ID   P20D1_AJECG             Reviewed;         437 AA.
AC   C0NAB3;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Probable carboxypeptidase HCBG_00059;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein HCBG_00059;
DE   Flags: Precursor;
GN   ORFNames=HCBG_00059;
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; GG663363; EEH10604.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NAB3; -.
DR   SMR; C0NAB3; -.
DR   STRING; 447093.C0NAB3; -.
DR   EnsemblFungi; EEH10604; EEH10604; HCBG_00059.
DR   VEuPathDB; FungiDB:HCBG_00059; -.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   InParanoid; C0NAB3; -.
DR   OrthoDB; 1432382at2759; -.
DR   Proteomes; UP000001631; 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..437
FT                   /note="Probable carboxypeptidase HCBG_00059"
FT                   /id="PRO_0000411221"
FT   ACT_SITE        195
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   437 AA;  46419 MW;  E5C63E9315017CA1 CRC64;
     MKLSNLAALL SASTVAPVAA GYVSQDIIRA DTMNVAVAAA ANAQDEDLLE KIISSSPLLS
     LHRTICQVES VSNHESAVGE ALIKYLGENG FATEKQMVPV DEDDDSTDKR FNIWAYPEGS
     PKPKIILTSH IDTVPPHIDY NLQAPEGDFD RANITIKGRG TVDAKASVAA MIIAALGHLK
     EHPDVPLGLL FVVSEEKGGT GMVHFSDSDL NTTPPFFHTL IFGEPTELKL VDGHKGNLRF
     DVEARGVSAH SGYPWLGHSA ISEILPVLER IDKLGDIPVK DGGLPASEKY GRTTLNIGML
     KGGAAGNVVP ESASASVAVR LAAGTIEDAQ NIIRKAVADA CGGSKNITIT FPDSKAYPPV
     DLDTDVDGFE LLTVNYGTDI PKLDIHDEDS DVKVKRYLYG PGTILVAHGA DEALTVGDLE
     KAVKGYAKLI DAAVRRG