ID   P20D1_ARTGP             Reviewed;         461 AA.
AC   E4UW91;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=Probable carboxypeptidase MGYG_04702;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein MGYG_04702;
DE   Flags: Precursor;
GN   ORFNames=MGYG_04702;
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893;
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR   EMBL; DS989825; EFR01699.1; -; Genomic_DNA.
DR   RefSeq; XP_003172110.1; XM_003172062.1.
DR   AlphaFoldDB; E4UW91; -.
DR   SMR; E4UW91; -.
DR   STRING; 63402.XP_003172110.1; -.
DR   PRIDE; E4UW91; -.
DR   EnsemblFungi; EFR01699; EFR01699; MGYG_04702.
DR   GeneID; 10027378; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   InParanoid; E4UW91; -.
DR   OMA; VSGHKGM; -.
DR   OrthoDB; 1432382at2759; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; SSF55031; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..461
FT                   /note="Probable carboxypeptidase MGYG_04702"
FT                   /id="PRO_0000411225"
FT   ACT_SITE        208
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   461 AA;  49743 MW;  8513CBA7EFEF3CA7 CRC64;
     MQKTYLLALV SLLASSLVEA RSTIADQTRL DVGGSDESFD GIDGIDPNNS NVLTHKLMDK
     VIASSELLSL HRSLVEIKSI SDNEQAVGGF LMDYLSSKNF TVEKQYVDYD DPTGKPIRSN
     RRFNIYAYPG DSASPGIILT SHIDTVPPFI PYSLSHPESD SFKRDDILIS GRGTVDDKAS
     VACQIIAAME HLEKHPDIPI GLLFVVSEEV GGKGMSTFSD SRLNSGTYHT IIFGEPTERA
     LVAGHKGMVS FGIRVHGKPA HSGYPWLGRS AVSEILPILA EVDRLGDIPV SQGGLPSSEK
     YGRTTLNIGF MSGGVAANVV PEQAVAKVAV RLAAGDPEDA KDIIFRAIRN AATKHRKDAT
     VVISNGHEQP KGDIEVIFGL EAYGVVDIDA DVDGFNVTTV NYGTDVPHWK IYGDNVKRYL
     YGPGTIFVAH GKDEALTVGE LEAGLEGYKT LVAKAAERER T