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_CP008924	Corynebacterium pseudotuberculosis strain Ft_2193/67 chromosome, complete genome	1 crisprs	csa3,DEDDh,cas5,cas3,WYL,cas4	0	0	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP008924_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP008924_1

26811-26899

Orphan

I-C,I-E,II-B

Consensus_repeat	Method
CTTTTCTCCGCGCACGCGGAGGTAGTTC	CRISPRCasFinder

1 spacers

DinG

The CRISPR arrays of NZ_CP008924_1

>merge|NZ_CP008924|1|26811-26899|CRISPRCasFinder
CTTTTCTCCGCGCACGCGGAGGTAGTTCCGGTGTTGGGTATGTATGCTGATCCGTCTGGTTCTTTTCTCCGCGCACGCGGAGGTAGTTC

>NZ_CP008924|1|1|26811-26899|CRISPRCasFinder
CTTTTCTCCGCGCACGCGGAGGTAGTTC	CGGTGTTGGGTATGTATGCTGATCCGTCTGGTT
CTTTTCTCCGCGCACGCGGAGGTAGTTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP008924.1\|WP_013242518.1\|21311_22670_+\|nicotinate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|236426
NZ_CP008924.1\|WP_013242516.1\|20175_20712_-\|DUF2017-domain-containing-protein	unknown	unknown	gnl\|CDD\|378185
NZ_CP008924.1\|WP_013242523.1\|29111_30833_-\|cytochrome-c-oxidase-subunit-I	unknown	unknown	gnl\|CDD\|238832
NZ_CP008924.1\|WP_013242520.1\|24739_25237_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379112
NZ_CP008924.1\|WP_013242528.1\|36164_36398_-\|glutaredoxin-like-protein-NrdH	unknown	unknown	gnl\|CDD\|131249
NZ_CP008924.1\|WP_013242526.1\|33291_35451_-\|class-1b-ribonucleoside-diphosphate-reductase-subunit-alpha	unknown	unknown	gnl\|CDD\|236179
NZ_CP008924.1\|WP_032802571.1\|20805_21105_-\|ATP-dependent-Clp-protease-adapter-ClpS	unknown	unknown	gnl\|CDD\|178809
NZ_CP008924.1\|WP_013242527.1\|35601_36039_-\|class-Ib-ribonucleoside-diphosphate-reductase-assembly-flavoprotein-NrdI	unknown	unknown	gnl\|CDD\|179603
NZ_CP008924.1\|WP_013242519.1\|22721_24716_+\|ATP-dependent-DNA-helicase	DinG	COG1199_DinG_CAS-IV-A	gnl\|CDD\|224120
NZ_CP008924.1\|WP_038615656.1\|25233_26517_-\|phosphoserine-phosphatase-SerB	unknown	unknown	gnl\|CDD\|319803
NZ_CP008924.1\|WP_014401348.1\|27753_27978_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP008924.1\|WP_032802570.1\|16690_17425_-\|ribonuclease-PH	unknown	unknown	gnl\|CDD\|178914
NZ_CP008924.1\|WP_014300909.1\|28279_28915_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP008924.1\|WP_014300907.1\|26916_27420_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|379154
NZ_CP008924.1\|WP_014367533.1\|32733_33219_+\|ferritin	unknown	unknown	gnl\|CDD\|153113
NZ_CP008924.1\|WP_013242513.1\|17463_18231_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293802
NZ_CP008924.1\|WP_042437289.1\|31301_32324_-\|class-1b-ribonucleoside-diphosphate-reductase-subunit-beta	unknown	unknown	gnl\|CDD\|275027
NZ_CP008924.1\|WP_038615653.1\|18303_19197_-\|glutamate-racemase	unknown	unknown	gnl\|CDD\|234851
NZ_CP008924.1\|WP_013242515.1\|19270_20089_-\|rhomboid-family-intramembrane-serine-protease	unknown	unknown	gnl\|CDD\|366759
NZ_CP008924.1\|WP_014300910.1\|31006_31186_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP008924.1\|WP_013242518.1\|21311_22670_+\|nicotinate-phosphoribosyltransferase	gnl\|CDD\|236426	PRK09243, PRK09243, nicotinate phosphoribosyltransferase; Validated.	0
NZ_CP008924.1\|WP_013242516.1\|20175_20712_-\|DUF2017-domain-containing-protein	gnl\|CDD\|378185	pfam09438, DUF2017, Domain of unknown function (DUF2017). This is an alpha-helical domain found in gene neighborhoods that contain genes encoding ubiquitin, cysteine synthases and JAB peptidases.	1.38837e-72
NZ_CP008924.1\|WP_013242523.1\|29111_30833_-\|cytochrome-c-oxidase-subunit-I	gnl\|CDD\|238832	cd01662, Ubiquinol_Oxidase_I, Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.	0
NZ_CP008924.1\|WP_013242520.1\|24739_25237_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	3.30578e-23
