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D9QFK5 (D9QFK5_BRESC) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 18. Feed History...

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

Sequence length308 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

Region109 – 1124Tetrahydrofolate (THF) binding By similarity HAMAP-Rule MF_00182

Sequences

Sequence LengthMass (Da)Tools
D9QFK5 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: FA2DDF2922AC4289

FASTA30832,264
        10         20         30         40         50         60 
MRLAFMGTPD FAVPSLAELI ASGHEVVAVY SQPPKPRGRG QKLTPSPVHA FAETMGLPVF 

        70         80         90        100        110        120 
TPASMKAPDA IETFASLDLD AACVVAYGQI LKAEVLSAPR LGCFNLHGSL LPRWRGAAPI 

       130        140        150        160        170        180 
QRAIMAGDRQ TGVQIMRMSE GLDEGAILLS EVLPIAPDDT AATLSDRMAT TGATLWTRAL 

       190        200        210        220        230        240 
AAIERGGVTE TEQAGEVTYA RKITPAEARI DWTRPAAELD CHIRGLSPFP GAWFEAPGPD 

       250        260        270        280        290        300 
GPVRVKALMS APVAQGSGAP GEVLDGDLLI GTGDGAVRLL RVQREGKAAQ GPADFLRGFA 


LPVGTILG

« Hide

References

[1]"Genome sequences of eight morphologically diverse alphaproteobacteria."
US DOE Joint Genome Institute
Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.
J. Bacteriol. 193:4567-4568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002102 Genomic DNA. Translation: ADL02520.1.
RefSeqYP_003820143.1. NC_014375.1.

3D structure databases

ProteinModelPortalD9QFK5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL02520; ADL02520; Bresu_3214.
GeneID9505113.
KEGGbsb:Bresu_3214.
PATRIC42205703. VBIBreSub37974_3241.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000261177.
KOK00604.
OMAGITLMQM.

Enzyme and pathway databases

BioCycBSUB633149:GHJJ-3270-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 nameD9QFK5_BRESC
AccessionPrimary (citable) accession number: D9QFK5
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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