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Protein

Translation initiation factor 2 subunit beta

Gene

eif2b

Organism
Metallosphaera sedula (strain ATCC 51363 / DSM 5348)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.UniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciMSED399549:GH1O-672-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor 2 subunit betaUniRule annotation
Alternative name(s):
aIF2-betaUniRule annotation
eIF-2-betaUniRule annotation
Gene namesi
Name:eif2bUniRule annotation
Ordered Locus Names:Msed_0658
OrganismiMetallosphaera sedula (strain ATCC 51363 / DSM 5348)
Taxonomic identifieri399549 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeMetallosphaera
ProteomesiUP000000242 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 140140Translation initiation factor 2 subunit betaPRO_0000336756Add
BLAST

Interactioni

Subunit structurei

Heterotrimer composed of an alpha, a beta and a gamma chain.UniRule annotation

Protein-protein interaction databases

STRINGi399549.Msed_0658.

Structurei

3D structure databases

ProteinModelPortaliA4YEI1.
SMRiA4YEI1. Positions 8-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eIF-2-beta/eIF-5 family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1601.
HOGENOMiHOG000107197.
KOiK03238.
OMAiILKCEAC.

Family and domain databases

Gene3Di3.30.30.50. 1 hit.
HAMAPiMF_00232. eIF_2_beta.
InterProiIPR004458. TIF2_bsu_arc.
IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.

Sequencei

Sequence statusi: Complete.

A4YEI1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSERDKLYHV LLDRLYAKLP KKDLASETQT LPTLSIINVG NTTIIRNFSE
60 70 80 90 100
YCDRIRREDK ICMRYLLKEL AAAGSISENG QLMIQGKFSN AIVNTFMDRF
110 120 130 140
LKTYVQCSTC KSLDTVLVKD KKIWYIQCLA CGAKNPVKPL
Length:140
Mass (Da):16,030
Last modified:May 29, 2007 - v1
Checksum:iCABC0330B51B4EB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000682 Genomic DNA. Translation: ABP94833.1.
RefSeqiWP_012020620.1. NC_009440.1.
YP_001190757.1. NC_009440.1.

Genome annotation databases

EnsemblBacteriaiABP94833; ABP94833; Msed_0658.
GeneIDi5103818.
KEGGimse:Msed_0658.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000682 Genomic DNA. Translation: ABP94833.1.
RefSeqiWP_012020620.1. NC_009440.1.
YP_001190757.1. NC_009440.1.

3D structure databases

ProteinModelPortaliA4YEI1.
SMRiA4YEI1. Positions 8-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi399549.Msed_0658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABP94833; ABP94833; Msed_0658.
GeneIDi5103818.
KEGGimse:Msed_0658.

Phylogenomic databases

eggNOGiCOG1601.
HOGENOMiHOG000107197.
KOiK03238.
OMAiILKCEAC.

Enzyme and pathway databases

BioCyciMSED399549:GH1O-672-MONOMER.

Family and domain databases

Gene3Di3.30.30.50. 1 hit.
HAMAPiMF_00232. eIF_2_beta.
InterProiIPR004458. TIF2_bsu_arc.
IPR002735. Transl_init_fac_IF2/IF5.
IPR016189. Transl_init_fac_IF2/IF5_N.
IPR016190. Transl_init_fac_IF2/IF5_Zn-bd.
[Graphical view]
PfamiPF01873. eIF-5_eIF-2B. 1 hit.
[Graphical view]
SUPFAMiSSF100966. SSF100966. 1 hit.
SSF75689. SSF75689. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of the metal-mobilizing, extremely thermoacidophilic archaeon Metallosphaera sedula provides insights into bioleaching-associated metabolism."
    Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.
    Appl. Environ. Microbiol. 74:682-692(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51363 / DSM 5348.

Entry informationi

Entry nameiIF2B_METS5
AccessioniPrimary (citable) accession number: A4YEI1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: May 27, 2015
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.