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A5WM89 (A5WM89_MYCTF) Unreviewed, UniProtKB/TrEMBL

Last modified April 16, 2014. Version 36. 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 length312 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

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region110 – 1134Tetrahydrofolate (THF) binding By similarity HAMAP-Rule MF_00182

Sequences

Sequence LengthMass (Da)Tools
A5WM89 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 1AD300DE45E39E2F

FASTA31232,692
        10         20         30         40         50         60 
MRLVFAGTPE PALASLRRLI ESPSHDVIAV LTRPDAASGR RGKPQPSPVA REAAERGIPV 

        70         80         90        100        110        120 
LRPSRPNSAE FVAELSDLAP ECCAVVAYGA LLGGPLLAVP PHGWVNLHFS LLPAWRGAAP 

       130        140        150        160        170        180 
VQAAIAAGDT ITGATTFQIE PSLDSGPIYG VVTEVIQPTD TAGDLLKRLA VSGAALLSTT 

       190        200        210        220        230        240 
LDGIADQRLT PRPQPADGVS VAPKITVANA RVRWDLPAAV VERRIRAVTP NPGAWTLIGD 

       250        260        270        280        290        300 
LRVKLGPVHL DAAHRPSKPL PPGGIHVERT SVWIGTGSEP VRLGQIQPPG KKLMNAADWA 

       310 
RGARLDLAAR AT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000717 Genomic DNA. Translation: ABR05778.1.
RefSeqYP_001287380.1. NC_009565.1.

3D structure databases

ProteinModelPortalA5WM89.
SMRA5WM89. Positions 1-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING336982.TBFG_11435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR05778; ABR05778; TBFG_11435.
GeneID5222114.
KEGGmtf:TBFG_11435.
PATRIC18133837. VBIMycTub9078_1572.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycMTUB336982:GH7I-1457-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 nameA5WM89_MYCTF
AccessionPrimary (citable) accession number: A5WM89
Entry history
Integrated into UniProtKB/TrEMBL: July 28, 2009
Last sequence update: July 28, 2009
Last modified: April 16, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)