GCW_00985







Uniprot: A0A0F6CK59
Description: tRNA dimethylallyltransferase
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:0000256|HAMAP-Rule:MF_00185}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_00185}.
Pathway: 
Active site: 
Binding site: 
Calcium binding: 
DNA binding: 
Metal binding: 
Nucleotide binding: NP_BIND 12 19 ATP. {ECO:0000256|HAMAP-Rule:MF_00185}.
Site: SITE 100 100 Interaction with substrate tRNA. {ECO:0000256|HAMAP-Rule:MF_00185}.
Gene names (primary): miaA
Gene names (synonym): 
Mass: 36,193
Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000256|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: 
Signal peptide: 
Domain [CC]: 
Sequence similarities: SIMILARITY: Belongs to the IPP transferase family. {ECO:0000256|HAMAP-Rule:MF_00185}.
Protein families: IPP transferase family
Coiled coil: 
Domain [FT]: DOMAIN 5 201 Guanylate kinase-like. {ECO:0000259|PROSITE:PS50052}.
Motif: 
Region: 
EMBL: CP006916
ProteinModelPortal: A0A0F6CK59
MEROPS: 
EnsemblBacteria KO: AHB99481
UniPathway: K00791
CDD: 
Gene3D: 
HAMAP: 3.40.50.300
InterPro: MF_00185
PANTHER: IPR008144;IPR018022;IPR027417
PIRSF: 
PRINTS: 
PROSITE: 
Pfam: PS50052
ProDom: PF01715
SMART: 
SUPFAM: 
TIGRFAMs: SSF52540
211416-212337(+)

>nucleotide sequence
ATGATTTATTCAAAACGATTAATTTTAGTTGTAGGTCCTACCGGAACTAAAAAATCATAT
TTAGCAAACATGTTGGCCAAGAAATTAAATGTGCCAATAATTTCTGCTGATGCTTATCAG
GTTTACAAGGAGTTAAACGCTGGAGTGAATAAACCATCAGAAAAAACATTATCAGAGATT
AAATATCATTTCATATCCAATATTTCGATTTTTGATGAATGATCAATTGCACACTTTAAC
AAAAGAGCCAAAGAAATTTTAGAACAAGCTCCTGATTGAACAATTGTGTGTGGAGGTAGT
CATCTTTATGTTAATAGTTTGATAAACGATTATCAGTTAGAAAAACAAGAGCTAGATACT
GACTTGTTTGATGCACTAGATAAATTAGATAATCAAGAGATCTTTAATCAATTATGTGAA
TACGATTTTCAAGAAGCAATTAAGATTGGTAAAAACAATCGAAAAAGATTATTACGAGCG
TTATATTTGTTTAAAAAATACGGTAAAAAAGCGAAAAATGATAGTAAAAAATTTGATTAC
GTAGTAGTTAAATGTATGTCAGATAAAGAAAAACTTTTTCCTTATTTAAGTAAGCGTTTA
GACGAAATGATTCACGACTTAAATTGAACTAAAGAAATTGAGTATCTGGATAAGATAATT
ACTGATAAGAAACTAGATAAAGAACTGATTGCAATGAAGGCGCTAGGCTATAAAGAAATT
TATGATGCCTGAAAAAATAACCAACCCATTGATAAAGAGATAATTAACAAGAAATTCAAA
AGACTAGTAAAACATCAATTAACTTGAACTAGGAATAAATTTAACGATGGTATGAAGCAG
TTTACTTTTAATTTCTTTGAAGACGATGCAAACAGAACTTGTGATGAAATAATTGAATAC
ATAAAAAGCAACCATGACTAA


>protein sequence
MIYSKRLILVVGPTGTKKSYLANMLAKKLNVPIISADAYQVYKELNAGVNKPSEKTLSEI
KYHFISNISIFDEWSIAHFNKRAKEILEQAPDWTIVCGGSHLYVNSLINDYQLEKQELDT
DLFDALDKLDNQEIFNQLCEYDFQEAIKIGKNNRKRLLRALYLFKKYGKKAKNDSKKFDY
VVVKCMSDKEKLFPYLSKRLDEMIHDLNWTKEIEYLDKIITDKKLDKELIAMKALGYKEI
YDAWKNNQPIDKEIINKKFKRLVKHQLTWTRNKFNDGMKQFTFNFFEDDANRTCDEIIEY
IKSNHD






















© Fisunov Lab of Proteomics, 2016.