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
CP034411	Corynebacterium pseudotuberculosis strain Cap1W chromosome, complete genome	1 crisprs	DEDDh,csa3,DinG,cas4,WYL,cas3	0	0	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: CP034411_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

CP034411_1

1025550-1025638

Orphan

I-C,I-E,II-B

Consensus_repeat	Method
GAACTACCTCCGCGTGCGCGGAGAAAAG	CRISPRCasFinder

1 spacers

DinG

The CRISPR arrays of CP034411_1

>merge|CP034411|1|1025550-1025638|CRISPRCasFinder
GAACTACCTCCGCGTGCGCGGAGAAAAGAACCAGACGGATCAGCATACATACCCAACACCGGAACTACCTCCGCGTGCGCGGAGAAAAG

>CP034411|1|1|1025550-1025638|CRISPRCasFinder
GAACTACCTCCGCGTGCGCGGAGAAAAG	AACCAGACGGATCAGCATACATACCCAACACCG
GAACTACCTCCGCGTGCGCGGAGAAAAG

Protein	Signature genes	Signature genes Name	Protein_function
CP034411.1\|AZN19837.1\|1031736_1032273_+\|Hypothetical-protein	unknown	unknown	gnl\|CDD\|378185
CP034411.1\|AZN19835.1\|1029778_1031137_-\|Nicotinate-phosphoribosyl-transferase	unknown	unknown	gnl\|CDD\|236426
CP034411.1\|AZN19824.1\|1019229_1019751_-\|Ferritin-like-protein	unknown	unknown	gnl\|CDD\|153113
CP034411.1\|AZN19833.1\|1027211_1027709_-\|Ribosomal-protein-alanine-acetyltransferase	unknown	unknown	gnl\|CDD\|379112
CP034411.1\|AZN19834.1\|1027732_1029760_-\|ATP-dependent-helicase-dinG-like-protein	DinG	COG1199_DinG_CAS-IV-A	gnl\|CDD\|224120
CP034411.1\|AZN19822.1\|1016409_1016847_+\|Protein-nrdI	unknown	unknown	gnl\|CDD\|179603
CP034411.1\|AZN19830.1\|1024722_1024863_-\|hypothetical-protein	unknown	unknown	unknown
CP034411.1\|AZN19828.1\|1023533_1024169_-\|Hypothetical-protein	unknown	unknown	unknown
CP034411.1\|AZN19836.1\|1031262_1031643_+\|ATP-dependent-Clp-protease-adaptor-protein-ClpS	unknown	unknown	gnl\|CDD\|178809
CP034411.1\|AZN19825.1\|1020160_1021147_+\|ribonucleoside-diphosphate-reductase-subunit-beta	unknown	unknown	gnl\|CDD\|275027
CP034411.1\|AZN19840.1\|1034187_1034985_+\|Metal-dependent-hydrolase	unknown	unknown	gnl\|CDD\|293802
CP034411.1\|AZN19831.1\|1024983_1025532_+\|Transposase-for-IS3511a	unknown	unknown	gnl\|CDD\|379154
CP034411.1\|AZN19827.1\|1021615_1023337_+\|Cytochrome-C-oxidase-polypeptide-I	unknown	unknown	gnl\|CDD\|238832
CP034411.1\|AZN19839.1\|1033251_1034145_+\|Glutamate-racemase	unknown	unknown	gnl\|CDD\|234851
CP034411.1\|AZN19829.1\|1024470_1024617_-\|hypothetical-protein	unknown	unknown	unknown
CP034411.1\|AZN19838.1\|1032359_1033178_+\|Rhomboid-family-protein	unknown	unknown	gnl\|CDD\|366759
CP034411.1\|AZN19823.1\|1016997_1019157_+\|Ribonucleoside-diphosphate-reductase-subunit-alpha	unknown	unknown	gnl\|CDD\|236179
CP034411.1\|AZN19832.1\|1025931_1027215_+\|Phosphoserine-phosphatase	unknown	unknown	gnl\|CDD\|319803
CP034411.1\|AZN19841.1\|1035014_1035758_+\|Ribonuclease-PH	unknown	unknown	gnl\|CDD\|178914
CP034411.1\|AZN19826.1\|1021262_1021442_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
CP034411.1\|AZN19824.1\|1019229_1019751_-\|Ferritin-like-protein	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.	1.41456e-58
CP034411.1\|AZN19833.1\|1027211_1027709_-\|Ribosomal-protein-alanine-acetyltransferase	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	3.30578e-23
CP034411.1\|AZN19834.1\|1027732_1029760_-\|ATP-dependent-helicase-dinG-like-protein	gnl\|CDD\|224120	COG1199, DinG, Rad3-related DNA helicases [Transcription / DNA replication, recombination, and repair].	1.11194e-153
CP034411.1\|AZN19822.1\|1016409_1016847_+\|Protein-nrdI	gnl\|CDD\|179603	PRK03600, nrdI, class Ib ribonucleoside-diphosphate reductase assembly flavoprotein NrdI.	2.30734e-77
CP034411.1\|AZN19823.1\|1016997_1019157_+\|Ribonucleoside-diphosphate-reductase-subunit-alpha	gnl\|CDD\|236179	PRK08188, PRK08188, ribonucleotide-diphosphate reductase subunit alpha; Validated.	0
CP034411.1\|AZN19836.1\|1031262_1031643_+\|ATP-dependent-Clp-protease-adaptor-protein-ClpS	gnl\|CDD\|178809	PRK00033, clpS, ATP-dependent Clp protease adaptor protein ClpS; Reviewed.	1.33955e-35
CP034411.1\|AZN19825.1\|1020160_1021147_+\|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
CP034411.1\|AZN19840.1\|1034187_1034985_+\|Metal-dependent-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.	8.26173e-76
CP034411.1\|AZN19831.1\|1024983_1025532_+\|Transposase-for-IS3511a	gnl\|CDD\|379154	pfam13384, HTH_23, Homeodomain-like domain.	8.47492e-06
CP034411.1\|AZN19839.1\|1033251_1034145_+\|Glutamate-racemase	gnl\|CDD\|234851	PRK00865, PRK00865, glutamate racemase; Provisional.	6.23933e-133
CP034411.1\|AZN19837.1\|1031736_1032273_+\|Hypothetical-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
CP034411.1\|AZN19841.1\|1035014_1035758_+\|Ribonuclease-PH	gnl\|CDD\|178914	PRK00173, rph, ribonuclease PH; Reviewed.	6.63779e-164
CP034411.1\|AZN19838.1\|1032359_1033178_+\|Rhomboid-family-protein	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
CP034411.1\|AZN19827.1\|1021615_1023337_+\|Cytochrome-C-oxidase-polypeptide-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
CP034411.1\|AZN19832.1\|1025931_1027215_+\|Phosphoserine-phosphatase	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.	2.02179e-94
CP034411.1\|AZN19835.1\|1029778_1031137_-\|Nicotinate-phosphoribosyl-transferase	gnl\|CDD\|236426	PRK09243, PRK09243, nicotinate phosphoribosyltransferase; Validated.	0

