Elongation factor 1-gamma 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P29547 (EF1G1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 134. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Elongation factor 1-gamma 1
Short name=EF-1-gamma 1

Alternative name(s):
Calcium and membrane-binding protein 1
Calcium phospholipid-binding protein
Short name=CPBP
Eukaryotic elongation factor 1Bgamma 1
Short name=eEF1Bgamma 1
Translation elongation factor 1B gamma 1

Gene names

Name:	CAM1
Synonyms:	TEF3
Ordered Locus Names:	YPL048W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components. May be involved in transcriptional regulation of MXR1. Ref.8
Pathway	Protein biosynthesis; polypeptide chain elongation.
Subunit structure	The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. The eEF1B subcomplex with the GEF activity is formed of eEF1Balpha and eEF1Bgamma. CAM1 interacts with EFB1. Component of a complex bound to MXR1 promoter region. Ref.10
Subcellular location	Cytoplasm. Nucleus Ref.6 Ref.8.
Domain	Ths GST-like domain mediates the interaction to eEFB1 and may be responsible for dimerization of the eEF1 complex.
Miscellaneous	Present with 60865 molecules/cell in log phase SD medium. There are 2 isoforms for eEF1Bgamma in yeast.
Sequence similarities	Contains 1 EF-1-gamma C-terminal domain. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm Nucleus
Molecular function	Elongation factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.8. Source: SGD ribosome biogenesis Inferred from genetic interaction PubMed 8041634. Source: SGD
Cellular_component	eukaryotic translation elongation factor 1 complex Inferred from electronic annotation. Source: InterPro nucleus Inferred from direct assay Ref.8. Source: SGD
Molecular_function	calcium ion binding Inferred from direct assay Ref.2. Source: SGD phospholipid binding Inferred from direct assay Ref.2. Source: SGD transcription coactivator activity Inferred from mutant phenotype Ref.8. Source: SGD translation elongation factor activity 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 – 415

415

Elongation factor 1-gamma 1

PRO_0000208831

Regions

Domain

1 – 78

GST N-terminal

Domain

89 – 215

127

GST C-terminal

Domain

254 – 415

162

EF-1-gamma C-terminal

Amino acid modifications

Modified residue

Phosphothreonine Ref.9

Experimental info

Sequence conflict

191

W → C in AAA16892. Ref.1

Secondary structure

415

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29547 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 17BCE60FFB7B2890
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FASTA

415

47,088

        10         20         30         40         50         60 
MSQGTLYANF RIRTWVPRGL VKALKLDVKV VTPDAAAEQF ARDFPLKKVP AFVGPKGYKL 

        70         80         90        100        110        120 
TEAMAINYYL VKLSQDDKMK TQLLGADDDL NAQAQIIRWQ SLANSDLCIQ IANTIVPLKG 

       130        140        150        160        170        180 
GAPYNKKSVD SAMDAVDKIV DIFENRLKNY TYLATENISL ADLVAASIFT RYFESLFGTE 

       190        200        210        220        230        240 
WRAQHPAIVR WFNTVRASPF LKDEYKDFKF ADKPLSPPQK KKEKKAPAAA PAASKKKEEA 

       250        260        270        280        290        300 
KPAATETETS SKKPKHPLEL LGKSTFVLDD WKRKYSNEDT RPVALPWFWE HYNPEEYSLW 

       310        320        330        340        350        360 
KVTYKYNDEL TLTFMSNNLV GGFFNRLSAS TKYMFGCLVV YGENNNNGIV GAVMVRGQDY 

       370        380        390        400        410 
VPAFDVAPDW ESYDYAKLDP TNDDDKEFIN NMWAWDKPVS VNGEPKEIVD GKVLK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae." Ripmaster T.L., Vaughn G.P., Woolford J.L. Jr. Mol. Cell. Biol. 13:7901-7912(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning and genetic characterization of a calcium- and phospholipid-binding protein from Saccharomyces cerevisiae that is homologous to translation elongation factor-1 gamma." Kambouris N.G., Burke D.J., Creutz C.E. Yeast 9:151-163(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Calcium-dependent secretory vesicle-binding and lipid-binding proteins of Saccharomyces cerevisiae." Creutz C.E., Snyder S.L., Kambouris N.G. Yeast 7:229-244(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 357-373.
[6]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"A homologue of elongation factor 1 gamma regulates methionine sulfoxide reductase A gene expression in Saccharomyces cerevisiae." Hanbauer I., Boja E.S., Moskovitz J. Proc. Natl. Acad. Sci. U.S.A. 100:8199-8204(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, MASS SPECTROMETRY.
[10]	"The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae." Jeppesen M.G., Ortiz P.A., Shepard W., Kinzy T.G., Nyborg J., Andersen G.R. J. Biol. Chem. 278:47190-47198(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-219, INTERACTION WITH EFB1, PUTATIVE STRUCTURE OF THE EEF1 COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L01879 Unassigned DNA. Translation: AAA16892.1.
X67917 Genomic DNA. Translation: CAA48116.1.
U44030 Genomic DNA. Translation: AAB68173.1.
BK006949 Genomic DNA. Translation: DAA11382.1.

PIR

S29345.

RefSeq

NP_015277.1. NM_001183862.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NHY	X-ray	3.00	A	1-219	[»]

ProteinModelPortal

P29547.

SMR

P29547. Positions 1-219, 255-415.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6813N.

IntAct

P29547. 11 interactions.

MINT

MINT-644858.

STRING

4932.YPL048W.

Proteomic databases

PaxDb

P29547.

PeptideAtlas

P29547.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPL048W; YPL048W; YPL048W.

GeneID

856059.

KEGG

sce:YPL048W.

Organism-specific databases

CYGD

YPL048w.

SGD

S000005969. CAM1.

Phylogenomic databases

eggNOG

COG0625.

GeneTree

ENSGT00390000007552.

HOGENOM

HOG000201196.

K03233.

OMA

GYSIWYS.

OrthoDB

EOG43FM66.

Enzyme and pathway databases

UniPathway

UPA00345.

Gene expression databases

Genevestigator

P29547.

GermOnline

YPL048W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.20.1050.10. 1 hit.
3.30.70.1010. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]

Pfam

PF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]

SUPFAM

SSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
SSF89942. Transl_elong_EF1_G_con. 1 hit.

PROSITE

PS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P29547.

NextBio

981032.

Entry information

Entry name

EF1G1_YEAST

Accession

Primary (citable) accession number: P29547
Secondary accession number(s): D6W3W6, Q9URC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents