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Q14HS3 (FMT_FRAT1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 49. 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:FTF0925
OrganismFrancisella tularensis subsp. tularensis (strain FSC 198) [Complete proteome] [HAMAP]
Taxonomic identifier393115 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

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 functionTransferase
   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_1000020063

Regions

Region113 – 1164Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q14HS3 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: D8B28F8E3E107BA4

FASTA31335,325
        10         20         30         40         50         60 
MKKLNIIFAG TPDISAQVLK DLYKSQHNIQ AVLTQPDRAK GRGKKVQFSP VKEVALANHT 

        70         80         90        100        110        120 
PVFQPLSFKK NPEVLEQIKQ LKPDVIVVIA YGIIVPQEFL DIPRYGCLNI HVSLLPKWRG 

       130        140        150        160        170        180 
AAPIQRAIQA GDTKTGVCIM QMDAGLDTGD ILNTLEIEIQ ETDTSQTLHD KFAKLSIKPL 

       190        200        210        220        230        240 
LETLEKIEII KPEPQQGEPT YAHKITKQEG LIDFTKSAWQ ISCHIRAFTP WPGAYFILDD 

       250        260        270        280        290        300 
EAIKVGEFEI LYQNTDNRKA GTIIDIYRSG FDIATSDKII RFRQLQFPNK KMLNIVDILN 

       310 
GKDLDKYIGY KLG 

« Hide

References

[1]"Genome sequencing shows that European isolates of Francisella tularensis subspecies tularensis are almost identical to US laboratory strain Schu S4."
Chaudhuri R.R., Ren C.-P., Desmond L., Vincent G.A., Silman N.J., Brehm J.K., Elmore M.J., Hudson M.J., Forsman M., Isherwood K.E., Gurycova D., Minton N.P., Titball R.W., Pallen M.J., Vipond R.
PLoS ONE 2:E352-E352(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FSC 198.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286280 Genomic DNA. Translation: CAL08941.1.
RefSeqYP_667053.1. NC_008245.1.

3D structure databases

ProteinModelPortalQ14HS3.
ModBaseSearch...

Protein-protein interaction databases

STRING393115.FTF0925.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL08941; CAL08941; FTF0925.
GeneID4199412.
KEGGftf:FTF0925.
PATRIC17960782. VBIFraTul133500_1056.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAGITLMQM.
ProtClustDBCLSK934754.

Enzyme and pathway databases

BioCycFTUL393115:GJUT-943-MONOMER.

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.
IPR001555. GART_AS.
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_FRAT1
AccessionPrimary (citable) accession number: Q14HS3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: May 29, 2013
This is version 49 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