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P35021 (EF1A_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Elongation factor 1-alpha

Short name=EF-1-alpha
Alternative name(s):
Elongation factor Tu
Short name=EF-Tu
Gene names
Name:tuf
Synonyms:tef1
Ordered Locus Names:SSO0216
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. HAMAP-Rule MF_00118_A

Subcellular location

Cytoplasm HAMAP-Rule MF_00118_A.

Sequence similarities

Belongs to the GTP-binding elongation factor family. EF-Tu/EF-1A subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Nucleotide-binding
   Molecular functionElongation factor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: HAMAP

GTPase activity

Inferred from electronic annotation. Source: InterPro

translation elongation factor activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 435435Elongation factor 1-alpha HAMAP-Rule MF_00118_A
PRO_0000090994

Regions

Nucleotide binding13 – 208GTP By similarity
Nucleotide binding90 – 945GTP By similarity
Nucleotide binding152 – 1554GTP By similarity

Natural variations

Natural variant1961A → S in strain: MT-3 and MT-4.
Natural variant2031R → K in strain: MT-3 and MT-4.
Natural variant3471I → L in strain: MT-3 and MT-4.

Experimental info

Sequence conflict141H → Q Ref.1
Sequence conflict2401V → R Ref.1
Sequence conflict2401V → R Ref.2

Secondary structure

.............................................................................. 435
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35021 [UniParc].

Last modified June 1, 2001. Version 3.
Checksum: 222B540A31768A59

FASTA43548,489
        10         20         30         40         50         60 
MSQKPHLNLI VIGHIDHGKS TLVGRLLMDR GFIDEKTVKE AEEAAKKLGK ESEKFAFLLD 

        70         80         90        100        110        120 
RLKEERERGV TINLTFMRFE TKKYFFTIID APGHRDFVKN MITGASQADA AILVVSAKKG 

       130        140        150        160        170        180 
EYEAGMSVEG QTREHIILAK TMGLDQLIVA VNKMDLTEPP YDEKRYKEIV DQVSKFMRSY 

       190        200        210        220        230        240 
GFNTNKVRFV PVVAPAGDNI THRSENMKWY NGPTLEEYLD QLELPPKPVD KPLRIPIQDV 

       250        260        270        280        290        300 
YSISGVGTVP VGRVESGVLK VGDKIVFMPA GKVGEVRSIE THHTKMDKAE PGDNIGFNVR 

       310        320        330        340        350        360 
GVEKKDIKRG DVVGHPNNPP TVADEFTARI IVVWHPTALA NGYTPVIHVH TASVACRVSE 

       370        380        390        400        410        420 
LVSKLDPRTG QEAEKNPQFL KQGDVAIVKF KPIKPLCVEK YNEFPPLGRF AMRDMGKTVG 

       430 
VGIIVDVKPA KVEIK 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of the elongation factor 1 alpha in Sulfolobus solfataricus."
Arcari P., Gallo M., Ianniciello G., Dello Russo A., Bocchini V.
Nucleic Acids Res. 21:1666-1666(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 5833 / MT-4.
[2]"The nucleotide sequence of the gene coding for the elongation factor 1 alpha in Sulfolobus solfataricus. Homology of the product with related proteins."
Arcari P., Gallo M., Ianniciello G., Dello Russo A., Bocchini V.
Biochim. Biophys. Acta 1217:333-337(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 5833 / MT-4.
[3]"The nucleotide sequence of the gene encoding the elongation factor 1 alpha from the archaeon Sulfolobus solfataricus isolate MT3."
Arcari P., Masullo M., Bocchini V.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: MT-3.
[4]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70701 Genomic DNA. Translation: CAA50033.1.
X76767 Genomic DNA. Translation: CAA54162.1.
AJ312397 Genomic DNA. Translation: CAC42886.1.
AE006641 Genomic DNA. Translation: AAK40559.1.
PIRH90162.
S43507.
RefSeqNP_341769.1. NC_002754.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JNYX-ray1.80A/B1-435[»]
1SKQX-ray1.80A/B1-435[»]
ProteinModelPortalP35021.
SMRP35021. Positions 4-430.
ModBaseSearch...

Protein-protein interaction databases

STRING273057.SSO0216.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK40559; AAK40559; SSO0216.
GeneID1455369.
KEGGsso:SSO0216.

Phylogenomic databases

eggNOGCOG5256.
HOGENOMHOG000229291.
KOK03231.
OMADPYEQNR.
ProtClustDBPRK12317.

Family and domain databases

HAMAPMF_00118_A. EF_Tu_A.
InterProIPR000795. EF_GTP-bd_dom.
IPR005225. Small_GTP-bd_dom.
IPR009001. Transl_elong_EF1A/Init_IF2_C.
IPR004539. Transl_elong_EF1A_euk/arc.
IPR004161. Transl_elong_EFTu/EF1A_2.
IPR004160. Transl_elong_EFTu/EF1A_C.
IPR009000. Transl_elong_init/rib_B-barrel.
[Graphical view]
PfamPF00009. GTP_EFTU. 1 hit.
PF03144. GTP_EFTU_D2. 1 hit.
PF03143. GTP_EFTU_D3. 1 hit.
[Graphical view]
PRINTSPR00315. ELONGATNFCT.
SUPFAMSSF50465. Elong_init_C. 1 hit.
SSF50447. Translat_factor. 1 hit.
TIGRFAMsTIGR00483. EF-1_alpha. 1 hit.
TIGR00231. small_GTP. 1 hit.
PROSITEPS00301. EFACTOR_GTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP35021.

Entry information

Entry nameEF1A_SULSO
AccessionPrimary (citable) accession number: P35021
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 1, 2001
Last modified: May 1, 2013
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families