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A8AXH0 (TRMFO_STRGC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO

EC=2.1.1.74
Alternative name(s):
Folate-dependent tRNA (uracil-5-)-methyltransferase
Folate-dependent tRNA(M-5-U54)-methyltransferase
Gene names
Name:trmFO
Synonyms:gid
Ordered Locus Names:SGO_1193
OrganismStreptococcus gordonii (strain Challis / ATCC 35105 / CH1 / DL1 / V288) [Complete proteome] [HAMAP]
Taxonomic identifier29390 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs By similarity. HAMAP-Rule MF_01037

Catalytic activity

5,10-methylenetetrahydrofolate + uracil54 in tRNA + FADH2 = tetrahydrofolate + 5-methyluracil54 in tRNA + FAD. HAMAP-Rule MF_01037

Cofactor

FAD By similarity. HAMAP-Rule MF_01037

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01037.

Sequence similarities

Belongs to the MnmG family. TrmFO subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO HAMAP-Rule MF_01037
PRO_1000084293

Regions

Nucleotide binding10 – 156FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
A8AXH0 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 83A40CD27DC2C548

FASTA44449,330
        10         20         30         40         50         60 
MSQSYINVIG AGLAGSEAAY QIAKRGIPVK LYEMRGVKST PQHKTADFAE LVCSNSLRGD 

        70         80         90        100        110        120 
ALTNAVGLLK EEMRRLDSVI LKSAEATRVP AGGALAVDRE GFSQMVTELV TNHPLIEVIR 

       130        140        150        160        170        180 
EEITEIPNDD ITVIATGPLT SDALAEKIHA LNGGNGFYFY DAAAPIIDVN TIDMTKIYLK 

       190        200        210        220        230        240 
SRYDKGEAAY LNAPMTKQEF MDFHDALVNA EEAPLNSFEK EKYFEGCMPI EVMAKRGIKT 

       250        260        270        280        290        300 
MLYGPMKPVG LEYPDDYQGP RDGEYKTPYA VVQLRQDNAA GSLYNIVGFQ THLKWGEQKR 

       310        320        330        340        350        360 
VFQMIPGLEN AEFVRYGVMH RNSYMDSPNL LEQTFRSKKQ PNLFFAGQMT GVEGYVESAA 

       370        380        390        400        410        420 
SGLVAGINAA RLFKGEEALV FPETTAIGSL PHYVTHADSK HFQPMNVNFG IIKELDGPRI 

       430        440 
RDKKERYEKI AERALQDLAP YLDK 

« Hide

References

[1]"Genome-wide transcriptional changes in Streptococcus gordonii in response to competence signaling peptide."
Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.
J. Bacteriol. 189:7799-7807(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Challis / ATCC 35105 / CH1 / DL1 / V288.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000725 Genomic DNA. Translation: ABV09583.1.
RefSeqYP_001450480.1. NC_009785.1.

3D structure databases

ProteinModelPortalA8AXH0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING467705.SGO_1193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV09583; ABV09583; SGO_1193.
GeneID5598455.
KEGGsgo:SGO_1193.
PATRIC19660339. VBIStrGor124371_1176.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1206.
HOGENOMHOG000252054.
KOK04094.
OMARFAGQIT.
OrthoDBEOG6J74VT.
ProtClustDBPRK05335.

Enzyme and pathway databases

BioCycSGOR467705:GH3R-1191-MONOMER.

Family and domain databases

HAMAPMF_01037. TrmFO.
InterProIPR004417. Folate-dep_Ribothymidyl_synth.
IPR002218. GIDA-rel.
IPR020595. GIDA-rel_CS.
[Graphical view]
PfamPF01134. GIDA. 1 hit.
[Graphical view]
TIGRFAMsTIGR00137. gid_trmFO. 1 hit.
PROSITEPS01281. GIDA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRMFO_STRGC
AccessionPrimary (citable) accession number: A8AXH0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families