. KdgM is a major outer membrane protein, whose synthesis is strongly induced in the presence of pectic derivatives. KdgM behaves like a voltage-dependent porin that is slightly selective for anions and that exhibits fast block in the presence of trigalacturonate. In contrast to most porins, KdgM seems to be monomeric.	3.08357e-24
CP023473.1\|AYF16873.1\|65119_65830_-\|DNA-polymerase-III-epsilon-subunit	gnl\|CDD\|236392	PRK09146, PRK09146, DNA polymerase III subunit epsilon; Validated.	7.60874e-39
CP023473.1\|AYF16867.1\|59021_60113_-\|Transcriptional-regulator-CdgA	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	5.06677e-44
CP023473.1\|AYF16878.1\|70134_70455_+\|Pectin-degradation-protein-KdgF	gnl\|CDD\|380366	cd02238, cupin_KdgF, pectin degradation protein KdgF and related proteins, cupin domain. This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.	1.13072e-54
CP023473.1\|AYF16869.1\|61019_61859_-\|S-formylglutathione-hydrolase	gnl\|CDD\|178061	PLN02442, PLN02442, S-formylglutathione hydrolase.	5.2905e-143
CP023473.1\|AYF16877.1\|69602_70127_+\|permease	gnl\|CDD\|378474	pfam10688, Imp-YgjV, Bacterial inner membrane protein. This is a family of inner membrane proteins. Many of the members are YgjV protein.	3.52613e-49
CP023473.1\|AYF16881.1\|72218_73148_+\|2-dehydro-3-deoxygluconate-kinase	gnl\|CDD\|238571	cd01166, KdgK, 2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.	9.63554e-103
CP023473.1\|AYF16875.1\|67784_68567_-\|Transcriptional-regulator-KdgR,-KDG-operon-repressor	gnl\|CDD\|185046	PRK15090, PRK15090, DNA-binding transcriptional regulator KdgR; Provisional.	0
CP023473.1\|AYF16882.1\|73159_73783_+\|hypothetical-protein	gnl\|CDD\|235577	PRK05718, PRK05718, keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional.	4.28455e-121

