ID   CBPYA_TALSN             Reviewed;         553 AA.
AC   B8M044;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; ORFNames=TSTA_083730;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
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; EQ962653; EED21141.1; -; Genomic_DNA.
DR   RefSeq; XP_002478104.1; XM_002478059.1.
DR   AlphaFoldDB; B8M044; -.
DR   SMR; B8M044; -.
DR   STRING; 441959.B8M044; -.
DR   ESTHER; penmq-cbpya; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; B8M044; 2 sites, No reported glycans.
DR   GeneID; 8101466; -.
DR   VEuPathDB; FungiDB:TSTA_083730; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; B8M044; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 1647009at2759; -.
DR   PhylomeDB; B8M044; -.
DR   Proteomes; UP000001745; 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; 1.10.287.410; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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:SF113; CARBOXYPEPTIDASE Y; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF05388; Carbpep_Y_N; 1.
DR   Pfam; PF00450; Peptidase_S10; 1.
DR   PRINTS; PR00724; CRBOXYPTASEC.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 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..134
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407480"
FT   CHAIN           135..553
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407481"
FT   ACT_SITE        276
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        467
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        529
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        518
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        189..428
FT                   /evidence="ECO:0000250"
FT   DISULFID        323..337
FT                   /evidence="ECO:0000250"
FT   DISULFID        347..370
FT                   /evidence="ECO:0000250"
FT   DISULFID        354..363
FT                   /evidence="ECO:0000250"
FT   DISULFID        392..398
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   553 AA;  61898 MW;  A1EB9702FD8701F4 CRC64;
     MRVLSTTLLI GAAAAAVSPP QQVLQAPEEA VENTHKSSPS LAESLSQPLR ELKEELKLLT
     NEVEEVWEEV SNIFPGALDN IFFSSAKKHT RRPDSHWDHI IRGSDVQNIW VENENGEKER
     EVGGRLEAFD LRVKAVDPSS LGIDPDVKQY SGYLDDNEND KHLFYWFFES RNDPKTDPVV
     LWLNGGPGCS SLTGLFFELG PSSIGKNIKP IYNPYSWNSN TSVIFLDQPV NVGFSYSGNS
     VSETSAAAKD VYALLTLFFK QFPEYSSQDF HIAGESYAGH YIPSFASEIL SHKKRNINLK
     SVLIGNGLTD GLTQYEYYRP MACGDGGYPA VLDETTCRSM DNALGRCQSM IQSCYDSESA
     WTCVPASIYC NNALLGPYQR TGQNVYDVRK PCEDSSLCYA DLEYVSTYLN QAEVMKALGA
     EVDSFDSCNF DINRNFLFKG DWMKPFHKLV PGLLEEIPVL IYAGDADFIC NWLGNKAWTD
     ALEWAGHEEY AATELEDLEI VDNKHKGKKI GQVKSSGNLT FMRLFGGGHM VPYDQPEASL
     EFFNRWIGGE WTK
//