ID A0A0N4W0K1_HAEPC Unreviewed; 500 AA.
AC A0A0N4W0K1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=HPLM_LOCUS3085 {ECO:0000313|EMBL:VDO20100.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000309301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0000309301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO20100.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO20100.1,
RC ECO:0000313|Proteomes:UP000268014};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, 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 EMBL; UZAF01016096; VDO20100.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4W0K1; -.
DR WBParaSite; HPLM_0000309301-mRNA-1; HPLM_0000309301-mRNA-1; HPLM_0000309301.
DR OMA; QYISIGW; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; Unassembled WGS sequence.
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); 1.
DR InterPro; IPR034035; Astacin-like_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 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; 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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000268014};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT DOMAIN 115..315
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT ACT_SITE 214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 500 AA; 56710 MW; 4DAAD5BC5C580C4A CRC64;
MTSNYRLTPV SQSNFASRPL THKMVDRTEY SVNRRILSKM FCFGSSCKRE SHTKKCSMKE
FGLRSYLILA LSNHLYTTFQ VFESDLVLTK PQMDEVMDNF NARITGRRRR NKRNAAIIGK
KFRWPNAVIP YEFKDSDSNN ITVNAAADWK KLIWRGMKEW QKETCIRFVE RTNETDYAVF
FKGAGCYSNV GRTGGRQYIS IGWGCESRGI VAHEIGHALG FWHEQSRPDR DQFININEDA
ISSGTKGNFE KRSDIMDSDI PYDFGSVMHY APQAFTKDWH LVTIETKDHR FQHTIGQRST
VSFTDVKHAN RLYCSRVCQT KISCANGGYQ DPRNCDRCKC PPGLGGVLCE RVADSTPGCG
GELFASSQWQ ILQNSQIGTC HWRIYVCSHA ICSFPYFYPS FNVNLQAPNG RISFETQCCN
PAPGRTVSHG NQVIVTSFSK TAPSNFTMRY ILANEVGIDN TFETLILKDV PRVLGRSRGG
PNFASLFGLL DTFLPRGPRG
//