ID   FNTA_PEA                Reviewed;         333 AA.
AC   O24304;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 74.
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   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=cv. Alaska; TISSUE=Root tip;
RX   PubMed=8989889; DOI=10.2307/3870476;
RA   Qian D., Zhou D., Ju R., Cramer C.L., Yang Z.;
RT   "Protein farnesyltransferase in plants: molecular characterization and
RT   involvement in cell cycle control.";
RL   Plant Cell 8:2381-2394(1996).
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:8989889}.
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:8989889};
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:8989889};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P29703};
CC   -!- SUBUNIT: Heterodimer of FTA and FTB (farnesyltransferase). Heterodimer
CC       of an alpha and a beta subunit. {ECO:0000269|PubMed:8989889}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U63298; AAB62580.1; -; mRNA.
DR   PIR; T06516; T06516.
DR   AlphaFoldDB; O24304; -.
DR   SMR; O24304; -.
DR   GO; GO:0005953; C:CAAX-protein geranylgeranyltransferase complex; ISS:UniProtKB.
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; Repeat; Transferase.
FT   CHAIN           1..333
FT                   /note="Protein
FT                   farnesyltransferase/geranylgeranyltransferase type-1
FT                   subunit alpha"
FT                   /id="PRO_0000119751"
FT   REPEAT          61..95
FT                   /note="PFTA 1"
FT   REPEAT          96..130
FT                   /note="PFTA 2"
FT   REPEAT          132..166
FT                   /note="PFTA 3"
FT   REPEAT          167..200
FT                   /note="PFTA 4"
FT   REPEAT          207..241
FT                   /note="PFTA 5"
SQ   SEQUENCE   333 AA;  38516 MW;  304926628B0C48C3 CRC64;
     MAGNIEVEED DRVPLRLRPE WSDVTPIPQD DGPSPVVPIN YSEEFSEVMD YFRAVYFAKE
     LSSRALALTA EAIGLNAGNY TVWHFRRLLL ESLKVDLHVE REFVERVASG NSKNYQIWHH
     RRWVAEKLGP EARNSELEFT KKILSVDAKH YHAWSHRQWV LQNLGGWEDE LSYCSELLAE
     DIFNNSAWNQ RYFVITRSPV LGGLKAMRES EVLFTVEAII SYPENESSWR YLRGLFKDES
     TLYVNDAQVS SLCLKILKTK SNYLFALSTL LDLSASVIQP NEDFRDAIEA LRLQILIKQD
     SDIAITICSI LEQVDPIRVN YWVWRKSRLP QAA