>CP034411.1|AZN19831.1|1024983_1025532_+|Transposase-for-IS3511a
MPNVSRHTSALSVPTMAKKHTFNKVIIDTIHATGITHTQAAEMFGVSTRWIRELLHRYNTGGYQALEPQSRCPHTSPRAITDDIIDSAGKVSLRWAGESKKLYIGTRYAGMPIILVCLNNKITAVNPETTEILGRYLLEKGRSYHRNLLKDPHQPNPDKKKSLETSNRNDVSRLHRKAPSGT
>CP034411.1|AZN19830.1|1024722_1024863_-|hypothetical-protein
MEPDTSEGTSAQQENPTTYPARNTPPTARADTRSTNFVLSKKTTPH
>CP034411.1|AZN19829.1|1024470_1024617_-|hypothetical-protein
MDRAENTTEQVTPTLDHAAANASSQDKEPDTPPETFDRKYVETLTRGS
>CP034411.1|AZN19828.1|1023533_1024169_-|Hypothetical-protein
MKKSKLFLCMALTTSLATASIPATAQESDPITKPWLFKKCEGFSVAIQSVHLKDKDQSRVPRWLRAKPNLGDTVKVQFKVTNNSYSNNADATYPKEEGNAYLVDDPLSVRNGVGVTIKPNPIYAWSNTDQKRNFILGRGDSVTVTYNHTITEQDLTNRGIPDGPNYPISNSGTATPVCTISPGITYSWSPLSHFFPWLAGFLRSITSFFSR
>CP034411.1|AZN19827.1|1021615_1023337_+|Cytochrome-C-oxidase-polypeptide-I
MTAVAPRLEDYSEPTRPAPTGGARKGTLAWKMLTTTDHKQLGIMYIIMSFVFFFLGGLMALLIRAELFSPGLQYLSNEQFNQLFTMHGTVMLLLFGTPIVWGFANYILPLQIGAPDVAFPRLNAFGFWVTMIGAAAMLSGFLTPGGAADFGWTMYLPLADSIHSPGIGSDMWIVGVGATGVGTISSAINMITTILCMRAPGMTMFRMPIFCWNIFVASVLVLMIFPLLTAAALGVLYDRKLGGHLFDPGNGGAIMWQHLFWFFGHPEVYVLALPFFGIVSEIVPVFARKPMFGYIGLVFATLSIGSLSMAVWAHHMFVTGAILLPFFSFMTFLISVPTGVKFFNWLGTMWKGHVSWETPMTWTMGFLVTFLFGGLTGIMLASPPLDFHISDTYFVVAHFHYTLFGTVVFASFAGVYFWFPKMTGRMLDERLGKIHFWITFVGFHGTFLVQHWLGNEGMPRRYADYLDSDGFTTLNQISTIFSFLLGMSVLPFIWNVIKSWRYGEVVTVDDPWGYGNSLEWATSCPPPRHNFTSLPRIRSERPAFELHYPHMVERMRREAHVGHHVEPVTVKAK
>CP034411.1|AZN19826.1|1021262_1021442_+|hypothetical-protein
MLWGGKGELTLYSSFGLITAGGEVGELVGVMYKYVPTLLCGAYHWNYLENAVFLAELIV
>CP034411.1|AZN19825.1|1020160_1021147_+|ribonucleoside-diphosphate-reductase-subunit-beta
