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O13782 (FNTB_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length382 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Protein farnesyltransferase subunit beta
PRO_0000119767

Regions

Repeat78 – 11942PFTB 1
Repeat129 – 17042PFTB 2
Repeat178 – 21942PFTB 3
Repeat226 – 26843PFTB 4
Repeat286 – 32843PFTB 5
Region204 – 2074Farnesyl diphosphate binding By similarity
Region247 – 2504Farnesyl diphosphate binding By similarity
Region256 – 2594Farnesyl diphosphate binding By similarity

Sites

Metal binding2531Zinc; catalytic By similarity
Metal binding2551Zinc; catalytic By similarity
Metal binding3161Zinc; via tele nitrogen; catalytic By similarity
Site581Important for selectivity against geranylgeranyl diphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
O13782 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: C3F2705D93F84203

FASTA38242,189
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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.
PIRT37836.
RefSeqNP_594251.1. NM_001019674.2.

3D structure databases

ProteinModelPortalO13782.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278844. 11 interactions.
MINTMINT-4667919.
STRING4896.SPAC17G6.04c-1.

Proteomic databases

MaxQBO13782.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC17G6.04c.1; SPAC17G6.04c.1:pep; SPAC17G6.04c.
GeneID2542380.
KEGGspo:SPAC17G6.04c.

Organism-specific databases

PomBaseSPAC17G6.04c.

Phylogenomic databases

eggNOGCOG5029.
HOGENOMHOG000190594.
KOK05954.
OMAGGEVDVX.
OrthoDBEOG7XSTQC.
PhylomeDBO13782.

Family and domain databases

Gene3D1.50.10.20. 1 hit.
InterProIPR026872. FTB.
IPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERPTHR11774:SF6. PTHR11774:SF6. 1 hit.
PfamPF00432. Prenyltrans. 1 hit.
[Graphical view]
SUPFAMSSF48239. SSF48239. 1 hit.
ProtoNetSearch...

Other

NextBio20803439.
PROO13782.

Entry information

Entry nameFNTB_SCHPO
AccessionPrimary (citable) accession number: O13782
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names