O93830 (PGTB2_CANAX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Geranylgeranyl transferase type-2 subunit beta
EC=2.5.1.60

Alternative name(s):
Geranylgeranyl transferase type II subunit beta
Short name=GGTase-II-beta
Type II protein geranyl-geranyltransferase subunit beta
Short name=PGGT
YPT1/SEC4 proteins geranylgeranyltransferase subunit beta

Gene names

Name:

BET2

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4 By similarity.
Catalytic activity	Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit By similarity.
Sequence similarities	Belongs to the protein prenyltransferase subunit beta family. Contains 6 PFTB repeats.

Ontologies

Keywords
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
Gene Ontology (GO)
Molecular function	Rab geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 341	341	Geranylgeranyl transferase type-2 subunit beta		PRO_0000119776
Regions
	Repeat	15 – 55	41	PFTB 1
	Repeat	62 – 104	43	PFTB 2
	Repeat	122 – 163	42	PFTB 3
	Repeat	170 – 211	42	PFTB 4
	Repeat	223 – 264	42	PFTB 5
	Repeat	271 – 313	43	PFTB 6
Sites
	Metal binding	249	1	Zinc By similarity
	Metal binding	251	1	Zinc By similarity
	Metal binding	301	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	O93830 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 24A89E11FF911488	FASTA	341	38,460
	10 20 30 40 50 60 MSNLPPDEKV ILFDKSKHVQ YIVEQESHRS FEYWLSEHLR MNGLYWGVTA LITMNELSAL 70 80 90 100 110 120 AQQDVIDYIM LCWDDKTGAF GSFPKHDGHI LSTLSALQVL KIYDQELTVL NDNNESSNGN 130 140 150 160 170 180 KRERLIKFIT GLQLPDGSFQ GDKYGEVDTR FVYTAVSSLS LLNALTDSIA DTASAFIMQC 190 200 210 220 230 240 FNFDGGFGLI PGSESHAAQV FTCVGALAIM NKLDLLDVEN KKVKLIDWLT ERQVLPSGGF 250 260 270 280 290 300 NGRPEKLPDV CYSWWVLSSL SILKRKNWVD LKILENFILT CQDLENGGFS DRPGNQTDVY 310 320 330 340 HTCFAIAGLS LIDYKKYGFK EIDPVYCMPV EVTSKFVRRS A

References

[1]	"Molecular cloning of BET2 gene from Candida albicans." Ishii N., Aoki Y., Arisawa M. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10231 / CBS 6431 / DSM 1386 / NBRC 1594.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB021171 Genomic DNA. Translation: BAA35193.1.
3D structure databases
ProteinModelPortal	O93830.
ModBase	Search...
Protein-protein interaction databases
STRING	O93830.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001330. Prenyltrans. IPR008930. Terpenoid_cyclase/PrenylTrfase. [Graphical view]
Pfam	PF00432. Prenyltrans. 4 hits. [Graphical view]
SUPFAM	SSF48239. Terp_cyc_toroid. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PGTB2_CANAX

Accession

Primary (citable) accession number: O93830

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 1999
Last modified:	October 19, 2011
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program