ID   CBPYA_BOTFB             Reviewed;         546 AA.
AC   A6RUD7;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=BC1G_03711;
OS   Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS   cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=332648;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B05.10;
RX   PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA   Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA   Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA   Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA   Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA   Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA   Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA   Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA   Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA   Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA   Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA   Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA   Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA   Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT   "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT   sclerotiorum and Botrytis cinerea.";
RL   PLoS Genet. 7:E1002230-E1002230(2011).
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         ECO:0000255|PROSITE-ProRule:PRU10075};
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR   EMBL; CH476857; EDN21690.1; -; Genomic_DNA.
DR   RefSeq; XP_001557447.1; XM_001557397.1.
DR   AlphaFoldDB; A6RUD7; -.
DR   SMR; A6RUD7; -.
DR   MEROPS; S10.001; -.
DR   GeneID; 5438040; -.
DR   KEGG; bfu:BCIN_10g04320; -.
DR   VEuPathDB; FungiDB:Bcin10g04320; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 625787at2759; -.
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; IPR033124; Ser_caboxypep_his_AS.
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; PS00560; CARBOXYPEPT_SER_HIS; 1.
DR   PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW   Signal; Vacuole; Zymogen.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   PROPEP          18..132
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407441"
FT   CHAIN           133..546
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407442"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        465
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        523
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        512
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        186..426
FT                   /evidence="ECO:0000250"
FT   DISULFID        320..334
FT                   /evidence="ECO:0000250"
FT   DISULFID        344..367
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        389..396
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   546 AA;  60852 MW;  57286623880833A9 CRC64;
     MKLLASTVLV GAAAASITPQ QQVLQNPFKS ATKPVSDAWS KSMESLGHLT GSMKGMTAEA
     KAIWDEVSML FPEAMEKAAF FSEPKPHTRK PDSTWDYIVK GADIQSVWVE NSKGEKEREI
     DGKLEQYNLR AKKVDPSKLG VDTVKQYSGY LDDEEDDKHL FYWFFESRND PKNDPVVLWL
     NGGPGCSSLT GLFLELGPSS IDKNLKLHNN PYSWNANASV IFLDQPVNVG YSYSGSSVSN
     TVAAGKDVYA LLTLFFKQFP EYAKQDFHIA GESYAGHYIP VFTSEILSHK KRNINLKSVL
     IGNGLTDGLT QYEHYRPMAC GDGGWPAVLG ASECQAMDNA LPRCQSLIQN CYDSESVWSC
     VPASIYCNNA MMGPYQRTGQ NVYDVRGKCE DTSNLCYSAL GWISEFLNKA DVQKELGVEV
     SSYDSCNFDI NRNFLFQGDW MKPFHRLVPG ILEQIPVLIY AGDADFICNW LGNQAWTDAL
     EWPGKKDFNA AKTKDLQLES GHKTGTFKSS GNFTFARIFG AGHMVPMDQP EASLDFLNKW
     LNDYTL