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Database: UniProt
Entry: A0A1I8CSZ3_9BILA
LinkDB: A0A1I8CSZ3_9BILA
Original site: A0A1I8CSZ3_9BILA 
ID   A0A1I8CSZ3_9BILA        Unreviewed;       489 AA.
AC   A0A1I8CSZ3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 28.
DE   RecName: Full=Zinc metalloproteinase {ECO:0000256|PIRNR:PIRNR036365};
OS   Rhabditophanes sp. KR3021.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC   Rhabditophanes.
OX   NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000745200.1};
RN   [1] {ECO:0000313|WBParaSite:RSKR_0000745200.1}
RP   IDENTIFICATION.
RC   STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000745200.1};
RG   WormBaseParasite;
RL   Submitted (NOV-2016) 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}.
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DR   AlphaFoldDB; A0A1I8CSZ3; -.
DR   WBParaSite; RSKR_0000745200.1; RSKR_0000745200.1; RSKR_0000745200.
DR   Proteomes; UP000095286; Unplaced.
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:SF879; METALLOENDOPEPTIDASE-RELATED; 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   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..489
FT                   /note="Zinc metalloproteinase"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR036365,
FT                   ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5009030095"
FT   DOMAIN          138..337
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   ACT_SITE        234
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         233
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         237
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   489 AA;  54311 MW;  AC8C9986AE5775AE CRC64;
     MQKIFFLIVL LSLFSISMAK KRGLFRQNLR DSMSMETRIQ FDKNVESMQK ISALANLVKP
     VNETQPEPDE DEDIEENPMF NPYLYGGDLM LTDDQMSQVV EDAEFEILEN AEFEILENAE
     FEILQGANID TSATRKKRSI KAVQNFKWAF PIKWYMNNTL PATTLPKIQA ALAEIQAQTC
     ISFAQQSAIW TGTPGLVFFK ENGCWAWLGN IYNNKPQEVS LGNGCDSHGI IEHEVGHALG
     LEHEQSRPDR DNYLTINLAN AQTGTEPQFV KSALTAVKDY GVGFAYDSTM LYFATAFSKD
     GRLKTQASKR LVYDETMGQQ DRLSFGDFKI LNYHYCNTTC TSKINDCQNG GYQNPRDCTK
     CKCPNGFGGA KCADVAASAA ACGTLELTAT TALQTLTKTG SMRCHFRIKT TDGYKIRIIL
     TSSVTAGGFC FINKGIEIKF WKDMALGGAV QCGSFTGAKT HISESNLAMV DFPGTAASHS
     FTLTYQRVQ
//
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