ID   CBPYA_ASPTN             Reviewed;         557 AA.
AC   Q0CSD3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; ORFNames=ATEG_03401;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476597; EAU36675.1; -; Genomic_DNA.
DR   RefSeq; XP_001212579.1; XM_001212579.1.
DR   AlphaFoldDB; Q0CSD3; -.
DR   SMR; Q0CSD3; -.
DR   STRING; 341663.Q0CSD3; -.
DR   ESTHER; asptn-cbpya; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; Q0CSD3; 2 sites, No reported glycans.
DR   EnsemblFungi; EAU36675; EAU36675; ATEG_03401.
DR   GeneID; 4317774; -.
DR   VEuPathDB; FungiDB:ATEG_03401; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000007963; 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..138
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407439"
FT   CHAIN           139..557
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407440"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        472
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        534
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        224
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        523
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        193..433
FT                   /evidence="ECO:0000250"
FT   DISULFID        327..341
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..374
FT                   /evidence="ECO:0000250"
FT   DISULFID        358..367
FT                   /evidence="ECO:0000250"
FT   DISULFID        396..403
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   557 AA;  62443 MW;  5789C84F886F2EB9 CRC64;
     MRVLPATLLV GAATAAVPPF QQQFQQVLGI PQEEVEQAAP VAPSAPTTPK PLQIFQDQLK
     SLSDEARKLW DEVSNFFPDS MDHNPVFSLP KKHTRRPDSH WDHIVRGSDV QGVWVTGADG
     EKQREVDGKL EAYDLRVKKT DPSALGIDPG VKQYTGYLDD NENDKHLFYW FFESRNDPEN
     DPVVLWLNGG PGCSSLTGLF MELGPSSINE KIKPVYNEYS WNSNASVIFL DQPVNVGYSY
     SGSAVSDTVA AGKDVYALLT LFFKQFPEYA KQDFHIAGES YAGHYIPVFA SEILSHKKRN
     INLQSVLIGN GLTDGYTQYE YYRPMGCGEG GYPAVLDKGT CQSMDNALPR CQSMIKSCYE
     SESSWVCIPA SIYCNNALIG PYQRTGQNVY DVRGKCEDES NLCYKGMGYV SEYLNKAEVR
     QAVGAEVDGY DSCNFDINRN FLFHGDWMKP YHRLVPGLLE QIPVLIYAGD ADYICNWLGN
     KAWTEALEWP GQKEYASAEM EDLVIEQNAN TGKKIGQVKS HGNFTFMRIY GGGHMVPMDQ
     PESGLEFFNR WLGGEWF
//