MESYDSYLESHKKPVSAINWNSIPDEKDLEVWDRLTGNFWLPEKVPVSNDLKSWGTLNDLEKTTTMRVFTGLTMLDTIQGTVGAVSMIPDAITPHEEAVYTNIAFMESVHAKSYSNIFMTLASTKEINEAFRWSEENENLQKKAKIVLSYYEGADPLKRKVASTLLESFLFYSGFYLPMYWSSHAKLTNTADIIRLIIRDEAVHGYYIGYKYQQAVREQTPERQEELKEYTFDLLYDLYDNEIQYTEDLYDDLGWTEDVKRFLRYNANKALNNLGYEGLFPADECKVSPAILSALSPNADENHDFFSGSGSSYVIGKAENTTDDDWDF
>CP034411.1|AZN19824.1|1019229_1019751_-|Ferritin-like-protein
MTHPILLLSIASMSINEKLAAALNNQITAELEASMVYLQLSYILDDLSLTGMRNWMQAQHKEELDHAAQFSKHLLDRDYRPQIGDIAPPKLDANSAVEAFEASLAHEQKVTAMIRELAEIADSVKDYDSRPLIDRFLEEQIEEEANVKEILDRLRIADTGSGILRIDAELAER
>CP034411.1|AZN19823.1|1016997_1019157_+|Ribonucleoside-diphosphate-reductase-subunit-alpha
MSQSLGKHVAEPVSRTEQLDYHALNALLNLYNADGKIQFDKDREAANQFFLQHVNQNTVFFHDLEEKIEYLVENNYYEPGIIEKYEFAFIKDLFKQAYAHKFRFKSFLGAYKYYTSYTLKTFDGRRYLERFEDRVCMVALTLADGDQNLARNLVDEIMTGRFQPATPTFLNSGKAQRGEPVSCFLLRIEDNMESIGRSINSALQLSKRGGGVALLLSNLREAGAPIKKIENQSSGVIPVMKLLEDSFSYANQLGARQGAGAVYLNAHHPDILNFLDTKRENADEKIRIKTLSLGVVIPDITFELAKRNDDMYLFSPYDVERVYGKAFADISVSEHYAEMVEDPRIRKSKINAREFFQTIAEIQFESGYPYIMFEDTVNKANPIEGRVNMSNLCSEILQVNTPSLFNDDLTYEEVGEDISCNLGSLNIAMTMDSPDFAKTIETAIRGLTAVSEQTAINSVPSIRKGNDAAHAIGLGQMNLHGYLGREHIYYGSEEGLDFTNAYFAAVLYQCLVASNKLARERGRTFVGFETSKYATGEYFDGFDPADFAPKTEKVAKIFADSSIYTPTAADWADLKDSVAAHGLYNRYLQAVPPTGSISYINHSTSSIHPIASKIEIRKEGKIGRVYYPAPHMDNENLDYFADAYEIGFEKVIDTYAVATKYVDQGLSLTLFFKDSATTRDINRAQIYAWRKGIKTLYYIRLRQVALMGTEVEGCVSCML
>CP034411.1|AZN19822.1|1016409_1016847_+|Protein-nrdI
MLVVYFSSATENTKRFVQKLGFPAKRIPLHKSSPELVVDEPYVLVCPTYGGGASISGGNTRPVPAQVIRFLNNEHNRSLLRAVIAGGNSNFGLDFGKAGDTIAAKCKVPYVYRFELLGTDEDVRLVRDGLLGNAAALGLLPEPVA
>CP034411.1|AZN19832.1|1025931_1027215_+|Phosphoserine-phosphatase
MIELDQPQVTVSLRPELTPAVITISGQDRQGVSAAAFRVLAANGVQILDVEQSQFRGFLGLAVFAGVEASKVEILEIGLKETLKTYGQNVKIELQEVAQSSRPRSTHEVVILGNPVEAHDLSRVAQTLANFDANIDTIRGISDYPVTGLELKITVAKREPGAAMPLRKALAELTAELGVDIAIERAGLLRRSKRLICFDCDSTLITGEVIEMLAAHAGREKEVAEVTERAMSGELDFEESLRERVKALAGLDASVIGEVADSIELTPGARTTIRTLKRLGYKTAVVSGGFIQVLEELAEDLGLDYVRANTLEVVDGKLTGRVIGKIVDRAAKAEFLEEFARESGIEMHQTVAVGDGANDIDMISAAGLGIAFNAKPALREIADTSVNSPFLDEVLHMLGITRADIDAADDSEGKIRRVPLPQQKNEY
