ID   CBPYA_COLGM             Reviewed;         545 AA.
AC   E3QR43;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=GLRG_08475;
OS   Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS   anthracnose fungus) (Glomerella graminicola).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=645133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M1.001 / M2 / FGSC 10212;
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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; GG697369; EFQ33331.1; -; Genomic_DNA.
DR   RefSeq; XP_008097351.1; XM_008099160.1.
DR   AlphaFoldDB; E3QR43; -.
DR   SMR; E3QR43; -.
DR   STRING; 645133.E3QR43; -.
DR   ESTHER; colgm-cbpya; Carboxypeptidase_S10.
DR   GlyCosmos; E3QR43; 2 sites, No reported glycans.
DR   EnsemblFungi; EFQ33331; EFQ33331; GLRG_08475.
DR   GeneID; 24413840; -.
DR   VEuPathDB; FungiDB:GLRG_08475; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000008782; 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..130
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407447"
FT   CHAIN           131..545
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407448"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        463
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        521
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        184..424
FT                   /evidence="ECO:0000250"
FT   DISULFID        318..332
FT                   /evidence="ECO:0000250"
FT   DISULFID        342..365
FT                   /evidence="ECO:0000250"
FT   DISULFID        349..358
FT                   /evidence="ECO:0000250"
FT   DISULFID        387..394
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  60571 MW;  BE47D30082A91640 CRC64;
     MRFSTSALVL GAASTAVALD QQVLGGNESP FDSIKVAGQE WLSTFEEKFG KMTTEAKAVW
     DEITLLAPDA VESFKKNAIP PKPKPAHRKS DKKWDHVVKG ADVQSMWVEK NGEKHRKIAG
     DLKNFNLRAK KVDPSALGID KVKQYSGYLD DEENDKHLFY WFFESRNDPK NDPVVLWLNG
     GPGCSSLTGL FMELGPASVD KKLKIVNNEW SWNNNASVIF LDQPVNVGYS YSGSSVSNTV
     AAGKDVYALL SLFFHQFPEY SKQDFHIAGE SYAGHYIPVF ASEILSHEDR NINLKSVLIG
     NGLTDGLTQY GYYRPMACGE GGYPAVLDAG ECQAMDNALP RCQSLINNCY ESGSVWSCVP
     ASIYCNNALI GPYQRTGQNV YDIRGKCEDS SNLCYSALGW ISEYLNQDEV KEALGAEVDS
     YDSCNFDINR NFLFAGDWFQ PFHRIVPKLL EKIPVLIYAG DADYICNWLG NRAWTEALEW
     PGQKGFNKAE VKSLAVGKGK EYGKVKSSGN FTFMQLYGAG HMVPMDQPEA SSDFLNRWLG
     GEWVA
//