ACL_RS04355
  | Uniprot: A9NGL4
Description: tRNA (adenosine(37)-N6)-dimethylallyltransferase MiaA EC number: 2.5.1.75 Annotation score: 3 out of 5 Miscellaneous [CC]: Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: Dimethylallyl diphosphate + adenine(37) in tRNA = diphosphate + N(6)-dimethylallyladenine(37) in tRNA. {ECO:0000255|HAMAP-Rule:MF_00185}. Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00185}; Enzyme regulation: Function [CC]: FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). {ECO:0000255|HAMAP-Rule:MF_00185}. Pathway: Active site: Binding site: Calcium binding: DNA binding: Metal binding: Nucleotide binding: NP_BIND 9 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00185}. Site: SITE 96 96 Interaction with substrate tRNA. {ECO:0000255|HAMAP-Rule:MF_00185}. Gene names (primary): miaA Gene names (synonym): Mass: 32,142 Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00185}. Gene ontology (GO): ATP binding [GO:0005524]; tRNA dimethylallyltransferase activity [GO:0052381]; tRNA processing [GO:0008033] Gene ontology IDs: GO:0005524; GO:0008033; GO:0052381 Chain: CHAIN 1 280 tRNA dimethylallyltransferase. /FTId=PRO_0000377042. Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the IPP transferase family. {ECO:0000255|HAMAP-Rule:MF_00185}. Protein families: IPP transferase family Coiled coil: Domain [FT]: Motif: Region: REGION 11 16 Substrate binding. {ECO:0000255|HAMAP-Rule:MF_00185}.; REGION 34 37 Interaction with substrate tRNA. {ECO:0000255|HAMAP-Rule:MF_00185}. EMBL: CP000896 ProteinModelPortal: A9NGL4 MEROPS: EnsemblBacteria KO: ABX81494 UniPathway: K00791 CDD: Gene3D: HAMAP: 3.40.50.300 InterPro: MF_00185 PANTHER: IPR018022;IPR027417 PIRSF: PRINTS: PROSITE: Pfam: ProDom: PF01715 SMART: SUPFAM: TIGRFAMs: SSF52540 |
909577-910420(-) >nucleotide sequence AGCATTATATACTTTAGGCTTCATTTGATTGATAAACCATGTTTTTTGTCTTTTAGCAAA TCTCATTGTTGCAGTAATAATCTTTTCTTTAGCAGTGTCTAAATCATTCATACCATTTAA ATAATCTTTGATTTCACGATAGCCTATAATATTTAAATCGTAGTTTATTAAAGCTTTAGT CTCTTCAATAAATCCCTTTTCAATCATGAGATCTAATCTAGTTTCTAATCTTTTTTTCAA GATTTTTCTATCCATATCCAAATAAATTAAATAGATGTCATAGAGTGGTTCGTTCTTTTT AGTTTTGTTACTTCGCTTTTGACCACTGATGATTGTTCTATATGCAGATTCTATACGTCT AGGATTATTTAGATCTATTTCAATATCCGGATCTGCTTTTCTAATAACTTCAATCATTTC ATTAATGTTTGGAAATTCAACGTTATCTTGTTGCTCAAATTCATAATTATAAAGCGCGGA CTTAACATATAAACCACTACCACCTACGATAAATGGTTTATCTATTTGATCAATTAGCGT GCGAACATCTTGTTGAAAATTATAAACTGTATAGGGTTCATCTAAGGCTACATGACTGAT TAAATGATGTTTTACACCATCCATTTCATCAGTTGTTATCTTAGCTGATCCAATATCTAG TTTCTTATAAATACTTACACTATCACCATTAATAATTTCAGCGCCTAATGATTTGGCAAG TTTTACAGATAATGCAGTCTTCCCACTACCTGTAGGTCCCACAATACAAACGACTTTTTT CAT >protein sequence LISHVALDEPYTVYNFQQDVRTLIDQIDKPFIVGGSGLYVKSALYNYEFEQQDNVEFPNI NEMIEVIRKADPDIEIDLNNPRRIESAYRTIISGQKRSNKTKKNEPLYDIYLIYLDMDRK ILKKRLETRLDLMIEKGFIEETKALINYDLNIIGYREIKDYLNGMNDLDTAKEKIITATM RFAKRQKTWFINQMKPKVYNALSPDLLDECLKDIKEFIGV |
© Fisunov Lab of Proteomics, 2016.