CBPYA_FUSV7
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 03-AUG-2022, entry version 56.
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 STRING; 140110.NechaP100110; -.
DR MEROPS; S10.001; -.
DR EnsemblFungi; NechaT100110; NechaP100110; NechaG100110.
DR GeneID; 9673570; -.
DR KEGG; nhe:NECHADRAFT_100110; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_10_4_1; -.
DR InParanoid; C7YQJ2; -.
DR OMA; GDWMKPF; -.
DR OrthoDB; 625787at2759; -.
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; 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..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