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Reviewed, UniProtKB/Swiss-Prot Q29387 (EF1G_PIG)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Elongation factor 1-gamma
      Short name=EF-1-gamma
Alternative name(s):
    eEF-1B gamma
Gene names
Name: EEF1G
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length432 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Probably plays a role in anchoring the complex to other cellular components.

Subunit structure

EF-1 is composed of four subunits: alpha, beta, delta, and gamma.

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 processProtein biosynthesis
   Molecular functionElongation factor
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processtranslational elongation

Inferred from electronic annotation. Source: InterPro

   Cellular componenteukaryotic translation elongation factor 1 complex

Inferred from electronic annotation. Source: InterPro

   Molecular functiontranslation elongation factor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 432›432Elongation factor 1-gamma
PRO_0000208815

Regions

Domain‹1 – 82›82GST N-terminal
Domain83 – 211129GST C-terminal
Domain271 – 432162EF-1-gamma C-terminal

Amino acid modifications

Modified residue381Phosphothreonine By similarity
Modified residue411Phosphothreonine By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
Q29387-1 [UniParc].

Last modified November 23, 2004. Version 2.
Checksum: 05AA91DDA100BFBC

FASTA43249,624
        10         20         30         40         50         60 
LYTYPENWRA FKALIAAQYS GAQVRVLSAP PHFHFGQTNH TPEFLRKFPA GKVPAFEGDD 

        70         80         90        100        110        120 
GFCVFESNAI AYYVSNEELR GSTPEAAAQV VQWVSFADSD IVPPASTWVF PTLGIMHYNK 

       130        140        150        160        170        180 
QATENAKDEV RRVLGLLDAH LKTRTFLVGE RVTLADITVV CTLLWLYKQV LEPSFRQAFP 

       190        200        210        220        230        240 
NTNRWFLTCI NQPQFRAVLG EVKLCEKMAQ FDAKKFAESQ PKKDTPRKEK GSREEKQKPQ 

       250        260        270        280        290        300 
AERKEEKKAA APAPEEELDE CEQALAAEPK AKDPFAHLPK STFVLDEFKR KYSNEDTLSV 

       310        320        330        340        350        360 
ALPYFWEHFD KDGWSLWYSE YRFPEELTQT FMSCNLITGM FQRLDKLRKN AFASVILFGT 

       370        380        390        400        410        420 
NNSSSISGVW VFRGQELAFP LSPDWQVDYE SYTWRKLDPG SEETQTLVRE YFSWEGAYQH 

       430 
VGKAFNQGKI FK 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning of porcine eukaryotic elongation factor(eEF)-1 gamma-like protein."
Kokuho T.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
Winteroe A.K., Fredholm M., Davies W.
Mamm. Genome 7:509-517(1996) [PubMed: 8672129] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-142.
Tissue: Small intestine.

Cross-references

Sequence databases

AF480162 mRNA. Translation: AAL85414.1.
F14608 mRNA. Translation: CAA23152.1.
UniGeneSsc.53702

3D structure databases

HSSPHSSP built from PDB template 1NHY based on UniProtKB P29547.
SMRQ29387. Positions 271-432.
ModBaseSearch...

Phylogenomic databases

HOVERGENQ29387.

Family and domain databases

InterProIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.30.70.1010. Transl_elong_EF1_G_con. 1 hit.
PfamPF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
ProDomPD006217. EF1_G. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEF1G_PIG
AccessionPrimary (citable) accession number: Q29387
Secondary accession number(s): Q8SPX8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 23, 2004
Last modified: June 16, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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