CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_CP009982	Vibrio parahaemolyticus strain FORC_008 chromosome 1, complete sequence	0 crisprs	DEDDh,PD-DExK,DinG,cas3,csx1,csa3	0	0	2	0
NZ_CP009983	Vibrio parahaemolyticus strain FORC_008 chromosome 2, complete sequence	1 crisprs	DEDDh,WYL,csa3,cas3	0	0	3	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP009983_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP009983_1

68761-68858

Orphan

Consensus_repeat	Method
TATTTTTAAAATGCCTTTTCAAAAA	CRISPRCasFinder

1 spacers

DEDDh

The CRISPR arrays of NZ_CP009983_1

>merge|NZ_CP009983|1|68761-68858|CRISPRCasFinder
TATTTTTAAAATGCCTTTTCAAAAATTTGAAACCGCGCAATTAAAGAATCCAGAAAAACTAGATCGCAATCAATATTTTTAAAACGCCTTTTCAAAAA

>NZ_CP009983|1|1|68761-68858|CRISPRCasFinder
TATTTTTAAAATGCCTTTTCAAAAA	TTTGAAACCGCGCAATTAAAGAATCCAGAAAAACTAGATCGCAATCAA
TATTTTTAAAACGCCTTTTCAAAAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP009983.1\|WP_021821224.1\|76665_78894_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP009983.1\|WP_005482833.1\|60247_60709_-\|oxidoreductase	unknown	unknown	gnl\|CDD\|226429
NZ_CP009983.1\|WP_082241157.1\|67919_68717_-\|DNA-binding-transcriptional-regulator-KdgR	unknown	unknown	gnl\|CDD\|185046
NZ_CP009983.1\|WP_005464966.1\|61154_61994_-\|S-formylglutathione-hydrolase	unknown	unknown	gnl\|CDD\|178061
NZ_CP009983.1\|WP_005460834.1\|73294_73918_+\|bifunctional-4-hydroxy-2-oxoglutarate-aldolase/2-dehydro-3-deoxy-phosphogluconate-aldolase	unknown	unknown	gnl\|CDD\|235577
NZ_CP009983.1\|WP_053047862.1\|65967_67836_-\|CBS-domain-containing-protein	unknown	unknown	gnl\|CDD\|225457
NZ_CP009983.1\|WP_053047863.1\|71343_72255_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223730
NZ_CP009983.1\|WP_053047864.1\|74103_75843_-\|transporter	unknown	unknown	gnl\|CDD\|271371
NZ_CP009983.1\|WP_005497706.1\|69737_70262_+\|YgjV-family-protein	unknown	unknown	gnl\|CDD\|378474
NZ_CP009983.1\|WP_005482845.1\|75972_76650_+\|porin	unknown	unknown	gnl\|CDD\|368776
NZ_CP009983.1\|WP_005464959.1\|59156_60248_-\|GGDEF-domain-containing-protein	unknown	unknown	gnl\|CDD\|143635
NZ_CP009983.1\|WP_005482916.1\|68957_69719_+\|2-dehydro-3-deoxy-D-gluconate-5-dehydrogenase-KduD	unknown	unknown	gnl\|CDD\|181605
NZ_CP009983.1\|WP_025537340.1\|65254_65965_-\|DNA-polymerase-III-subunit-epsilon	DEDDh	cd06127_DEDDh_CAS-I	gnl\|CDD\|236392
NZ_CP009983.1\|WP_005467181.1\|70269_70590_+\|cupin-domain-containing-protein	unknown	unknown	gnl\|CDD\|380366
NZ_CP009983.1\|WP_005464972.1\|64384_65254_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176159
NZ_CP009983.1\|WP_005482884.1\|72353_73283_+\|sugar-kinase	unknown	unknown	gnl\|CDD\|238571
NZ_CP009983.1\|WP_031831553.1\|58742_59147_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP009983.1\|WP_025501292.1\|63497_64304_+\|arylamine-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366312
NZ_CP009983.1\|WP_005460779.1\|70630_71266_+\|RpiB/LacA/LacB-family-sugar-phosphate-isomerase	unknown	unknown	gnl\|CDD\|181746
NZ_CP009983.1\|WP_005464962.1\|62055_63204_-\|S-(hydroxymethyl)glutathione-dehydrogenase/class-III-alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|176260

