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C6A7A9 (C6A7A9_BIFLB) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Protein attributes

Sequence length303 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. SAAS SAAS005794

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). SAAS SAAS005794

Ontologies

Keywords
   Biological processProtein biosynthesis SAAS SAAS005794
   Molecular functionTransferase SAAS SAAS005794 EMBL ACS46007.1
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_functionmethionyl-tRNA formyltransferase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
C6A7A9 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: AB992E26BDBFBC98

FASTA30332,253
        10         20         30         40         50         60 
MLAKDTEHFE VVAVLTRPDA PTGRGRKIMP SPVKMAAREL GLDVIECDPA DECFLSALKA 

        70         80         90        100        110        120 
TGAQCAAVVA YGKILRESVL EALPLGWYNL HFSLLPQWRG AAPVQRAIWA GDEVTGCSVF 

       130        140        150        160        170        180 
RITAGMDRGP VLGQSTVTIG AHENAGELLD RLAEDGAGLL AASLQALDEG VVNAVDQPAG 

       190        200        210        220        230        240 
SYDVAAKITT QDAHMRFDVP AFALDRQIRA CTPAPGAWAN LHPHGDDANE TLHVSKAIPA 

       250        260        270        280        290        300 
DMTADESPRN LKPGELHVTK HHVWVGTSTD PLELLVVKAA GKREMGAPEW ARGAHLAEGA 


YLD 

« Hide

References

[1]"Comparison of the complete genome sequences of Bifidobacterium animalis subsp. lactis DSM 10140 and Bl-04."
Barrangou R., Briczinski E.P., Traeger L.L., Loquasto J.R., Richards M., Horvath P., Coute-Monvoisin A.C., Leyer G., Rendulic S., Steele J.L., Broadbent J.R., Oberg T., Dudley E.G., Schuster S., Romero D.A., Roberts R.F.
J. Bacteriol. 191:4144-4151(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bl-04 / DGCC2908 / RB 4825 / SD5219.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001515 Genomic DNA. Translation: ACS46007.1.
RefSeqYP_002968069.1. NC_012814.1.

3D structure databases

ProteinModelPortalC6A7A9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING580050.Balac_0634.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS46007; ACS46007; Balac_0634.
GeneID8008600.
KEGGblc:Balac_0634.
PATRIC21107491. VBIBifAni84420_0643.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAKVWKAEV.
OrthoDBEOG6B09WV.
ProtClustDBCLSK573224.

Enzyme and pathway databases

BioCycBANI580050:GI23-634-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.
ProtoNetSearch...

Entry information

Entry nameC6A7A9_BIFLB
AccessionPrimary (citable) accession number: C6A7A9
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)