CBPYA_AJEDR
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 03-AUG-2022, entry version 47.
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}.
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DR EMBL; EQ999975; EEQ87294.1; -; Genomic_DNA.
DR AlphaFoldDB; C5GEU5; -.
DR SMR; C5GEU5; -.
DR STRING; 559297.C5GEU5; -.
DR MEROPS; S10.001; -.
DR EnsemblFungi; EEQ87294; EEQ87294; BDCG_02414.
DR VEuPathDB; FungiDB:BDCG_02414; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR OMA; GDWMKPF; -.
DR Proteomes; UP000002039; 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; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 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..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