ID   P20D1_AJEDR             Reviewed;         434 AA.
AC   C5GFX4;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Probable carboxypeptidase BDCG_03757;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein BDCG_03757;
DE   Flags: Precursor;
GN   ORFNames=BDCG_03757;
OS   Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ER-3 / ATCC MYA-2586;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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; EQ999975; EEQ88637.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5GFX4; -.
DR   SMR; C5GFX4; -.
DR   STRING; 559297.C5GFX4; -.
DR   EnsemblFungi; EEQ88637; EEQ88637; BDCG_03757.
DR   VEuPathDB; FungiDB:BDCG_03757; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OMA; VSGHKGM; -.
DR   Proteomes; UP000002039; 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..434
FT                   /note="Probable carboxypeptidase BDCG_03757"
FT                   /id="PRO_0000411222"
FT   ACT_SITE        192
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        343
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   434 AA;  46285 MW;  0FC0E401767C9D25 CRC64;
     MKLSHLAAAL SAQLVAPVAA GYLRQDILTA GTLRDTTVPA APNEDLNQIV SDSQLLSLHR
     TICEIESVSN HESTVGEALI KYLGEHDFTT EKQIVPVDED DDSTDERYNV WAYPKGSPKP
     KIILTSHIDT VPPHINYSLH APEGDFDRAN ITIKGRGTVD AKASVAAMII AALDHMKESP
     DVPVGLLFVV SEERGGTGMI HFSDSELNTS PPFFHTLIFG EPTELKLVDG HKGNLRFDVE
     AKGVSAHSGY PWLGHSAISE ILPVLARIDG LGDIPVEDGG LPSSEKYGST TLNIGTVRGG
     AAGNVVPESA SASVAVRLAD GTVEDAQDII RKAVADASGG SKNITLKFPD DKAYPPIDLD
     TDVDGFELLT VNYGTDIPKL DIHDEDSDVK VKRYLYGPGT ILVAHGVDEG LTVGDLEKAV
     EGYSKLIDAA VKRG