Protein	Function_ID	Function_description	E-value
NZ_CP009983.1\|WP_005482833.1\|60247_60709_-\|oxidoreductase	gnl\|CDD\|226429	COG3915, COG3915, Uncharacterized protein conserved in bacteria [Function unknown].	3.9997e-40
NZ_CP009983.1\|WP_082241157.1\|67919_68717_-\|DNA-binding-transcriptional-regulator-KdgR	gnl\|CDD\|185046	PRK15090, PRK15090, DNA-binding transcriptional regulator KdgR; Provisional.	0
NZ_CP009983.1\|WP_005464966.1\|61154_61994_-\|S-formylglutathione-hydrolase	gnl\|CDD\|178061	PLN02442, PLN02442, S-formylglutathione hydrolase.	5.2905e-143
NZ_CP009983.1\|WP_005460834.1\|73294_73918_+\|bifunctional-4-hydroxy-2-oxoglutarate-aldolase/2-dehydro-3-deoxy-phosphogluconate-aldolase	gnl\|CDD\|235577	PRK05718, PRK05718, keto-hydroxyglutarate-aldolase/keto-deoxy-phosphogluconate aldolase; Provisional.	4.28455e-121
NZ_CP009983.1\|WP_053047862.1\|65967_67836_-\|CBS-domain-containing-protein	gnl\|CDD\|225457	COG2905, COG2905, Predicted signal-transduction protein containing cAMP-binding and CBS domains [Signal transduction mechanisms].	2.28404e-139
NZ_CP009983.1\|WP_053047863.1\|71343_72255_+\|alpha/beta-hydrolase	gnl\|CDD\|223730	COG0657, Aes, Esterase/lipase [Lipid metabolism].	3.83438e-18
NZ_CP009983.1\|WP_053047864.1\|74103_75843_-\|transporter	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.	8.25956e-107
NZ_CP009983.1\|WP_005497706.1\|69737_70262_+\|YgjV-family-protein	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.	9.00507e-50
NZ_CP009983.1\|WP_005482845.1\|75972_76650_+\|porin	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
NZ_CP009983.1\|WP_005464959.1\|59156_60248_-\|GGDEF-domain-containing-protein	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
NZ_CP009983.1\|WP_005482916.1\|68957_69719_+\|2-dehydro-3-deoxy-D-gluconate-5-dehydrogenase-KduD	gnl\|CDD\|181605	PRK08993, PRK08993, 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase KduD.	0
NZ_CP009983.1\|WP_025537340.1\|65254_65965_-\|DNA-polymerase-III-subunit-epsilon	gnl\|CDD\|236392	PRK09146, PRK09146, DNA polymerase III subunit epsilon; Validated.	8.97149e-39
NZ_CP009983.1\|WP_005467181.1\|70269_70590_+\|cupin-domain-containing-protein	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
NZ_CP009983.1\|WP_005464972.1\|64384_65254_+\|LysR-family-transcriptional-regulator	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
NZ_CP009983.1\|WP_005482884.1\|72353_73283_+\|sugar-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.	1.15929e-102
NZ_CP009983.1\|WP_025501292.1\|63497_64304_+\|arylamine-N-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.	1.53608e-97
NZ_CP009983.1\|WP_005460779.1\|70630_71266_+\|RpiB/LacA/LacB-family-sugar-phosphate-isomerase	gnl\|CDD\|181746	PRK09273, PRK09273, hypothetical protein; Provisional.	2.15977e-144
NZ_CP009983.1\|WP_005464962.1\|62055_63204_-\|S-(hydroxymethyl)glutathione-dehydrogenase/class-III-alcohol-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

