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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP.UniRule annotation

Catalytic activityi

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).UniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Protein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotation (EC:2.1.2.9UniRule annotation)
Gene namesi
Name:fmtUniRule annotation
Ordered Locus Names:tlr1874
OrganismiThermosynechococcus elongatus (strain BP-1)
Taxonomic identifieri197221 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 331331Methionyl-tRNA formyltransferasePRO_0000083067Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi197221.tlr1874.

Structurei

3D structure databases

ProteinModelPortaliQ8DHS1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni111 – 1144Tetrahydrofolate (THF) bindingUniRule annotation

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
OrthoDBiEOG6B09WV.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8DHS1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIVYFGTPE FALAPLQRLL QTETYQVLGV VTQPDRRRGR GNQLSPSPVK
60 70 80 90 100
AFALRHGLPI WQPPRLRQDP QLPEVLRSLA ADVFVVVAYG QILPQSILDI
110 120 130 140 150
PRYGCINIHG SLLPRYRGAA PIQWALYHGE EETGVTTMLM DAGLDTGPML
160 170 180 190 200
LKRKVRIHLE DNATTLSAKL SETGADLLLD TLQQLPQLQA EPQNDAEATY
210 220 230 240 250
APLIQKSDYA IDWGRSALAL HNQVRAFYPY AYTQWQGTAL KILQTWPLIP
260 270 280 290 300
EVAAKLPEPL QSYVREPEAA APPGTVLALI KGWGPVVQTG KGPLLLSQVQ
310 320 330
LSGRKAQSGW DFVNGVRLAI ATQFAIVPSA L
Length:331
Mass (Da):36,445
Last modified:December 15, 2003 - v2
Checksum:iE06D97BC390435F0
GO

Sequence cautioni

The sequence BAC09426.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09426.1. Different initiation.
RefSeqiNP_682664.1. NC_004113.1.

Genome annotation databases

EnsemblBacteriaiBAC09426; BAC09426; BAC09426.
GeneIDi1010839.
KEGGitel:tlr1874.
PATRICi23929136. VBITheElo119873_1957.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000039 Genomic DNA. Translation: BAC09426.1. Different initiation.
RefSeqiNP_682664.1. NC_004113.1.

3D structure databases

ProteinModelPortaliQ8DHS1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi197221.tlr1874.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC09426; BAC09426; BAC09426.
GeneIDi1010839.
KEGGitel:tlr1874.
PATRICi23929136. VBITheElo119873_1957.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
OrthoDBiEOG6B09WV.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans.
InterProiIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
[Graphical view]
PfamiPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiPS00373. GART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BP-1.

Entry informationi

Entry nameiFMT_THEEB
AccessioniPrimary (citable) accession number: Q8DHS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: July 6, 2016
This is version 83 of the entry and version 2 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. 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.