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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Thermotoga sp. (strain RQ2)
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

Enzyme and pathway databases

BioCyciTSP126740:GH49-415-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferaseUniRule annotation (EC:2.1.2.9UniRule annotation)
Gene namesi
Name:fmtUniRule annotation
Ordered Locus Names:TRQ2_0409
OrganismiThermotoga sp. (strain RQ2)
Taxonomic identifieri126740 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000001687 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Methionyl-tRNA formyltransferasePRO_1000098454Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB1L8W7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 1124Tetrahydrofolate (THF) bindingUniRule annotation

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0223.
HOGENOMiHOG000261177.
KOiK00604.
OMAiLGCYNIH.
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.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERiPTHR11138. PTHR11138. 1 hit.
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.

B1L8W7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIVFVGTPE FAAEILEHLI KNGFNVVGVV TQPDKPRGRG RKVEPTPVKV
60 70 80 90 100
VAEKHRVPFI QPESINKKEA LEFLRSVGPD VIIVASYGKI LGEKVLSLPS
110 120 130 140 150
LGCYNIHPSL LPKYRGASPI QRVLENGEER TGVTIYKMVR ELDAGPIALQ
160 170 180 190 200
REISIDPFET FDQLEKRLIE LSKEMSIEFL EKLKVGDIEL KEQDHSRATY
210 220 230 240 250
APMIKKEDLI VDFSKDAESV KNKIRAYDSR PGARAFLGND EVKLFGVTAI
260 270 280 290 300
DSSGDEPGLI HYIDREGAWI GTGKGMVKVK YLQLPGKKKL TFWELRNGRL
310
IEEGMKLEGR YES
Length:313
Mass (Da):35,216
Last modified:April 29, 2008 - v1
Checksum:i48055C0CDEF4FD92
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000969 Genomic DNA. Translation: ACB08765.1.
RefSeqiWP_012310526.1. NC_010483.1.

Genome annotation databases

EnsemblBacteriaiACB08765; ACB08765; TRQ2_0409.
KEGGitrq:TRQ2_0409.
PATRICi23947331. VBITheSp108950_0414.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000969 Genomic DNA. Translation: ACB08765.1.
RefSeqiWP_012310526.1. NC_010483.1.

3D structure databases

ProteinModelPortaliB1L8W7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB08765; ACB08765; TRQ2_0409.
KEGGitrq:TRQ2_0409.
PATRICi23947331. VBITheSp108950_0414.

Phylogenomic databases

eggNOGiCOG0223.
HOGENOMiHOG000261177.
KOiK00604.
OMAiLGCYNIH.
OrthoDBiEOG6B09WV.

Enzyme and pathway databases

BioCyciTSP126740:GH49-415-MONOMER.

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.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERiPTHR11138. PTHR11138. 1 hit.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RQ2.

Entry informationi

Entry nameiFMT_THESQ
AccessioniPrimary (citable) accession number: B1L8W7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: July 22, 2015
This is version 51 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.