ID   CBPYA_SORMK             Reviewed;         554 AA.
AC   D1ZG13; F7VS77;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, 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=SMAC_01911;
OS   Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Sordaria.
OX   NCBI_TaxID=771870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-333 / DSM 997 / K(L3346) / K-hell;
RX   PubMed=20386741; DOI=10.1371/journal.pgen.1000891;
RA   Nowrousian M., Stajich J.E., Chu M., Engh I., Espagne E., Halliday K.,
RA   Kamerewerd J., Kempken F., Knab B., Kuo H.-C., Osiewacz H.D., Poeggeler S.,
RA   Read N.D., Seiler S., Smith K.M., Zickler D., Kueck U., Freitag M.;
RT   "De novo assembly of a 40 Mb eukaryotic genome from short sequence reads:
RT   Sordaria macrospora, a model organism for fungal morphogenesis.";
RL   PLoS Genet. 6:E1000891-E1000891(2010).
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; CABT02000005; CCC08363.1; -; Genomic_DNA.
DR   RefSeq; XP_003348887.1; XM_003348839.1.
DR   AlphaFoldDB; D1ZG13; -.
DR   SMR; D1ZG13; -.
DR   STRING; 771870.D1ZG13; -.
DR   ESTHER; neucr-CBPYA; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   EnsemblFungi; CCC08363; CCC08363; SMAC_01911.
DR   GeneID; 10806348; -.
DR   KEGG; smp:SMAC_01911; -.
DR   VEuPathDB; FungiDB:SMAC_01911; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; D1ZG13; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 625787at2759; -.
DR   Proteomes; UP000001881; 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..137
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407478"
FT   CHAIN           138..554
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407479"
FT   ACT_SITE        278
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        470
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        529
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        518
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        191..431
FT                   /evidence="ECO:0000250"
FT   DISULFID        325..339
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..372
FT                   /evidence="ECO:0000250"
FT   DISULFID        356..365
FT                   /evidence="ECO:0000250"
FT   DISULFID        394..401
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   554 AA;  62144 MW;  F12D1F1AB69EFF3D CRC64;
     MRISASTVLL GAASAASAAS FQNQAQQVLA DNFHKAHDAI KPVADSFAHT TLESFEEAFN
     GMNSQAKALW DEIKLLVPES AFDKPTWFSK PKAAKRRKDW DHVVKGADVQ KLWVKGADGE
     KHREVGGQLD NFNLRVKSVD PSKLGVDKVK QYSGYLDDEA NDKHLFYWFF ESRNDPKNDP
     VVLWLNGGPG CSSLTGLFLE LGPSSIDKKL KVINNEYAWN NNASVIFLDQ PVNVGYSYSG
     NAVSNTVAAG KDVYALLTLF FHQFPEYAKQ DFHIAGESYA GHYIPVFASE ILSHKDRNIN
     LKSVLIGNGL TDPLTQYEHY RPMACGEGGY PAVLSESECR SMDNALPRCQ SLIRNCYESG
     SVWSCVPAAI YCNNQFIGPY QRTGQNVYDI RGKCEDDNNL CYSALGWISD YLNQKDVMDA
     LGVEVESYDS CNFDINRNFL FQGDWMQPFH RLVPGILKEI PVLIYAGDAD FICNWLGNKA
     WSEALEWPGK KGFNKAELED LSLPEADKEY GKVKSSGNFT FMQIYQAGHM VPMDQPENSL
     DFLNRWLGGE WFEQ