>CP034411.1|AZN19833.1|1027211_1027709_-|Ribosomal-protein-alanine-acetyltransferase
MTAHVPTLSNDSVKLRPLLLSDAHDLTATCRDPLTQKYTTVPANYTFAMAEEFIKTEHDNLRWVITVPTSDRFCGQIELRSLAIEHNAMNVGYMTAPWARGQGLMTSALLLAVDYAFSRSVRRIELQADSQNKASQRVAEKAGFILIDSSQDTMVYSLLADEYHS
>CP034411.1|AZN19834.1|1027732_1029760_-|ATP-dependent-helicase-dinG-like-protein
MPLVGRGPWASMLDATSTLCPMSDSPLALSTDELLDAAVAALGGSRRNGQVSMANAVTKALESERHLAVQAGTGTGKSLAYLVPALRHAQATDSTIIVSTATIALQRQLVERDLPRLADALEPHMSRRPTFAIMKGRANYVCMNKIAAAEEPEDALIDEEDLSWLGKHVARIYEWANETEVGDRDSLDPGVPDLAWRQVSVNAQECIGASRCPHGEECFAELARKKAHDVDVIVTNHALLAIDALSDVNVLPEHEVVIVDEAHELDGRITAVATNEIGVTALTMSSRRAGKLGAGEKDQKLIDIAKEWEDAMLAIEPGRLTSLPDYLKQQTVALRDAIWSLREHISRVPEGEAANDPERHAERMSLSNHLNDQHDSVIRVLSVFEEEDAASQEDVVWVLHDERRGVMIKVAPLSIAGLLHTRLFSENTVVLASATLNIGGNFNAMAASWGLPKGSWDSLDAGTPFNPATSGILYTPNSLPDPGRDGLSPEVLDEIYELIMAAGGRTLGLFSSRRAAQQATDAMRTRLPFDVLCQGDDTTGALVEKFSKQENTCLFGTLSLWQGVDVPGRSCSLVIIDRIPFPRPDDPLLQARKDAADADGRNGFMEVAATHAALLIAQGAGRLLRSVTDRGVVAILDRRIVTKRYGAFFIRSLPAFWRTNDPQVVRGALSRLVAR
>CP034411.1|AZN19835.1|1029778_1031137_-|Nicotinate-phosphoribosyl-transferase
MSCASALSVFKAKLVCVTEFESTALLTDMYELTMLQSALADGTASRSCTFEVFSRRLPNERRYGVVAGTARVLEAIKHYRFTEEQLASLTFLDATTIDFLRSYKFQGQIDGYREGELYFPSSPILTIRGTFAECVILETLILSIMNADSAVASAAARMVTAADGRPIFEMGSRRTHEYAAVTAARAAYLAGFVGTSNLEAVHRYGIPGSGTAAHAWTLLHVNDDGTPNESAAFQSQINVLGVGTTLLVDTYDIAKGVKTAIEVAGPQLGAVRIDSGDLGVMTRKVRQELDSLGAHNTGIVVSSDLDEYAIAGLRGNPVDAFGVGTSVVTGSGAPTAGMVYKLVEVDGHPVAKRSRGKAMVGGTKRAIRTHRATGTAVEEIVFPYDHDTPQIGQLNSYELAIPLMRNGIAVDNLPTLEESRAYLAEQLITLPWEGLALSKDEPVLSTRFIGFK
