ID   CBPYA_FUSV7             Reviewed;         537 AA.
AC   C7YQJ2;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=Carboxypeptidase Y homolog A;
DE            EC=3.4.16.5;
DE   Flags: Precursor;
GN   Name=CPYA; ORFNames=NECHADRAFT_100110;
OS   Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL
OS   45880 / 77-13-4) (Fusarium solani subsp. pisi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex; Fusarium vanettenii.
OX   NCBI_TaxID=660122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4;
RX   PubMed=19714214; DOI=10.1371/journal.pgen.1000618;
RA   Coleman J.J., Rounsley S.D., Rodriguez-Carres M., Kuo A., Wasmann C.C.,
RA   Grimwood J., Schmutz J., Taga M., White G.J., Zhou S., Schwartz D.C.,
RA   Freitag M., Ma L.-J., Danchin E.G.J., Henrissat B., Coutinho P.M.,
RA   Nelson D.R., Straney D., Napoli C.A., Barker B.M., Gribskov M., Rep M.,
RA   Kroken S., Molnar I., Rensing C., Kennell J.C., Zamora J., Farman M.L.,
RA   Selker E.U., Salamov A., Shapiro H., Pangilinan J., Lindquist E.,
RA   Lamers C., Grigoriev I.V., Geiser D.M., Covert S.F., Temporini E.,
RA   VanEtten H.D.;
RT   "The genome of Nectria haematococca: contribution of supernumerary
RT   chromosomes to gene expansion.";
RL   PLoS Genet. 5:E1000618-E1000618(2009).
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; GG698898; EEU46033.1; -; Genomic_DNA.
DR   RefSeq; XP_003051746.1; XM_003051700.1.
DR   AlphaFoldDB; C7YQJ2; -.
DR   SMR; C7YQJ2; -.
DR   ESTHER; fusv7-cbpya; Carboxypeptidase_S10.
DR   MEROPS; S10.001; -.
DR   GlyCosmos; C7YQJ2; 2 sites, No reported glycans.
DR   EnsemblFungi; NechaT100110; NechaP100110; NechaG100110.
DR   GeneID; 9673570; -.
DR   KEGG; nhe:NECHADRAFT_100110; -.
DR   VEuPathDB; FungiDB:NECHADRAFT_100110; -.
DR   eggNOG; KOG1282; Eukaryota.
DR   HOGENOM; CLU_008523_10_4_1; -.
DR   InParanoid; C7YQJ2; -.
DR   OMA; GDWMKPF; -.
DR   OrthoDB; 1647009at2759; -.
DR   Proteomes; UP000005206; 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..124
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000407455"
FT   CHAIN           125..537
FT                   /note="Carboxypeptidase Y homolog A"
FT                   /id="PRO_0000407456"
FT   ACT_SITE        265
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        457
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   ACT_SITE        514
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        503
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        178..418
FT                   /evidence="ECO:0000250"
FT   DISULFID        312..326
FT                   /evidence="ECO:0000250"
FT   DISULFID        336..359
FT                   /evidence="ECO:0000250"
FT   DISULFID        343..352
FT                   /evidence="ECO:0000250"
FT   DISULFID        381..388
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   537 AA;  60161 MW;  08BE047930A51F10 CRC64;
     MRLSTSALVL GAASSAVAFD QKVLGDLKKP AIDLDLSSWL NFGEEITAEA KAVWEEVSML
     APDAVEAFKK QVIGTKPKKA NRRPDNHWDH VVKGADVQSI WVDKNNEKHR KVGGRLDNYN
     LRAKKVDPSK LGVDKVKQYS GYLDDEEQDK HLFYWFFESR NDPENDPVVL WLNGGPGCSS
     LTGLFLELGP ASINKKIEIV NNPWSWNNNA SVIFLDQPVN VGYSYSGGSV SNTVAAGKDI
     YALLTLFFHQ FPEYAKQDFH IAGESYAGHY IPVFANEILS HEDRNINLKS VLIGNGLTDG
     YTQYEYYRPM ACGEGGYPSV LSESECQSMD NALPRCQSLI KGCYESGSAW SCVPASIYCN
     NAMMGPYQRT GRNVYDIRGN CEDSSNLCYS GLGYIAEYLN RQDVQDALGA EVSSYDSCNM
     DINRNFLFAG DWMQPYHQVV PNLLEKIPVL IYAGDADFIC NWLGNQAWTN KLEWPGHKDF
     KNADIKNLKV EGKEYGKIKT SGNFTFMQIY GAGHMVPMDQ PEASSDFFNR WLGGEWF
//