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 CAGTTAGCAAAACGTGGGTTAAAAGTAAAATTATATGAAGCAAAAACATTATTTAAAAAT CCAGTTCAAAAATTAGATACATTTGCAGAATTAGTTTGTTCTAATTCTTTTCGTAGTGTT TCGAAAGAAAATGCAATTGGTATTTTAAAAGAAGAGTTAAAATTATTAGATTCTTTAATT TTAAAAACAGCTTATGATGTCCAAGTTCCTGCTGATGATGCGCTTAGTGTTGACCGCGAG TTATTTTCACAAAAAGTTACAGCAACTTTAATAAATCATCCTAATATTAATATTATTTAT GATGAATTTATTAAAATAGATCCAAAACAAATTACCATTATTGCTGTTGGACCATTAGTA ACAGCAAATTTTGCTTTTGAACTTAAGAAGTTAATTGGTAAGAAAGCATTGTATTATTAT GATGGTTCAGCTCCAATTATAACAAAAGCTGGAATTGATTTTTCAAAAGCATATTATGGC GCACGACACTCAGAACAAAAGGATTATATTATTTGTCCATTAACAGAAGATGAATTTAAT CAATTAGTTACCGAATTAGTAAAAGCAAAACGAGTACCTATTGCAGATTTTGAAAAATAT TTTAAAGGTTGTCAACCAATTGAGATTATGGCACAAACATCACGAAAAATTCTTTTGAAT GGGCCAATGAGTAGTAATCATTTAATAGACAAAAATGGTAAGCAACCGTTTGCGGTGGTT CAATTACGACAAGATAATGTAATTGATAGTTTATATAATTTAGTAGGCTGACAGACAAAT CTAACGTGACCAGAACAAAAACGAATTATTAAACAATTTATTCCAGGGTTAGCAAAAGTA GATATTGTTCGATATGGAGTTTTACATAAAAATAATTATATTAATTCTCCAAAAGTTTTA AATCAATTTTTACAATATAAACAAAATAATAATATTTTTTTTGCTGGTCAAATTATTGGT GTAGAAGGTTATTTAGAATCAGCGGCAGCAGGCTTATTATGTGCCTTAAATGTCTATCAA TATGTAATGGATTTACCATTAATTAAATTTCCTTCAGAAACTATGCTAGGAGCATTAGTT AACTATGTTACAAATCCAAAACAACGAGATTTAAAACCGATGAAAGCAAATATTGGCATC GTGCCAACTTTAACAACTAAATTCAAAAGTAAAACAGAGAAAAATTTAGCAATTTATTCT CGAGCAATAAAAAAATTAAAAGAAACTATTAAAAAATATCAAATTAAATTATAA >protein sequence SKENAIGILKEELKLLDSLILKTAYDVQVPADDALSVDRELFSQKVTATLINHPNINIIY DEFIKIDPKQITIIAVGPLVTANFAFELKKLIGKKALYYYDGSAPIITKAGIDFSKAYYG ARHSEQKDYIICPLTEDEFNQLVTELVKAKRVPIADFEKYFKGCQPIEIMAQTSRKILLN GPMSSNHLIDKNGKQPFAVVQLRQDNVIDSLYNLVGWQTNLTWPEQKRIIKQFIPGLAKV DIVRYGVLHKNNYINSPKVLNQFLQYKQNNNIFFAGQIIGVEGYLESAAAGLLCALNVYQ YVMDLPLIKFPSETMLGALVNYVTNPKQRDLKPMKANIGIVPTLTTKFKSKTEKNLAIYS RAIKKLKETIKKYQIKL |
© Fisunov Lab of Proteomics, 2016.