ID   A0A0N5A148_PARTI        Unreviewed;       378 AA.
AC   A0A0N5A148;
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_0001534850.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0001534850.1}
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; A0A0N5A148; -.
DR   STRING; 131310.A0A0N5A148; -.
DR   WBParaSite; PTRK_0001534850.1; PTRK_0001534850.1; PTRK_0001534850.
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; IPR000859; CUB_dom.
DR   InterPro; IPR000742; EGF-like_dom.
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: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; PF00431; CUB; 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.
DR   PROSITE; PS00022; EGF_1; 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};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           18..378
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5005733313"
FT   DOMAIN          39..228
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
SQ   SEQUENCE   378 AA;  42014 MW;  455E2F190C66F754 CRC64;
     MKKVVLILSS LYVVTFPSIV IDPSHESYNY SFINQRNKRA VIYKNVKWIF PIKYSVGSNV
     NSKLVEDVLT GIRSQTCITF QKVQSFSGPG IQFKKGASCG IFSSNNSPAI IGIAEYCGKR
     GKIQKKTLNI LGLLDEEDRP NRNNYVTVNM NNVIDSVKHY LVVQDSSLVN SYNIRYDYGS
     IMHNGKYYVS KNGKMTIVPK DKLYFDTIGQ IEMIGFNDIK CLNLYYCSGK CSSQLNCLNG
     GYTDPNNCSV CRCPRFFTGK LCNEIVSSPP SCGTTKISSL TNSQILTVSG KKNCIYQISA
     PPESKVKVII LNTNLPVKNP CPPNVGLEVK FSDDKSISGA TFCGIKKNIT ITSLDNLVLI
     KYSGLKQNNN IKISYKKV
//