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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Borrelia recurrentis (strain A1)
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

BioCyciBREC412418:GJIA-67-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:BRE_67
OrganismiBorrelia recurrentis (strain A1)
Taxonomic identifieri412418 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesBorreliaceaeBorrelia
Proteomesi
  • UP000000612 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309Methionyl-tRNA formyltransferasePRO_1000098381Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB5RQP3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni107 – 1104Tetrahydrofolate (THF) bindingUniRule annotation

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiQRDKPFG.
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.

B5RQP3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRIFFASSDG IALEVLKKIS DQYDVVGVLT APDKPSGRGL SLKVNDIKRE
60 70 80 90 100
ALSRKITVLQ PVVLDADVIN LVKSLEPELM LVFSYGKIFK QEFLDIFPVG
110 120 130 140 150
CINIHPSLLP KYRGPSPIQT VILNGDSVSG ITVQKMTLEM DSGNILAQSQ
160 170 180 190 200
FEIKSFNTSV DIFEYVSLNS FDLVIEALNK LLKGDIGIVQ DKNNATYCSF
210 220 230 240 250
LGKEHRTIDF KLSAFDIKNK INAYNPWPLA RARLDNNEII FYRADFISTN
260 270 280 290 300
DYDDQVIGKI IAFDPSKGLL VKTGDGILVV LELQRIGKKV LDCVSFYHGN

RDLIGKVFS
Length:309
Mass (Da):34,473
Last modified:November 4, 2008 - v1
Checksum:iC513BA8427FC43AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000993 Genomic DNA. Translation: ACH94327.1.
RefSeqiWP_012538632.1. NC_011244.1.

Genome annotation databases

EnsemblBacteriaiACH94327; ACH94327; BRE_67.
KEGGibre:BRE_67.
PATRICi20569257. VBIBorRec40566_0080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000993 Genomic DNA. Translation: ACH94327.1.
RefSeqiWP_012538632.1. NC_011244.1.

3D structure databases

ProteinModelPortaliB5RQP3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACH94327; ACH94327; BRE_67.
KEGGibre:BRE_67.
PATRICi20569257. VBIBorRec40566_0080.

Phylogenomic databases

HOGENOMiHOG000261177.
KOiK00604.
OMAiQRDKPFG.
OrthoDBiPOG091H01YM.

Enzyme and pathway databases

BioCyciBREC412418:GJIA-67-MONOMER.

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_BORRA
AccessioniPrimary (citable) accession number: B5RQP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 4, 2008
Last modified: September 7, 2016
This is version 57 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

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.