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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)

 A0A0M2EDP4_9BACI        Unreviewed;       360 AA.
A0A0M2EDP4;
11-NOV-2015, integrated into UniProtKB/TrEMBL.
11-NOV-2015, sequence version 1.
27-SEP-2017, entry version 16.
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=BSA145_15630 {ECO:0000313|EMBL:APT47166.1},
BSA171_11765 {ECO:0000313|EMBL:APT54218.1},
BSA41_05950 {ECO:0000313|EMBL:APT49505.1},
ER50_13685 {ECO:0000313|EMBL:KEP29569.1};
Bacillus safensis.
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=561879 {ECO:0000313|EMBL:KEP29569.1, ECO:0000313|Proteomes:UP000027852};
[1] {ECO:0000313|EMBL:KEP29569.1, ECO:0000313|Proteomes:UP000027852}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CFA06 {ECO:0000313|EMBL:KEP29569.1,
ECO:0000313|Proteomes:UP000027852};
Laborda P.R., Fonseca F.S., Angolini C.F., de Oliveira V.M.,
Marsaioli A.J., Souza A.P.;
"Genome sequence of Bacillus safensis CFA06, isolated from biodegraded
petroleum in Brazil.";
Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|Proteomes:UP000185426, ECO:0000313|Proteomes:UP000185451, ECO:0000313|Proteomes:UP000185476}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=U14-5 {ECO:0000313|EMBL:APT47166.1,
ECO:0000313|Proteomes:UP000185426},
U17-1 {ECO:0000313|EMBL:APT54218.1,
ECO:0000313|Proteomes:UP000185476}, and
U41 {ECO:0000313|EMBL:APT49505.1, ECO:0000313|Proteomes:UP000185451};
Fomenkov A., Akimov V.N., Vasilyeva L.V., Andersen D., Vincze T.,
Roberts R.J.;
"Complete Genome and Methylome Analysis of Psychrotrophic Bacterial
Isolates from Antarctic Lake Untersee.";
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
-!- 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}.
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EMBL; CP015607; APT47166.1; -; Genomic_DNA.
EMBL; CP015610; APT49505.1; -; Genomic_DNA.
EMBL; CP015611; APT54218.1; -; Genomic_DNA.
EMBL; JNBO01000042; KEP29569.1; -; Genomic_DNA.
RefSeq; WP_024424208.1; NZ_MKXN01000001.1.
EnsemblBacteria; KEP29569; KEP29569; ER50_13685.
PATRIC; fig|561879.6.peg.168; -.
Proteomes; UP000027852; Unassembled WGS sequence.
Proteomes; UP000185426; Chromosome.
Proteomes; UP000185451; Chromosome.
Proteomes; UP000185476; Chromosome.
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.
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:UP000027852,
ECO:0000313|Proteomes:UP000185426, ECO:0000313|Proteomes:UP000185451,
ECO:0000313|Proteomes:UP000185476};
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:KEP29569.1};
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:KEP29569.1};
tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
ECO:0000256|SAAS:SAAS00721837}.
DOMAIN 117 287 Radical_SAM. {ECO:0000259|Pfam:PF04055}.
REGION 173 174 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_01849}.
REGION 228 230 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_01849}.
ACT_SITE 103 103 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01849}.
ACT_SITE 347 347 S-methylcysteine intermediate.
{ECO:0000256|HAMAP-Rule:MF_01849}.
METAL 123 123 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01849}.
METAL 127 127 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01849}.
METAL 130 130 Iron-sulfur (4Fe-4S-S-AdoMet).
{ECO:0000256|HAMAP-Rule:MF_01849}.
BINDING 205 205 S-adenosyl-L-methionine.
{ECO:0000256|HAMAP-Rule:MF_01849}.
BINDING 304 304 S-adenosyl-L-methionine; via amide
nitrogen and carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01849}.
SEQUENCE 360 AA; 41416 MW; 0E121A8FB2E27942 CRC64;
MTEQKVRKEL KTEMPSIYSF ELHEMKEWLK EQGEKPFRAA QIFEWLYEKR VTSFDDMSNL
SKDLREKLKN QFAITTLKTV IKQTSQDGTI KFLFELHDGY TIETVLMRHE YGNSVCVTTQ
VGCRIGCTFC ASTLGGLKRN LEAGEIVAQV LKVQQALDET DERVSSVVIM GIGEPFDNFD
EMLAFLKIIN HDNGLNIGAR HITVSTSGII PKIYQFADEQ MQINFAVSLH APNTEIRSRL
MPINKAYKLP KLMEAIEYYI QKTGRRVSFE YGLFGGVNDQ VHHAEELADL LKGIKCHVNL
IPVNYVPERD YVRTPREQIF LFEKTLKERG VNVTIRREQG HDIDAACGQL RAKERQEETR


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