Release factor glutamine methyltransferase
Details
- Name
- Release factor glutamine methyltransferase
- Synonyms
- 2.1.1.297
- N5-glutamine methyltransferase PrmC
- Protein-(glutamine-N5) MTase PrmC
- Protein-glutamine N-methyltransferase PrmC
- RF MTase
- Gene Name
- prmC
- Organism
- Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
- Amino acid sequence
>lcl|BSEQ0011793|Release factor glutamine methyltransferase MDTRKNVSGAERKIWSLIRDCSGKLEGVTETSVLEVLLIVSRVLGIRKEDLFLKDLGVSP TEEKRILELVEKRASGYPLHYILGEKEFMGLSFLVEEGVFVPRPETEELVELALELIRKY GIKTVADIGTGSGAIGVSVAKFSDAIVFATDVSSKAVEIARKNAERHGVSDRFFVRKGEF LEPFKEKFASIEMILSNPPYVKSSAHLPKDVLFEPPEALFGGEDGLDFYREFFGRYDTSG KIVLMEIGEDQVEELKKIVSDTVFLKDSAGKYRFLLLNRRSS
- Number of residues
- 282
- Molecular Weight
- 31609.085
- Theoretical pI
- 5.19
- GO Classification
- Functionsnucleic acid binding / protein-glutamine N-methyltransferase activityProcessespeptidyl-glutamine methylation
- General Function
- Protein-glutamine n-methyltransferase activity
- Specific Function
- Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
- Pfam Domain Function
- MTS (PF05175)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0011794|Release factor glutamine methyltransferase (prmC) ATGGACACCAGAAAGAATGTCTCCGGAGCTGAGAGAAAAATTTGGAGTCTGATAAGAGAC TGCTCTGGAAAACTCGAGGGAGTGACCGAAACTTCTGTTCTTGAGGTGTTACTCATCGTT TCCCGGGTGCTTGGGATCCGCAAGGAAGATCTCTTTTTGAAAGACCTGGGAGTTTCTCCA ACTGAGGAAAAAAGGATTCTGGAACTCGTGGAGAAAAGAGCAAGTGGATATCCCCTGCAC TATATCCTCGGTGAGAAAGAGTTCATGGGCCTTTCTTTCCTCGTGGAAGAAGGCGTTTTT GTTCCAAGGCCGGAGACGGAGGAACTGGTCGAACTCGCCCTCGAGCTGATAAGAAAGTAC GGAATAAAGACAGTCGCAGACATAGGAACAGGAAGCGGAGCCATTGGAGTGAGCGTTGCG AAGTTCTCCGATGCGATCGTTTTCGCGACGGACGTTTCTTCCAAAGCCGTTGAAATCGCC AGAAAAAACGCGGAAAGACACGGTGTTTCCGACAGATTCTTTGTGAGAAAAGGTGAGTTT CTTGAACCGTTCAAAGAAAAATTCGCATCGATCGAGATGATCCTTTCGAATCCTCCATAC GTGAAATCGAGTGCTCATCTGCCAAAAGATGTTCTTTTCGAGCCTCCAGAGGCACTTTTT GGAGGAGAGGACGGTCTTGACTTTTACAGAGAATTTTTCGGCAGGTACGATACGAGCGGA AAGATTGTGCTGATGGAGATAGGAGAAGACCAGGTGGAGGAGTTGAAAAAGATCGTTTCC GACACTGTTTTCCTGAAGGATTCCGCCGGAAAGTACCGTTTTCTCCTTCTCAACCGGCGT TCCTCTTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q9WYV8 UniProtKB Entry Name PRMC_THEMA GenBank Gene ID AE000512 - General References
- Nelson KE, Clayton RA, Gill SR, Gwinn ML, Dodson RJ, Haft DH, Hickey EK, Peterson JD, Nelson WC, Ketchum KA, McDonald L, Utterback TR, Malek JA, Linher KD, Garrett MM, Stewart AM, Cotton MD, Pratt MS, Phillips CA, Richardson D, Heidelberg J, Sutton GG, Fleischmann RD, Eisen JA, White O, Salzberg SL, Smith HO, Venter JC, Fraser CM: Evidence for lateral gene transfer between Archaea and bacteria from genome sequence of Thermotoga maritima. Nature. 1999 May 27;399(6734):323-9. [Article]
- Yoon HJ, Kang KY, Ahn HJ, Shim SM, Ha JY, Lee SK, Mikami B, Suh SW: X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase. Mol Cells. 2003 Oct 31;16(2):266-9. [Article]
- Schubert HL, Phillips JD, Hill CP: Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase. Biochemistry. 2003 May 20;42(19):5592-9. [Article]
- Agarwal R, Burley SK, Swaminathan S: A novel mode of dimerization via formation of a glutamate anhydride crosslink in a protein crystal structure. Proteins. 2008 May 1;71(2):1038-41. doi: 10.1002/prot.21962. [Article]