ID   P20D1_PARBD             Reviewed;         442 AA.
AC   C1G9X6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Probable carboxypeptidase PADG_04062;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein PADG_04062;
DE   Flags: Precursor;
GN   ORFNames=PADG_04062;
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KN275960; EEH47978.1; -; Genomic_DNA.
DR   RefSeq; XP_010759703.1; XM_010761401.1.
DR   AlphaFoldDB; C1G9X6; -.
DR   SMR; C1G9X6; -.
DR   STRING; 121759.XP_010759703.1; -.
DR   EnsemblFungi; EEH47978; EEH47978; PADG_04062.
DR   GeneID; 22583257; -.
DR   KEGG; pbn:PADG_04062; -.
DR   VEuPathDB; FungiDB:PADG_04062; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OMA; VSGHKGM; -.
DR   Proteomes; UP000001628; 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..442
FT                   /note="Probable carboxypeptidase PADG_04062"
FT                   /id="PRO_0000411238"
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        102
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   442 AA;  47873 MW;  BD48BE1C112A0457 CRC64;
     MKLQYLVALL SVQAVPPVTA GYIHQYALVG SVIRQPIDQK TQRENLNKLV SDSPLLSLHR
     TICEIESVSN REGAVGEVLL KYLRDRGFTV EKQIVPADRG TNSTAERFNI WAYPKGCPRP
     KIILTSHIDT VPPHIKYSLH APDGDFDRAK VRIMGRGTVD AKASVAAQII AALKHLKSNK
     DIPLGLLFVV SEEVGGSGMV HFSNSELNTN PPFFHTLIFG EPTDLTLVDG HKGNLRVTIE
     AKGVAAHSGY PWLGRSAISE ILPILARMDE LGDIPVETGG LPSSEKYGRT TVNIGTIKGG
     AADNVVPETA SASIAVRLAA GTPEEAEEII RRAVHDVSGG STNITVNFPD SMPYPPIDLD
     VDVEGFDIST VNYGTDIPKL EIHDEELEVK VKRYLYGPGT IFVAHGAEEG ITVGDLEKAV
     EGYSKLIDAA VKRGWPREVV VN