ID F6H1D7_VITVI Unreviewed; 488 AA.
AC F6H1D7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Carboxypeptidase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=VIT_18s0001g11100 {ECO:0000313|EMBL:CCB45872.1};
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB45872.1, ECO:0000313|Proteomes:UP000009183};
RN [1] {ECO:0000313|Proteomes:UP000009183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX PubMed=17721507; DOI=10.1038/nature06148;
RG The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA Wincker P.;
RT "The grapevine genome sequence suggests ancestral hexaploidization in major
RT angiosperm phyla.";
RL Nature 449:463-467(2007).
CC -!- SIMILARITY: Belongs to the peptidase S10 family.
CC {ECO:0000256|ARBA:ARBA00009431}.
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DR EMBL; FN595227; CCB45872.1; -; Genomic_DNA.
DR RefSeq; XP_002282331.1; XM_002282295.4.
DR AlphaFoldDB; F6H1D7; -.
DR STRING; 29760.F6H1D7; -.
DR PaxDb; 29760-VIT_18s0001g11100-t01; -.
DR EnsemblPlants; Vitvi18g00836_t001; Vitvi18g00836_P001; Vitvi18g00836.
DR GeneID; 100255855; -.
DR Gramene; Vitvi18g00836_t001; Vitvi18g00836_P001; Vitvi18g00836.
DR KEGG; vvi:100255855; -.
DR eggNOG; KOG1282; Eukaryota.
DR HOGENOM; CLU_008523_13_2_1; -.
DR InParanoid; F6H1D7; -.
DR OrthoDB; 1647009at2759; -.
DR Proteomes; UP000009183; Chromosome 18.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.11320; -; 1.
DR Gene3D; 6.10.250.940; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR033124; Ser_caboxypep_his_AS.
DR PANTHER; PTHR11802:SF470; CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR11802; SERINE PROTEASE FAMILY S10 SERINE CARBOXYPEPTIDASE; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..488
FT /note="Carboxypeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003335280"
SQ SEQUENCE 488 AA; 54071 MW; 8E42A44FBF80A349 CRC64;
MKVAPLTWLL PLLLCYQLAL LLPYSGATET ENLYRLINSR RSANPPRSEL WDELDGRDGN
ASPLYIGPQD GLMQDDKIES LPGQPEGVNF DQYAGYVTVD PKAGRALFYY FVESPEDSST
KPLVLWLNGG PGCSSLGYGA MEELGPFRVN PDGKTLFRNE YAWNNVSNVI FLESPAGVGF
SYSNTSSDYV NVGDKKTAED SYTFLINWLE RFPQYKTRDF FITGESYSGH YVPQLAYTIL
SNNNKTNQTV INLKGIAIGN AWIDDNTSLK GIYDYIWTHA LSSDESNAGI QKYCDFTTGN
FSTKCLDYTY QAEGEVGNID IYNIYAPLCH SSGPTSRSVG SVNDFDPCSD YYVESYLNLA
EVQKALHARN TTWGACSGVG WTDSPTTILP TIKQLMASGI SVWIYSGDTD GRVPVTSSRY
SINTFKLPVK TAWRPWYYNK EVGGYVVEYK GVVFATVRGA GHLVPSYQPG RALTMIASFL
QGTLPPPS
//
