ID A0A0W0GDR6_9AGAR Unreviewed; 597 AA.
AC A0A0W0GDR6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Extracellular metalloproteinase {ECO:0000256|RuleBase:RU364017};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU364017};
DE AltName: Full=Fungalysin {ECO:0000256|RuleBase:RU364017};
GN ORFNames=WG66_742 {ECO:0000313|EMBL:KTB46676.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB46676.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB46676.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB46676.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601842-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601842-2};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU364017}.
CC -!- SIMILARITY: Belongs to the peptidase M36 family.
CC {ECO:0000256|ARBA:ARBA00006006, ECO:0000256|RuleBase:RU364017}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTB46676.1}.
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DR EMBL; LATX01000283; KTB46676.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0GDR6; -.
DR Proteomes; UP000054988; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09596; M36; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR001842; Peptidase_M36.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR33478; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR PANTHER; PTHR33478:SF1; EXTRACELLULAR METALLOPROTEINASE MEP; 1.
DR Pfam; PF02128; Peptidase_M36; 1.
DR PRINTS; PR00999; FUNGALYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU364017};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601842-2,
KW ECO:0000256|RuleBase:RU364017};
KW Metalloprotease {ECO:0000256|RuleBase:RU364017};
KW Protease {ECO:0000256|RuleBase:RU364017};
KW Reference proteome {ECO:0000313|Proteomes:UP000054988};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364017};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601842-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|RuleBase:RU364017}.
FT ACT_SITE 398
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-1"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
FT BINDING 426
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601842-2"
SQ SEQUENCE 597 AA; 65388 MW; 68C1679CEF6FE884 CRC64;
MPCTKTSDPD FHRLKGEALY KRLMLMLAIF LETVGSRALK IESYHPPTTF KTFGQVKTEK
RAADVDIDVE SSSVDFVKSE LNLDDSKFSY KTGYTSEGRG YGYLKQQHNG IPFANAVANV
AFKDTQPVSF GNSFVDPSNI ADSTPTFDVK QAIEVAEAAL EGKHNDIEPT LEYLARPDGS
VALTHVIQVK NNDARTWYEA FVDAHSGELL SITDFVSHAT YRVVPIEKPN LPAGYETLVD
PQDLSASPLG WHNDGTGPTN TTSGNNVLSF KATRSAVTTQ SADGLVFDYE YNDSLTPIEG
DNVDASRTQA FYLGNKVHDV LYKYGFTEAA YNFQNTNFGK GGRGHDRLLM FVQYSSGVNN
ANIAVPPDGQ SPECHMFIFT ITTPNRDGIF ELSIPVHEIT HGLTNRMTGG GTARCLETAE
AGGLGEGWSD AFADWTEHQS GPEIKDFVTG AYVLDSPGGA RQYPYSTDPT VNPLRYSSVE
PEGEVHDTGE VWANLLHNVY AALVTEHGWS RTAFTDPTGL AGNVVYLHLF VDGLAIQPCN
PTFLDARDSW IQADEVRYSG AHKCLLWKTF ASRGLGVNAA NFQDDDTIPA ECQTDVN
//
