ID   CBPYA_AJECN             Reviewed;         545 AA.
AC   A6RGA0;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=HCAG_08666;
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC   unclassified Histoplasma.
OX   NCBI_TaxID=2059318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
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; CH476666; EDN05012.1; -; Genomic_DNA.
DR   RefSeq; XP_001536345.1; XM_001536295.1.
DR   AlphaFoldDB; A6RGA0; -.
DR   SMR; A6RGA0; -.
DR   STRING; 339724.A6RGA0; -.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; EDN05012; EDN05012; HCAG_08666.
DR   GeneID; 5442623; -.
DR   KEGG; aje:HCAG_08666; -.
DR   VEuPathDB; FungiDB:HCAG_08666; -.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000009297; 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   Reference proteome; Signal; Vacuole; Zymogen.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..125
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407418"
FT   CHAIN           126..545
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407419"
FT   ACT_SITE        266
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        518
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        210
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        507
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        179..418
FT                   /evidence="ECO:0000250"
FT   DISULFID        313..327
FT                   /evidence="ECO:0000250"
FT   DISULFID        337..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..353
FT                   /evidence="ECO:0000250"
FT   DISULFID        382..388
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  60747 MW;  4E49F04D1C55BB8D CRC64;
     MKSSLALALL VGGAIASGPQ QQVLREPVDH PQAAETPLQK ISDIFGHLSE QAGNVWEDVM
     DKFPDTLMDA ITQTPPPKKH NRRPDSEWDH IVRGSDVQAV WVEGDAGEKH RKVGGRLDTY
     DLRVKAVDPS NLGVDTVKQY SGYLDDNEND KHLFYWFFES RNDPKNDPVV LWLNGGPGCS
     SLTGLFLELG PSSITKQLKV EYNEFSWNSN ASVIFLDQPV NVGYSYSSSS VSNTQAAAKD
     VYALLTLFFE QFPEYSRQDF HIAGESYAGH YIPVFASEIM SHSHRNINLK SILVGNGLTD
     PLSQYPHYRP MACGEGGYPA VLSSSSCQAM DNALPRCLAM IQACYNTESR WSCVPASIYC
     NNALIGPYQR SGMNPYDVRS KCEGGSLCYT QLDDISKYLN RNAVMESLGA EVSSYESCNM
     DINRNFLFQG DWMQPYMRVV PTLLAQMPVL IYAGDADFIC NWLGNKAWTE ALEYPGHNEF
     AAAEMKNLTS QNHEDVRVIG QVKSAGNFTF MRLFGGGHMV PMDQPEASLE FFNRWLGGEW
     SDKSP