Q54RT9 (FNTA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
EC=2.5.1.58
EC=2.5.1.59

Alternative name(s):
CAAX farnesyltransferase subunit alpha
FTase-alpha
Ras proteins prenyltransferase subunit alpha
Type I protein geranyl-geranyltransferase subunit alpha
Short name=GGTase-I-alpha

Gene names

Name:	fntA
ORF Names:	DDB_G0283053

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate By similarity.
Catalytic activity	Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate. Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Subunit structure	Heterodimer of an alpha and a beta subunit By similarity.
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 6 PFTA repeats.

Ontologies

Keywords
Domain	Repeat
Molecular function	Prenyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein farnesylation Inferred from sequence or structural similarity. Source: dictyBase
Cellular component	protein farnesyltransferase complex Inferred from sequence or structural similarity. Source: dictyBase
Molecular function	CAAX-protein geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC protein farnesyltransferase activity Inferred from sequence or structural similarity. Source: dictyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 322	322	Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha		PRO_0000328341
Regions
	Repeat	62 – 95	34	PFTA 1
	Repeat	103 – 136	34	PFTA 2
	Repeat	138 – 171	34	PFTA 3
	Repeat	173 – 205	33	PFTA 4
	Repeat	213 – 246	34	PFTA 5
	Repeat	287 – 321	35	PFTA 6

Sequences

	Sequence		Length	Mass (Da)
	Q54RT9 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 8510FAFB16265428	FASTA	322	38,207
	10 20 30 40 50 60 MSSSEEDDGY VPFSKRPEWS DVKPLAQDDG PHPICPILYS EVFKDKMNYF RAILKSKEKS 70 80 90 100 110 120 LRVLDLLEEV IQENPSNYTI WYYRREVLKA IEQDETIEYD IQQEMNLLND MGETDPKNYQ 130 140 150 160 170 180 IWNHRRFIVE KYIGSDNKEK EFLSGVLLED AKNYHAWSHR QWLLKTYRDW NGELAMVDKL 190 200 210 220 230 240 LSLDHRNNSV WNHRFFVISN LNPSPFPLSL IEREVEFAFN HIRHSPNNES PWSYLKGLFK 250 260 270 280 290 300 GQKISTIYPS LLDILLEMKS KYIGCSHVNS IILDIYQEQN TKISLENSLN ICKLLSETID 310 320 PIHKNYWNFK YNTISDQLKL IN

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000049 Genomic DNA. Translation: EAL65970.1.
RefSeq	XP_639262.1. XM_634170.1.
3D structure databases
HSSP	HSSP built from PDB template 1S63 based on UniProtKB P49354.
ProteinModelPortal	Q54RT9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q54RT9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0237551; DDB0237551; DDB_G0283053.
GeneID	8623832.
GenomeReviews	Gene locus fntA in contig CM000153_GR.
KEGG	ddi:DDB_G0283053.
Organism-specific databases
dictyBase	DDB_G0283053. fntA.
Phylogenomic databases
eggNOG	KOG0530.
GeneTree	EPrGT00050000003104.
HOGENOM	HBG623262.
OMA	VEWLRDP.
PhylomeDB	Q54RT9.
ProtClustDB	CLSZ2728981.
Family and domain databases
InterPro	IPR002088. Prenyl_trans_a. IPR008940. Prenyltransferase. [Graphical view]
Gene3D	G3DSA:1.25.40.120. Prenyl_trans. 1 hit.
KO	K05955.
Pfam	PF01239. PPTA. 4 hits. [Graphical view]
PROSITE	PS51147. PFTA. 5 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FNTA_DICDI

Accession

Primary (citable) accession number: Q54RT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 16, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)