ID   CBPYA_UNCRE             Reviewed;         541 AA.
AC   C4JNM2;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=cpyA; ORFNames=UREG_03020;
OS   Uncinocarpus reesii (strain UAMH 1704).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX   NCBI_TaxID=336963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 1704;
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}.
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DR   EMBL; CH476616; EEP78175.1; -; Genomic_DNA.
DR   RefSeq; XP_002543504.1; XM_002543458.1.
DR   AlphaFoldDB; C4JNM2; -.
DR   SMR; C4JNM2; -.
DR   STRING; 33188.XP_002543504.1; -.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; EEP78175; EEP78175; UREG_03020.
DR   GeneID; 8439365; -.
DR   KEGG; ure:UREG_03020; -.
DR   VEuPathDB; FungiDB:UREG_03020; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; C4JNM2; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000002058; 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..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..122
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407490"
FT   CHAIN           123..541
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407491"
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   541 AA;  60405 MW;  67D2CE6C1BB51FB4 CRC64;
     MKTFTAALLV GTALAAVPQQ QPLQTQVEDS AWAKPLEDLK DTIKSMGAEA KQAWDQLASA
     FPDALNEYTL FSAPKKHTRR PDSHWDHVVR GADVQGIWVD GVDGQKHREV DGKLENYDLR
     VKAVDPSKLG IDPGVKQFSG YLDDNENDKH LFYWFFESRN DPKNDPVVLW LNGGPGCSSL
     TGLFFELGPA SIDKNLKVIH NPYSWNSNAS VIFLDQPVNV GFSYSGSSVS DTIAAGKDVY
     ALLTLFFKQF PQYAKQDFHI AGESYAGHYI PAFASEILSH KNRNINLKSV LIGNGLTDPL
     TQYPHYRPMA CGEGGYPAVL DESSCRSMDN ALPRCQSMIE SCYSSESAWV CVPASIYCNN
     AMIGPYQRTG QNVYDVRTKC EDGSLCYTGL NYITQWLNQK PVMEALGAEV ESYDSCNMDI
     NRNFLFHGDW MKPYHRLVPG LIEKLPVLIY AGDADFICNW LGNKAWTETL EWSGRAEFAS
     AEMKNLTIVD NKSKGKNIGQ VKSHGNFTFM RLFGGGHMVP LDQPEASLEF FNRWLGGEWK
     A