O13782 (FNTB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein farnesyltransferase subunit beta
Short name=FTase-beta
EC=2.5.1.58

Alternative name(s):
CAAX farnesyltransferase subunit beta
Ras proteins prenyltransferase subunit beta

Gene names

Name:	cpp1
ORF Names:	SPAC17G6.04c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding. Ref.1
Catalytic activity	Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit. Ref.1
Sequence similarities	Belongs to the protein prenyltransferase subunit beta family. Contains 5 PFTB repeats.

Ontologies

Keywords
Domain	Repeat
Ligand	Metal-binding Zinc
Molecular function	Prenyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to nitrogen starvation Inferred from genetic interaction. Source: GeneDB_Spombe protein farnesylation Inferred from direct assay. Source: GeneDB_Spombe protein targeting to membrane Inferred by curator. Source: GeneDB_Spombe regulation of amino acid import Inferred from genetic interaction. Source: GeneDB_Spombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	protein farnesyltransferase activity Inferred from electronic annotation. Source: EC zinc ion binding Non-traceable author statement. Source: GeneDB_Spombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 382	382	Protein farnesyltransferase subunit beta		PRO_0000119767
Regions
	Repeat	78 – 119	42	PFTB 1
	Repeat	129 – 170	42	PFTB 2
	Repeat	178 – 219	42	PFTB 3
	Repeat	226 – 268	43	PFTB 4
	Repeat	286 – 328	43	PFTB 5
Sites
	Metal binding	253	1	Zinc By similarity
	Metal binding	255	1	Zinc By similarity
	Metal binding	316	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13782 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: C3F2705D93F84203	FASTA	382	42,189
	10 20 30 40 50 60 MDELSETQVM QNETATAVLP LLNGESQSFN LQKHLKYLTK MLDPLPSPFT VLDASRAWMV 70 80 90 100 110 120 YWELSSLAIL GKLDSSVCER AISSVRQLKG PSGGFCGGNG QDEHLLSTYA SILSICLCDS 130 140 150 160 170 180 TDAYSLIERD RLYDWLFSLK NPDGSFRVNN EGESDARSVY AAVCVSSLVG ISMDDPLFEG 190 200 210 220 230 240 TLQWLCKCQT YEGGLSGVPY AEAHGGYTFC ALAAIALLGG LDNLNEIKLS TWLVQRQDPA 250 260 270 280 290 300 LYGFSGRSNK LVDGCYSWWV GASHVIVASG YGSASHKSLP NLFYNPEKLL GYILQCCQST 310 320 330 340 350 360 SGGLRDKPPK RPDQYHTCYC LLGLSSIAYD YRYHTSDGWS YKPSILHSSL SSLLPAHPIY 370 380 CVPFGFEERI KSYFLSQESS KF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Protein farnesylation is critical for maintaining normal cell morphology and canavanine resistance in Schizosaccharomyces pombe." Yang W., Urano J., Tamanoi F. J. Biol. Chem. 275:429-438(2000) [PubMed: 10617635] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB16215.1.
PIR	T37836.
RefSeq	NP_594251.1. NM_001019674.1.
3D structure databases
ProteinModelPortal	O13782.
ModBase	Search...
Protein-protein interaction databases
STRING	O13782.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC17G6.04c.1; SPAC17G6.04c.1:pep; SPAC17G6.04c.
GeneID	2542380.
GenomeReviews	Gene locus cpp1 in contig CU329670_GR.
KEGG	spo:SPAC17G6.04c.
NMPDR	fig|4896.1.peg.4221.
Organism-specific databases
GeneDB_Spombe	SPAC17G6.04c.
Phylogenomic databases
eggNOG	fuNOG08969.
GeneTree	EFGT00050000004981.
HOGENOM	HBG736019.
OMA	QEYILLC.
OrthoDB	EOG4ZPJ4B.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001861-MONOMER.
Gene expression databases
ArrayExpress	O13782.
Family and domain databases
InterPro	IPR001330. Prenyltrans. IPR008930. Terpenoid_cyclase/PrenylTrfase. [Graphical view]
KO	K05954.
Pfam	PF00432. Prenyltrans. 3 hits. [Graphical view]
SUPFAM	SSF48239. Terp_cyc_toroid. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FNTB_SCHPO

Accession

Primary (citable) accession number: O13782

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 6, 2002
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program