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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Trichodesmium erythraeum (strain IMS101)
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:Tery_1769
OrganismiTrichodesmium erythraeum (strain IMS101)
Taxonomic identifieri203124 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesMicrocoleaceaeTrichodesmium
Proteomesi
  • UP000008878 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000202001 – 336Methionyl-tRNA formyltransferaseAdd BLAST336

Interactioni

Protein-protein interaction databases

STRINGi203124.Tery_1769.

Structurei

3D structure databases

ProteinModelPortaliQ114P5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni112 – 115Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

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

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
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.

Q114P5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKIIFFGTP LFAVPTLKKL LDNPKIEVTA VVTQPDKRRG RGNKLIPSPV
60 70 80 90 100
KSVAVAHNIP VWQPRRVKKN PETLNLLREA QADVFVVVAY GQILSTEILE
110 120 130 140 150
MPKLGCVNVH GSILPKYRGA APIQWSIYHG EAETGNTTML MDVGMDTGPM
160 170 180 190 200
LLKSIIPIGL LDNAVSIAEI LAKDGADLLL ETLLRLEDKE IEPIPQDNSL
210 220 230 240 250
ATYAPLIQNS DYEIDWSRSA LDIHNQIRGF FPNCFTSFRG QSLKVMATIP
260 270 280 290 300
VGTEYWSELP PELQKLEKVW SSESEVVGNI GEVVKVIKGL GPVVQTGSGW
310 320 330
LLLWQVQLAG KKVVSGWDFA NGTRLLVGEV SEVFSR
Length:336
Mass (Da):37,076
Last modified:August 22, 2006 - v1
Checksum:iE5CAFA7CF39AACFF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000393 Genomic DNA. Translation: ABG51029.1.

Genome annotation databases

EnsemblBacteriaiABG51029; ABG51029; Tery_1769.
KEGGiter:Tery_1769.
PATRICi23987613. VBITriEry99848_2241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000393 Genomic DNA. Translation: ABG51029.1.

3D structure databases

ProteinModelPortaliQ114P5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi203124.Tery_1769.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG51029; ABG51029; Tery_1769.
KEGGiter:Tery_1769.
PATRICi23987613. VBITriEry99848_2241.

Phylogenomic databases

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

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
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...

Entry informationi

Entry nameiFMT_TRIEI
AccessioniPrimary (citable) accession number: Q114P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: November 2, 2016
This is version 68 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. 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.