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C4K6Y1 (FMT_HAMD5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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

Protein attributes

Sequence length319 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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_1000203862

Regions

Region113 – 1164Tetrahydrofolate (THF) binding By similarity

Sequences

Sequence LengthMass (Da)Tools
C4K6Y1 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 2E12DE7552ABA9CF

FASTA31935,594
        10         20         30         40         50         60 
MSESLKIIFA GTPDFSACHL QHLLSHRQKI LGVFTQPDRP AGRGKKLAFS PVKILATQHH 

        70         80         90        100        110        120 
IPVYQPHSLG LKEEQQSILD LDADVMVVVA YGLLLPQAVL NMPRLGCINV HPSLLPRWRG 

       130        140        150        160        170        180 
AAPIQRAIWA GDQETGVTIM QMDSGLDTGN MLYKTVYPIQ PDDTGASLQA KLAALGSQDL 

       190        200        210        220        230        240 
LLTLKKMAEG KMHGETQDEQ KTTYAHKLTK KEARLDWLLP AAHLERCVRA FNPWPVSYFI 

       250        260        270        280        290        300 
INEQIIKVWE AQAMPDSQQV SHLQPGTVLK ADKNGIQILT SEGVLNMTKF QLPGKKIISA 

       310 
WDFLNSRNEW FQIGKQLLS 

« Hide

References

[1]"Hamiltonella defensa, genome evolution of protective bacterial endosymbiont from pathogenic ancestors."
Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.
Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5AT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001277 Genomic DNA. Translation: ACQ68324.1.
RefSeqYP_002924472.1. NC_012751.1.

3D structure databases

ProteinModelPortalC4K6Y1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING572265.HDEF_1721.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ68324; ACQ68324; HDEF_1721.
GeneID7951318.
KEGGhde:HDEF_1721.
PATRIC31974901. VBICanHam112931_1711.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
KOK00604.
OMARGDWFTP.
OrthoDBEOG6B09WV.

Enzyme and pathway databases

BioCycHDEF572265:GJAB-1737-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.
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.
ProtoNetSearch...

Entry information

Entry nameFMT_HAMD5
AccessionPrimary (citable) accession number: C4K6Y1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: May 14, 2014
This is version 35 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