ID   P20D1_PARBP             Reviewed;         442 AA.
AC   C0S1J6;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=Probable carboxypeptidase PABG_01461;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein PABG_01461;
DE   Flags: Precursor;
GN   ORFNames=PABG_01461;
OS   Paracoccidioides brasiliensis (strain Pb03).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=482561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb03;
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}.
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DR   EMBL; KN305532; EEH19142.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0S1J6; -.
DR   SMR; C0S1J6; -.
DR   EnsemblFungi; EEH19142; EEH19142; PABG_01461.
DR   VEuPathDB; FungiDB:PABG_01461; -.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   InParanoid; C0S1J6; -.
DR   Proteomes; UP000002740; 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; Secreted; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..442
FT                   /note="Probable carboxypeptidase PABG_01461"
FT                   /id="PRO_0000411239"
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;  47872 MW;  760A680BE3481CAF CRC64;
     MKLQYLVALL SVQAVPPVTA GYIHQYALVG SAIRQPIDQK TQREDLNKLV 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 RRAVYDVSGG STNITVNFPD SMPYPPIDLD
     VDVEGFDIST VNYGTDIPKL EIHDEELEVK VKRYLYGPGT IFVAHGAEEG ITVGDLEKAV
     EGYSKLIDAA VKRGWPREVV VN