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Database: UniProt
Entry: A0A0N4ZBE6_PARTI
LinkDB: A0A0N4ZBE6_PARTI
Original site: A0A0N4ZBE6_PARTI 
ID   A0A0N4ZBE6_PARTI        Unreviewed;       307 AA.
AC   A0A0N4ZBE6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000485800.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000485800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Metalloprotease. {ECO:0000256|ARBA:ARBA00002657}.
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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01005}.
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DR   AlphaFoldDB; A0A0N4ZBE6; -.
DR   STRING; 131310.A0A0N4ZBE6; -.
DR   WBParaSite; PTRK_0000485800.1; PTRK_0000485800.1; PTRK_0000485800.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 1.10.10.1940; -; 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; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR003582; ShKT_dom.
DR   PANTHER; PTHR10127:SF887; ASTACIN-LIKE METALLOENDOPEPTIDASE; 1.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF01549; ShK; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00254; ShKT; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS51670; SHKT; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU01005};
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   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   DOMAIN          27..221
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          271..305
FT                   /note="ShKT"
FT                   /evidence="ECO:0000259|PROSITE:PS51670"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         117
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         121
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         127
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   DISULFID        271..305
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ   SEQUENCE   307 AA;  35254 MW;  E24EE4377AFC6FC7 CRC64;
     MESGKFQGDI AGVNEAMLHS HSGSMYNALK NKQLIWPQGI VPYVLDEAFT SSEVSELLKS
     FSTYKKLTCI RFIERTDEKD YLNIVKGYGC YSQVGRTGGK QEISLGRGCL FHEIIIHELM
     HSLGFWHEHS RFDRNEHIKI IWDNILPGMK SQFDIISPAL QDTQGEPYDY NSIMHYDSTA
     FSKNGKNTIE TTLDGFTDII GNSVMFSKLD IIKINKLYKC NKEESSEKIP EPKINNSNFK
     KTNNIIKKDK FISENSNEEN ELVMSTVSPT CQDHFIDCPV FKNYCKRASF FYVMKSYCPY
     TCGHCRP
//
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