CBPYA_MAGO7
ID CBPYA_MAGO7 Reviewed; 552 AA.
AC A4RPY8; G4MP00;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=CPYA; ORFNames=MGG_05663;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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; CM001231; EHA57949.1; -; Genomic_DNA.
DR RefSeq; XP_003710561.1; XM_003710513.1.
DR AlphaFoldDB; A4RPY8; -.
DR SMR; A4RPY8; -.
DR STRING; 318829.MGG_05663T0; -.
DR MEROPS; S10.001; -.
DR EnsemblFungi; MGG_05663T0; MGG_05663T0; MGG_05663.
DR GeneID; 2676004; -.
DR KEGG; mgr:MGG_05663; -.
DR VEuPathDB; FungiDB:MGG_05663; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; A4RPY8; -.
DR OMA; GDWMKPF; -.
DR OrthoDB; 625787at2759; -.
DR Proteomes; UP000009058; Chromosome 1.
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..133
FT /evidence="ECO:0000250"
FT /id="PRO_0000407453"
FT CHAIN 134..552
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407454"
FT ACT_SITE 274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 187..427
FT /evidence="ECO:0000250"
FT DISULFID 321..335
FT /evidence="ECO:0000250"
FT DISULFID 345..368
FT /evidence="ECO:0000250"
FT DISULFID 352..361
FT /evidence="ECO:0000250"
FT DISULFID 390..397
FT /evidence="ECO:0000250"
SQ SEQUENCE 552 AA; 61593 MW; B0F1815B4BD601B5 CRC64;
MRIATSTLLV GAASAAFAPQ DGTQRVLNGF DSIKSAAHSI QKPLQTFEEA MASMTSEAKA
NWDHLKLLVP DAEEQAKTFF PKKPKPASRK PDSAWDHIVK GADIQAMWVE GATPEETHRK
IDGKLDNYNL RARSVDPSKL GVDTVKQYSG YLDDEANDKH LFYWFFESRN DPKNDPVVLW
LNGGPGCSSL TGLLFELGPG AINAKIEIVH NPYAWNNNAS VIFLDQPVNV GYSYSGGSVS
NTVAAGKDIY ALLTLFFHQF PEYAKQDFHI AGESYAGHYI PVFASEILSH KKRNINLKSV
LIGNGLTDGL TQYEYYRPMA CGEGGWKAVL SESECQAMDN ALPRCQSMIQ NCYDSGSVWS
CVPASIYCNN AMIGPYQRTG RNVYDIRGPC KDSGNLCYPE LGYISEYLNR REVMEALGAE
VSSYDSCNFD INRNFLFQGD WMQPYHRLVP ELLNQIPVLI YAGDADFICN WLGNQGWTEA
LEWKGKKDYN RADYSPLTLA SAHDVKPYGK VKSSGNFTFM KIFEAGHMVP YDQAEPSVDF
VNRWLAGEWF AA