>NZ_CP009983.1|WP_082241157.1|67919_68717_-|DNA-binding-transcriptional-regulator-KdgR
MKGVTMEKSTQPEAVSSVLKVFHILQALGEQKAIGVSELSQRLMMSKATTYRFLQTMKSLGYVSQEGEADKYSLTLKLFELGAKSLEYVDLIELADKEMRHISEQTNEALHLGALDENAIIYIHKIDSGYNLRMQSRIGRRNPLYSTAIGKVLLSERDESFVRDVLSDVEFIKHTEKTLENTDQVLEELAKVRDFHYAEDNEEQEPGLRCIAAPIYDRFGQIIAGLSISFPTIRFDEERMEYYVGLLHQAGKNISEQLGYHDYPA
>NZ_CP009983.1|WP_053047862.1|65967_67836_-|CBS-domain-containing-protein
MGTSVTPNIFDFLIKIDPFDKLPEPVVESIANSVKVKYLVRGETIGFSALCDQRYLYIIRTGAIEQRTPNGELRARLGQDDQFGFTFLDPLENAEDGYQAEAIEDSLLYLIPHSELKLVSEEHPEFADYFAAQANVRLSSAVKYVCRKEEKGLFFRTVGEIASENIAIVDVNDSIRSVAQTMCGKQRSSCAVVMKEGEIIGLVTDRDMTKSVVAQDMDTNQPIADVMTPNPVLIEDDAKVIQAISLMLQYNIRCLPVVHGKQVKGLLTTTHLVHNHRTQSLFLIEKIKYASSLNALAALKEERQTIFQALVESGVSAEIQGRVMSMIMDAFTRRIIQLNEELLGQPPCDYAWLVAGSHARNEVHMLSDQDSAIVLSDDATEEHKLYFTHLAMRVCNGLAACGYPLCDGKYMAASPKWCQPIRRWKEYYQKWVASPEYNKLLSISVFLEVRAIHGNREFVDQIQQHLHDCIQKSPSFIPALVRDAIDTQPPLGIFNNLVLEKGGENSNTLNIKKYALNLIIDLARIFSLAAGGSLTGTEERFRYAAQHGTLSKDSVENIIGAYRFITQVRFRHQLNAILAGTTPDNHIAPDDFSSFERKHLKDAFKIISELQDVAKLKFVKGA
>NZ_CP009983.1|WP_025537340.1|65254_65965_-|DNA-polymerase-III-subunit-epsilon
MIKRWFKRWETPLSPEQKRQAIHVVDDWPMVLKDYLQRPLVDDSTTLKDLSFVALDFETTGVDAQGDKILSIGVVDLTLDGIDIASSKEWYICHGQFIKPETAQINGLTPQDLAKGLPLDEGMNRLLERITGKVVLAHGCCIEKAFIHAYFSSRYQVEDFPAYFIDTLQIEKQFSYAGKSGAHSSYQLDDLRRYYHLPGYLSHSAASDALACAELFLVQSKKLTALPDVTLRQLMR
>NZ_CP009983.1|WP_005464972.1|64384_65254_+|LysR-family-transcriptional-regulator
MANWEGVSEFVAVAETNSFTGAAAKLKTSVAQISRRVSALEERLAVKLLHRTTRKVSLSEAGQLYYQQCKHLVEGLELAELAVTQMQTEPRGLLRVTAPVTYGEMNLAPLLHQFLEKYPRVDLDLVLTNQKLDLIEQGVDVAIRLGRLQDSSMIAKRLSSRQTYVCASPMYLERFGEPHTLSELGRHQCLVGSVDYWHFKENKRDKSLRVSGRIKCNSGFALVDAAKRGLGLVQLPDYYVQEALDSGELVEVLTDYRDDREGIWALYPQSRNLSPKVRLLIDFLAQELA
>NZ_CP009983.1|WP_025501292.1|63497_64304_+|arylamine-N-acetyltransferase
MNKTDLNAYLTKLGLPSELPADLESLHKIHVAQHRCLPFENFDISLQRGISVEIEDIIQKTVYHSRGGYCFELNGLMLDVLKTLGFEARSLLGRVHVMGTPTGRSHQITLVTLDEQAWIVDVGFGSNTPRAPLPFILNQVIQTDLQTFRFVEDAQFGYFLQVLSTDGTDTWNNLYSFDLEFVFAGDIACGNFFTSTSPHSRFTSARVAAKATESGLVTLLNYTLKYTSEGEQTELELEPGQAYLDALKEYFGIELDAQYGDLRPLPDA
>NZ_CP009983.1|WP_005464962.1|62055_63204_-|S-(hydroxymethyl)glutathione-dehydrogenase/class-III-alcohol-dehydrogenase
MTLEIKPGQTHIKSKAMVAWAAGEPLKMEEVDVQLPKAGEVLVRIVATGVCHTDAFTLSGDDPEGIFPSILGHEGGGIVEMVGEGVTSVEVGDHVIPLYTAECGECKFCKSGKTNLCQAVRETQGKGLMPDGTSRFSINGETIFHYMGCSTFSEYTVLPEISLAKVNKQAPLEEVCLLGCGVTTGMGAVLNTAKVEKGDTVAIFGLGGIGLSAIIGARMAGASRIIGIDINESKFDLAKQLGATDVINPQKFDKPIQEVIVEMTDGGVDYSFECIGNVNVMRQALECCHKGWGESVIIGVAGAGQEISTRPFQLVTGRVWRGSAFGGVKGRSELPEIVNRYMAGEFGLQEFITHTMGLEDVNKAFDLMHEGKSIRTVIHMDK
