FNTA_DICDI
ID FNTA_DICDI Reviewed; 322 AA.
AC Q54RT9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=fntA; ORFNames=DDB_G0283053;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the transfer of a farnesyl or geranyl-geranyl
CC moiety from farnesyl or geranyl-geranyl diphosphate to a cysteine at
CC the fourth position from the C-terminus of several proteins having the
CC C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is
CC thought to participate in a stable complex with the substrate. The beta
CC subunit binds the peptide substrate (By similarity). {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P29703};
CC -!- SUBUNIT: Heterodimer of fntA and fntB (farnesyltransferase).
CC Heterodimer of an alpha and a beta subunit (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit alpha
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000049; EAL65970.1; -; Genomic_DNA.
DR RefSeq; XP_639262.1; XM_634170.1.
DR AlphaFoldDB; Q54RT9; -.
DR SMR; Q54RT9; -.
DR STRING; 44689.DDB0237551; -.
DR PaxDb; Q54RT9; -.
DR EnsemblProtists; EAL65970; EAL65970; DDB_G0283053.
DR GeneID; 8623832; -.
DR KEGG; ddi:DDB_G0283053; -.
DR dictyBase; DDB_G0283053; fntA.
DR eggNOG; KOG0530; Eukaryota.
DR HOGENOM; CLU_026582_1_1_1; -.
DR InParanoid; Q54RT9; -.
DR OMA; RRKYWQY; -.
DR PhylomeDB; Q54RT9; -.
DR Reactome; R-DDI-9648002; RAS processing.
DR PRO; PR:Q54RT9; -.
DR Proteomes; UP000002195; Chromosome 4.
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:0018343; P:protein farnesylation; ISS:UniProtKB.
DR GO; GO:0018344; P:protein geranylgeranylation; ISS:UniProtKB.
DR InterPro; IPR002088; Prenyl_trans_a.
DR Pfam; PF01239; PPTA; 4.
DR PROSITE; PS51147; PFTA; 5.
PE 3: Inferred from homology;
KW Magnesium; Prenyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..322
FT /note="Protein
FT farnesyltransferase/geranylgeranyltransferase type-1
FT subunit alpha"
FT /id="PRO_0000328341"
FT REPEAT 62..95
FT /note="PFTA 1"
FT REPEAT 103..136
FT /note="PFTA 2"
FT REPEAT 138..171
FT /note="PFTA 3"
FT REPEAT 173..205
FT /note="PFTA 4"
FT REPEAT 213..246
FT /note="PFTA 5"
FT REPEAT 287..321
FT /note="PFTA 6"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 322 AA; 38207 MW; 8510FAFB16265428 CRC64;
MSSSEEDDGY VPFSKRPEWS DVKPLAQDDG PHPICPILYS EVFKDKMNYF RAILKSKEKS
LRVLDLLEEV IQENPSNYTI WYYRREVLKA IEQDETIEYD IQQEMNLLND MGETDPKNYQ
IWNHRRFIVE KYIGSDNKEK EFLSGVLLED AKNYHAWSHR QWLLKTYRDW NGELAMVDKL
LSLDHRNNSV WNHRFFVISN LNPSPFPLSL IEREVEFAFN HIRHSPNNES PWSYLKGLFK
GQKISTIYPS LLDILLEMKS KYIGCSHVNS IILDIYQEQN TKISLENSLN ICKLLSETID
PIHKNYWNFK YNTISDQLKL IN
