tRNA guanosine-2'-O-methyltransferase (P0AGJ2)

Identification
Name:tRNA guanosine-2'-O-methyltransferase
Synonyms:
  • tRNA [Gm18] methyltransferase
Gene Name:trmH
Enzyme Class:
Biological Properties
General Function:Involved in tRNA (guanosine-2'-O-)-methyltransferase activity
Specific Function:Specifically methylates guanosine-18 in various tRNAs
Cellular Location:Cytoplasm (Potential)
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb
1.0S-Adenosylmethionine ↔ 1.0S-Adenosylhomocysteine
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00939S-AdenosylhomocysteineMetaboCard
GO Classification:
Function
binding
catalytic activity
methyltransferase activity
nucleic acid binding
RNA binding
RNA methyltransferase activity
transferase activity
transferase activity, transferring one-carbon groups
Process
cellular macromolecule metabolic process
macromolecule metabolic process
metabolic process
RNA metabolic process
RNA processing
Gene Properties
Blattner:b3651
Gene OrientationClockwise
Centisome Percentage:82.39
Left Sequence End3822538
Right Sequence End3823227
Gene Sequence:
>690 bp
ATGGCGAGACGTATTCTGGTCGTAGAAGATGAAGCTCCAATTCGCGAAATGGTCTGCTTC
GTGCTCGAACAAAATGGCTTTCAGCCGGTCGAAGCGGAAGATTATGACAGTGCTGTGAAT
CAACTGAATGAACCCTGGCCGGATTTAATTCTCCTCGACTGGATGTTACCTGGCGGCTCC
GGTATCCAGTTCATCAAACACCTCAAGCGCGAGTCGATGACCCGGGATATTCCAGTGGTG
ATGTTGACCGCCAGAGGGGAAGAAGAAGATCGCGTGCGCGGCCTTGAAACCGGCGCGGAT
GACTATATCACCAAGCCGTTTTCGCCGAAGGAGCTGGTGGCGCGAATCAAAGCGGTAATG
CGCCGTATTTCGCCAATGGCGGTGGAAGAGGTGATTGAGATGCAGGGATTAAGTCTCGAC
CCGACATCTCACCGAGTGATGGCGGGCGAAGAGCCGCTGGAGATGGGGCCGACAGAATTT
AAACTGCTGCACTTTTTTATGACGCATCCTGAGCGCGTGTACAGCCGCGAGCAGCTGTTA
AACCACGTCTGGGGAACTAACGTGTATGTGGAAGACCGCACGGTCGATGTCCACATTCGT
CGCCTGCGTAAAGCACTGGAGCCCGGCGGGCATGACCGCATGGTGCAGACCGTGCGCGGT
ACAGGATATCGTTTTTCAACCCGCTTTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:229
Protein Molecular Weight:25343
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>tRNA guanosine-2'-O-methyltransferase
MNPTRYARICEMLARRQPDLTVCMEQVHKPHNVSAIIRTADAVGVHEVHAVWPGSRMRTM
ASAAAGSNSWVQVKTHRTIGDAVAHLKGQGMQILATHLSDNAVDFREIDYTRPTCILMGQ
EKTGITQEALALADQDIIIPMIGMVQSLNVSVASALILYEAQRQRQNAGMYLRENSMLPE
AEQQRLLFEGGYPVLAKVAKRKGLPYPHVNQQGEIEADADWWATMQAAG
References
External Links:
ResourceLink
Uniprot ID:P0AGJ2
Uniprot Name:TRMH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674539
Ecogene ID:EG10967
Ecocyc:EG10967
ColiBase:b3651
Kegg Gene:b3651
EchoBASE ID:EB0960
CCDB:TRMH_ECOLI
BacMap:16131522
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Koonin, E. V., Rudd, K. E. (1993). "SpoU protein of Escherichia coli belongs to a new family of putative rRNA methylases." Nucleic Acids Res 21:5519. Pubmed: 8265370
  • Persson, B. C., Jager, G., Gustafsson, C. (1997). "The spoU gene of Escherichia coli, the fourth gene of the spoT operon, is essential for tRNA (Gm18) 2'-O-methyltransferase activity." Nucleic Acids Res 25:4093-4097. Pubmed: 9321663
  • Sarubbi, E., Rudd, K. E., Xiao, H., Ikehara, K., Kalman, M., Cashel, M. (1989). "Characterization of the spoT gene of Escherichia coli." J Biol Chem 264:15074-15082. Pubmed: 2549050
  • Xiao, H., Kalman, M., Ikehara, K., Zemel, S., Glaser, G., Cashel, M. (1991). "Residual guanosine 3',5'-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations." J Biol Chem 266:5980-5990. Pubmed: 2005134