ID   Y3613_METPP             Reviewed;         352 AA.
AC   A2SLX7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Probable RNA methyltransferase Mpe_A3613;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=Mpe_A3613;
OS   Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX   NCBI_TaxID=420662;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX   PubMed=17158667; DOI=10.1128/jb.01259-06;
RA   Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA   Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA   Hristova K.R.;
RT   "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT   proteobacterium Methylibium petroleiphilum PM1.";
RL   J. Bacteriol. 189:1931-1945(2007).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3
CC       cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. RlmN family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000555; ABM96566.1; -; Genomic_DNA.
DR   RefSeq; WP_011831186.1; NC_008825.1.
DR   AlphaFoldDB; A2SLX7; -.
DR   SMR; A2SLX7; -.
DR   STRING; 420662.Mpe_A3613; -.
DR   EnsemblBacteria; ABM96566; ABM96566; Mpe_A3613.
DR   KEGG; mpt:Mpe_A3613; -.
DR   eggNOG; COG0820; Bacteria.
DR   HOGENOM; CLU_029101_3_3_4; -.
DR   OMA; KVVFMGM; -.
DR   OrthoDB; 1111428at2; -.
DR   Proteomes; UP000000366; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR040072; Methyltransferase_A.
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   PROSITE; PS51918; RADICAL_SAM; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Cytoplasm; Disulfide bond; Iron; Iron-sulfur; Metal-binding;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..352
FT                   /note="Probable RNA methyltransferase Mpe_A3613"
FT                   /id="PRO_0000350251"
FT   DOMAIN          91..317
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   ACT_SITE        88
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        322
FT                   /note="S-methylcysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..151
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         203..205
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   DISULFID        98..322
FT                   /note="(transient)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   352 AA;  38011 MW;  6187299708F3F596 CRC64;
     MRIEQLREHL RALGARPGHE QSVLRHWACA LPQQRRSARE DVLPLALREA LPALEAELQG
     LARLRSEHSA EDGSARLLVA LADGQTVESV LLPRDGLCVS TQVGCAVGCV FCMTGQGGLL
     RQLGSAEIVA QVALARGHRA VKKVVFMGMG EPAHNLDNVL EAIELLGTAG GIGHKNLVFS
     TVGDERVFER LPQGAVKPAL ALSLHTTKPE LRAQLLPRAP RIAPEDLVAH GERYARATGY
     PVQYQWTLID GVNDGDDELD GIVRLLAGRY AVMNLIPYNT VDGLAFQRPA WERAVAMAGA
     LHRRGVLTKL RRSAGQDVEG GCGQLRARAL GGARWIKIEP VSGTGAHHVD QF