ID   A0A0N4ZDE3_PARTI        Unreviewed;       389 AA.
AC   A0A0N4ZDE3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
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_0000558800.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000558800.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361183};
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; A0A0N4ZDE3; -.
DR   WBParaSite; PTRK_0000558800.1; PTRK_0000558800.1; PTRK_0000558800.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF813; ZINC METALLOPROTEINASE DPY-31; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|RuleBase:RU361183};
KW   Metal-binding {ECO:0000256|RuleBase:RU361183};
KW   Metalloprotease {ECO:0000256|RuleBase:RU361183};
KW   Protease {ECO:0000256|RuleBase:RU361183};
KW   Signal {ECO:0000256|RuleBase:RU361183};
KW   Zinc {ECO:0000256|RuleBase:RU361183}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           21..389
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5005733368"
FT   DOMAIN          24..225
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
SQ   SEQUENCE   389 AA;  45113 MW;  312FB007F47F77DE CRC64;
     MFYQLLFLSI LGCLSSIIFG EEDSKIINKR AILKRHVYNY STNINYWYEG SKIEAIDTAV
     KHLSQYTCLE FRKRSKKLTK RGLIFEIFDF KQIIDNLDKN EPSIVRLDGD CAEDVGCVKH
     MLALALGLIP HHNRWDRDKY VTVNKKNIND DFKMSYNKVK GTRVRILNTA FDFGSITNYD
     PFETSKKNLT RTYKSKLNPL YNKMLGQRHE FSHNDLKLLN DFYCGKSCAK KLKGCRNGGF
     QDPNQCNACR CPLGYDGKYC DKIKKTDYEC GKRFYEATKG YQTFAVNGTK ICNYFIQSPP
     GTKVELHVVD AYVRREPRKC VENFGIEIKN RHDRGTSGLV LCGRNKNVTI KGVFSQVLIH
     YIGFDNTDYA TFKYRAVKRK NTKSFSYDN
//