>CP034411.1|AZN19836.1|1031262_1031643_+|ATP-dependent-Clp-protease-adaptor-protein-ClpS
MQVKQEDVTHSLNELPSVVLAPTMDVVVSSPMATPELDEALSVDVASSENLPWMCIVWDDPVNLMSYVTYVFQTILGYSKRRAIELMMQVHTEGKAVVSSGERDKVEGDVKKLHTAGLWATMQQGG
>CP034411.1|AZN19837.1|1031736_1032273_+|Hypothetical-protein
MQPWKKKKGLMRGVHFACVFEPMEREVLGNLASTVSEALIHRAQSAPKDELAELTGMPSGHKEAPKDPALARLLPDFEKEGDEEFEGDNSLLRCLHETDITRAKIEHLYVLGQALGPDGGVHVDITETEAHAWVAALNDIRLYVASGEVFGEDAEQDRESLVEWLAYNQESLLNAMMG
>CP034411.1|AZN19838.1|1032359_1033178_+|Rhomboid-family-protein
MSLRYFFTRLCFIMTNRFNPYAQSDKKTYGGVSTSGGYLPHEYGTQYLPTSDYPVNRAVQRGVKRTSLCSMGRKRLADATVLALGYVVVIWAVHIVNTVFFGGTLAQELGVHPLDGSSIWHIFTSPLVHGSYMHISANTLPGLIFVFLIGLSGRRPFWEVTMITAVVGGMGTWIFGGIGTTHIGASGLIYGWLAYLVVRGIFNKSFSQVVLGVVLAFMYGGLIWGVLPGDVGVSWQAHLFGAIGGLIAGATITSDDPPALKARREQQALHRV
>CP034411.1|AZN19839.1|1033251_1034145_+|Glutamate-racemase
MAYVKKDLGADSLHPEAPSVKPSVVYEGTIDASSPIGIFDSGVGGLTVARAIMEQLPQESVIYIGDTANSPYGSKPIAQVRELSMRIGDELVARGCKMIVIACNTATSAALRDLRERYSIPVVGVILPAVRRAVAATRNGKIGVLGTQGTIASGAYQELFAASPGVEVYAQACPSFVSFVERGITSGRQILGVAQGYTEGLQSAGVDTLVLGCTHYPLLTGVIQLAVGDNVTLISSSEECVKDVLKVLSRNDMLAEATADKPPSRSFESTGDPALFEQLAMRFLGPHVTYVEKLREV
>CP034411.1|AZN19840.1|1034187_1034985_+|Metal-dependent-hydrolase
MIRNRGTVKNMKLTILGSSGSLGAPDNAASGYLIQMDNAPSILMDMGPGVLAQLERAQNPSDAHVVFSHLHADHCVDFPSLLVWRRYHPTAAAKGRNLCFGPTDTPVRLGRLSADSVDNIDDMSDTFAFTPWQNAKEELVGAVSITPYSVVHPIESFALRVEHKRSGKVVAYSGDSSYTENLIECARDADVFLCEATWGETSEGKVPNMHMSGEEAGRIARIAGAKRLILVHIPPWGNAKAALEKARSEFDGPVDISYQGMEIHI
>CP034411.1|AZN19841.1|1035014_1035758_+|Ribonuclease-PH
MVDMTTSNFKRADGRAVDQMRTVKITRGFTTNPAGSVLVEFGNTRVMCTASAEIGVPRFKRDSGEGWLTAEYAMLPAATLDRNPRESMRGKVKGRTHEISRLIGRSLRAAVDLSELGENTINIDCDVLQADGGTRTASITGAYVALADAISHLQKQGVVPGNPLKDPVAAVSVGVIDGAVCLDLPYEEDSRADVDMNVIMQNGRFVEIQGTGEHNTFDRDELARILDFAEKGCTELVAAQKAALGIA

