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Q1CCX5 (FMT_YERPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase

EC=2.1.2.9
Gene names
Name:fmt
Ordered Locus Names:YPN_3828
ORF Names:YP516_4350
OrganismYersinia pestis bv. Antiqua (strain Nepal516) [Complete proteome] [HAMAP]
Taxonomic identifier377628 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length315 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)
   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

methyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 315315Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000020208

Regions

Region113 – 1164Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1CCX5 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 24F167229DC2E0C8

FASTA31534,140
        10         20         30         40         50         60 
MSDSLRIIFA GTPDFAARHL GALLSSQHKI VGVFTQPDRP AGRGNKLTPS PVKILAEHHG 

        70         80         90        100        110        120 
IPVFQPKSLR PEENQHLVAD LNADIMVVVA YGLILPAAVL AMPRLGCINV HGSLLPRWRG 

       130        140        150        160        170        180 
AAPIQRSVWA GDEKTGITIM QMDIGLDTGA MLHKIECAIQ PEDTSATLYD KLAQLGPQGL 

       190        200        210        220        230        240 
LITLQQLAAG TALAEVQNET QATYAEKLSK EEAKLDWTLS ATQLERCIRA FNPWPVSYFI 

       250        260        270        280        290        300 
VDEQPIKVWQ AQVLPAGEDA EPGTIIHADK HGIQVATADG VLNITQLQPA GKKAMSAADL 

       310 
LNSRREWFIP GSQLV 

« Hide

References

[1]"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nepal516.
[2]"Yersinia pestis Nepal516A whole genome shotgun sequencing project."
Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L., Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R., Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.
Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000305 Genomic DNA. Translation: ABG20155.1.
ACNQ01000019 Genomic DNA. Translation: EEO74742.1.
RefSeqYP_649755.1. NC_008149.1.

3D structure databases

ProteinModelPortalQ1CCX5.
SMRQ1CCX5. Positions 2-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING377628.YPN_3828.

Proteomic databases

PRIDEQ1CCX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG20155; ABG20155; YPN_3828.
EEO74742; EEO74742; YP516_4350.
GeneID4123299.
KEGGypn:YPN_3828.
PATRIC18607783. VBIYerPes46733_4519.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMARGDWFTP.
OrthoDBEOG6B09WV.

Enzyme and pathway databases

BioCycYPES377628:GIXK-3929-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. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
PROSITEPS00373. GART. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_YERPN
AccessionPrimary (citable) accession number: Q1CCX5
Secondary accession number(s): D1Q2I9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 56 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