NZ_CP008924.1\|WP_013242528.1\|36164_36398_-\|glutaredoxin-like-protein-NrdH	gnl\|CDD\|131249	TIGR02194, Glutaredoxin-like_protein_NrdH, Glutaredoxin-like protein NrdH. NrdH-redoxin is a representative of a class of small redox proteins that contain a conserved CXXC motif and are characterized by a glutaredoxin-like amino acid sequence and thioredoxin-like activity profile. Unlike other the glutaredoxins to which it is most closely related, NrdH aparrently does not interact with glutathione/glutathione reductase, but rather with thioredoxin reductase to catalyze the reduction of ribonucleotide reductase.	1.51252e-32
NZ_CP008924.1\|WP_013242526.1\|33291_35451_-\|class-1b-ribonucleoside-diphosphate-reductase-subunit-alpha	gnl\|CDD\|236179	PRK08188, PRK08188, ribonucleotide-diphosphate reductase subunit alpha; Validated.	0
NZ_CP008924.1\|WP_032802571.1\|20805_21105_-\|ATP-dependent-Clp-protease-adapter-ClpS	gnl\|CDD\|178809	PRK00033, clpS, ATP-dependent Clp protease adaptor protein ClpS; Reviewed.	6.42082e-37
NZ_CP008924.1\|WP_013242527.1\|35601_36039_-\|class-Ib-ribonucleoside-diphosphate-reductase-assembly-flavoprotein-NrdI	gnl\|CDD\|179603	PRK03600, nrdI, class Ib ribonucleoside-diphosphate reductase assembly flavoprotein NrdI.	2.30734e-77
NZ_CP008924.1\|WP_013242519.1\|22721_24716_+\|ATP-dependent-DNA-helicase	gnl\|CDD\|224120	COG1199, DinG, Rad3-related DNA helicases [Transcription / DNA replication, recombination, and repair].	2.85406e-153
NZ_CP008924.1\|WP_038615656.1\|25233_26517_-\|phosphoserine-phosphatase-SerB	gnl\|CDD\|319803	cd07500, HAD_PSP, phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p. This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	1.59046e-94
NZ_CP008924.1\|WP_032802570.1\|16690_17425_-\|ribonuclease-PH	gnl\|CDD\|178914	PRK00173, rph, ribonuclease PH; Reviewed.	5.09274e-164
NZ_CP008924.1\|WP_014300907.1\|26916_27420_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|379154	pfam13384, HTH_23, Homeodomain-like domain.	1.0561e-05
NZ_CP008924.1\|WP_014367533.1\|32733_33219_+\|ferritin	gnl\|CDD\|153113	cd01055, Nonheme_Ferritin, nonheme-containing ferritins. Nonheme Ferritin domain, found in archaea and bacteria, is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The ferritin protein shell is composed of 24 protein subunits arranged in 432 symmetry. Each protein subunit, a four-helix bundle with a fifth short terminal helix, contains a dinuclear ferroxidase center (H type). Unique to this group of proteins is a third metal site in the ferroxidase center. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite.	3.42302e-58
NZ_CP008924.1\|WP_013242513.1\|17463_18231_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293802	cd07716, RNaseZ_short-form-like_MBL-fold, uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain. The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.	4.17064e-75
NZ_CP008924.1\|WP_042437289.1\|31301_32324_-\|class-1b-ribonucleoside-diphosphate-reductase-subunit-beta	gnl\|CDD\|275027	TIGR04171, ribonucleotide-diphosphate_reductase_subunit_beta, ribonucleoside-diphosphate reductase, class 1b, beta subunit. Members of this family are NrdF, the beta subunit of class 1b ribonucleotide reductase. This form uses a dimanganese moiety associated with a tyrosine radical to reduce the cellular requirement for iron. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism].	0
NZ_CP008924.1\|WP_038615653.1\|18303_19197_-\|glutamate-racemase	gnl\|CDD\|234851	PRK00865, PRK00865, glutamate racemase; Provisional.	1.88044e-132
NZ_CP008924.1\|WP_013242515.1\|19270_20089_-\|rhomboid-family-intramembrane-serine-protease	gnl\|CDD\|366759	pfam01694, Rhomboid, Rhomboid family. This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.	2.8809e-23

