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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212))
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

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:CbuG_2005
OrganismiCoxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212))
Taxonomic identifieri434923 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000983971 – 314Methionyl-tRNA formyltransferaseAdd BLAST314

Structurei

3D structure databases

ProteinModelPortaliB6J3C2.
SMRiB6J3C2.
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

HOGENOMiHOG000261177.
KOiK00604.
OMAiLRIVFMG.

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.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
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.

B6J3C2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLKIVFAGT PQFAVPTLRA LIDSSHRVLA VYTQPDRPSG RGQKIMESPV
60 70 80 90 100
KEIARQNEIP IIQPFSLRDE VEQEKLIAMN ADVMVVVAYG LILPKKALNA
110 120 130 140 150
FRLGCVNVHA SLLPRWRGAA PIQRAILAGD RETGISIMQM NEGLDTGDVL
160 170 180 190 200
AKSACVISSE DTAADLHDRL SLIGADLLLE SLAKLEKGDI KLEKQDEASA
210 220 230 240 250
TYASKIQKQE ALIDWRKSAV EIARQVRAFN PTPIAFTYFE GQPMRIWRAT
260 270 280 290 300
VVDEKTDFEP GVLVDADKKG ISIAAGSGIL RLHQLQLPGK RVCSAGDFIN
310
AHGDKLIPGK TVFG
Length:314
Mass (Da):34,288
Last modified:December 16, 2008 - v1
Checksum:i11A4B3CCB9ED0AD8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001019 Genomic DNA. Translation: ACJ19247.1.
RefSeqiWP_010958586.1. NC_011527.1.

Genome annotation databases

EnsemblBacteriaiACJ19247; ACJ19247; CbuG_2005.
GeneIDi31484676.
KEGGicbg:CbuG_2005.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001019 Genomic DNA. Translation: ACJ19247.1.
RefSeqiWP_010958586.1. NC_011527.1.

3D structure databases

ProteinModelPortaliB6J3C2.
SMRiB6J3C2.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACJ19247; ACJ19247; CbuG_2005.
GeneIDi31484676.
KEGGicbg:CbuG_2005.

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiLRIVFMG.

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.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiFMT_COXB2
AccessioniPrimary (citable) accession number: B6J3C2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: June 7, 2017
This is version 54 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.