Tag | Content |
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CPLM ID | CPLM-006699 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 23S rRNA (guanine(745)-N(1))-methyltransferase |
Protein Synonyms/Alias | 23S rRNA m1G745 methyltransferase; Ribosomal RNA large subunit methyltransferase A |
Gene Name | rlmA |
Gene Synonyms/Alias | rrmA; yebH; b1822; JW1811 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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31 | RHQFDMAKEGYVNLL | acetylation | [1] | 43 | NLLPVQHKRSRDPGD | acetylation | [1] | 160 | IRIYAPCKAEELARV | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Specifically methylates the guanosine in position 745 of 23S rRNA. |
Sequence Annotation | REGION 96 97 S-adenosyl-L-methionine binding. METAL 5 5 Zinc. METAL 8 8 Zinc. METAL 21 21 Zinc. METAL 25 25 Zinc. BINDING 67 67 S-adenosyl-L-methionine. BINDING 183 183 S-adenosyl-L-methionine. |
Keyword | 3D-structure; Complete proteome; Metal-binding; Methyltransferase; Reference proteome; rRNA processing; S-adenosyl-L-methionine; Transferase; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 269 AA |
Protein Sequence | MSFSCPLCHQ PLSREKNSYI CPQRHQFDMA KEGYVNLLPV QHKRSRDPGD SAEMMQARRA 60 FLDAGHYQPL RDAIVAQLRE RLDDKATAVL DIGCGEGYYT HAFADALPEI TTFGLDVSKV 120 AIKAAAKRYP QVTFCVASSH RLPFSDTSMD AIIRIYAPCK AEELARVVKP GGWVITATPG 180 PRHLMELKGL IYNEVHLHAP HAEQLEGFTL QQSAELCYPM RLRGDEAVAL LQMTPFAWRA 240 KPEVWQTLAA KEVFDCQTDF NIHLWQRSY 269 |
Gene Ontology | GO:0052911; F:23S rRNA (guanine(745)-N(1))-methyltransferase activity; IEA:EC. GO:0008989; F:rRNA (guanine-N1-)-methyltransferase activity; IDA:EcoCyc. GO:0008270; F:zinc ion binding; IDA:EcoCyc. GO:0070475; P:rRNA base methylation; IMP:EcoCyc. |
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