O60052 (FNTA_SCHPO) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 73.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
| ||||
| 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 | 294 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. Ref.1 |
| 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. Ref.1 |
| Sequence similarities | Belongs to the protein prenyltransferase subunit alpha family. Contains 5 PFTA repeats. |
Ontologies
| Keywords | |
|---|---|
| Domain | Repeat |
| Molecular function | Prenyltransferase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cell wall (1->3)-beta-D-glucan biosynthetic process Inferred from physical interaction. Source: GeneDB_Spombe protein geranylgeranylationInferred by curator. Source: GeneDB_Spombe protein targeting to membraneInferred by curator. Source: GeneDB_Spombe |
| Cellular component | CAAX-protein geranylgeranyltransferase complex Non-traceable author statement. Source: GeneDB_Spombe nucleusInferred from direct assay. Source: GeneDB_Spombe |
| Molecular function | CAAX-protein geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC protein bindingInferred from physical interaction. Source: GeneDB_Spombe protein farnesyltransferase activityInferred 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 – 294 | 294 | Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha | PRO_0000119753 | |||||
Regions | |||||||||
| Repeat | 57 – 91 | 35 | PFTA 1 | ||||||
| Repeat | 92 – 125 | 34 | PFTA 2 | ||||||
| Repeat | 126 – 160 | 35 | PFTA 3 | ||||||
| Repeat | 161 – 194 | 34 | PFTA 4 | ||||||
| Repeat | 199 – 233 | 35 | PFTA 5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of the geranylgeranyl transferase type I from Schizosaccharomyces pombe." Arellano M., Coll P.M., Yang W., Duran A., Tamanoi F., Perez P. Mol. Microbiol. 29:1357-1367(1998) [PubMed: 9781874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT. Strain: 972 / ATCC 24843. |
| [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. 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 | AJ223304 Genomic DNA. Translation: CAA11246.1. CU329670 Genomic DNA. Translation: CAC21477.1. |
| RefSeq | NP_593518.1. NM_001018952.1. |
3D structure databases | |
| ProteinModelPortal | O60052. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O60052. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | SPAPB1A10.04c.1; SPAPB1A10.04c.1:pep; SPAPB1A10.04c. |
| GeneID | 2543143. |
| GenomeReviews | Gene locus cwp1 in contig CU329670_GR. |
| KEGG | spo:SPAPB1A10.04c. |
| NMPDR | fig|4896.1.peg.3488. |
Organism-specific databases | |
| GeneDB_Spombe | SPAPB1A10.04c. |
Phylogenomic databases | |
| eggNOG | fuNOG08714. |
| GeneTree | EFGT00050000004025. |
| OMA | FNNSAWN. |
| OrthoDB | EOG43NBNJ. |
Enzyme and pathway databases | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-001199-MONOMER. |
Gene expression databases | |
| ArrayExpress | O60052. |
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. 5 hits. [Graphical view] |
| PROSITE | PS51147. PFTA. 5 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FNTA_SCHPO | ||||||||
| Accession | Primary (citable) accession number: O60052 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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