GenomeNet

Database: UniProt
Entry: A0A0K0EVV3_STRVS
LinkDB: A0A0K0EVV3_STRVS
Original site: A0A0K0EVV3_STRVS 
ID   A0A0K0EVV3_STRVS        Unreviewed;       386 AA.
AC   A0A0K0EVV3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   22-FEB-2023, entry version 31.
DE   RecName: Full=Zinc metalloproteinase {ECO:0000256|PIRNR:PIRNR036365};
OS   Strongyloides venezuelensis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=75913 {ECO:0000313|Proteomes:UP000035680, ECO:0000313|WBParaSite:SVE_0065300.1};
RN   [1] {ECO:0000313|Proteomes:UP000035680}
RP   NUCLEOTIDE SEQUENCE.
RA   Martin A.A, De Silva N.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|WBParaSite:SVE_0065300.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC         ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|PIRNR:PIRNR036365}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0K0EVV3; -.
DR   WBParaSite; SVE_0065300.1; SVE_0065300.1; SVE_0065300.
DR   Proteomes; UP000035680; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR017050; Metallopeptidase_nem.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF877; ZINC METALLOPROTEINASE NAS-34; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035680};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036365};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR036365};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|PIRNR:PIRNR036365,
FT                   ECO:0000256|RuleBase:RU361183"
FT   CHAIN           20..386
FT                   /note="Zinc metalloproteinase"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR036365,
FT                   ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5005120741"
FT   DOMAIN          44..234
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   386 AA;  44160 MW;  DC32CEA72F714AB7 CRC64;
     MNSVLKIFLF FQCISQITSK NEGKLKADGN SESYETRVKK SIITFMKLKW TFPIDYSIRN
     GVDRRTIKAA LAAIEKETCI RFRETDRFTN GGLMYVNKSV GCFSFIGKVS KSKPQNINLG
     GGCNKLMIAI HETLHALGLI HEMSRHDRDS YIKLKYENMG NNSMFNFMLF DLSAATPYGL
     KYDYGSVMQY DRVSGTLDGR ITTVPKYRNY LKTIGQKTRF GFNDAKQLNI HYCSDKCRDS
     KLKCKMGGYP DPNKKCIVCK CPPFYEGKLC TKLSPSDEKC GITKLKATNT EKLLIVKGIK
     TCYIQITAPR RRKVLMNILE TNFRDSFVCQ PNKGLEVKFF TDKTVSGSMF CGKNFRKIVK
     SQNNVVVMKY VGLIPSNRIR IRYHFV
//
DBGET integrated database retrieval system