>NZ_CP009983.1|WP_005464966.1|61154_61994_-|S-formylglutathione-hydrolase
MTIENVSQTKVFGGWHKQYTHDSKALNCTMRFAIFLPPNATKSNPVPALYWLSGLTCTDENFMQKAGAFRMAAELGIAIIAPDTSPRGEGVADDASYDLGQGAGFYLNATQAPWSLHYHMYDYVTQELPAIIEANFPVSDVKSISGHSMGGHGALTIGLKNPTLYRSISAFSPISNPMQCPWGQKAFTAYLGTDIESWKQYDASELLKKEKSPLPILVDQGDADGFLSEQLKPEVLLAAAKQHGSELNLRMQSGYDHSYYFISSFIDNHLNFHAKYLFA
>NZ_CP009983.1|WP_005482833.1|60247_60709_-|oxidoreductase
MKKIVSLSLLLFAPFLSANSITFSSPQQPSVTLKLEELQSLPTTSYTTDLPWIQQSSEFLGVKLSTLLTHVYGSIPEQVDIGSLNNYHSTLSRKDIVRYQPILAYQQDHHYIKVRNKGPYWVIYPLSQYPELDHNEYHAQMVWQVNEMKIKQK
>NZ_CP009983.1|WP_005464959.1|59156_60248_-|GGDEF-domain-containing-protein
MKLSEAYPIKQKNYSTTSKMLLLVFATSLLLANVILLQQTRVLAQSFTDEQKQATWFLFQLSKELSELVSEARRLDENVLKIEGAELQYELAWSRFDLLINSKDVYTFFSRNHIQQYFLQLFNEFKELEPLLVEAKTGDSQAAAQFYRATQTLYLNLVEFVNQNFRLTSQVYETQKDESQRLMKAQYMLFATFVLSILSLTYFFYRESHFHRKLALSDPLTGLGNRNALFVTLRNNTRNRTAFSLCLLDLNGFKNVNDTYGHQAGDTVLCEIAKRLKDMNIDSFSTYRMGGDEFAVVIESSDVDAEEAKKHIHSVFDTPVLNANNVSSLSTSIGVAHYPSDSDNVDFLISIADKRMYKMKFQR
>NZ_CP009983.1|WP_031831553.1|58742_59147_-|hypothetical-protein
MMRKFMQVLLLLAVIAAGVLAWVFIPSHETIGQKTLEQALNDDYSLVGHRIYSTDPDAGNRFGYFVLATGQSIEEQEPFLVTSDQFIRMEQTGDNTLSVTVNGRIYQYHNDLWVPKSDGKLQHFLVSATAKYVR
>NZ_CP009983.1|WP_005482916.1|68957_69719_+|2-dehydro-3-deoxy-D-gluconate-5-dehydrogenase-KduD
MILDSFNLEGKVAIVTGCDTGLGQGMALGLAKAGCDIVGVNISEPTETIEKVEAEGRKFVDIRANLMKLDDIPTIVDRAVTELGRIDILVNNAGIIRRNDAIEFSEQDWDDVMNINVKSVFFMSQAVAKQFIAQGEGGKIINIASMLSFQGGIRVPSYTASKSGVMGVTRLMANEWASHGINVNAIAPGYMATNNTAALRADEQRNKEIVDRIPAARWGTPEDLAGPCVFLASKAADYINGYTIAVDGGWLAR
>NZ_CP009983.1|WP_005497706.1|69737_70262_+|YgjV-family-protein
MVDTTILAQALGFISFGLGFSVFYQKNDRHLKILMLIFNLNHLLHFLLLGSMVSALSALLSALRTTTAIFVSSKRVAAVFIVISLVSGFWVAEQWRDLWPIIGTVIGTYSVFCLSGIRMRIGFLLGASCWLTNNILVGSIGGTLLEMTVIVMNLLTIYRLHRQQSESMINQSSY
>NZ_CP009983.1|WP_005467181.1|70269_70590_+|cupin-domain-containing-protein
MFVFNQDIPMEDLGEGISRKVLAHSDNMMSVEVHFEEGAIGAMHSHPHEQLTYVLSGEFEFTIGDEKKIVKTGDTMYKEPNIEHGCVCLKAGVLIDTFTPMRKDFV
>NZ_CP009983.1|WP_005460779.1|70630_71266_+|RpiB/LacA/LacB-family-sugar-phosphate-isomerase
MKIALMMENSQAAKNAMVAGELNSVAGGLGHDVFNVGMTDENDHHLTYIHLGIMASILLNSKAVDFVVTGCGTGQGALMSCNLHPGVVCGYCLEPSDAFLFNQINNGNAISLAFAKGFGWAGELNVRYIFEKAFTGKRGEGYPIERAAPQQANAAILNNVKSAVAKDVVEGLRAIDQELVKTAVGSTQFQECFFAHCQVPEIAEYVKSLLD
>NZ_CP009983.1|WP_053047863.1|71343_72255_+|alpha/beta-hydrolase
MHVAPITSLQTWFPEHLVLPLWSEPQIRSHLVQSYQERNPNELLPDRAVFDITHPEMVVFEPEQSNGIGILLMPGGGYQRVSVDKEGADSARVLNQAGFTVFVMTYRMPNEGHEFGAWTPLADAQRAMRLVRQLPLASHLSSIGVLGFSAGGHVAASLATSHALDIYPLQDEVDRVSAKPDFCALMYPVISMNTDIAHMGSRAELLANLEREPDLLRFSLEKQVTSDMPPCFLLHASDDTAVSVENSIVFWQALRQHEIVTEMHLFEQGKHGFGIRDAQGLPVAAWPQLLAAWLQNLAEKARR
>NZ_CP009983.1|WP_005482884.1|72353_73283_+|sugar-kinase
MNPISRVAIIGECMVELKKHDGVLQQGFGGDTLNTAVYLSRLTKQHGVETSYVTGLGHDPFSREMLTAWREEGINTDMVYLSEDKLPGIYAIETAEDGERSFFYWRNDAAAKYWLRERALLSLVKDLCQHQMIYLSGISLAIISDDCRQMLIELLTMCRKEGVKIAFDNNFRPKLWPNIEQARDFYSKILSVTDMAFLTFDDEVMLWGDKHEDEAISRTKNFGVKEIIVKRGADDCFVVTQDQQHTVAALKVDAVVDTTAAGDSFSAGYLAKRILGGDVAESALAGHKVAGTVIQHRGAIIPSQAMPTI
>NZ_CP009983.1|WP_005460834.1|73294_73918_+|bifunctional-4-hydroxy-2-oxoglutarate-aldolase/2-dehydro-3-deoxy-phosphogluconate-aldolase
MKDLNQQLSEIKVVPVIAIKDAGKAVKLAQVLIENGLPCAEVTFRTEDAALAIKNMREAYPEMLIGAGTVLTSAQVDEAIDAGVDFIVSPGFNPTTVKYCQQRNVTIVPGVNNPSLVEQAMEMGLRTLKFFPAEPSGGVAMLKALSAVYPVKFMPTGGVSPSNVKDYLSISSVLACGGTWMVPGDLIDNEQWDELAKLVREVAGIIE
>NZ_CP009983.1|WP_053047864.1|74103_75843_-|transporter
MTLLDSMIVMIYLLFIGIAAWLFRRFSTSSNDFLQGGGTMMWWMAGATAFMTQFSAWTFTGAAAKAYEDGISVMFIFWGNALRFFVAAAFFARRYRRLRVETAMEVIRVRFGHTSEQLFTWLSFPLTLIACAIWMNGLASFFSAVFAIEMSTTILAMGVIVTLIAVSGGAWTVSVTNVIQLVLLIGITLVIGYTALQHFDSPSEVFAYTTPIYGEQIRMPSLFVMWAIAMLLQQTMSNNHTLSCYRFLTTANDKGATKAAFVAGVLFVFAPVLWFMPAWFVAAQNIDLLAIYPALEQSANNAAYLYYIQHYMPQGLLGLVMVALVAATIAPLSSAHNRNAGIVVKSLYQVWFNPNATSRQQLMVGKIATIVSGVLATVTALLLASVESYSLFDMMIVFAAFIQMPINIPSLLALVSLQTPNWSGWATVMVGCAVSLFMMFIFDVQWISSSPLTPRESKDLSVVATLAVHLLVTGGFFLFTRVFYAKEPPSIQQSRTALAIQLATPISDEEQSPINHKQGLYVGSITALAGMLLILAGVVLAGSSQSIFVAIGCIVLLFSLFLLQPTLHSKRAWQKQKTK
>NZ_CP009983.1|WP_005482845.1|75972_76650_+|porin
MKVRYLTSALLLAMTSGLAAAASVDIRHEYVPDRDGDEHRDRIYVSHRFDNQIGFSVEAKWNYKDGHMGNAGHETGVSYRWKATDNFSLTPGINIDASPSGASVFKYNLTGAYKINDEWDVAARIRHGYKNTDDSRYNQLNLYANRKFEWGKLGVEAEYKDIHGGEGGWKDKGHDQLIDFKGEYTKLESGVIPFFAIAAITHKGDGSEFKDEYVPRFRVGLKYNF
>NZ_CP009983.1|WP_021821224.1|76665_78894_+|hypothetical-protein
MKKHTLALCLAAILAPAAHAAEIKVEDLTWKAITFGQSTDMNFGSTILPEKVGVNQVTVNGEAVAAGKLASTFTIESRGGKLANSHEGLTFYYTELPTDVNFTLSADVVLEQLGPETGATPNRQEGAGLMVRDILGAERLVPQPEGHEEFPSASNMVMNLMRSHTRTNDGMTNINASFREGVYQPWGTPGNRLSRVDYVEGVPYGTAETYRMTLTRTNDGFKVSYRNGEKFVEQAVKGANANIVEMQNSDSQYVGFFASRNAKMTVSNVDLQLAAADTVDAPKYAAKQGELVFQIASSPRSATKEYPVQARANYSGEFEVLHNGKVVAKQTVTAGELFSQWLTLDSGANQMEVRFTAIDGPNKETQAHRYSVDVVSLPDPMTLYVAPNGSDKGNGSQAQPLDLATAVELLPAGGTIILKDGDYQGMEIPLTASGSVDKLKHLRAEGDNVRFVSELRHEANYWHYQGIEVAGAQFIVHGSHNTFEKMVTHGAPDTGFVITSPENIGRALWASYNQVIESESYNNMDPSQINADGFAAKMRIGDGNTFIRCLSHHNIDDGWDLFNKVEDGANGAVTILDSISFSNGRTLDVANKGGTIGNGFKLGGEGIPVPHVVKNSLSFNNNMDGFTDNFNPGALVLSDNVSIDNKRFNYLFRKSPYSGEIEQGTFTNNRSYRFHVSSKYDDVINSAKSTGNALVENGTTYTSDGKAVDSKMLAPLKQASVIDTQQAIPGKQEAMQLKQLIH

