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Protein

Translation initiation factor IF-1

Gene

infA

Organism
Brucella suis biovar 1 (strain 1330)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initation complex.UniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding, rRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Translation initiation factor IF-1UniRule annotation
Gene namesi
Name:infAUniRule annotation
Ordered Locus Names:BR0249, BS1330_I0250
OrganismiBrucella suis biovar 1 (strain 1330)
Taxonomic identifieri204722 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000007104 Componenti: Chromosome I

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7272Translation initiation factor IF-1PRO_0000095755Add
BLAST

Interactioni

Subunit structurei

Component of the 30S ribosomal translation pre-initiation complex which assembles on the 30S ribosome in the order IF-2 and IF-3, IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at any time during PIC assembly.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8G2R5.
SMRiQ8G2R5. Positions 2-70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7272S1-likeUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the IF-1 family.UniRule annotation
Contains 1 S1-like domain.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000221323.
KOiK02518.
OMAiKGRIIWR.
OrthoDBiEOG6384SC.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00075. IF_1.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR022967. S1_dom.
IPR004368. TIF_IF1.
[Graphical view]
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00008. infA. 1 hit.
PROSITEiPS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8G2R5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKEEVLEFP GVVTELLPNA MFRVKLENEH EIIAHTAGRM RKNRIRVLAG
60 70
DKVLVEMTPY DLTKGRITYR LK
Length:72
Mass (Da):8,338
Last modified:March 1, 2003 - v1
Checksum:i67DFD20EB09AE093
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN29198.1.
CP002997 Genomic DNA. Translation: AEM17611.1.
RefSeqiWP_004691460.1. NZ_KN046804.1.

Genome annotation databases

EnsemblBacteriaiAAN29198; AAN29198; BR0249.
AEM17611; AEM17611; BS1330_I0250.
KEGGibms:BR0249.
bsi:BS1330_I0250.
PATRICi17788775. VBIBruSui107850_0258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014291 Genomic DNA. Translation: AAN29198.1.
CP002997 Genomic DNA. Translation: AEM17611.1.
RefSeqiWP_004691460.1. NZ_KN046804.1.

3D structure databases

ProteinModelPortaliQ8G2R5.
SMRiQ8G2R5. Positions 2-70.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN29198; AAN29198; BR0249.
AEM17611; AEM17611; BS1330_I0250.
KEGGibms:BR0249.
bsi:BS1330_I0250.
PATRICi17788775. VBIBruSui107850_0258.

Phylogenomic databases

HOGENOMiHOG000221323.
KOiK02518.
OMAiKGRIIWR.
OrthoDBiEOG6384SC.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00075. IF_1.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR022967. S1_dom.
IPR004368. TIF_IF1.
[Graphical view]
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
SMARTiSM00316. S1. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00008. infA. 1 hit.
PROSITEiPS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 1330.

Entry informationi

Entry nameiIF1_BRUSU
AccessioniPrimary (citable) accession number: Q8G2R5
Secondary accession number(s): G0KBU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 1, 2003
Last modified: November 11, 2015
This is version 81 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

Documents

  1. Brucella suis
    Brucella suis (strain 1330): entries and gene names
  2. Translation initiation factors
    List of translation initiation factor entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.