Reviewed, UniProtKB/Swiss-Prot Q9Y765 (FNTA_CANAL)

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
    Ras proteins prenyltransferase subunit alpha
    FTase-alpha
    Type I protein geranyl-geranyltransferase subunit alpha
      Short name=GGTase-I-alpha

Gene names

Name:

RAM2

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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.
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.
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 5 PFTA repeats.

Ontologies

Keywords
Domain	Repeat
Molecular function	Prenyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein amino acid prenylation Inferred from electronic annotation. Source: InterPro
Molecular function	CAAX-protein geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC protein farnesyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 306

306

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

PRO_0000119752

Regions

Repeat

48 – 82

35

PFTA 1

Repeat

84 – 118

35

PFTA 2

Repeat

125 – 159

35

PFTA 3

Repeat

161 – 195

35

PFTA 4

Repeat

201 – 235

35

PFTA 5

Secondary structure

1

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306

Helix Strand Turn

Details...

Helix

30 – 35

6

Helix

39 – 44

6

Helix

50 – 57

8

Helix

67 – 78

12

Helix

85 – 98

14

Helix

105 – 112

8

Helix

116 – 119

4

Turn

120 – 122

3

Helix

127 – 139

13

Helix

144 – 156

13

Helix

163 – 175

13

Helix

180 – 191

12

Helix

194 – 196

3

Helix

199 – 215

17

Helix

220 – 226

7

Turn

230 – 235

6

Helix

237 – 240

4

Helix

241 – 245

5

Helix

250 – 252

3

Beta strand

254 – 256

3

Helix

258 – 270

13

Helix

274 – 286

13

Helix

290 – 292

3

Helix

293 – 301

9

Sequences

	Sequence		Length	Mass (Da)
	Q9Y765-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: BC42924AC96DD920	FASTA	306	36,601
	10 20 30 40 50 60 MTDSKYDYSD ITPVDINTEE PQICQILYDE DYKQIMGLLL ALMKAEEYSE RALHITELGI 70 80 90 100 110 120 NELASHYTIW IYRFNILKNL PNRNLYDELD WCEEIALDNE KNYQIWNYRQ LIIGQIMELN 130 140 150 160 170 180 NNDFDPYREF PILEAMLSSD PKNHHVWSYR KWLVDTFDLH NDAKELSFVD KVIDTDLKNN 190 200 210 220 230 240 SAWSHRFFLL FSKKHLATDN TIDEELNYVK DKIVKCPQNP STWNYLLGIH ERFDRSITQL 250 260 270 280 290 300 EEFSLQFVDL EKDQVTSSFA LETLAKIYTQ QKKYNESRTV YDLLKSKYDP IRSNFWDYQI SKLTSV

References

[1]	"Purification of geranylgeranyltransferase I from Candida albicans and cloning of the CaRAM2 and CaCDC43 genes encoding its subunits." Mazur P., Register E., Bonfiglio C.A., Yuan X., Kurtz M.B., Williamson J.M., Kelly R. Microbiology 145:1123-1135(1999) [PubMed: 10376828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF110691 Genomic DNA. Translation: AAD32540.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DRA	X-ray	1.80	A	1-306	[»]

ModBase

Search...

Phylogenomic databases

OMA

FNNSAWN.

Enzyme and pathway databases

BRENDA

2.5.1.58. 1124.
2.5.1.59. 1124.

Family and domain databases

InterPro

IPR002088. Prenyl_trans_a.
IPR008940. Prenyltransferase.
[Graphical view]

Gene3D

G3DSA:1.25.40.120. Prenyl_trans. 1 hit.

Pfam

PF01239. PPTA. 4 hits.
[Graphical view]

PROSITE

PS51147. PFTA. 5 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FNTA_CANAL

Accession

Primary (citable) accession number: Q9Y765

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	November 1, 1999
Last modified:	January 19, 2010
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)