>NZ_CP008924.1|WP_038615656.1|25233_26517_-|phosphoserine-phosphatase-SerB
MIELDQPQVTVSLRPELTPAVITISGQDRQGVSAAAFRVLAANGVQILDVEQSQFRGFLGLAVFAGVEASKVEIFEIGLKETLKTYGQNVKIELQEVAQSSRPRSTHEVVILGNPVEAHDLSRVAQTLANFDANIDTIRGISDYPVTGLELKITVAKREPGAAMPLRKALAELTAELGVDIAIERAGLLRRSKRLICFDCDSTLITGEVIEMLAAHAGREKEVAEVTERAMSGELDFEESLRERVKALAGLDASVIGEVADSIELTPGARTTIRTLKRLGYKTAVVSGGFIQVLEELAEDLGLDYVRANTLEVVDGKLTGRVIGKIVDRAAKAEFLEEFARESGIEMHQTVAVGDGANDIDMISAAGLGIAFNAKPALREIADTSVNSPFLDEVLHMLGITRADIDAADDSEGKIRRVPLPQQKNEY
>NZ_CP008924.1|WP_013242520.1|24739_25237_+|GNAT-family-N-acetyltransferase
MTAHVPTLSNDSVKLRPLLLSDAHDLTATCRDPLTQKYTTVPANYTFAMAEEFIKTEHDNLRWVITVPTSDRFCGQIELRSLAIEHNAMNVGYMTAPWARGQGLMTSALLLAVDYAFSRSVRRIELQADSQNKASQRVAEKAGFILIDSSQDTMVYSLLADEYHS
>NZ_CP008924.1|WP_013242519.1|22721_24716_+|ATP-dependent-DNA-helicase
MLDATSTLCPMSDSPLALSTDELLDAAVAALGGSRRNGQVSMANAVTKALESERHLAVQAGTGTGKSLAYLVPALRHAQATDSTIIVSTATIALQRQLVERDLPRLADALEPHMSRRPTFAIMKGRANYVCMNKIAAAEEPEDALIDEEDLSWLGKHVARIYEWANETEVGDRDSLDPGVPDLAWRQVSVNAQECIGASRCPHGEECFAELARKKAHDVDVIVTNHALLAIDALSDVNVLPEHEVVIVDEAHELDGRITAVATNEIGVTALTMSSRRAGKLGAGEKDQKLIDIAKEWEDAMLAIEPGRLTSLPDYLKQQTVALRDAIWSLREHISRVPEGEAANDPERHAERMSLSNHLNDQHDSVIRVLSVFEEEDAASQEDVVWVLHDERRGVMIKVAPLSIAGLLHTRLFSENTVVLASATLNIGGNFNAMAASWGLPKGSWDSLDAGTPFNPATSGILYTPNSLPDPGRDGLSPEVLDEIYELIMAAGGRTLGLFSSRRAAQQATDAMRTRLPFDVLCQGDDTTGALVEKFSKQENTCLFGTLSLWQGVDVPGRSCSLVIIDRIPFPRPDDPLLQARKDAADADGRNGFMEVAATHAALLIAQGAGRLLRSVTDRGVVAILDRRIVTKRYGAFFIRSLPAFWRTNDPQVVRGALSRLVAR
>NZ_CP008924.1|WP_013242518.1|21311_22670_+|nicotinate-phosphoribosyltransferase
MSCASALSVFKAKLVCVTEFESTALLTDMYELTMLQSALADGTASRSCTFEVFSRRLPNERRYGVVAGTARVLEAIKHYRFTEEQLASLTFLDATTIDFLRSYKFQGQIDGYREGELYFPSSPILTIRGTFAECVILETLILSIMNADSAVASAAARMVTAADGRPIFEMGSRRTHEYAAVTAARAAYLAGFVGTSNLEAVHRYGIPGSGTAAHAWTLLHVNDDGTPNESAAFQSQINVLGVGTTLLVDTYDIAKGVKTAIEVAGPQLGAVRIDSGDLGVMTRKVRQELDSLGAHNTGIVVSSDLDEYAIAGLRGNPVDAFGVGTSVVTGSGAPTAGMVYKLVEVDGHPVAKRSRGKAMVGGTKRAIRTHRATGTAVEEIVFPYDHDTPQIGQLNSYELAIPLMRNGIAVDNLPTLEESRAYLAEQLITLPWEGLALSKDEPVLSTRFIGFK
>NZ_CP008924.1|WP_032802571.1|20805_21105_-|ATP-dependent-Clp-protease-adapter-ClpS
MSSPMATPELDEALSVDVASSENLPWMCIVWDDPVNLMSYVTYVFQTILGYSKRRAIELMMQVHTEGKAVVSSGERDKVEGDVKKLHTAGLWATMQQGG
>NZ_CP008924.1|WP_013242516.1|20175_20712_-|DUF2017-domain-containing-protein
MQPWKKKKGLMRGVHFACVFEPMEREVLGNLASTVSEALIHRAQSAPKDELAELTGMPSGHKEAPKDPALARLLPDFEKEGDEEFEGDNSLLRCLHETDITRAKIEHLYVLGQALGPDGGVHVDITETEAHAWVAALNDIRLYVASGEVFGEDAEQDRESLVEWLAYNQESLLNAMMG
