Elongation factor 1-gamma 1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P29547 (EF1G1_YEAST)

Last modified June 16, 2009. Version 100. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:	CAM1
Synonyms:	TEF3
Ordered Locus Names:	YPL048W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	415 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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.7
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.9
Subcellular location	Cytoplasm. Nucleus. Ref.7 Ref.5
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. Ref.6 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.

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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
Gene Ontology (GO)
Biological process	positive regulation of transcription from RNA polymerase II promoter Ref.7 Inferred from mutant phenotype. Source: SGD ribosome biogenesis Inferred from genetic interaction. Source: SGD translational elongation Inferred from electronic annotation. Source: InterPro
Cellular component	eukaryotic translation elongation factor 1 complex Inferred from electronic annotation. Source: InterPro nucleus Ref.7 Inferred from direct assay. Source: SGD
Molecular function	calcium ion binding Ref.2 Inferred from direct assay. Source: SGD phospholipid binding Ref.2 Inferred from direct assay. Source: SGD transcription coactivator activity Ref.7 Inferred from mutant phenotype. Source: SGD translation elongation factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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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.8

Experimental info

Sequence conflict

191

W → C in AAA16892. Ref.1

Secondary structure

415

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P29547-1 [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

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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: 8247005] [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: 8465602] [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: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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: 1882548] [Abstract] Cited for: PROTEIN SEQUENCE OF 357-373.
[5]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"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: 12824466] [Abstract] Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[8]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32, MASS SPECTROMETRY.
[9]	"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: 12972429] [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.

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Cross-references

Sequence databases

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

PIR

S29345.

RefSeq

NP_015277.1.

3D structure databases

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6813N.

IntAct

P29547. 11 interactions.

Proteomic databases

PeptideAtlas

P29547.

PRIDE

P29547.

Genome annotation databases

Ensembl

YPL048W. Saccharomyces cerevisiae. [Contig view]

GeneID

856059.

GenomeReviews

Gene locus YPL048W in contig U00094_GR.

KEGG

sce:YPL048W.

NMPDR

fig|4932.3.peg.6410.

Organism-specific databases

CYGD

YPL048w.

SGD

S000005969. CAM1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P29547.

OMA

P29547. KSIPYFW.

Gene expression databases

ArrayExpress

P29547.

GermOnline

YPL048W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR012335. Thioredoxin_fold.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]

Gene3D

G3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
G3DSA:3.30.70.1010. Transl_elong_EF1_G_con. 1 hit.

Pfam

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

ProDom

PD006217. EF1_G. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

981032.

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Entry information

Entry name

EF1G1_YEAST

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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