CBPYA_SCLS1
ID CBPYA_SCLS1 Reviewed; 546 AA.
AC A7F4H5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Carboxypeptidase Y homolog A;
DE EC=3.4.16.5;
DE Flags: Precursor;
GN Name=cpyA; ORFNames=SS1G_12500;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
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; CH476641; EDN97646.1; -; Genomic_DNA.
DR RefSeq; XP_001586513.1; XM_001586463.1.
DR AlphaFoldDB; A7F4H5; -.
DR SMR; A7F4H5; -.
DR STRING; 665079.A7F4H5; -.
DR MEROPS; S10.001; -.
DR PRIDE; A7F4H5; -.
DR EnsemblFungi; EDN97646; EDN97646; SS1G_12500.
DR GeneID; 5482640; -.
DR KEGG; ssl:SS1G_12500; -.
DR VEuPathDB; FungiDB:sscle_06g054270; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; A7F4H5; -.
DR OMA; GDWMKPF; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
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 Reference proteome; Signal; Vacuole; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..132
FT /evidence="ECO:0000250"
FT /id="PRO_0000407476"
FT CHAIN 133..546
FT /note="Carboxypeptidase Y homolog A"
FT /id="PRO_0000407477"
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; 61151 MW; 02150015494651E2 CRC64;
MKLLASTVLM GAAAASIAPQ QQVLKNPFQS ASKPISEAWS KSMESLNHLT DSMKDMTSEA
KAVWDEVSTL FPEAMDRATF FQQPKPHTRK PDTAWDYVVK GADIQNVWVE NSKGEKEREI
DGKLEKYNMR AKKVDPTKLG VDKVKQYSGY LDDEENDKHL FYWFFESRND PKNDPVVLWL
NGGPGCSSLT GLFLELGPAS IDKNGKLHNN PYSWNANASV IFLDQPVNVG YSYSGGSVSN
TIAAGKDVYA LLTLFFKQFP EYAKQDFHIA GESYAGHYIP VFTHEILSHK KRNINLKSVL
IGNGLTDGLT QYEHYRPMAC GEGGYPAVLD SSECKAMDNA LPRCQSLIQS CYDSESVWSC
VPASIYCNNA MMGPYQRTGQ NVYDIRGKCE DSSNLCYSAL GWISDYLNQA AVQKELGVEV
SSYDSCNFDI NRNFLFQGDW MQPFHRLVPD ILEQIPVLIY AGDADFICNW LGNQAWTEAL
EWPGQKGFNA AKTKDLQLEN GHKTGTFKSS GNFTFARIFG AGHMVPMDQP EASLDFLNKW
LNDYTL