>NZ_CP008924.1|WP_013242515.1|19270_20089_-|rhomboid-family-intramembrane-serine-protease
MSLRYFFTRLCFIMTNRFNPYAQSDKKTYGGVSTSGGYLPHEYGTQYLPTSDYPVNRAVQRGVKRTSLCSMGRKRLADATVLALGYVVVIWAVHIVNTVFFGGTLAQELGVHPLDGSSIWHIFTSPLVHGSYMHISANTLPGLIFVFLIGLSGRRPFWEVTMITAVVGGMGTWIFGGIGTTHIGASGLIYGWLAYLVVRGIFNKSFSQVVLGVVLAFMYGGLIWGVLPGDVGVSWQAHLFGAIGGLIAGATITSDDPPALKARREQQALHRV
>NZ_CP008924.1|WP_038615653.1|18303_19197_-|glutamate-racemase
MAYVKKDLGADSLHPEAPSVKPSVVYEGTIDASSPIGIFDSGVGGLTVARAIMEQLPQESVIYIGDTANSPYGSKPIAQVRELSMRIGDELVARGCKMIVIACNTATSAALRDLRERYSVPVVGVILPAVRRAVAATRNGKIGVLGTQGTIASGAYQELFAASPGVEVYAQACPSFVSFVERGITSGRQILGVAQGYTEGLQSAGVDTLVLGCTHYPLLTGVIQLAVGDNVTLISSSEECVKDVLKVLSRNDMLAEATADKPPSRSFESTGDPALFEQLAMRFLGPHVTYVEKLREV
>NZ_CP008924.1|WP_013242513.1|17463_18231_-|MBL-fold-metallo-hydrolase
MKLTILGSSGSLGAPDNAASGYLIQMDNAPSILMDMGPGVLAQLERAQNPSDAHVVFSHLHADHCVDFPSLLVWRRYHPTAAAKGRNLCFGPTDTPVRLGRLSADSVDNIDDMSDTFAFTPWQNAKEELVGAVSITPYSVVHPIESFALRVEHKRSGKVVAYSGDSSYTENLIECARDADVFLCEATWGETSEGKVPNMHMSGEEAGRIARIAGAKRLILVHIPPWGNAKAALEKARSEFDGPVDISYQGMEIHI
>NZ_CP008924.1|WP_032802570.1|16690_17425_-|ribonuclease-PH
MTTSNFKRADGRAVDQMRTVKITRGFTTNPAGSVLVEFGNTRVMCTASAEIGVPRFKRDSGEGWLTAEYAMLPAATLDRNPRESMRGKVKGRTHEISRLIGRSLRAAVDLSELGENTINIDCDVLQADGGTRTASITGAYVALADAISHLQKQGVVPGNPLKDPVAAVSVGVIDGAVCLDLPYEEDSRADVDMNVIMQNGRFVEIQGTGEHNTFDRDELARILDFAEKGCTELVAAQKAALGIA
>NZ_CP008924.1|WP_014300907.1|26916_27420_-|helix-turn-helix-domain-containing-protein
MAKKHTFNKVIIDTIHATGITHTQAAEMFGVSTRWIRELLHRYNTGGYQALEPQSRCPHTSPRAITDDIIDSAGKVSLRWAGESKKLYIGTRYAGMPIILVCLNNKITAVNPETTEILGRYLLEKGRSYHRNLLKDPHQPNPDKKKSLETSNRNDVSRLHRKAPSGT
>NZ_CP008924.1|WP_014401348.1|27753_27978_+|hypothetical-protein
MGSSSPCEGGGVLCYPQKINPRRIYIMDRAENTTEQVTPTLDHAAANASSQDKEPDTPPETFDRKYVETLTRGS
>NZ_CP008924.1|WP_014300909.1|28279_28915_+|hypothetical-protein
MKKSKLFLCMALTTSLATASIPATAQESDPITKPWLFKKCEGFSVAIQSVHLKDKDQSRVPRWLRAKPNLGDTVKVQFKVTNNSYSNNADATYPKEEGNAYLVDDPLSVRNGVGVTIKPNPIYAWSNTDQKRNFILGRGDSVTVTYNHTITEQDLTNRGIPDGPNYPISNSGTATPVCTISPGITYSWSPLSHFFPWLAGFLRSITSFFSR
>NZ_CP008924.1|WP_013242523.1|29111_30833_-|cytochrome-c-oxidase-subunit-I