You can click texts colored in the table to view more detailed information

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

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

939686 : 947758

Vibrio_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_053048103.1\|939686_940055_-	hypothetical protein	R9TE55	Vibrio_phage	1.8e-42	71.1
WP_046875305.1\|940181_940400_+	hypothetical protein	A0A1W6UGD1	Vibrio_phage	3.3e-31	94.3
WP_071936901.1\|940323_941532_+	phage replication protein	Q7DKP2	Vibrio_phage	5.2e-243	98.8
WP_017822035.1\|941535_941889_+	DUF1293 domain-containing protein	A0A1W6UG87	Vibrio_phage	2.2e-61	100.0
WP_017822034.1\|941900_942146_+	hypothetical protein	A0A1W6UH23	Vibrio_phage	2.6e-37	98.8
WP_017447548.1\|942156_942390_+	membrane protein	A0A1W6UG80	Vibrio_phage	1.7e-30	98.7
WP_053048104.1\|942523_943999_+	methyl-accepting chemotaxis protein	A0A1W6UG63	Vibrio_phage	2.0e-209	95.9
WP_017822026.1\|944000_944315_+	DUF2523 domain-containing protein	A0A1W6UG81	Vibrio_phage	6.1e-47	100.0
WP_053048105.1\|944311_945454_+	assembly protein	O88128	Vibrio_phage	2.5e-215	99.7
WP_053048106.1\|945854_946859_+	DUF4238 domain-containing protein	NA	NA	NA	NA
WP_053048107.1\|946868_947168_+	hypothetical protein	NA	NA	NA	NA
WP_053048108.1\|947193_947559_-	phage protein	Q9MCC4	Vibrio_phage	6.9e-50	79.3
WP_153884739.1\|947536_947758_-	hypothetical protein	Q9MCC3	Vibrio_phage	1.9e-23	79.2

