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B3CTU0 (B3CTU0_ORITI) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 34. 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 length302 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

Region104 – 1074Tetrahydrofolate (THF) binding By similarity HAMAP-Rule MF_00182

Sequences

Sequence LengthMass (Da)Tools
B3CTU0 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: DF7335DB317D8AD8

FASTA30233,732
        10         20         30         40         50         60 
MGSPEFAIPA LKELALSKHN VIAVFTSKPK KRDRYLNIQR SPIHKLASAL SIPVYTPDSL 

        70         80         90        100        110        120 
KTNDVQNLIA TLDADVIVVA AYGLIIPKAI LKMKKYGCIN IHPSMLPKYR GAAPIQRTII 

       130        140        150        160        170        180 
NGEKETAVCI IQMDQGVDTG DIILCQKFHL AKNICFSELH DQCAKVGAKL LVKAINYIHT 

       190        200        210        220        230        240 
LPRIPQSQDR ASYAHKLSKS ESKINWYESA YTIDCKIRGM NPWPGTFFTY NNCNIKVLKA 

       250        260        270        280        290        300 
KIVNNSHNLQ PGTVKIVNNN KLLVACQEHF LELLSLQLPG RKELSSSQFL CGYHILPDTV 


LQ 

« Hide

References

[1]"The whole-genome sequencing of the obligate intracellular bacterium Orientia tsutsugamushi revealed massive gene amplification during reductive genome evolution."
Nakayama K., Yamashita A., Kurokawa K., Morimoto T., Ogawa M., Fukuhara M., Urakami H., Ohnishi M., Uchiyama I., Ogura Y., Ooka T., Oshima K., Tamura A., Hattori M., Hayashi T.
DNA Res. 15:185-199(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ikeda.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008981 Genomic DNA. Translation: BAG40787.1.
RefSeqYP_001938021.1. NC_010793.1.

3D structure databases

ProteinModelPortalB3CTU0.
ModBaseSearch...

Protein-protein interaction databases

STRING334380.OTT_1329.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAG40787; BAG40787; OTT_1329.
GeneID6337195.
KEGGott:OTT_1329.
PATRIC22828962. VBIOriTsu129072_1495.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMADWNKSAR.
ProtClustDBPRK00005.

Enzyme and pathway databases

BioCycOTSU334380:GC7O-1355-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. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB3CTU0_ORITI
AccessionPrimary (citable) accession number: B3CTU0
Entry history
Integrated into UniProtKB/TrEMBL: July 22, 2008
Last sequence update: July 22, 2008
Last modified: May 29, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)