>CP023473.1|AYF16875.1|67784_68567_-|Transcriptional-regulator-KdgR,-KDG-operon-repressor
MEKSTQPEAVSSVLKVFHILQALGEQKAIGVSELSQRLMMSKATTYRFLQTMKSLGYVSQEGEADKYSLTLKLFELGAKSLEYVDLIELADKEMRHISEQTNEALHLGALDENAIIYIHKIDSGYNLRMQSRIGRRNPLYSTAIGKVLLSERDESFVRDVLSDVEFIKHTEKTLENTDQVLEELAKVRDFHYAEDNEEQEPGLRCIAAPIYDRFGQIIAGLSISFPTIRFDEERMEYYVGLLHQAGKNISEQLGYHDYPA
>CP023473.1|AYF16874.1|65832_67701_-|putative-signal-transduction-protein-containing-cAMP-binding-and-CBS-domains
MGTSVTPNIFDFLIKIDPFDKLPEPVVESIANSVKVKYLVRGETIGFSALCDQRYLYIIRTGAIEQRTPNGELRARLGQDDQFGFTFLDPLENAEDGYQAEAIEDSLLYLIPHSELKLVSEEHPEFADYFAAQANVRLSSAVKYVCRKEEKGLFFRTVGEIASENIAIVDVNDSIRSVAQTMCGKQRSSCAVVMKEGEIIGLVTDRDMTKSVVAQDMDTNQPIADVMTPNPVLIEDDAKVIQAISLMLQYNIRCLPVVHGKQVKGLLTTTHLVHNHRTQSLFLIEKIKYASSLNALAALKEERQTIFQALVESGVSAEIQGRVMSMIMDAFTRRIIQLNEELLGPPPCDYAWLVAGSHARNEVHMLSDQDSAIVLSDDATEEHKLYFTHLAMRVCNGLAACGYPLCDGKYMAASPKWCQPIRRWKEYYQKWVASPEYNKLLSISVFLEVRAIHGNREFVDQIQQHLHDCIQKSPSFIPALVRDAIDTQPPLGIFNNLVLEKGGENSNTLNIKKYALNLIIDLARIFSLAAGGSLTGTEERFRYAAQHGTLSKDSVENIIGAYRFITQVRFRHQLNAILAGTTPDNHIAPDDFSSFERKHLKDAFKIISELQDVAKLKFLKGA
>CP023473.1|AYF16873.1|65119_65830_-|DNA-polymerase-III-epsilon-subunit
MIKRWFKRWETPLSPEQKRQAIHVIDDWPMVLKDYLQQPLVDDSTTLKNLSFVALDFETTGVDAQGDKILSIGVVDLTLDGIDIASSKEWYICHGQFIKPETAKINGLTPQDLAKGLPLDEGMNRLLERITGKVVLAHGCCIEKAFIHAYFSSRYQVEDFPAYFVDTLQIEKQFSYAGKSGAHSSYQLDDLRRYYHLPGYLSHSAASDALACAELFLVQSKKLTALPDVTLRQLMR
>CP023473.1|AYF16872.1|64249_65119_+|Transcriptional-regulator-in-formaldehyde-detoxification-operon
MANWEGVSEFVAVAETNSFTGAAAKLKTSVAQISRRVSALEERLAVKLLHRTTRKVSLSEAGQLYYQQCKHLVEGLELAELAVTQMQTEPRGLLRVTAPVTYGEMNLAPLLHQFLEKYPRVDLDLVLTNQKLDLIEQGVDVAIRLGRLQDSSMIAKRLSSRQTYVCASPMYLERFGEPHTLSELGRHQCLVGSVDYWHFKENKRDKSLRVSGRIKCNSGFALVDAAKRGLGLVQLPDYYVQEALDSGELVEVLTDYRDDREGIWALYPQSRNLSPKVRLLIDFLAQELA
>CP023473.1|AYF16871.1|63362_64169_+|N-hydroxyarylamine-O-acetyltransferase
MNKTDLNAYLTKLGLPSELPADLESLHKIHVAQHRCLPFENFDISLQRGISVEIEDIIQKTVYHSRGGYCFELNGLMLDVLKTLGFEARSLLGRVHVMRTPTGRSHQITLVTLDEQAWIVDVGFGSNTPRAPLPFILNQVIQTDLQTFRFVEDAQFGYFLQVLSTDGTDTWNNLYSFDLEFVFAGDIACGNFFTSTSPHSRFTSARVAAKATESGLVTLLNYTLKYTSQGEQTELELEPGQAYLDALKEYFGIELDAQYGDLRPLPDA
>CP023473.1|AYF16870.1|61920_63069_-|S-(hydroxymethyl)glutathione-dehydrogenase
MTLEIKPGQTHIKSKAMVAWAAGEPLKMEEVDVQLPKAGEVLVRIVATGVCHTDAFTLSGDDPEGIFPSILGHEGGGIVEMVGEGVTSVEVGDHVIPLYTAECGECKFCKSGKTNLCQAVRETQGKGLMPDGTSRFSINGETIFHYMGCSTFSEYTVLPEISLAKVNKQAPLEEVCLLGCGVTTGMGAVLNTAKVEKGDTVAIFGLGGIGLSAIIGARMAGASRIIGIDINESKFDLAKQLGATDVINPQKFDKPIQEVIVEMTDGGVDYSFECIGNVNVMRQALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGRSELPEIVNRYMAGEFGLQEFITHTMGLEDVNKAFDLMHEGTSIRTVIHMDK
>CP023473.1|AYF16869.1|61019_61859_-|S-formylglutathione-hydrolase