DBSCAN-SWA_2

1210007 : 1217149

Vibrio_phage(66.67%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_025558364.1\|1210007_1210682_-	Rha family transcriptional regulator	K7PLX4	Enterobacteria_phage	1.1e-27	60.6
WP_025558366.1\|1211194_1211458_+	hypothetical protein	NA	NA	NA	NA
WP_025558368.1\|1212130_1212430_+	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_025558370.1\|1213037_1213235_-	hypothetical protein	A0A2I7RNJ8	Vibrio_phage	4.9e-18	75.4
WP_053048182.1\|1213234_1214002_-	hypothetical protein	A0A2I7RNK2	Vibrio_phage	7.6e-107	74.0
WP_053048183.1\|1213992_1214682_-	hypothetical protein	A0A2I7RNK1	Vibrio_phage	8.6e-118	86.5
WP_025558373.1\|1214695_1215232_-	hypothetical protein	A0A2I7RNK5	Vibrio_phage	3.0e-78	85.9
WP_153884738.1\|1215235_1217149_-	hypothetical protein	I2GUG1	Acinetobacter_phage	3.9e-11	25.0

DBSCAN-SWA_3

1220787 : 1245640

Vibrio_phage(71.43%)

integrase,terminase,head,tail,capsid,portal

attL 1231146:1231160|attR 1250333:1250347

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_053048186.1\|1220787_1221051_-	hypothetical protein	A0A2I7RNJ9	Vibrio_phage	2.0e-30	78.3
WP_053048187.1\|1221059_1221284_-	hypothetical protein	A0A1D9C9R8	Salinivibrio_phage	4.7e-09	42.5
WP_025558380.1\|1221286_1221517_-	hypothetical protein	NA	NA	NA	NA
WP_053048188.1\|1221516_1222026_-	hypothetical protein	A0A2I7S7C4	Vibrio_phage	1.9e-21	41.7
WP_025558382.1\|1222022_1222232_-	molecular chaperone DnaK	A0A2I7RNJ6	Vibrio_phage	2.0e-17	70.6
WP_053048189.1\|1222259_1222715_-	DUF2597 family protein	A0A2I7RNI0	Vibrio_phage	3.1e-76	93.4
WP_053048190.1\|1222718_1223759_-	DUF2586 family protein	A0A2I7RNI8	Vibrio_phage	7.2e-169	79.5
WP_053048191.1\|1223774_1224431_-	virion morphogenesis protein	A0A2I7RNI6	Vibrio_phage	5.1e-104	87.2
WP_053048192.1\|1224414_1224909_-\|tail	phage tail protein	A0A2I7RNH2	Vibrio_phage	2.4e-82	93.2
WP_025558387.1\|1224905_1225325_-\|head	head protein	A0A2I7RNH7	Vibrio_phage	9.4e-43	61.2
WP_025558388.1\|1225446_1226157_-\|terminase	terminase	A0A2I7RNJ0	Vibrio_phage	4.7e-71	55.8
WP_025558389.1\|1226160_1227165_-\|capsid	phage major capsid protein, P2 family	R9TPZ5	Vibrio_phage	5.8e-99	59.3
WP_053048193.1\|1229997_1231005_+\|portal	phage portal protein	A0A1D9C9P9	Salinivibrio_phage	9.9e-115	60.1
1231146:1231160	attL	NA	NA	NA	NA
WP_025558391.1\|1231528_1232629_+	hypothetical protein	NA	NA	NA	NA
WP_071936904.1\|1232686_1232938_+	ogr/Delta-like zinc finger family protein	R9TNQ2	Vibrio_phage	1.7e-28	73.5
WP_053048194.1\|1232888_1233872_-	hypothetical protein	NA	NA	NA	NA
WP_025558393.1\|1233880_1234099_-	hypothetical protein	Q8HA64	Vibrio_phage	1.1e-13	58.3
WP_082241199.1\|1234226_1235870_-	replication endonuclease	A0A2P1CKY6	Pseudoalteromonas_phage	2.8e-66	37.7
WP_053048195.1\|1235869_1236148_-	hypothetical protein	NA	NA	NA	NA
WP_053048196.1\|1236222_1236711_-	hypothetical protein	NA	NA	NA	NA
WP_025558397.1\|1236718_1236949_-	hypothetical protein	A0A2I7RNG5	Vibrio_phage	2.3e-19	59.2
WP_025558398.1\|1237053_1237335_-	hypothetical protein	NA	NA	NA	NA
WP_025558400.1\|1237998_1238211_-	hypothetical protein	U3PFJ1	Vibrio_phage	1.9e-12	51.4
WP_025558401.1\|1238302_1238929_+	phage repressor protein CI	A0A1D9C9M6	Salinivibrio_phage	4.5e-33	36.2
WP_053048197.1\|1238932_1239508_+	GIY-YIG nuclease family protein	A0A140B3N4	Vibrio_phage	1.5e-06	40.9
WP_053048198.1\|1239517_1241731_+	GHKL domain-containing protein	NA	NA	NA	NA
WP_053048199.1\|1241741_1242851_+	hypothetical protein	NA	NA	NA	NA
WP_053048200.1\|1242853_1244377_-	DNA cytosine methyltransferase	M1PSQ0	Streptococcus_phage	6.3e-20	24.5
WP_053048201.1\|1244608_1245640_+\|integrase	tyrosine-type recombinase/integrase	E5G6L0	Salmonella_phage	3.4e-94	50.4
1250333:1250347	attR	NA	NA	NA	NA

