ID   CBPYA_AJEDR             Reviewed;         545 AA.
AC   C5GEU5;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=BDCG_02414;
OS   Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) (Blastomyces
OS   dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559297;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ER-3 / ATCC MYA-2586;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EQ999975; EEQ87294.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5GEU5; -.
DR   SMR; C5GEU5; -.
DR   STRING; 559297.C5GEU5; -.
DR   ESTHER; ajedr-cbpya; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; C5GEU5; 4 sites, No reported glycans.
DR   VEuPathDB; FungiDB:BDCG_02414; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 1647009at2759; -.
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; IPR018202; Ser_caboxypep_ser_AS.
DR   PANTHER; PTHR11802:SF113; CARBOXYPEPTIDASE Y; 1.
DR   PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 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   Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..123
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407420"
FT   CHAIN           124..545
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407421"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        455
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        517
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        485
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        491
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        506
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        177..416
FT                   /evidence="ECO:0000250"
FT   DISULFID        311..325
FT                   /evidence="ECO:0000250"
FT   DISULFID        335..358
FT                   /evidence="ECO:0000250"
FT   DISULFID        342..351
FT                   /evidence="ECO:0000250"
FT   DISULFID        380..386
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  60313 MW;  0585AD0619F2B453 CRC64;
     MKSLALALLV GGAIAAGPQQ QVLQAPVDNP DVAEPPLQTI ADTFDHLRGQ ATNLWNDVID
     KVPNIMDTIT HTPPPKKFNR RPDSEWNHIV RGAEIQAVWV EGDDGEKHRK VGGKLEAYDL
     RVKAVDPKSL GVDTVRQYSG YLDDNENDKH LFYWFFESRN DPENDPVVLW LNGGPGCSSL
     TGLFLELGPS SITEDLKVNY NPYSWNANAS VIFLDQPVNV GYSYSGGSVS DTNAAGKDVY
     ALLTLFFEQF PEYAKQDFHI AGESYAGHYI PVFASEIMAH KERNINLKSI LIGNGLTDPL
     TQYPLYRPMA CGEGGYPAVL DQASCQSMDN ALPRCLSMIE ACYSSESAWT CVPASIYCNN
     AIIGPYQRTG RNPYDVRTDC EGGNLCYTQL GDISKYLNQA EVMKALGAEV STYDSCNMDI
     NRNFLFRGDW MKPFHRLVPG LIAEMPVLLY AGDADFICNW LGNKAWAEAL EYPGHAKFAA
     AEMKNLTIVD NKSKGKVIGQ VKSAGNFTFM RLYGGGHMVP LDQPEASLEF MNRWLKGEWS
     AKSSS
//