SPM_004670


  Uniprot: A0A037UN14
Description: tRNA (uracil-5-)-methyltransferase
EC number: 2.1.1.74
Annotation score: 3 out of 5
Miscellaneous [CC]: 
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + uracil(54) in tRNA + FADH(2) = tetrahydrofolate + 5-methyluracil(54) in tRNA + FAD. {ECO:0000256|HAMAP-Rule:MF_01037, ECO:0000256|SAAS:SAAS00326707}.
Cofactor: COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-Rule:MF_01037, ECO:0000256|SAAS:SAAS00326714};
Enzyme regulation: 
Function [CC]: FUNCTION: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs. {ECO:0000256|HAMAP-Rule:MF_01037, ECO:0000256|SAAS:SAAS00326709}.
Pathway: 
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: NP_BIND 10 15 FAD. {ECO:0000256|HAMAP-Rule:MF_01037}.
Site: 
Gene names (primary): trmFO
Gene names (synonym): 
Mass: 49,329
Subunit structure [CC]: 
Gene ontology (GO): cytoplasm [GO:0005737]; 5,10-methylenetetrahydrofolate-dependent tRNA (m5U54) methyltransferase activity [GO:0030698]; flavin adenine dinucleotide binding [GO:0050660]; methylenetetrahydrofolate-tRNA-(uracil-5-)-methyltransferase (FADH2-oxidizing) activity [GO:0047151]; oxidoreductase activity [GO:0016491]
Gene ontology IDs: GO:0005737; GO:0016491; GO:0030698; GO:0047151; GO:0050660
Chain: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the MnmG family. TrmFO subfamily. {ECO:0000256|HAMAP-Rule:MF_01037, ECO:0000256|SAAS:SAAS00571554}.
Protein families: MnmG family, TrmFO subfamily
Coiled coil: COILED 409 437 {ECO:0000256|SAM:Coils}.
Domain [FT]: 
Motif: 
Region: 
EMBL: AGBZ02000004
ProteinModelPortal: 
MEROPS: 
EnsemblBacteria KO: KAI92033
UniPathway: 
CDD: 
Gene3D: 
HAMAP: 3.50.50.60
InterPro: MF_01037
PANTHER: IPR023753;IPR002218;IPR004417
PIRSF: 
PRINTS: 
PROSITE: 
Pfam: 
ProDom: PF01134
SMART: 
SUPFAM: 
TIGRFAMs: SSF51905
6298-7612(+)

>nucleotide sequence
ATGAAACAAAAAGAAACTAATGTTATTGGCGCTGGGTTAGCAGGCTGTGAAATTGCTTAC
CAGTTAGCAAAACGTGGGTTAAAAGTAAAATTATATGAAGCAAAAACATTATTTAAAAAT
CCAGTTCAAAAATTAGATACATTTGCAGAATTAGTTTGTTCTAATTCTTTTCGTAGTGTT
TCGAAAGAAAATGCAATTGGTATTTTAAAAGAAGAGTTAAAATTATTAGATTCTTTAATT
TTAAAAACAGCTTATGATGTCCAAGTTCCTGCTGATGATGCGCTTAGTGTTGACCGCGAG
TTATTTTCACAAAAAGTTACAGCAACTTTAATAAATCATCCTAATATTAATATTATTTAT
GATGAATTTATTAAAATAGATCCAAAACAAATTACCATTATTGCTGTTGGACCATTAGTA
ACAGCAAATTTTGCTTTTGAACTTAAGAAGTTAATTGGTAAGAAAGCATTGTATTATTAT
GATGGTTCAGCTCCAATTATAACAAAAGCTGGAATTGATTTTTCAAAAGCATATTATGGC
GCACGACACTCAGAACAAAAGGATTATATTATTTGTCCATTAACAGAAGATGAATTTAAT
CAATTAGTTACCGAATTAGTAAAAGCAAAACGAGTACCTATTGCAGATTTTGAAAAATAT
TTTAAAGGTTGTCAACCAATTGAGATTATGGCACAAACATCACGAAAAATTCTTTTGAAT
GGGCCAATGAGTAGTAATCATTTAATAGACAAAAATGGTAAGCAACCGTTTGCGGTGGTT
CAATTACGACAAGATAATGTAATTGATAGTTTATATAATTTAGTAGGCTGACAGACAAAT
CTAACGTGACCAGAACAAAAACGAATTATTAAACAATTTATTCCAGGGTTAGCAAAAGTA
GATATTGTTCGATATGGAGTTTTACATAAAAATAATTATATTAATTCTCCAAAAGTTTTA
AATCAATTTTTACAATATAAACAAAATAATAATATTTTTTTTGCTGGTCAAATTATTGGT
GTAGAAGGTTATTTAGAATCAGCGGCAGCAGGCTTATTATGTGCCTTAAATGTCTATCAA
TATGTAATGGATTTACCATTAATTAAATTTCCTTCAGAAACTATGCTAGGAGCATTAGTT
AACTATGTTACAAATCCAAAACAACGAGATTTAAAACCGATGAAAGCAAATATTGGCATC
GTGCCAACTTTAACAACTAAATTCAAAAGTAAAACAGAGAAAAATTTAGCAATTTATTCT
CGAGCAATAAAAAAATTAAAAGAAACTATTAAAAAATATCAAATTAAATTATAA


>protein sequence
MKQKETNVIGAGLAGCEIAYQLAKRGLKVKLYEAKTLFKNPVQKLDTFAELVCSNSFRSV
SKENAIGILKEELKLLDSLILKTAYDVQVPADDALSVDRELFSQKVTATLINHPNINIIY
DEFIKIDPKQITIIAVGPLVTANFAFELKKLIGKKALYYYDGSAPIITKAGIDFSKAYYG
ARHSEQKDYIICPLTEDEFNQLVTELVKAKRVPIADFEKYFKGCQPIEIMAQTSRKILLN
GPMSSNHLIDKNGKQPFAVVQLRQDNVIDSLYNLVGWQTNLTWPEQKRIIKQFIPGLAKV
DIVRYGVLHKNNYINSPKVLNQFLQYKQNNNIFFAGQIIGVEGYLESAAAGLLCALNVYQ
YVMDLPLIKFPSETMLGALVNYVTNPKQRDLKPMKANIGIVPTLTTKFKSKTEKNLAIYS
RAIKKLKETIKKYQIKL






















© Fisunov Lab of Proteomics, 2016.