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_CP009982

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

539678 : 556861

uncultured_Mediterranean_phage(20.0%)

tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_005455581.1\|539678_541319_+	CTP synthase	A0A1J0FA14	Only_Syngen_Nebraska_virus	4.2e-155	52.4
WP_005455579.1\|541397_542699_+	phosphopyruvate hydratase	A0A1X9I5Z8	Streptococcus_phage	4.2e-134	59.2
WP_031849042.1\|543112_543394_+	cell division protein FtsB	NA	NA	NA	NA
WP_005478544.1\|543395_544100_+	2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase	A0A2H4UTB4	Bodo_saltans_virus	5.9e-05	23.6
WP_005380896.1\|544117_544594_+	2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase	NA	NA	NA	NA
WP_053046852.1\|544640_545684_+\|tRNA	tRNA pseudouridine(13) synthase TruD	NA	NA	NA	NA
WP_005478553.1\|545683_546460_+	5'/3'-nucleotidase SurE	A0A1B1ITZ2	uncultured_Mediterranean_phage	5.0e-66	52.4
WP_005455562.1\|546459_547086_+	protein-L-isoaspartate(D-aspartate) O-methyltransferase	A0A1B1IU40	uncultured_Mediterranean_phage	1.3e-35	52.1
WP_005455560.1\|547100_548024_+	peptidoglycan DD-metalloendopeptidase family protein	D7RWE0	Brochothrix_phage	4.1e-06	35.2
WP_025579176.1\|549172_551734_-	DNA mismatch repair protein MutS	A0A1V0SC35	Catovirus	2.2e-33	23.7
WP_053046854.1\|551818_552301_+	nicotinamide-nucleotide amidase	B5TK85	Pseudomonas_phage	2.9e-27	48.7
WP_005478550.1\|552501_553545_+	recombinase RecA	A0A2D1GPX2	Mycobacterium_phage	8.1e-112	60.7
WP_005455548.1\|553668_554136_+	recombination regulator RecX	NA	NA	NA	NA
WP_005455546.1\|554278_556861_+\|tRNA	alanine--tRNA ligase	A0A1V0SK38	Klosneuvirus	1.0e-78	37.9

DBSCAN-SWA_2

2544815 : 2551516

Staphylococcus_phage(50.0%)

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_005440184.1\|2544815_2545286_-	6,7-dimethyl-8-ribityllumazine synthase	A0A2H4PQS3	Staphylococcus_phage	1.7e-32	49.3
WP_005496254.1\|2545455_2546565_-	bifunctional 3,4-dihydroxy-2-butanone-4-phosphate synthase/GTP cyclohydrolase II	A0A2H4PQS2	Staphylococcus_phage	1.5e-63	39.6
WP_005483039.1\|2546734_2547388_-	riboflavin synthase	A0A2H4PQS5	Staphylococcus_phage	1.6e-33	37.5
WP_017448802.1\|2547400_2548525_-	bifunctional diaminohydroxyphosphoribosylaminopyrimidine deaminase/5-amino-6-(5-phosphoribosylamino)uracil reductase RibD	A0A1V0SE20	Indivirus	4.0e-48	36.0
WP_005482986.1\|2548532_2548982_-	transcriptional regulator NrdR	NA	NA	NA	NA
WP_029854872.1\|2549108_2550359_-	glutamate-5-semialdehyde dehydrogenase	A0A1X9I5D4	Streptococcus_phage	2.1e-98	47.9
WP_025500012.1\|2550376_2551516_-	glutamate 5-kinase	A0A1X9I5D0	Streptococcus_phage	1.3e-62	41.7

Anti-CRISPR protein detection

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

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_CP009983

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

2. NZ_CP009982

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