ID   A0A4R5LIY8_9BURK        Unreviewed;       387 AA.
AC   A0A4R5LIY8;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-SEP-2019, entry version 2.
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   ECO:0000313|EMBL:TDG09509.1};
GN   ORFNames=E1N52_06910 {ECO:0000313|EMBL:TDG09509.1};
OS   Paraburkholderia sp. CNPSo 3008.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2546446 {ECO:0000313|EMBL:TDG09509.1, ECO:0000313|Proteomes:UP000295606};
RN   [1] {ECO:0000313|EMBL:TDG09509.1, ECO:0000313|Proteomes:UP000295606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNPSo 3008 {ECO:0000313|EMBL:TDG09509.1,
RC   ECO:0000313|Proteomes:UP000295606};
RA   Paulitsch F., Hungria M., Delamuta J.R.M., Ribeiro R.A.,
RA   Dall'Agnol R., Silva J.S.B.;
RT   "Paraburkholderia sp. isolated from native Mimosa gymnas in Guartela
RT   State Park, Brazil.";
RL   Submitted (MAR-2019) 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:
CC       Reaction=adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-
CC         [ferredoxin] + 2 S-adenosyl-L-methionine = 2-
CC         methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-
CC         methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:42916, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10152, Rhea:RHEA-
CC         COMP:10282, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74497;
CC         EC=2.1.1.192; Evidence={ECO:0000256|HAMAP-Rule:MF_01849,
CC         ECO:0000256|SAAS:SAAS01114928};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] +
CC         2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-
CC         deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43332, Rhea:RHEA-
CC         COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10162,
CC         Rhea:RHEA-COMP:10485, ChEBI:CHEBI:17319, ChEBI:CHEBI:33737,
CC         ChEBI:CHEBI:33738, ChEBI:CHEBI:57844, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74497;
CC         EC=2.1.1.192; Evidence={ECO:0000256|HAMAP-Rule:MF_01849,
CC         ECO:0000256|SAAS:SAAS01114934};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01849};
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};
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, ECO:0000256|SAAS:SAAS00571858}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {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:TDG09509.1}.
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DR   EMBL; SMOD01000004; TDG09509.1; -; Genomic_DNA.
DR   Proteomes; UP000295606; Unassembled WGS sequence.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01849; RNA_methyltr_RlmN; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR040072; Methyltransferase_A.
DR   InterPro; IPR027492; RNA_MTrfase_RlmN.
DR   InterPro; IPR004383; rRNA_lsu_MTrfase_RlmN/Cfr.
DR   InterPro; IPR007197; rSAM.
DR   PANTHER; PTHR30544; PTHR30544; 1.
DR   Pfam; PF04055; Radical_SAM; 1.
DR   PIRSF; PIRSF006004; CHP00048; 1.
DR   SFLD; SFLDF00275; adenosine_C2_methyltransferase; 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:SAAS00297782};
KW   Complete proteome {ECO:0000313|Proteomes:UP000295606};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297764};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00721829};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01849, ECO:0000256|SAAS:SAAS00297790};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297787};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297793};
KW   Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297761, ECO:0000313|EMBL:TDG09509.1};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00536180};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297766};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00297763, ECO:0000313|EMBL:TDG09509.1};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01849,
KW   ECO:0000256|SAAS:SAAS00721837}.
FT   DOMAIN      110    294       Radical_SAM. {ECO:0000259|Pfam:PF04055}.
FT   REGION      181    182       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   REGION      235    237       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   ACT_SITE     95     95       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01849}.
FT   ACT_SITE    355    355       S-methylcysteine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       115    115       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       119    119       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   METAL       122    122       Iron-sulfur (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     213    213       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
FT   BINDING     312    312       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01849}.
SQ   SEQUENCE   387 AA;  42327 MW;  B02DE84C3A26A507 CRC64;
     MTSSSTVNLL DLDAQGLVAY CESLGEKPFR AKQLQRWIHQ YNAADFDGMT DLAKSLREKL
     KGRATIGMPG IISDNVSSDG TRKWLVDVGN GNAVETVFIP EDNRGTLCVS SQAGCAVNCR
     FCSTGKQGFS RNLTTAEIIG QLRMAEFALR ASLLGEAGGR ATGGDGKGER VITNVVMMGM
     GEPLLNYDAV VPAMRLMLDD NAYGLSRRRV TLSTSGVVPM MDRLGAELPV ALAVSLHAPN
     DALRDELVPL NRKYPLRELM AACQRYLEVA PRDFITFEYC MLDGVNDTEE HARQLLAVTR
     DVPCKFNLIP FNPFPESGLL RSKSDQIKRF AQILMDAGVV TTVRKTRGDD IDAACGQLAG
     EVKDRTRLAE RMGRAPGKVI EVRPVQH
//