MTIENVSQTKVFGGWHKQYTHDSKALNCTMRFAIFLPPNATKSNPVPALYWLSGLTCTDENFMQKAGAFRMAAELGIAIIAPDTSPRGEGVADDASYDLGQGAGFYLNATQAPWSLHYHMYDYVTQELPAIIEANFPVSDVKSISGHSMGGHGALTIGLKNPTLYRSISAFSPISNPMQCPWGQKAFTAYLGTDIESWKQYDASELLKKEKSPLPILVDQGDADGFLSEQLKPEVLLAAAKQHGSELNLRMQSGYDHSYYFISSFIDNHLNFHAKYLFA
>CP023473.1|AYF16868.1|60112_60574_-|hypothetical-protein
MKKIVSLSLLLFAPFLSANSITFSSPQQPSVTLKLEELQSLPTTSYTTDLPWIQQSSEFLGVKLSTLLTHVYGSIPEQVDIGSLNNYHSTLSRKDIVRYQPILAYQQDHHYIKVRNKGPYWVIYPLSQYPELDHNEYHAQMVWQVNEMKIKQK
>CP023473.1|AYF16867.1|59021_60113_-|Transcriptional-regulator-CdgA
MKLSEAYPIKQKNYSTTSKMLLLVFATSLLLANVILLQQTRVLAQSFTDEQKQATWFLFQLSKELSELVSEARRLDENVLKIEGAELQYELAWSRFDLLINSKDVYTFFSRNHIQQYFLQLFNEFKELEPLLVEAKTGDSQAAAQFYRATQTLYLNLVEFVNQNFRLTSQVYETQKDESQRLMKAQYMLFATFVLSILSLTYFFYRESHFHRKLALSDPLTGLGNRNALFVTLRNNTRNRTAFSLCLLDLNGFKNVNDTYGHQAGDTVLCEIAKRLKDMNIDSFSTYRMGGDEFAVVIESSDVDAEEAKKHIHSVFDTPVLNANNVSSLSTSIGVAHYPSDSDNVDFLISIADKRMYKMKFQR
>CP023473.1|AYF16866.1|58607_58997_-|hypothetical-protein
MQVLLLLAVIAAGVLAWVFIPSHETIGQKTLEQALNDDYSLVGHRIYSTDPDAGNRFGYFVLATGQSIEEQEPFLVTSDQFIRMEQTGDNTLSVTVNGRIYQYHNDLWVPKSDGKLQHFLVSATANYVR
>CP023473.1|AYF16876.1|68822_69584_+|2-deoxy-D-gluconate-3-dehydrogenase
MILDSFNLEGKVAIVTGCDTGLGQGMALGLAKAGCDIVGVNISEPTETIEKVEAEGRKFVDIRANLMKLDDIPTIVDRAVTELGRIDILVNNAGIIRRNDAIEFSEQDWDDVMNINVKSVFFMSQAVAKQFIAQGEGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWASHGINVNAIAPGYMATNNTAALRADEQRNKEIVDRIPAARWGTPEDLAGPCVFLASKAADYINGYTIAVDGGWLAR
>CP023473.1|AYF16877.1|69602_70127_+|permease
MVDTTILAQALGFISFGLGFSVFYQKNDRHLKILMLIFNLNHLLHFLLLGSMISALSALLSALRTTTAIFVSSKRVAAVFIVISLVSGFWVAEQWRDLWPIIGTVIGTYSVFCLSGIRMRIGFLLGASCWLTNNILVGSIGGTLLEMTVIVMNLLTIYRLHRQQSESMINQSSY
>CP023473.1|AYF16878.1|70134_70455_+|Pectin-degradation-protein-KdgF
MFVFNQDIPMEDLGEGISRKVLAHSDNMMSVEVHFEEGAIGAMHSHPHEQLTYVLSGEFEFTIGDEKKIVKTGDTMYKEPNIEHGCVCLKAGVLIDTFTPMRKDFV
>CP023473.1|AYF16879.1|70495_71131_+|putative-4-deoxy-L-threo-5-hexosulose-uronate-ketol-isomerase
MKIALMMENSQAAKNAMVAGELNSVAGGLGHDVFNVGMTDENDHHLTYIHLGIMASILLNSKAVDFVVTGCGTGQGALMSCNLHPGVVCGYCLEPSDAFLFNQINNGNAISLAFAKGFGWAGELNVRYIFEKAFTGKRGEGYPIERAAPQQANAAILNNVKSAVAKDVVEGLRAIDQELVKTAVGSTQFQECFFAHCQVPEIAEYVKSLLD
>CP023473.1|AYF16880.1|71208_72120_+|Xylanase
MHVAPITSLQTWFPEHPVLPLWSEPQIPSHLVQSYQERNPNELLPDRAVFDITHPEIVVFEPEQSNGMGILLMPGGGYQRVSVDKEGADSARVLNQAGFTVFVMTYRMPNEGHEFGSWTPLADAQRAMRLVRQLPLASHLSSIGVLGFSAGGHVAASLATSHALDIYPLQDEADRVSAKPDFCALMYPVISMNTDIAHMGSRAELLANLERESDLLRFSLEKQVTSDMPPCFLLHASDDTAVSVENSIVFWQALRQHGIATEMHLFEQGKHGFGIRDAQGLPVAAWPQLLSAWLQNLTEKARR
>CP023473.1|AYF16881.1|72218_73148_+|2-dehydro-3-deoxygluconate-kinase
