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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

Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.UniRule annotation

Catalytic activityi

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

GO - Molecular functioni

Keywordsi

Molecular functionTransferase
Biological processProtein 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 lineageiBacteriaCyanobacteriaSynechococcalesSynechococcaceaeThermosynechococcus
Proteomesi
  • UP000000440 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000830671 – 331Methionyl-tRNA formyltransferaseAdd BLAST331

Interactioni

Protein-protein interaction databases

STRINGi197221.tlr1874.

Structurei

3D structure databases

ProteinModelPortaliQ8DHS1.
SMRiQ8DHS1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 114Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiLRIVFMG.
OrthoDBiPOG091H01YM.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiView protein in InterPro
IPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR037022. Formyl_trans_C_sf.
IPR002376. Formyl_transf_N.
IPR036477. Formyl_transf_N_sf.
IPR011034. Formyl_transferase-like_C_sf.
IPR001555. GART_AS.
PfamiView protein in Pfam
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiView protein in PROSITE
PS00373. GART. 1 hit.

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 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.
PATRICifig|197221.4.peg.1957.

Similar proteinsi

Entry informationi

Entry nameiFMT_THEEB
AccessioniPrimary (citable) accession number: Q8DHS1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: December 15, 2003
Last modified: November 22, 2017
This is version 96 of the entry and version 2 of the sequence. See 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