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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Frankia alni (strain ACN14a)
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:FRAAL5225
OrganismiFrankia alni (strain ACN14a)
Taxonomic identifieri326424 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaFrankialesFrankiaceaeFrankia
Proteomesi
  • UP000000657 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000200611 – 331Methionyl-tRNA formyltransferaseAdd BLAST331

Interactioni

Protein-protein interaction databases

STRINGi326424.FRAAL5225.

Structurei

3D structure databases

ProteinModelPortaliQ0RF89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 113Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

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

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.

Q0RF89-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLVFAGTPA VALPSLRALI DSPRHEVVAV VTRPDRPAGR GRKIKPPPVH
60 70 80 90 100
LLADEAGIPV LSPERPRDPD FLAALTDLAP DCCPVVAYGA LLPREALAIP
110 120 130 140 150
RHGWVNLHFS LLPAYRGAAP VQRTVLAGDD LTGASVFQIE PAMDSGPVFG
160 170 180 190 200
VVTERVRPTD TSGDLLDRLA DSGAHLLAAV MDGIDDGTLQ AVPQPAEGVS
210 220 230 240 250
FAPKLTAQDA LIDWTLPAVA VDRLTRAAAP APGAWTVFRD RRIKIGPVRL
260 270 280 290 300
GAQNVPDELA PGRLVALADG AVAVGTGTAP VLLDEVRPEG RGPMKAADWA
310 320 330
RGARLTDDDL LHAPAERVSA AGSPAGAGGA P
Length:331
Mass (Da):34,397
Last modified:September 5, 2006 - v1
Checksum:iEDED1EA1E3002143
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT573213 Genomic DNA. Translation: CAJ63858.1.
RefSeqiWP_011606320.1. NC_008278.1.

Genome annotation databases

KEGGifal:FRAAL5225.
PATRICi21919676. VBIFraAln347_4789.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT573213 Genomic DNA. Translation: CAJ63858.1.
RefSeqiWP_011606320.1. NC_008278.1.

3D structure databases

ProteinModelPortaliQ0RF89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi326424.FRAAL5225.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGifal:FRAAL5225.
PATRICi21919676. VBIFraAln347_4789.

Phylogenomic databases

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

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_FRAAA
AccessioniPrimary (citable) accession number: Q0RF89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: November 2, 2016
This is version 67 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.