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C8TXR7 (C8TXR7_ECO10) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 35. Feed History...

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

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 SAAS SAAS005794

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP-Rule MF_00182 SAAS SAAS005794

Sequence similarities

Belongs to the Fmt family. HAMAP-Rule MF_00182

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region113 – 1164Tetrahydrofolate (THF) binding By similarity HAMAP-Rule MF_00182

Sequences

Sequence LengthMass (Da)Tools
C8TXR7 [UniParc].

Last modified November 3, 2009. Version 1.
Checksum: 318CFA5BB2A77B1B

FASTA31534,154
        10         20         30         40         50         60 
MSESLRIIFA GTPDFAARHL DALLSSGHNV VGVFTQPDRP AGRGKKLMPS PVKVLAEEKG 

        70         80         90        100        110        120 
LPVFQPVSLR PQENQQLVAD LQADVMVVVA YGLILPKAVL EMPRLGCINV HGSLLPRWRG 

       130        140        150        160        170        180 
AAPIQRSLWA GDAETGVTIM QMDVGLDTGD MLYKLSCPIT AEDTSGTLYD KLAELGPQGL 

       190        200        210        220        230        240 
ITTLKQLADG TAKPEVQDET LVTYAEKLSK EEARIDWSLS AAQLERCIRA FNPWPMSWLE 

       250        260        270        280        290        300 
IEGQPVKVWK ASVIDTATNA APGTILEANK QGIQVATGDG ILNLLSLQPA GKKAMSAQDL 

       310 
LNSRREWFVP GNRLV 

« Hide

References

[1]"Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 12009 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010958 Genomic DNA. Translation: BAI32729.1.
RefSeqYP_003223863.1. NC_013353.1.

3D structure databases

ProteinModelPortalC8TXR7.
SMRC8TXR7. Positions 2-315.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING585395.ECO103_4019.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAI32729; BAI32729; ECO103_4019.
GeneID8475055.
KEGGeoh:ECO103_4019.
PATRIC32100113. VBIEscCol146794_4204.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAKVWKAEV.
OrthoDBEOG6B09WV.
ProtClustDBPRK00005.

Enzyme and pathway databases

BioCycECOL585395:GJA9-4164-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 nameC8TXR7_ECO10
AccessionPrimary (citable) accession number: C8TXR7
Entry history
Integrated into UniProtKB/TrEMBL: November 3, 2009
Last sequence update: November 3, 2009
Last modified: April 16, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)