ID   A0A0N5A6I8_PARTI        Unreviewed;       400 AA.
AC   A0A0N5A6I8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
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_0001761200.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001761200.1}
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; A0A0N5A6I8; -.
DR   WBParaSite; PTRK_0001761200.1; PTRK_0001761200.1; PTRK_0001761200.
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   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
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:SF888; ZINC METALLOPROTEINASE NAS-38; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU01211}; 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..19
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           20..400
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5005733325"
FT   DOMAIN          1..224
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DISULFID        88..110
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   400 AA;  47102 MW;  5DF4D2888D9FC207 CRC64;
     MIILFYLFTI FSINIHSKGV IKFPKEVGKF QNWTNPIHFN CPPIICKAVD KAIEEIEKHT
     CLKFKDQRNK LHNQEGIQFI WGNHDKHCGT NHVGYINSTT PVTVFLGSDC LRIIPKVQSI
     IHIALGVIPE HRRPDRDKFL IMQDQNIRPS GKTFYEIINS SQPYLKEVDY DYGVITHANR
     WEYIHWKDPA FYSTTFKHYY QHIMGQKEVT TFNDYKILNI MFCTETCTHE ERDKLKCLNN
     GYTSPKNCNK CVCPFGYFGR RCQFIEIGKV RDYFRTIECQ PEKLIATIES AKRILYGEKS
     CFIEIRSQLK LVHVCLNILK INSFRADVCR SGRSIEVKYR KDKGAMGLCF CNQHTKPIYI
     ISEGDSILIH YMGNGPWYRL EFEYEMCMHR YLSNQLPEYQ
//