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Q3SZV3 (EF1G_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Subunit structure

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

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
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   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

Initiator methionine11Removed By similarity
Chain2 – 440439Elongation factor 1-gamma
PRO_0000284654

Regions

Domain2 – 8786GST N-terminal
Domain88 – 216129GST C-terminal
Domain279 – 440162EF-1-gamma C-terminal

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue431Phosphothreonine By similarity
Modified residue461Phosphothreonine By similarity
Modified residue1321N6-acetyllysine By similarity
Modified residue1471N6-acetyllysine By similarity
Modified residue4371N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SZV3 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 295A874E422B825C

FASTA44050,378
        10         20         30         40         50         60 
MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA 

        70         80         90        100        110        120 
FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI 

       130        140        150        160        170        180 
MHHNKQATEN AKEEVRRILG LLDAHLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF 

       190        200        210        220        230        240 
RQAFPNTNRW FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAESQPKKDT PRKEKGSREE 

       250        260        270        280        290        300 
KLKPQAERKE GKEEKKAAAP APEEELDECE QALAAEPKAK DPFAHLPKST FVLDEFKRKY 

       310        320        330        340        350        360 
SNEDTLSVAL PYFWDHFDKD GWSLWYSEYR FPEELTQTFM SCNLITGMFQ RLDKLRKNAF 

       370        380        390        400        410        420 
ASVILFGTNN SSSISGVWDF RGQELAFPLS PDWQVDYESY TWRKLDPGSE ETQTLVREYF 

       430        440 
CWEGAFQHVG KAFNQGKIFK 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Testis.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC102691 mRNA. Translation: AAI02692.1.
IPIIPI00706632.
RefSeqNP_001035577.1. NM_001040487.1.
UniGeneBt.62921.

3D structure databases

ProteinModelPortalQ3SZV3.
SMRQ3SZV3. Positions 279-440.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3SZV3.

Proteomic databases

PRIDEQ3SZV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID326581.
KEGGbta:326581.

Organism-specific databases

CTD1937.

Phylogenomic databases

HOVERGENHBG051444.
InParanoidQ3SZV3.
OrthoDBEOG43JC4V.
PhylomeDBQ3SZV3.

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.
IPR012336. Thioredoxin-like_fold.
IPR001662. Transl_elong_EF1_G_con.
[Graphical view]
Gene3DG3DSA: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.
KOK03233.
PfamPF00647. EF1G. 1 hit.
PF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMSSF47616. GST_C_like. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.
SSF89942. Transl_elong_EF1_G_con. 1 hit.
PROSITEPS50040. EF1G_C. 1 hit.
PS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEF1G_BOVIN
AccessionPrimary (citable) accession number: Q3SZV3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 11, 2005
Last modified: November 16, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families