ID   CBPYA_ASPFN             Reviewed;         542 AA.
AC   B8NXS9;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; ORFNames=AFLA_008990;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(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; EQ963486; EED45015.1; -; Genomic_DNA.
DR   RefSeq; XP_002385144.1; XM_002385103.1.
DR   AlphaFoldDB; B8NXS9; -.
DR   SMR; B8NXS9; -.
DR   STRING; 5059.CADAFLAP00013009; -.
DR   ESTHER; aspor-q2tya1; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; EED45015; EED45015; AFLA_008990.
DR   VEuPathDB; FungiDB:AFLA_008990; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OMA; GDWMKPF; -.
DR   Proteomes; UP000001875; 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   Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..123
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407432"
FT   CHAIN           124..542
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407433"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        519
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        178..418
FT                   /evidence="ECO:0000250"
FT   DISULFID        312..326
FT                   /evidence="ECO:0000250"
FT   DISULFID        336..359
FT                   /evidence="ECO:0000250"
FT   DISULFID        343..352
FT                   /evidence="ECO:0000250"
FT   DISULFID        381..388
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   542 AA;  60878 MW;  C9A6E7A124D3DA17 CRC64;
     MRVLPATLLV GAASAAVPPL QQVLGRPEEG MSFSKPLHAF QEQLKTLSED ARKLWDEVAN
     YFPDSMDHSP IFSLPKKHTR RPDSHWDHIV RGSDVQKIWV NNADGEKERE IDGKLEAYDL
     RVKKADPSAL GIDPNVKQYT GYLDDNGNDK HLFYWFFESR NDPKNDPVVL WLNGGPGCSS
     LTGLFMELGP SSIDENIKPV YNDFSWNSNA SVIFLDQPVN VGYSYSGSAV SDTVAAGKDV
     YALLSLFFKQ FPEYAEQDFH IAGESYAGHY IPVFASEILA HKNRNINLKS VLIGNGLTDG
     LTQYGYYRPM GCGEGGYKAV LDEATCESMD NALPRCRSMI ESCYNSESAW VCVPASIYCN
     NALIGPYQRT GQNVYDVRSK CEDESNLCYK GMGYVSEYLN KAEVREAVGA EVGGYDSCNF
     DINRNFLFHG DWMKPYHRLV PGLLEQIPVL IYAGDADYIC NWLGNKAWTE ALEWPGQKEY
     ASAELEDLKI EQNEHTGKKI GQVKSHGNFT FMRLYGGGHM VPMDQPEASL EFFNRWLGGE
     WF