CBPYA_COLGM
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 03-AUG-2022, entry version 45.
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 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; 625787at2759; -.
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; 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..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