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
TTATTTTCTAATAATCCCTTCATTTTTAGCTCGTAATTGACCGCAAGCAGCATCAATATC
GTGACCAAATTCACGACGAACAATACAATTAATTTTTTGTTGTTGTAAAGTTTCAAAGAA
TTGATTAATTTTAGTACTACGTTGATACCCATTTTCTGCAACTGTGTTATAAGGAATTAA
ATTAACATACGCATTTAATCCTCGAATTAATTTTGCTAATTCTAATGCTGTTTCACGACT
ATCATTAACATTCTCAATTAAAATATACTCAAAAGTAACACGTCGATTAGTTAACTCAAT
ATAATAACGAACTGCATCCATTAATTTTTCTACTGGGTAAGCTTTATTAATTGGCATTAA
TTGATTCCGAATCGTATTGTTTGGAGCATGTAATGAAATCGCTAAATTAACTTGCGTCTT
TAACTCTGCAAATTGTTTAATTTTTGGAACTAACCCACAAGTAGAAATTGTAATATGGCG
CGCACCAATTTGATAACCTTTTGGGTCATTAATAATGTTGACAAACTTAAGCGTATTATC
AAAATTATCAAATGGTTCACCAATTCCCATTACTACAATATGACTCACACGTTCATTTGT
TGTTGCTAGATAACGATTAACCATCATAACTTGTTGAACAATTTCTGCCGTTGATAAATT
CCGTGTTTTTTTTAATAATCCTGAGGCACAAAAAGTACATGCCATATTACAACCAACTTG
TGTTGTAACACAAACAGAATTACCATAACTTTGGGGCATTAAAACTGTTTCAATTTTATA
GCCATCGGCTAATTGAAACAAAAACTTTACTGTTCCATCTTTCGACTGTTGTTGAACAAC
AATTTTTAATGGCTCAATCGTATAATATTCTTGTAATTTATTACGATCAGTTTTAGAAAT
ATTTGTCATTTCATCAAAAGAATATATGTTTTTGACATATATTCAATCAAAAATTTGCTC
TGCTAAATATTTCTTAAAACCATGCGCAACTAAATCTAACTGTAATTCTTCTTTTGGATA
TCCAAAAATTGATGTCAT


>protein sequence
MTSIFGYPKEELQLDLVAHGFKKYLAEQIFDWIYVKNIYSFDEMTNISKTDRNKLQEYYT
IEPLKIVVQQQSKDGTVKFLFQLADGYKIETVLMPQSYGNSVCVTTQVGCNMACTFCASG
LLKKTRNLSTAEIVQQVMMVNRYLATTNERVSHIVVMGIGEPFDNFDNTLKFVNIINDPK
GYQIGARHITISTCGLVPKIKQFAELKTQVNLAISLHAPNNTIRNQLMPINKAYPVEKLM
DAVRYYIELTNRRVTFEYILIENVNDSRETALELAKLIRGLNAYVNLIPYNTVAENGYQR
STKINQFFETLQQQKINCIVRREFGHDIDAACGQLRAKNEGIIRK






















© Fisunov Lab of Proteomics, 2016.