ID   A0A1I8BUM4_MELHA        Unreviewed;       476 AA.
AC   A0A1I8BUM4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   22-FEB-2023, entry version 23.
DE   SubName: Full=ZnMc domain-containing protein {ECO:0000313|WBParaSite:MhA1_Contig586.frz3.gene31};
OS   Meloidogyne hapla (Root-knot nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC   Meloidogyne.
OX   NCBI_TaxID=6305 {ECO:0000313|Proteomes:UP000095281, ECO:0000313|WBParaSite:MhA1_Contig586.frz3.gene31};
RN   [1] {ECO:0000313|WBParaSite:MhA1_Contig586.frz3.gene31}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-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; A0A1I8BUM4; -.
DR   WBParaSite; MhA1_Contig586.frz3.gene31; MhA1_Contig586.frz3.gene31; MhA1_Contig586.frz3.gene31.
DR   Proteomes; UP000095281; 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   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
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:SF802; ZINC METALLOPROTEINASE NAS-10; 1.
DR   Pfam; PF01400; Astacin; 1.
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   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..476
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009316182"
FT   DOMAIN          356..476
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   REGION          38..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        460
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         459
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         463
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         469
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   476 AA;  51990 MW;  2A2880C056E28DD5 CRC64;
     MLILSIYQLL LIIISSNAQF NLDQLGLGNL GGALNGLLGG GRQQPQHNPP IQQQNTNNNP
     NIGGQVEGLL NQFGLGNQLT HQIGGLINGI SANFVSDLII LFNYFTVVRS KPKLSNTSTR
     TKEDYAFLQQ KSKSSKMPVG FLIKLFDSES IRSLIILSRG HPEWILPQGS IPAASNVGNA
     LDLNAIFPNL VHFQLPPIPQ LPLQNLLNGD FISQVPNILK QVVPLVGQIT AIAKQAILNI
     CSQRGDCLKQ KPESLNMRAS IAEQEAAIAR AHHPGRPQEQ LDNEVEIRLA RTFQVKKALL
     RKAGLEGQVE PANNGVYQED ILLTEQQANA LINQINQNSA GVGVVPQPSR FKRAGNSLYL
     EGVPNQQWPI GQPIQYMFDV SVTSEADKNA VRQAINEIQS KVQCLSFQEV NAKPAGSHLY
     YVKYALPGFC GQGYVGRLDV VNPIYLSFSC GNPAGVALHE TLHALGLQHE QLRIGE
//