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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Borrelia turicatae (strain 91E135)
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:BT0064
OrganismiBorrelia turicatae (strain 91E135)
Taxonomic identifieri314724 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorrelia
Proteomesi
  • UP000001205 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001900091 – 309Methionyl-tRNA formyltransferaseAdd BLAST309

Interactioni

Protein-protein interaction databases

STRINGi314724.BT0064.

Structurei

3D structure databases

ProteinModelPortaliA1QYL4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni107 – 110Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiNCITTFR.
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.
[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.

Sequencei

Sequence statusi: Complete.

A1QYL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIFFASSDS IALEVLRKVS DHYNVVGVLT APDKPSGRGL FLKVNDIKVE
60 70 80 90 100
AINRNITVLD PVVLNSDVIG MVKKLKPDLM LVFSYGKIFR QEFLDIFPMG
110 120 130 140 150
CINVHPSLLP KYRGPSPIQT AILNGDTIGG ITVQKMALEM DSGNILAQSQ
160 170 180 190 200
FEIKSFNTSA DIFRYVSLNS FNLVLEALSK LNKGHIGIVQ DSNQATYCSF
210 220 230 240 250
FNKQHRMLNF NLSAFEIKNK INACNPWPLA RAKLDKDEII FHRADFIKTT
260 270 280 290 300
DYSDQAIGKI VSFDPSKGIL VKTEDGILLL LELQRSGRKV VDYKSFYNGN

RDLIGKIFS
Length:309
Mass (Da):34,645
Last modified:April 14, 2009 - v1
Checksum:i1F33A459B02500E5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000049 Genomic DNA. Translation: AAX17406.1.
RefSeqiWP_011772025.1. NC_008710.1.

Genome annotation databases

EnsemblBacteriaiAAX17406; AAX17406; BT0064.
KEGGibtu:BT0064.
PATRICi20571819. VBIBorTur92789_0062.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000049 Genomic DNA. Translation: AAX17406.1.
RefSeqiWP_011772025.1. NC_008710.1.

3D structure databases

ProteinModelPortaliA1QYL4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi314724.BT0064.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAX17406; AAX17406; BT0064.
KEGGibtu:BT0064.
PATRICi20571819. VBIBorTur92789_0062.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiNCITTFR.
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.
[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.
ProtoNetiSearch...

Entry informationi

Entry nameiFMT_BORT9
AccessioniPrimary (citable) accession number: A1QYL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: April 14, 2009
Last modified: November 2, 2016
This is version 54 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.