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Database: UniProt
Entry: Q1LHE2_CUPMC
LinkDB: Q1LHE2_CUPMC
Original site: Q1LHE2_CUPMC 
ID   Q1LHE2_CUPMC            Unreviewed;       457 AA.
AC   Q1LHE2;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   SubName: Full=tRNA and rRNA cytosine-C5-methylase (Sun protein) {ECO:0000313|EMBL:ABF10434.1};
DE            EC=2.1.1.61 {ECO:0000313|EMBL:ABF10434.1};
GN   Name=sun {ECO:0000313|EMBL:ABF10434.1};
GN   OrderedLocusNames=Rmet_3562 {ECO:0000313|EMBL:ABF10434.1};
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF10434.1, ECO:0000313|Proteomes:UP000002429};
RN   [1] {ECO:0000313|Proteomes:UP000002429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC   {ECO:0000313|Proteomes:UP000002429};
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. RsmB/NOP family. {ECO:0000256|ARBA:ARBA00007494,
CC       ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CP000352; ABF10434.1; -; Genomic_DNA.
DR   RefSeq; WP_011517978.1; NC_007973.1.
DR   AlphaFoldDB; Q1LHE2; -.
DR   STRING; 266264.Rmet_3562; -.
DR   KEGG; rme:Rmet_3562; -.
DR   eggNOG; COG0144; Bacteria.
DR   HOGENOM; CLU_005316_0_4_4; -.
DR   Proteomes; UP000002429; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0004808; F:tRNA (5-methylaminomethyl-2-thiouridylate)(34)-methyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.10.287.730; Helix hairpin bin; 1.
DR   Gene3D; 1.10.940.10; NusB-like; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR035926; NusB-like_sf.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR004573; rRNA_ssu_MeTfrase_B.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00563; rsmB; 1.
DR   PANTHER; PTHR22807:SF61; NOL1_NOP2_SUN FAMILY PROTEIN _ ANTITERMINATION NUSB DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF48013; NusB-like; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
DR   PROSITE; PS51686; SAM_MT_RSMB_NOP; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}; Reference proteome {ECO:0000313|Proteomes:UP000002429};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU01023};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|PROSITE-ProRule:PRU01023};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW   ProRule:PRU01023}.
FT   DOMAIN          183..456
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   ACT_SITE        391
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         271..277
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         293
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         319
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         338
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   457 AA;  49733 MW;  0681E8E28708D1CF CRC64;
     MRLPPDSLAF QMLGAAAAVR GVHEGTALPQ AIEDATNLLR LDRVRDAATR GAIQDLAYRT
     VRQFGATRAL VTQLVTRPPG ALVDSLLAVA LALLLEGEEG DRSKVGRGGY SDFTVVDQAV
     SAAASEPKTA HARGLVNAVL RRFLRERKAL MDAIAKDEEA RWNLPTWWLE QLRAAYPDRW
     MALAESVNVR PPMTLRVNTK RLSVDEYLKE LANAGMAGTA IGPQAVRLVR AFPVSQVPGF
     ATGDVSVQDA GAQLAAPLCE VADGMRVLDA CAAPGGKTGH LLELADIHVT AVESDAERAA
     RIHENLARLD QRAEVIVGDA SRPKDWWDGQ QFDRILADVP CSASGIVRRH PDIRWLRRES
     DIAKLVNEQR RIVSQLWSLL KPGGILVYVT CSIFPTEGEE QALWFGAQLP DAIRLQAPGQ
     LLPGTKAQET AGTNMAGQPS LPSDHDGFYY ARFQKRA
//
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