ID   CBPYA_TALMQ             Reviewed;         555 AA.
AC   B6QAN5;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; ORFNames=PMAA_064090;
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   -!- FUNCTION: Vacuolar carboxypeptidase involved in degradation of small
CC       peptides. Digests preferentially peptides containing an aliphatic or
CC       hydrophobic residue in P1' position, as well as methionine, leucine or
CC       phenylalanine in P1 position of ester substrate (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity.;
CC         EC=3.4.16.5; Evidence={ECO:0000255|PROSITE-ProRule:PRU10074};
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; DS995900; EEA25293.1; -; Genomic_DNA.
DR   RefSeq; XP_002145840.1; XM_002145804.1.
DR   AlphaFoldDB; B6QAN5; -.
DR   SMR; B6QAN5; -.
DR   STRING; 441960.B6QAN5; -.
DR   ESTHER; penmq-cbpya; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; EEA25293; EEA25293; PMAA_064090.
DR   GeneID; 7023551; -.
DR   KEGG; tmf:PMAA_064090; -.
DR   VEuPathDB; FungiDB:PMAA_064090; -.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OrthoDB; 625787at2759; -.
DR   PhylomeDB; B6QAN5; -.
DR   Proteomes; UP000001294; Unassembled WGS sequence.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001563; Peptidase_S10.
DR   InterPro; IPR008442; Propeptide_carboxypepY.
DR   InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802; PTHR11802; 1.
DR   Pfam; PF05388; Carbpep_Y_N; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..136
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407468"
FT   CHAIN           137..555
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407469"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        469
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        531
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        520
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        191..430
FT                   /evidence="ECO:0000250"
FT   DISULFID        325..339
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..372
FT                   /evidence="ECO:0000250"
FT   DISULFID        356..365
FT                   /evidence="ECO:0000250"
FT   DISULFID        394..400
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   555 AA;  61987 MW;  E6367B12FD265AF3 CRC64;
     MRGLATTLLI GAAAAATYPA QQVLKAPEEV LEKTHKTSSS SLAETLARPL HELNEELKSL
     TAEAEEVWEQ VSNMFPGALD NIPFFSSPKK HTRRPDSHWD HIVRGADVQN IWVENENGEK
     EREVGGRLET FDLRVKAVDP SSLGIDPDVK QYSGYLDDNE NDKHLFYWFF ESRNDPKNDP
     VVLWLNGGPG CSSLTGLFFE LGPSSIGKNI KPIYNPYSWN SNASVIFLDQ PVNVGFSYSG
     NSVSETSAAA KDVYALLTLF FKQFPEYATQ DFHIAGESYA GHYIPSFASE ILSHKKRNIN
     LKSVLIGNGL TDGFTQYEYY RPMACGDGGY PAVLDESACR SMDNALGRCQ SMIQSCYDSE
     SAWTCVPASI YCNNALLGPY QRTGQNVYDI RKPCEGSSLC YADLEYISTY LNQAEVLKAV
     GAEVDSFDSC NFDINRNFLF KGDWMKPFHK LVPGILEEIP VLIYAGDADF ICNWLGNKAW
     SDALEWSGHE EYAATELEDL EIVDNEHKGK KIGQVKSSGN LTFMRLFGGG HMVPYDQPEA
     SLEFFNRWIG GEWTK