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Probable dual-specificity RNA methyltransferase RlmN (EC 2.1.1.192) (23S rRNA (adenine(2503)-C(2))-methyltransferase) (23S rRNA m2A2503 methyltransferase) (Ribosomal RNA large subunit methyltransferase N) (tRNA (adenine(37)-C(2))-methyltransferase) (tRNA m2A37 methyltransferase)

 W7RBR5_9FLAO            Unreviewed;       347 AA.
W7RBR5;
16-APR-2014, integrated into UniProtKB/TrEMBL.
16-APR-2014, sequence version 1.
25-OCT-2017, entry version 28.
RecName: Full=Probable dual-specificity RNA methyltransferase RlmN {ECO:0000256|HAMAP-Rule:MF_01849};
EC=2.1.1.192 {ECO:0000256|HAMAP-Rule:MF_01849};
AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000256|HAMAP-Rule:MF_01849};
AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
AltName: Full=tRNA m2A37 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
Name=rlmN {ECO:0000256|HAMAP-Rule:MF_01849};
ORFNames=KLA_01210 {ECO:0000313|EMBL:EWH15135.1};
Cellulophaga geojensis KL-A.
Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
Flavobacteriaceae; Cellulophaga.
NCBI_TaxID=1328323 {ECO:0000313|EMBL:EWH15135.1, ECO:0000313|Proteomes:UP000019275};
[1] {ECO:0000313|EMBL:EWH15135.1, ECO:0000313|Proteomes:UP000019275}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=KL-A {ECO:0000313|EMBL:EWH15135.1,
ECO:0000313|Proteomes:UP000019275};
PubMed=24604651;
Shan D., Ying J., Li X., Gao Z., Wei G., Shao Z.;
"Draft Genome Sequence of the Carrageenan-Degrading Bacterium
Cellulophaga sp. Strain KL-A, Isolated from Decaying Marine Algae.";
Genome Announc. 2:e00145-14(2014).
-!- FUNCTION: Specifically methylates position 2 of adenine 2503 in
23S rRNA and position 2 of adenine 37 in tRNAs.
{ECO:0000256|SAAS:SAAS00721833}.
-!- 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:SAAS00721810}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00385725}.
-!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism
involving intermediate methylation of a conserved cysteine
residue. {ECO:0000256|HAMAP-Rule:MF_01849}.
-!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
{ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00571858}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01849}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EWH15135.1}.
-----------------------------------------------------------------------
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EMBL; ARZX01000001; EWH15135.1; -; Genomic_DNA.
RefSeq; WP_034643018.1; NZ_ARZX01000001.1.
ProteinModelPortal; W7RBR5; -.
EnsemblBacteria; EWH15135; EWH15135; KLA_01210.
PATRIC; fig|1328323.3.peg.244; -.
Proteomes; UP000019275; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-UniRule.
Gene3D; 3.20.20.70; -; 1.
HAMAP; MF_01849; RNA_methyltr_RlmN; 1.
InterPro; IPR013785; Aldolase_TIM.
InterPro; IPR027492; RNA_MTrfase_RlmN.
InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
InterPro; IPR007197; rSAM.
PANTHER; PTHR30544; PTHR30544; 1.
Pfam; PF04055; Radical_SAM; 1.
PIRSF; PIRSF006004; CHP00048; 1.
SFLD; SFLDF00275; adenosine_C2_methyltransferase; 1.
SFLD; SFLDS00029; Radical_SAM; 1.
TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00463035};
Complete proteome {ECO:0000313|Proteomes:UP000019275};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00462865};
Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00721829};
Iron {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00463035};
Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00463035};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00463035};
Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00462825, ECO:0000313|EMBL:EWH15135.1};
rRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00536180};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00462941};
Transferase {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00462825, ECO:0000313|EMBL:EWH15135.1};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00721837}.
DOMAIN 110 275 Radical_SAM. {ECO:0000259|Pfam:PF04055}.
REGION 166 167 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_01849}.
REGION 221 223 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_01849}.
ACT_SITE 95 95 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01849}.
ACT_SITE 340 340 S-methylcysteine intermediate.
{ECO:0000256|HAMAP-Rule:MF_01849}.
METAL 115 115 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01849}.
METAL 119 119 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01849}.
METAL 122 122 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01849}.
BINDING 198 198 S-adenosyl-L-methionine.
{ECO:0000256|HAMAP-Rule:MF_01849}.
BINDING 297 297 S-adenosyl-L-methionine; via amide
nitrogen and carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01849}.
SEQUENCE 347 AA; 39356 MW; 9C9678A90CCDF9C3 CRC64;
MEKNKKKDIR ALTKEQIRAF FVAQGDKAFR GNQVYEWLWQ KGAHSFEAMT NVSKETRQLL
DDNFVINHIK VDQMQRSSDG TIKNAVQLHD GLIVESVLIP TKTRTTACVS SQVGCSLDCR
FCATSRLKRM RNLNPDEIYD QVVAIDNESR LYFDRKLSNI VFMGMGEPLM NYNNVLKAID
KITSTEGLAM SPKRITVSTS GVPKMIKKMA DDEVKFKLAV SLHSAVDEIR TSIMPFNATF
PLKDLREALQ YWYAKTKSRI TYEYVVWDGI NDTQNDANAL VDFCRFAPSK VNLIEYNPID
DGEFQQASNK AIDMYVATLE RNGITVTVRR SRGKDIDAAC GQLANKS


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