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B1L8W7 (FMT_THESQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase

EC=2.1.2.9
Gene names
Name:fmt
Ordered Locus Names:TRQ2_0409
OrganismThermotoga sp. (strain RQ2) [Complete proteome] [HAMAP]
Taxonomic identifier126740 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length313 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_00182

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP-Rule MF_00182

Sequence similarities

Belongs to the fmt family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtranslational initiation

Inferred from electronic annotation. Source: GOC

   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: HAMAP

methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 313313Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000098454

Regions

Region109 – 1124Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
B1L8W7 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 48055C0CDEF4FD92

FASTA31335,216
        10         20         30         40         50         60 
MRIVFVGTPE FAAEILEHLI KNGFNVVGVV TQPDKPRGRG RKVEPTPVKV VAEKHRVPFI 

        70         80         90        100        110        120 
QPESINKKEA LEFLRSVGPD VIIVASYGKI LGEKVLSLPS LGCYNIHPSL LPKYRGASPI 

       130        140        150        160        170        180 
QRVLENGEER TGVTIYKMVR ELDAGPIALQ REISIDPFET FDQLEKRLIE LSKEMSIEFL 

       190        200        210        220        230        240 
EKLKVGDIEL KEQDHSRATY APMIKKEDLI VDFSKDAESV KNKIRAYDSR PGARAFLGND 

       250        260        270        280        290        300 
EVKLFGVTAI DSSGDEPGLI HYIDREGAWI GTGKGMVKVK YLQLPGKKKL TFWELRNGRL 

       310 
IEEGMKLEGR YES 

« Hide

References

[1]"Complete sequence of Thermotoga sp. RQ2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RQ2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000969 Genomic DNA. Translation: ACB08765.1.
RefSeqYP_001738448.1. NC_010483.1.

3D structure databases

ProteinModelPortalB1L8W7.
ModBaseSearch...

Protein-protein interaction databases

STRING126740.TRQ2_0409.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB08765; ACB08765; TRQ2_0409.
GeneID6091814.
KEGGtrq:TRQ2_0409.
PATRIC23947331. VBITheSp108950_0414.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAGITLMQM.
ProtClustDBCLSK875200.

Family and domain databases

Gene3D3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPMF_00182. Formyl_trans.
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERPTHR11138. PTHR11138. 1 hit.
PfamPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF50486. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
PROSITEPS00373. GART. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_THESQ
AccessionPrimary (citable) accession number: B1L8W7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: May 1, 2013
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families