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FNTA_SOLLC
ID   FNTA_SOLLC              Reviewed;         346 AA.
AC   P93227;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha;
DE            EC=2.5.1.58;
DE            EC=2.5.1.59;
DE   AltName: Full=CAAX farnesyltransferase subunit alpha;
DE   AltName: Full=FTase-alpha;
DE   AltName: Full=Ras proteins prenyltransferase subunit alpha;
DE   AltName: Full=Type I protein geranyl-geranyltransferase subunit alpha;
DE            Short=GGTase-I-alpha;
GN   Name=FTA;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=cv. VFNT Cherry LA1221;
RX   PubMed=9121446; DOI=10.1128/mcb.17.4.1986;
RA   Yalovsky S., Trueblood C.E., Callan K.L., Narita J.O., Jenkins S.M.,
RA   Rine J., Gruissem W.;
RT   "Plant farnesyltransferase can restore yeast Ras signaling and mating.";
RL   Mol. Cell. Biol. 17:1986-1994(1997).
CC   -!- FUNCTION: Essential subunit of both the farnesyltransferase and the
CC       geranylgeranyltransferase complex. Contributes to the transfer of a
CC       farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl
CC       diphosphate to a cysteine at the fourth position from the C-terminus of
CC       several proteins having the C-terminal sequence Cys-aliphatic-
CC       aliphatic-X. {ECO:0000269|PubMed:9121446}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] =
CC         diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019,
CC         ChEBI:CHEBI:175763; EC=2.5.1.58;
CC         Evidence={ECO:0000269|PubMed:9121446};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC         diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC         ChEBI:CHEBI:86021; EC=2.5.1.59;
CC         Evidence={ECO:0000269|PubMed:9121446};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P29703};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC       {ECO:0000269|PubMed:9121446}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC       family. {ECO:0000305}.
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DR   EMBL; U83707; AAC49665.1; -; mRNA.
DR   PIR; T07665; T07665.
DR   AlphaFoldDB; P93227; -.
DR   SMR; P93227; -.
DR   STRING; 4081.Solyc06g073390.2.1; -.
DR   PaxDb; P93227; -.
DR   PRIDE; P93227; -.
DR   eggNOG; KOG0530; Eukaryota.
DR   InParanoid; P93227; -.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P93227; baseline.
DR   GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004662; F:CAAX-protein geranylgeranyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004660; F:protein farnesyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004661; F:protein geranylgeranyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblPlants.
DR   GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IEA:EnsemblPlants.
DR   GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR   GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:EnsemblPlants.
DR   GO; GO:0048509; P:regulation of meristem development; IEA:EnsemblPlants.
DR   GO; GO:0009414; P:response to water deprivation; IEA:EnsemblPlants.
DR   InterPro; IPR002088; Prenyl_trans_a.
DR   Pfam; PF01239; PPTA; 4.
DR   PROSITE; PS51147; PFTA; 5.
PE   1: Evidence at protein level;
KW   Magnesium; Prenyltransferase; Reference proteome; Repeat; Transferase.
FT   CHAIN           1..346
FT                   /note="Protein
FT                   farnesyltransferase/geranylgeranyltransferase type-1
FT                   subunit alpha"
FT                   /id="PRO_0000119750"
FT   REPEAT          59..93
FT                   /note="PFTA 1"
FT   REPEAT          94..128
FT                   /note="PFTA 2"
FT   REPEAT          130..164
FT                   /note="PFTA 3"
FT   REPEAT          165..198
FT                   /note="PFTA 4"
FT   REPEAT          205..239
FT                   /note="PFTA 5"
SQ   SEQUENCE   346 AA;  40103 MW;  17952611F8D8CACE CRC64;
     MDSCEVTKTR IPFKERPDWA DVKPVPQDDG PCPVVPIAYT EDFSETMDYF RAIYVADERS
     TRALQLTGEA IQLNPGNYTV WQFRRVVLEA LGVDLREELK FVDRIAGENT KNYQIWHHRR
     WLAEKLGADA VTNELEFTKK IFSQDAKNYH AWSHRQWVLQ ALGGWEDELA YCQQLLEDDI
     YNNSAWNQRY FVVTRSPLLG GLVAMRELEV NYTVQAIRAS PENESPWRYL RGLYKNDTQS
     LVQDSQVASV LWDVLTSQNS HVHALRFLLD LLCHDLEPSQ ELKSAVDVLT PQSCSPDLAL
     TKKICSILEH ADPMRVKYWN WRKSMVRVQL LQSQNAERLA NLSVQE
 
 
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