MNPISRVAIIGECMVELKKHDGVLQQGFGGDTLNTAVYLSRLTKQHGVETSYVTGLGHDPFSREMLTAWREEGINTDMVYLSEDKLPGIYAIETAEDGERSFFYWRNDAAAKYWLRERALLSLVKDLCQHQMIYLSGISLAIISDDCRQMLIELLTMCRKEGVKIAFDNNFRPKLWPNIEQARDFYSKILSVTDMAFLTFDDEVMLWGDKHEDEAISRTKNFGVKEIIVKRGADDCFVVTQDQQHTVAALKVDAVVDTTAAGDSFSAGYLAKRILGGDVAESALAGHKLAGTVIQHRGAIIPSQAMPTI
>CP023473.1|AYF16882.1|73159_73783_+|hypothetical-protein
MKDLNQQLSEIKVVPVIAIKDAGKAVKLAQVLIENGLPCAEVTFRTEDAALAIKNMREAYPEMLIGAGTVLTSAQVDEAIDAGVDFIVSPGFNPTTVKYCQQRNVTIVPGVNNPSLVEQAMEMGLRTLKFFPAEPSGGVAMLKALSAVYPVKFMPTGGVSPSNVKDYLSISSVLACGGTWMVPGDLIDNEQWDELAKLVREVAGIIE
>CP023473.1|AYF16883.1|73963_75589_-|solute-symporter-family-protein
MMWWMAGATAFMTQFSAWTFTGAAAKAYEDGISVMFIFWGNALGFFVAAAFFARRYRRLRVETAMEVIRVRFGHTSEQLFTWLSFPLTLIACAIWMNGLASFFSAVFAIEMSTTILAMGVIVTLIAVSGGAWTVSVTNVIQLILLIAITLVIGYTALQRFDSPSEVFAHATPIYGEQIRMPSLFVMWAIAMLLQQTMSNNHTLSCYRFLTTANDKDATKAAFVAGVLFVFAPVLWFMPAWFVAAQNIDLLAIYPALEQSANNAAYLYYIQHYMPQGLLGLVMVALVAATIAPLSSAHNRNAGIVVKSLYQVWFNPNATSRQQLMVGKIATVVSGVLATATALLLASVESYSLFDMMIVFAAFIQMPINIPSLLALVSLKTPNWSGWATVMVGCAVSLFMMFIFDVQWLSSSPLTPRESKDLSVVATLAVHLLVTGGFFLSTRVFYAKEPPSIQQSRTALAIQLATPISDEEQSPINHKQGLYVGSITALAGMLLILAGVVLAGSSQSIFVAIGCIVLLFSLFLLQPTQHSKRAWQKQKLSK
>CP023473.1|AYF16884.1|75835_76513_+|Oligogalacturonate-specific-porin-protein-KdgM
MKVRYLTSALLLAMTSGLAAAASVDIRHEYVPDRDGDEHRDRIYVSHRFDNQIGFSVEAKWNYKDGHMGNAGHETGVSYRWKATDNFSLTPGINIDASPSGASVFKYNLTGAYKINDEWDVAARIRHGYKNTDDSRYNQLNLYANRKFEWGKLGVEAEYKDIHGGEGGWKDKGHDQLIDFKGEYTKLESGVIPFFAIAAITHKGDGSEFKDEYVPRFRVGLKYNF
>CP023473.1|AYF16885.1|76528_78757_+|Exopolygalacturonate-lyase
MKKHTLALCLAAILAPAAHAAEIKVEDLTWKASTFGQSTDMNFGSTILPEKVGVNQVTVNGEAVAAGKLASTFTIESRGGKLANSHEGLTFYYTELPTDVNFTLSADVVLEQLGPETGATPNRQEGAGLMVRDILGAERLVPQPEGHEEFPSASNMVMNLMRSHTRTNDGMTNINASFREGVYQPWGTPGNRLSRVDYVEGVPYGTAETYRMTLTRTNDGFKVSYRNGEKFVEQAVKGANANIVEMQNSDSQYVGFFASRNAKMTVSNVDLQLAAADTVDAPKYAAKQGELVFQIASSPRSATKEYPVQARANYSGEFEVLHNGKVVAKQTVTAGELFSQWLTLDSGANQMEVRFTAIDGPNKETQAHRYSVDVVSLPDPMTLYVAPNGSDKGNGSQAQPLDFATAVELLPAGGTIILKDGDYQGMEIPLTASGSVDKLKHLRAEGDKVRFVSELRHEANYWHYQGIEVAGAQFIVHGSHNTFEKMVTHGAPDTGFVITSPENIGRALWASYNQVIESESYNNMDPSQINADGFAAKMRIGDGNTFIRCLSHHNIDDGWDLFNKVEDGANGAVTILDSISFSNGRTLDVANKGGTIGNGFKLGGEGIPVPHVVKNSLSFNNNMDGFTDNFNPGALVLSDNVSIDNKRFNYLFRKSPYSGEIEQGTFTNNRSYRFHVSSKYDDVINSAKSTGNALVENGTTYTSDGKAVDSKTLAPLKQASVIDTQQAIPGKQEAMQLKQLIR

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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

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. CP023472

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CRISPR-Cas detection and classification

Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection

2. CP023473

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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