MTAVAPRLEDYSEPTRPAPTGGARKGTLAWKMLTTTDHKQLGIMYIIMSFVFFFLGGLMALLIRAELFSPGLQYLSNEQFNQLFTMHGTVMLLLFGTPIVWGFANYILPLQIGAPDVAFPRLNAFGFWVTMIGAAAMLSGFLTPGGAADFGWTMYLPLADSIHSPGIGSDMWIVGVGATGVGTISSAINMITTILCMRAPGMTMFRMPIFCWNIFVASVLVLMIFPLLTAAALGVLYDRKLGGHLFDPGNGGAIMWQHLFWFFGHPEVYVLALPFFGIVSEIVPVFARKPMFGYIGLVFATLSIGSLSMAVWAHHMFVTGAILLPFFSFMTFLISVPTGVKFFNWLGTMWKGHVSWETPMTWTMGFLVTFLFGGLTGIMLASPPLDFHISDTYFVVAHFHYTLFGTVVFASFAGVYFWFPKMTGRMLDERLGKIHFWITFVGFHGTFLVQHWLGNEGMPRRYADYLDSDGFTTLNQISTIFSFLLGMSVLPFIWNVIKSWRYGEVVTVDDPWGYGNSLEWATSCPPPRHNFTSLPRIRSERPAFELHYPHMVERMRREAHVGHHVEPVTVKAK
>NZ_CP008924.1|WP_014300910.1|31006_31186_-|hypothetical-protein
MLWGGKGELTLYSSFGLITAGGEVGELVGVMYKYVPTLLCGAYHWNYLENAVFLAELIV
>NZ_CP008924.1|WP_042437289.1|31301_32324_-|class-1b-ribonucleoside-diphosphate-reductase-subunit-beta
MGDESPSRKGETVESYDSYLESHKKPVSAINWNSIPDEKDLEVWDRLTGNFWLPEKVPVSNDLKSWGTLNDLEKTTTMRVFTGLTMLDTIQGTVGAVSMIPDAITPHEEAVYTNIAFMESVHAKSYSNIFMTLASTKEINEAFRWSEENENLQKKAKIVLSYYEGADPLKRKVASTLLESFLFYSGFYLPMYWSSHAKLTNTADIIRLIIRDEAVHGYYIGYKYQQAVREQTPERQEELKEYTFDLLYDLYDNEIQYTEDLYDDLGWTEDVKRFLRYNANKALNNLGYEGLFPADECKVSPAILSALSPNADENHDFFSGSGSSYVIGKAENTTDDDWDF
>NZ_CP008924.1|WP_014367533.1|32733_33219_+|ferritin
MSINEKLAAALNNQITAELEASMVYLQLSYILDDLSLTGMRNWMQAQHKEELDHAAQFSKHLLDRDYRPQIGDIAPPKLDANSAVEAFEASLAHEQKVTAMIRELAEIADSVKDYDSRPLIDRFLEEQIEEEANVKEILDRLRIADTGSGILRIDAELAER
>NZ_CP008924.1|WP_013242526.1|33291_35451_-|class-1b-ribonucleoside-diphosphate-reductase-subunit-alpha
MSQSLGKHVAEPVSRTEQLDYHALNALLNLYNADGKIQFDKDREAANQFFLQHVNQNTVFFHDLEEKIEYLVENNYYEPGIIEKYEFAFIKDLFKQAYAHKFRFKSFLGAYKYYTSYTLKTFDGRRYLERFEDRVCMVALTLADGDQNLARNLVDEIMTGRFQPATPTFLNSGKAQRGEPVSCFLLRIEDNMESIGRSINSALQLSKRGGGVALLLSNLREAGAPIKKIENQSSGVIPVMKLLEDSFSYANQLGARQGAGAVYLNAHHPDILNFLDTKRENADEKIRIKTLSLGVVIPDITFELAKRNDDMYLFSPYDVERVYGKAFADISVSEHYAEMVEDPRIRKSKINAREFFQTIAEIQFESGYPYIMFEDTVNKANPIEGRVNMSNLCSEILQVNTPSLFNDDLTYEEVGEDISCNLGSLNIAMTMDSPDFAKTIETAIRGLTAVSEQTAINSVPSIRKGNDAAHAIGLGQMNLHGYLGREHIYYGSEEGLDFTNAYFAAVLYQCLVASNKLARERGRTFVGFETSKYATGEYFDGFDPADFAPKTEKVAKIFADSSIYTPTAADWADLKDSVAAHGLYNRYLQAVPPTGSISYINHSTSSIHPIASKIEIRKEGKIGRVYYPAPHMDNENLDYFADAYEIGFEKVIDTYAVATKYVDQGLSLTLFFKDSATTRDINRAQIYAWRKGIKTLYYIRLRQVALMGTEVEGCVSCML
>NZ_CP008924.1|WP_013242527.1|35601_36039_-|class-Ib-ribonucleoside-diphosphate-reductase-assembly-flavoprotein-NrdI
MLVVYFSSATENTKRFVQKLGFPAKRIPLHKSSPELVVDEPYVLVCPTYGGGASISGGNTRPVPAQVIRFLNNEHNRSLLRAVIAGGNSNFGLDFGKAGDTIAAKCKVPYVYRFELLGTDEDVRLVRDGLLGNAAALGLLPEPVA
>NZ_CP008924.1|WP_013242528.1|36164_36398_-|glutaredoxin-like-protein-NrdH
MSITVYTKPACVQCNATKKALDRAGLDYTLVDISIDDEARDYVMALGYLQAPVVEVNGEHWSGFRPERISSLVAQVA

