ID   A0A0M3AZW4_9SPHN        Unreviewed;       419 AA.
AC   A0A0M3AZW4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   16-MAR-2016, entry version 5.
DE   RecName: Full=Dual-specificity RNA methyltransferase RlmN {ECO:0000256|HAMAP-Rule:MF_01849};
DE            EC=2.1.1.192 {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=23S rRNA (adenine(2503)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=23S rRNA m2A2503 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=Ribosomal RNA large subunit methyltransferase N {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=tRNA (adenine(37)-C(2))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
DE   AltName: Full=tRNA m2A37 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849};
GN   Name=rlmN {ECO:0000256|HAMAP-Rule:MF_01849};
GN   ORFNames=YP76_00100 {ECO:0000313|EMBL:KKW94099.1};
OS   Sphingobium chungbukense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW94099.1, ECO:0000313|Proteomes:UP000033874};
RN   [1] {ECO:0000313|EMBL:KKW94099.1, ECO:0000313|Proteomes:UP000033874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ77 {ECO:0000313|EMBL:KKW94099.1,
RC   ECO:0000313|Proteomes:UP000033874};
RA   Kim Y.-C., Chae J.-C.;
RT   "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT   chungbukense DJ77.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates position 2 of adenine 2503 in
CC       23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503
CC       modification seems to play a crucial role in the proofreading step
CC       occurring at the peptidyl transferase center and thus would serve
CC       to optimize ribosomal fidelity. {ECO:0000256|HAMAP-Rule:MF_01849}.
CC   -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(2503) in
CC       23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-
CC       homocysteine + L-methionine + 5'-deoxyadenosine + 2-
CC       methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin.
CC       {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00181435}.
CC   -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + adenine(37) in
CC       tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine +
CC       L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2
CC       oxidized [2Fe-2S] ferredoxin. {ECO:0000256|HAMAP-Rule:MF_01849,
CC       ECO:0000256|SAAS:SAAS00181423}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01849,
CC         ECO:0000256|SAAS:SAAS00201826};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine.
CC       {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00201826};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
CC       ECO:0000256|SAAS:SAAS00297762}.
CC   -!- MISCELLANEOUS: Reaction proceeds by a ping-pong mechanism
CC       involving intermediate methylation of a conserved cysteine
CC       residue. {ECO:0000256|HAMAP-Rule:MF_01849}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
CC       {ECO:0000256|HAMAP-Rule:MF_01849}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKW94099.1}.
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DR   EMBL; LBIC01000001; KKW94099.1; -; Genomic_DNA.
DR   RefSeq; WP_046762530.1; NZ_LBIC01000001.1.
DR   Proteomes; UP000033874; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070040; F:rRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0002935; F:tRNA (adenine-C2-)-methyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0070475; P:rRNA base methylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01849; RNA_methyltr_RlmN; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR027492; RNA_MTrfase_RlmN.
DR   InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30544; PTHR30544; 2.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF006004; CHP00048; 1.
DR   TIGRFAMs; TIGR00048; rRNA_mod_RlmN; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00463035};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033874};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462865};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00463011};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00462960};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462907};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462842};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462825, ECO:0000313|EMBL:KKW94099.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033874};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00417446};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00462941};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00463018, ECO:0000313|EMBL:KKW94099.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00417452}.
FT   DOMAIN      139    330       Radical_SAM. {ECO:0000259|Pfam:PF04055}.
FT   REGION      216    217       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   REGION      270    272       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   ACT_SITE    124    124       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01849}.
FT   ACT_SITE    392    392       S-methylcysteine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       144    144       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       148    148       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       151    151       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     248    248       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     349    349       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   DISULFID    137    392       (transient). {ECO:0000256|HAMAP-Rule:
FT                                MF_01849}.
SQ   SEQUENCE   419 AA;  46382 MW;  6C8356BA65450E6C CRC64;
     MQTAANPLMP IPGLIDPVPV PRAVTPREDG RVDLMGLSRP QIKGVLEEAG LDQKQAKLRS
     KQLFHWLYHR GETDFDAMTD LAKPMRGWMA ERFVVGRPEV VEAQVSSDGT RKWLLRSDDG
     QDYEMVFIPD ADRGTLCVSS QVGCTLNCRF CHTGTMRLVR NLTPGEIVGQ VMLARDALGE
     WPKGSMASAN DDEADDASQY SPDGRMLTNI VMMGMGEPLY NFDHVRDALK VVMDGDGLAL
     SKRRITLSTS GVVPMMARAG EEIGVNLAVS LHAVTKDVRD ELVPLNKKYG IEQLLQACAD
     YPNANNARRI TFEYVMIKDK NDSDDDAREL VRLLRQYKLP AKVNLIPFNP WPGTDYECST
     PERIRAFSTI VFEGGISAPV RTPRGRDIMA ACGQLKSASE KKSRAELDRL AAEKQAALG
//