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P20D1_TALMQ
ID   P20D1_TALMQ             Reviewed;         451 AA.
AC   B6QHD2;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Probable carboxypeptidase PMAA_093910;
DE            EC=3.4.17.-;
DE   AltName: Full=Peptidase M20 domain-containing protein PMAA_093910;
DE   Flags: Precursor;
GN   ORFNames=PMAA_093910;
OS   Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS   (Penicillium marneffei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18224 / CBS 334.59 / QM 7333;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(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; DS995902; EEA22777.1; -; Genomic_DNA.
DR   RefSeq; XP_002148944.1; XM_002148908.1.
DR   AlphaFoldDB; B6QHD2; -.
DR   SMR; B6QHD2; -.
DR   STRING; 441960.B6QHD2; -.
DR   EnsemblFungi; EEA22777; EEA22777; PMAA_093910.
DR   GeneID; 7026509; -.
DR   KEGG; tmf:PMAA_093910; -.
DR   VEuPathDB; FungiDB:PMAA_093910; -.
DR   HOGENOM; CLU_021802_3_0_1; -.
DR   OrthoDB; 1432382at2759; -.
DR   PhylomeDB; B6QHD2; -.
DR   Proteomes; UP000001294; 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; IPR001261; ArgE/DapE_CS.
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.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Metal-binding; Protease; Reference proteome;
KW   Secreted; Signal; Zinc.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..451
FT                   /note="Probable carboxypeptidase PMAA_093910"
FT                   /id="PRO_0000411240"
FT   ACT_SITE        203
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        149
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   451 AA;  48575 MW;  D81E8A304B775FBF CRC64;
     MKVSSLLPSV LLLVGATRAS PHPAQPPQQQ PLNNIIEESN TQTNPPNKHD LEHVIDTSPL
     LSLHRDLVKF ESISGNEADV GDFLIQYLQA RDFKVEKQIV VPKGPKGQGE RFNIYAYPNS
     TPEPRVLLSS HMDTVPPYIP YSLDLPSSNG STTDSLNWRD NILIAGRGSV DAKASVASQI
     LAVLEYLQLH PEAPLGLLFV VGEEVDGIGM QYFSQSELNT SPPTVHTVIF GEPTELALVS
     GHKGSLFFKI SAKGKAAHSG YPWLGQSAVS ALLPALVKLD TLADIPVEDG GIPGSEKLGK
     STINIGRIDA GIASNVVPAS AEASVNIRLA YHDVEKVKEI VTKAVDEATN GDENVTIEWG
     NKGKGHAPID FDTDVDGFKV MTVNYATDAW YLKFHEGSGG SPEGRVHTYL YGPGSIFVAH
     GADEAITVRD LEDAVSGYKK LIEAAFERNK V
 
 
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