ID   Y1951_THIDA             Reviewed;         362 AA.
AC   Q3SHI2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Probable RNA methyltransferase Tbd_1951;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=Tbd_1951;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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}.
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DR   EMBL; CP000116; AAZ97904.1; -; Genomic_DNA.
DR   RefSeq; WP_011312463.1; NC_007404.1.
DR   AlphaFoldDB; Q3SHI2; -.
DR   SMR; Q3SHI2; -.
DR   STRING; 292415.Tbd_1951; -.
DR   EnsemblBacteria; AAZ97904; AAZ97904; Tbd_1951.
DR   KEGG; tbd:Tbd_1951; -.
DR   eggNOG; COG0820; Bacteria.
DR   HOGENOM; CLU_029101_3_3_4; -.
DR   OMA; KVVFMGM; -.
DR   OrthoDB; 1111428at2; -.
DR   Proteomes; UP000008291; 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..362
FT                   /note="Probable RNA methyltransferase Tbd_1951"
FT                   /id="PRO_0000350506"
FT   DOMAIN          92..318
FT                   /note="Radical SAM core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT   REGION          342..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        89
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        323
FT                   /note="S-methylcysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="4Fe-4S-S-AdoMet"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..152
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..206
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   DISULFID        99..323
FT                   /note="(transient)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   362 AA;  39526 MW;  02B7FAFC053796A6 CRC64;
     MRLPELRQRL RDHGAAPCHA GRVLRAWVAG RPLDNRRQRA EDFLPLRLRN ALPGLFDELR
     NLAQVHSEHP GEDGSARLLV RLADGQTVES VLLPRDGVCV STQVGCAVGC VFCMTGRAGL
     LRQLSGAEIV AQVVLARSRR PVRKVVFMGM GEPAHNLDNV LDAIELLGLE GGIGHKNLVF
     STVGDRRVFE RLPQSTVKPA RALSLHTTDR ALRRRLLPRA PDIAPQELVE LGEAYARRTG
     YPIQYQWTLL EGINDTEAEL EGIARLLAGR YAVMNLIPYN ATEADGFNRP SWARAAEMAR
     RLHRRGVLAK LRHSAGQDVD GGCGQLRARA LDAAPVLARR PLPSAETPAA SPKAAASIGF
     PG