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Protein

Translation initiation factor IF-1

Gene

infA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

One of the essential components for the initiation of protein synthesis. Binds in the vicinity of the A-site (ECO:0000269|PubMed:11228145). 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 annotation1 Publication

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:TTHA1669
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000958931 – 72Translation initiation factor IF-1Add BLAST72

Interactioni

Subunit structurei

Binds to the 30S ribosomal subunit, contacting protein S12 and the 16S rRNA (ECO:0000269|PubMed:11228145). 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 annotation1 Publication

Protein-protein interaction databases

STRINGi300852.TTHA1669.

Structurei

Secondary structure

172
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Turni19 – 21Combined sources3
Beta strandi26 – 30Combined sources5
Helixi39 – 43Combined sources5
Beta strandi53 – 57Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HR0X-ray3.20W2-72[»]
5LMNelectron microscopy3.55W1-72[»]
5LMOelectron microscopy4.30W1-72[»]
5LMPelectron microscopy5.35W1-72[»]
5LMQelectron microscopy4.20W1-72[»]
5LMRelectron microscopy4.45W1-72[»]
5LMSelectron microscopy5.10W1-72[»]
5LMTelectron microscopy4.15W1-72[»]
5LMVelectron microscopy4.90W1-72[»]
ProteinModelPortaliQ5SHR1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SHR1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 72S1-likeUniRule annotationAdd BLAST72

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105K9U. Bacteria.
COG0361. LUCA.
HOGENOMiHOG000221323.
KOiK02518.
OMAiKGRIIWR.
PhylomeDBiQ5SHR1.

Family and domain databases

CDDicd04451. S1_IF1. 1 hit.
HAMAPiMF_00075. IF_1. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR004368. TIF_IF1.
[Graphical view]
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00008. infA. 1 hit.
PROSITEiPS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5SHR1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKEKDTIRT EGVVTEALPN ATFRVKLDSG PEILAYISGK MRMHYIRILP
60 70
GDRVVVEITP YDPTRGRIVY RK
Length:72
Mass (Da):8,234
Last modified:December 21, 2004 - v1
Checksum:i981E63B61223DDFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71492.1.
RefSeqiWP_008633373.1. NC_006461.1.
YP_144935.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD71492; BAD71492; BAD71492.
GeneIDi3168806.
KEGGittj:TTHA1669.
PATRICi23958293. VBITheThe93045_1639.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD71492.1.
RefSeqiWP_008633373.1. NC_006461.1.
YP_144935.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HR0X-ray3.20W2-72[»]
5LMNelectron microscopy3.55W1-72[»]
5LMOelectron microscopy4.30W1-72[»]
5LMPelectron microscopy5.35W1-72[»]
5LMQelectron microscopy4.20W1-72[»]
5LMRelectron microscopy4.45W1-72[»]
5LMSelectron microscopy5.10W1-72[»]
5LMTelectron microscopy4.15W1-72[»]
5LMVelectron microscopy4.90W1-72[»]
ProteinModelPortaliQ5SHR1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA1669.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD71492; BAD71492; BAD71492.
GeneIDi3168806.
KEGGittj:TTHA1669.
PATRICi23958293. VBITheThe93045_1639.

Phylogenomic databases

eggNOGiENOG4105K9U. Bacteria.
COG0361. LUCA.
HOGENOMiHOG000221323.
KOiK02518.
OMAiKGRIIWR.
PhylomeDBiQ5SHR1.

Miscellaneous databases

EvolutionaryTraceiQ5SHR1.

Family and domain databases

CDDicd04451. S1_IF1. 1 hit.
HAMAPiMF_00075. IF_1. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR006196. RNA-binding_domain_S1_IF1.
IPR004368. TIF_IF1.
[Graphical view]
PfamiPF01176. eIF-1a. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00008. infA. 1 hit.
PROSITEiPS50832. S1_IF1_TYPE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIF1_THET8
AccessioniPrimary (citable) accession number: Q5SHR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: December 21, 2004
Last modified: November 30, 2016
This is version 82 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.