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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

886691 : 895152

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
AZN19704.1\|886691_887273_+	Hypoxanthine-guanine phosphoribosyltransferase	A0A218MMB5	uncultured_virus	3.0e-15	31.4
AZN19705.1\|887269_889273_+	Cell division protein	E5EQU5	Bathycoccus_sp._RCC1105_virus	7.8e-111	50.3
AZN19706.1\|889265_889829_+	GTP cyclohydrolase 1	A0A1W7AF02	Streptococcus_virus	3.4e-48	57.8
AZN19707.1\|889830_890613_+	Dihydropteroate synthase	A0A0B5J4J5	Pandoravirus	1.9e-20	32.2
AZN19708.1\|890623_890941_+	Dihydroneopterin aldolase	NA	NA	NA	NA
AZN19709.1\|890942_891398_+	2-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase	S4W084	Pandoravirus	3.9e-10	34.5
AZN19710.1\|891394_891841_+	Hypothetical protein	NA	NA	NA	NA
AZN19711.1\|891851_892367_+	Hypothetical protein	NA	NA	NA	NA
AZN19712.1\|892363_892750_+	Hypothetical protein	NA	NA	NA	NA
AZN19713.1\|892757_893426_+	Pantothenate synthetase	NA	NA	NA	NA
AZN19714.1\|893403_895152_-\|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