UniProt: B7PC82

Database: UniProt
Entry: B7PC82_IXOSC

LinkDB:  B7PC82_IXOSC 
Original site:  B7PC82_IXOSC

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (5)   
   EMBL (5)   
Protein domain (6)   
   InterPro (5)   
   Pfam (1)   
All databases (19)   

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ID   B7PC82_IXOSC            Unreviewed;       607 AA.
AC   B7PC82;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   SubName: Full=Thimet oligopeptidase, putative {ECO:0000313|EMBL:EEC04204.1, ECO:0000313|EnsemblMetazoa:ISCW017437-PA};
DE            EC=3.4.24.15 {ECO:0000313|EMBL:EEC04204.1};
GN   ORFNames=IscW_ISCW017437 {ECO:0000313|EMBL:EEC04204.1};
OS   Ixodes scapularis (Black-legged tick) (Deer tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX   NCBI_TaxID=6945;
RN   [1] {ECO:0000313|EMBL:EEC04204.1, ECO:0000313|Proteomes:UP000001555}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Wikel {ECO:0000313|Proteomes:UP000001555}, and Wikel colony
RC   {ECO:0000313|EMBL:EEC04204.1};
RG   Ixodes scapularis Genome Project Consortium;
RA   Caler E., Hannick L.I., Bidwell S., Joardar V., Thiagarajan M., Amedeo P.,
RA   Galinsky K.J., Schobel S., Inman J., Hostetler J., Miller J., Hammond M.,
RA   Megy K., Lawson D., Kodira C., Sutton G., Meyer J., Hill C.A., Birren B.,
RA   Nene V., Collins F., Alarcon-Chaidez F., Wikel S., Strausberg R.;
RT   "Annotation of Ixodes scapularis.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ISCW017437-PA}
RP   IDENTIFICATION.
RC   STRAIN=wikel {ECO:0000313|EnsemblMetazoa:ISCW017437-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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DR   EMBL; ABJB010378117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010394411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010638827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ABJB010978305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DS682300; EEC04204.1; -; Genomic_DNA.
DR   RefSeq; XP_002409490.1; XM_002409446.1.
DR   AlphaFoldDB; B7PC82; -.
DR   STRING; 6945.B7PC82; -.
DR   PaxDb; 6945-B7PC82; -.
DR   EnsemblMetazoa; ISCW017437-RA; ISCW017437-PA; ISCW017437.
DR   KEGG; isc:IscW_ISCW017437; -.
DR   VEuPathDB; VectorBase:ISCI017437; -.
DR   VEuPathDB; VectorBase:ISCP_026146; -.
DR   VEuPathDB; VectorBase:ISCW017437; -.
DR   HOGENOM; CLU_001805_2_1_1; -.
DR   InParanoid; B7PC82; -.
DR   OMA; RSGAWCS; -.
DR   Proteomes; UP000001555; Unassembled WGS sequence.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006518; P:peptide metabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd06455; M3A_TOP; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR024080; Neurolysin/TOP_N.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   PANTHER; PTHR11804:SF84; SACCHAROLYSIN; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:B7PC82};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001555};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          218..602
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   COILED          147..174
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   607 AA;  70000 MW;  8F0995B2221F1C7E CRC64;
     MEPNKTTAPG ILRAWDYDLE PKELLARARR LIEDCRALCD NIGALEGDQI TFNNVLGELA
     EVERLFMNEK LYLKRAMYVS MNKELRDASS EASRMLDEFE VECGMRLDIF EKLQALEKMD
     TSSLSAEMKR FLEKLIRLRK RDGLHLSPEV QKQVKDLKNE INELSLKFTK AMNEENTILE
     FTEEELKGLP EEFVKNLDTA ESGKRRVTLK YPHVVPIMKM AVNAETRRRV NFAFENRCVE
     ENTPLLEKAI SLKHKKAKLL DYETHADFIT EILMARNSGN VRCFLTELAQ KLQPLWQKEK
     ELLLQYKKEE CESQGIPFDG KLNAWDVSYY KNLVEERVYK VDQEKLRAFF PLDVVTKGLL
     GIYEMLLGLK FDKVENVKLW HPEAELFKVT DVASQELLGY FLMDLFPREG KYSHFCNIPM
     QPGCQTADGS RQLAVVGVLC NFPKPTADKP ALLTHNEVTT FFHEFGHTMH HICSRANLVE
     FGGTRVERDF LECPSQMLEN WCWDLEALRL MSSHYSTGEP IPEDLAEKLM ASRLANVAQF
     NLRQVSLALF DLELHSRPEA DTRKVFREIQ ESLLGYPPQE GTNFAASFGH LMGGYDAQYY
     GYMVFGG
//

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