ID   A0A183CUS8_9BILA        Unreviewed;       310 AA.
AC   A0A183CUS8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=ZnMc domain-containing protein {ECO:0000313|WBParaSite:GPUH_0000021801-mRNA-1};
OS   Gongylonema pulchrum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Spiruroidea; Gongylonematidae; Gongylonema.
OX   NCBI_TaxID=637853 {ECO:0000313|Proteomes:UP000050760, ECO:0000313|WBParaSite:GPUH_0000021801-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:GPUH_0000021801-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211};
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; A0A183CUS8; -.
DR   WBParaSite; GPUH_0000021801-mRNA-1; GPUH_0000021801-mRNA-1; GPUH_0000021801.
DR   Proteomes; UP000050760; 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; 3.40.390.10; Collagenase (Catalytic Domain); 2.
DR   InterPro; IPR034035; Astacin-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:SF890; ZINC METALLOPROTEINASE NAS-30; 1.
DR   Pfam; PF01400; Astacin; 2.
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   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT   DOMAIN          96..257
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         159
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   310 AA;  36514 MW;  7711C632F0CA81E1 CRC64;
     LYRRRWNQED SENVRELLRG FLRLTADVPL TPKRRSNFAS QPIKYKIVDR TEYAVNKRIL
     NDVFETDLVL TTPQMRKIIS DFQQQRTRKT RRNKRKAIAG DSFRWPRQTV PYFLKETDRE
     WRRLVIEGMN KWERETCVHF KERTDEKDYG GIVAHELGHT LGFWHEQSRP DRDKFININE
     DHIYPGTKGN FEKRNDIAVL DTPYDFGSVM HYGPQAFTND YHYVTIETKD HRFQHTIGQR
     NDLSFIDIKE ANRLYCSDKC KVKLNCLHGG YENPRNCAVC KCPTGIAGIR CESIPRSSGK
     LCSTSYAPVL
//