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