Tag | Content |
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CPLM ID | CPLM-011744 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | tRNA (guanine-N(7)-)-methyltransferase |
Protein Synonyms/Alias | Transfer RNA methyltransferase 8; tRNA (guanine(46)-N(7))-methyltransferase; tRNA(m7G46)-methyltransferase |
Gene Name | TRM8 |
Gene Synonyms/Alias | YDL201W; D1075 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
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32 | RKELKHVKINESSLV | acetylation | [1] | 149 | LRNNTASKHGFQNIN | acetylation | [1] |
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Reference | [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Methyltransferase that catalyzes the formation of N(7)- methylguanine at position 46 (m7G46) in tRNA, a modification required to maintain stability of tRNAs; its absence resulting in tRNA decay. Both the D-stem and T-stem structures of tRNAs are required for efficient methyltransferase activity. |
Sequence Annotation | REGION 126 127 S-adenosyl-L-methionine binding. REGION 161 162 S-adenosyl-L-methionine binding. REGION 259 261 S-adenosyl-L-methionine binding. ACT_SITE 184 184 Probable. BINDING 103 103 S-adenosyl-L-methionine; via carbonyl BINDING 181 181 S-adenosyl-L-methionine; via carbonyl MOD_RES 7 7 Phosphoserine; by ATM or ATR. MOD_RES 59 59 Phosphoserine. |
Keyword | 3D-structure; Complete proteome; Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 286 AA |
Protein Sequence | MKAKPLSQDP GSKRYAYRIN KEENRKELKH VKINESSLVQ EGQKIDLPKK RYYRQRAHSN 60 PFSDHQLEYP VSPQDMDWSK LYPYYKNAEN GQMTKKVTIA DIGCGFGGLM IDLSPAFPED 120 LILGMEIRVQ VTNYVEDRII ALRNNTASKH GFQNINVLRG NAMKFLPNFF EKGQLSKMFF 180 CFPDPHFKQR KHKARIITNT LLSEYAYVLK EGGVVYTITD VKDLHEWMVK HLEEHPLFER 240 LSKEWEENDE CVKIMRNATE EGKKVERKKG DKFVACFTRL PTPAIL 286 |
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