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Q1WU04 (TRMFO_LACS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. 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
Synonyms:gid
Ordered Locus Names:LSL_0721
OrganismLactobacillus salivarius (strain UCC118) [Complete proteome] [HAMAP]
Taxonomic identifier362948 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus

Protein attributes

Sequence length436 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

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase TrmFO HAMAP MF_01037
PRO_1000072978

Regions

Nucleotide binding9 – 146FAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1WU04 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: 01571FADDDE6DB3C

FASTA43648,676
        10         20         30         40         50         60 
MTASVNVIGA GLAGSEAAWQ IANQGVKVRL YEMRPQKLTP AHHNENFAEL VCTNSLRANR 

        70         80         90        100        110        120 
LTNAAGLLKE EMRTFNSIIM ESADKHSVPA GGALAVDRET FSKEVTEKLH NHPNVEIINE 

       130        140        150        160        170        180 
EIDEIPEGLT VIATGPLTSD ALAKDITKFT GSDGLFFFDA AAPILEKSSL DMDKVYLKSR 

       190        200        210        220        230        240 
YDKGEAAYLN APMTKDEFYN FYNELIKAET AELHDFEDDK FFEGCMPIEE IASRGAQTML 

       250        260        270        280        290        300 
YGPLKPVGLE DPRTGKEPFA VVQLRQDNAA GDLYNIVGFQ THLKWGEQKR VFSMIPGLEN 

       310        320        330        340        350        360 
ARFVRYGVMH RNTFLCSPEV MQATYQTKKR LDLFFAGQMT GVEGYVESAA SGLYAGLNAA 

       370        380        390        400        410        420 
RIAQGKDPVI FPEETMMGAM AHYITHASVK NFQPINANFG IVPKLQERIR NKQERNLKIS 

       430 
ERAIDRIKKF KNLNFD

« Hide

References

[1]"Multireplicon genome architecture of Lactobacillus salivarius."
Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P., Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K., Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.
Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006) [PubMed: 16617113] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCC118.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000233 Genomic DNA. Translation: ABD99531.1.
RefSeqYP_535614.1. NC_007929.1.

3D structure databases

ProteinModelPortalQ1WU04.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1WU04.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3976950.
GenomeReviewsGene locus LSL_0721 in contig CP000233_GR.
KEGGlsl:LSL_0721.
PATRIC22278351. VBILacSal43464_0800.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1206.
HOGENOMHBG285041.
OMARFAGQIT.
ProtClustDBPRK05335.

Family and domain databases

HAMAPMF_01037. TrmFO.
[Tree]
InterProIPR004417. Folate-dep_Ribothymidyl_synth.
IPR002218. GIDA-rel.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK04094.
PfamPF01134. GIDA. 1 hit.
[Graphical view]
TIGRFAMsTIGR00137. Gid_trmFO. 1 hit.
PROSITEPS01280. GIDA_1. False negative.
PS01281. GIDA_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRMFO_LACS1
AccessionPrimary (citable) accession number: Q1WU04
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 2, 2006
Last modified: January 25, 2012
This is version 46 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

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