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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
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:Mmc1_0143
OrganismiMagnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
Taxonomic identifieri156889 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus
Proteomesi
  • UP000002586 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000984161 – 312Methionyl-tRNA formyltransferaseAdd BLAST312

Interactioni

Protein-protein interaction databases

STRINGi156889.Mmc1_0143.

Structurei

3D structure databases

ProteinModelPortaliA0L3X7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni112 – 115Tetrahydrofolate (THF) bindingUniRule annotation4

Sequence similaritiesi

Belongs to the Fmt family.UniRule annotation

Phylogenomic databases

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

A0L3X7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAWRVVFMG TPDFATGTLQ ALLDGPDTVV AVFTQPDKPV GRGMKMQKTP
60 70 80 90 100
VKQLAEQHGI PVYQPNRLRE AEAVTALRAL RPDVVVVVAY GQILSREVLE
110 120 130 140 150
IPTHGCINVH ASLLPRWRGA APIQRAILAG DAQSGVTIMA MEEGLDTGPM
160 170 180 190 200
YSTVVQSIDN HTTGGQLHDQ LMAAGGGLLV ETLARIKHEG LTPQIQPEQG
210 220 230 240 250
VTYAAKLKKE EGLVDWSQPA IQIQRAVQAF DPWPCAFTLW QGKPLKLFAA
260 270 280 290 300
SVVVGHGTPG EVIEVEKDGF VVACGDGALR VAQVQAAGKK RMSSGEWLRG
310
HGVKQGERLG EG
Length:312
Mass (Da):33,499
Last modified:December 12, 2006 - v1
Checksum:i65CF1B00BBCB1028
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK42670.1.
RefSeqiWP_011711843.1. NC_008576.1.

Genome annotation databases

EnsemblBacteriaiABK42670; ABK42670; Mmc1_0143.
KEGGimgm:Mmc1_0143.
PATRICi22426740. VBIMagSp23654_0141.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000471 Genomic DNA. Translation: ABK42670.1.
RefSeqiWP_011711843.1. NC_008576.1.

3D structure databases

ProteinModelPortaliA0L3X7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi156889.Mmc1_0143.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABK42670; ABK42670; Mmc1_0143.
KEGGimgm:Mmc1_0143.
PATRICi22426740. VBIMagSp23654_0141.

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
KOiK00604.
OMAiGCINSHA.
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_MAGMM
AccessioniPrimary (citable) accession number: A0L3X7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 12, 2006
Last modified: November 2, 2016
This is version 63 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.