SPM_001070
  | Uniprot: A0A037UMP5
Description: ribosomal RNA large subunit methyltransferase N EC number: 2.1.1.192 Annotation score: 4 out of 5 Miscellaneous [CC]: MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue. {ECO:0000256|HAMAP-Rule:MF_01849}. Protein existence: Inferred from homology Catalytic activity: CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin. {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00536154}.; CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2 oxidized [2Fe-2S] ferredoxin. {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00536173}. Cofactor: Enzyme regulation: Function [CC]: FUNCTION: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. {ECO:0000256|SAAS:SAAS00536189}. Pathway: Active site: ACT_SITE 90 90 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_01849}.; ACT_SITE 332 332 S-methylcysteine intermediate. {ECO:0000256|HAMAP-Rule:MF_01849}. Binding site: BINDING 192 192 S-adenosyl-L-methionine. {ECO:0000256|HAMAP-Rule:MF_01849}.; BINDING 291 291 S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen. {ECO:0000256|HAMAP-Rule:MF_01849}. Calcium binding: DNA binding: Metal binding: METAL 110 110 Iron-sulfur (4Fe-4S-S-AdoMet). {ECO:0000256|HAMAP-Rule:MF_01849}.; METAL 114 114 Iron-sulfur (4Fe-4S-S-AdoMet). {ECO:0000256|HAMAP-Rule:MF_01849}.; METAL 117 117 Iron-sulfur (4Fe-4S-S-AdoMet). {ECO:0000256|HAMAP-Rule:MF_01849}. Nucleotide binding: Site: Gene names (primary): rlmN Gene names (synonym): Mass: 39,518 Subunit structure [CC]: Gene ontology (GO): cytoplasm [GO:0005737]; 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; rRNA (adenine-C2-)-methyltransferase activity [GO:0070040]; rRNA binding [GO:0019843]; tRNA (adenine-C2-)-methyltransferase activity [GO:0002935]; tRNA binding [GO:0000049]; rRNA base methylation [GO:0070475] Gene ontology IDs: GO:0000049; GO:0002935; GO:0005737; GO:0019843; GO:0046872; GO:0051539; GO:0070040; GO:0070475 Chain: Signal peptide: Domain [CC]: Sequence similarities: SIMILARITY: Belongs to the radical SAM superfamily. RlmN family. {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00571858}. Protein families: Radical SAM superfamily, RlmN family Coiled coil: Domain [FT]: DOMAIN 104 271 Radical_SAM. {ECO:0000259|Pfam:PF04055}. Motif: Region: REGION 160 161 S-adenosyl-L-methionine binding. {ECO:0000256|HAMAP-Rule:MF_01849}.; REGION 215 217 S-adenosyl-L-methionine binding. {ECO:0000256|HAMAP-Rule:MF_01849}. EMBL: AGBZ02000001 ProteinModelPortal: A0A037UMP5 MEROPS: EnsemblBacteria KO: KAI92662 UniPathway: CDD: Gene3D: HAMAP: 3.20.20.70 InterPro: MF_01849 PANTHER: IPR013785;IPR027492;IPR004383;IPR007197 PIRSF: PTHR30544 PRINTS: PIRSF006004 PROSITE: Pfam: ProDom: PF04055 SMART: SUPFAM: TIGRFAMs: |
190289-191327(-) >nucleotide sequence GTGACCAAATTCACGACGAACAATACAATTAATTTTTTGTTGTTGTAAAGTTTCAAAGAA TTGATTAATTTTAGTACTACGTTGATACCCATTTTCTGCAACTGTGTTATAAGGAATTAA ATTAACATACGCATTTAATCCTCGAATTAATTTTGCTAATTCTAATGCTGTTTCACGACT ATCATTAACATTCTCAATTAAAATATACTCAAAAGTAACACGTCGATTAGTTAACTCAAT ATAATAACGAACTGCATCCATTAATTTTTCTACTGGGTAAGCTTTATTAATTGGCATTAA TTGATTCCGAATCGTATTGTTTGGAGCATGTAATGAAATCGCTAAATTAACTTGCGTCTT TAACTCTGCAAATTGTTTAATTTTTGGAACTAACCCACAAGTAGAAATTGTAATATGGCG CGCACCAATTTGATAACCTTTTGGGTCATTAATAATGTTGACAAACTTAAGCGTATTATC AAAATTATCAAATGGTTCACCAATTCCCATTACTACAATATGACTCACACGTTCATTTGT TGTTGCTAGATAACGATTAACCATCATAACTTGTTGAACAATTTCTGCCGTTGATAAATT CCGTGTTTTTTTTAATAATCCTGAGGCACAAAAAGTACATGCCATATTACAACCAACTTG TGTTGTAACACAAACAGAATTACCATAACTTTGGGGCATTAAAACTGTTTCAATTTTATA GCCATCGGCTAATTGAAACAAAAACTTTACTGTTCCATCTTTCGACTGTTGTTGAACAAC AATTTTTAATGGCTCAATCGTATAATATTCTTGTAATTTATTACGATCAGTTTTAGAAAT ATTTGTCATTTCATCAAAAGAATATATGTTTTTGACATATATTCAATCAAAAATTTGCTC TGCTAAATATTTCTTAAAACCATGCGCAACTAAATCTAACTGTAATTCTTCTTTTGGATA TCCAAAAATTGATGTCAT >protein sequence IEPLKIVVQQQSKDGTVKFLFQLADGYKIETVLMPQSYGNSVCVTTQVGCNMACTFCASG LLKKTRNLSTAEIVQQVMMVNRYLATTNERVSHIVVMGIGEPFDNFDNTLKFVNIINDPK GYQIGARHITISTCGLVPKIKQFAELKTQVNLAISLHAPNNTIRNQLMPINKAYPVEKLM DAVRYYIELTNRRVTFEYILIENVNDSRETALELAKLIRGLNAYVNLIPYNTVAENGYQR STKINQFFETLQQQKINCIVRREFGHDIDAACGQLRAKNEGIIRK |
© Fisunov Lab of Proteomics, 2016.