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Q28PE7 (TRMFO_JANSC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
Ordered Locus Names:Jann_2498
OrganismJannaschia sp. (strain CCS1) [Complete proteome] [HAMAP]
Taxonomic identifier290400 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeJannaschia

Protein attributes

Sequence length458 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 MF_01037

Catalytic activity

5,10-methylenetetrahydrofolate + tRNA containing uridine at position 54 + FADH2 = tetrahydrofolate + tRNA containing ribothymidine at position 54 + FAD. HAMAP MF_01037

Cofactor

FAD By similarity. HAMAP MF_01037

Subcellular location

Cytoplasm By similarity HAMAP MF_01037.

Sequence similarities

Belongs to the MnmG family. TrmFO subfamily.

Ontologies

Keywords
   Biological processtRNA processing
   Cellular componentCytoplasm
   LigandFAD
Flavoprotein
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionflavin adenine dinucleotide binding

Inferred from electronic annotation. Source: InterPro

methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 458458Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO HAMAP MF_01037
PRO_0000346345

Regions

Nucleotide binding11 – 166FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q28PE7 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: C5BC5B0F50820C58

FASTA45849,479
        10         20         30         40         50         60 
MTQNTQLTII GGGMAGSEAA WQAANLGVNV RLIEMRPKVE TFAHRTGNLA EMVCSNSFRS 

        70         80         90        100        110        120 
DDSEQNAVGL LHWEMRAANS VIMHTADSHK LPAGGALAVD RDPFAEAVTA KLHAHPNIEI 

       130        140        150        160        170        180 
TYGEVTDLPA AGPTIIATGP LTGSALADAI AREAGQDALA FFDAIAPIVY ADSIDMDIAW 

       190        200        210        220        230        240 
RQSRYDKGDT LEEQQAYINC PLTRDQYEAF IDALLSADKT QFKDGETAGY FDGCLPIEVM 

       250        260        270        280        290        300 
AERGRETLRF GPMKPVGLTN PHDPQTKAYA VVQLRRDNAL GTLYNIVGFQ TKMTYGAQKQ 

       310        320        330        340        350        360 
VFAMIPGLQE ASFARLGGIH RNTFINSPTL LDDQMRLRSK PHIRFAGQIT GVEGYVESAS 

       370        380        390        400        410        420 
MGLLAGRMAA AEILGETLPD LPDTTAMGAL VTHITGGADA KTFQPMNVNF GLFPPVEGLK 

       430        440        450 
GGRRGRKDRY KAYTDRAKAA WTNWLTPQTS LGGSQAAE 

« Hide

References

[1]"Complete sequence of chromosome of Jannaschia sp. CCS1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J., Larimer F. expand/collapse author list , Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W., Buchan A., Gonzalez J.M., Schell M.A., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCS1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000264 Genomic DNA. Translation: ABD55415.1.
RefSeqYP_510440.1. NC_007802.1.

3D structure databases

ProteinModelPortalQ28PE7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ28PE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3934957.
GenomeReviewsGene locus Jann_2498 in contig CP000264_GR.
KEGGjan:Jann_2498.
PATRIC22148782. VBIJanSp43325_2652.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1206.
HOGENOMHBG285041.
OMARFAGQIT.
ProtClustDBPRK05335.

Enzyme and pathway databases

BioCycJSP290400:JANN_2498-MONOMER.

Family and domain databases

HAMAPMF_01037. TrmFO.
[Tree]
InterProIPR004417. Folate-dep_Ribothymidyl_synth.
IPR002218. GIDA-rel.
IPR020595. GIDA-rel_CS.
[Graphical view]
KOK04094.
PfamPF01134. GIDA. 1 hit.
[Graphical view]
TIGRFAMsTIGR00137. Gid_trmFO. 1 hit.
PROSITEPS01280. GIDA_1. False negative.
PS01281. GIDA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRMFO_JANSC
AccessionPrimary (citable) accession number: Q28PE7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: April 4, 2006
Last modified: January 25, 2012
This is version 50 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