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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

1050880 : 1059341

Pandoravirus(33.33%)

holin

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_014300955.1\|1050880_1051462_+	hypoxanthine phosphoribosyltransferase	A0A218MMB5	uncultured_virus	3.0e-15	31.4
WP_013242646.1\|1051458_1053462_+	ATP-dependent metallopeptidase FtsH/Yme1/Tma family protein	E5EQU5	Bathycoccus_sp._RCC1105_virus	7.8e-111	50.3
WP_013242645.1\|1053454_1054018_+	GTP cyclohydrolase I FolE	A0A1W7AF02	Streptococcus_virus	3.4e-48	57.8
WP_013242644.1\|1054019_1054802_+	dihydropteroate synthase	A0A0B5J4J5	Pandoravirus	1.9e-20	32.2
WP_013242643.1\|1054788_1055130_+	dihydroneopterin aldolase	NA	NA	NA	NA
WP_014300954.1\|1055131_1055587_+	2-amino-4-hydroxy-6- hydroxymethyldihydropteridine diphosphokinase	S4W084	Pandoravirus	3.9e-10	34.5
WP_013242641.1\|1055583_1056030_+	DUF3180 domain-containing protein	NA	NA	NA	NA
WP_014300953.1\|1056040_1056556_+	hypothetical protein	NA	NA	NA	NA
WP_014300952.1\|1056552_1056939_+	hypothetical protein	NA	NA	NA	NA
WP_013242638.1\|1056946_1057615_+	pantoate--beta-alanine ligase	NA	NA	NA	NA
WP_013242637.1\|1057592_1059341_-\|holin	choline dehydrogenase	A0A1V0SI18	Klosneuvirus	1.7e-61	31.5

Anti-CRISPR protein detection

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