ID   CBPYA_AJECG             Reviewed;         544 AA.
AC   C0NX46;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=HCBG_08038;
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) 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; GG663375; EEH03912.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NX46; -.
DR   SMR; C0NX46; -.
DR   STRING; 447093.C0NX46; -.
DR   ESTHER; ajecg-cbpya; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; C0NX46; 2 sites, No reported glycans.
DR   VEuPathDB; FungiDB:I7I50_08293; -.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; C0NX46; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000001631; 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..124
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407416"
FT   CHAIN           125..544
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407417"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        456
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        517
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        209
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        178..417
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..387
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   544 AA;  60584 MW;  B885B537E0B9C911 CRC64;
     MKSLALALLV GGAIASGPQQ QVLREPVDDP QAAETPLQKI SDIFGHLSEQ AGNVWEDVMD
     KFPDTLMDAI TQTPPPKKHN RRPDSQWDHI VRGSDVQAVW VEGDAGEKHR KVGGRLDTYD
     LRVKAVDPSN LGIDTVKQYS GYLDDNENDK HLFYWFFESR NDPKNDPVVL WLNGGPGCSS
     LTGLFLELGP SSITKQLKVK YNEFSWNSNA SVIFLDQPVN VGYSYSSSSV SNTQAAGKDV
     YALLTLFFEQ FPEYSQQDFH IAGESYAGHY IPVFASEIMS HSHRNINLKS ILVGNGLTDP
     LSQYPHYRPM ACGEGGYPAV LSSSSCQAMD NALPRCLAMI QACYNTESRW SCVPASIYCN
     NALIGPYQRS GMNPYDVRSK CEGGNLCYTQ LDDISKYLNQ DAVMESLGAE VSSYESCNMD
     INRNFLFQGD WMQPYMRVVP TLLTQMPVLI YAGDADFICN WLGNKAWTEA LEYPGHDEFA
     AAEMKNLTSL NHEDMKVIGQ VKSAGNFTFM RLFGGGHMVP MDQPEASLEF FNRWLGGEWS
     AKSP
//