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Database: UniProt
Entry: Q1LJC6_CUPMC
LinkDB: Q1LJC6_CUPMC
Original site: Q1LJC6_CUPMC 
ID   Q1LJC6_CUPMC            Unreviewed;       466 AA.
AC   Q1LJC6;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=tRNA and rRNA cytosine-C5-methylase {ECO:0000313|EMBL:ABF09750.1};
GN   Name=sun1 {ECO:0000313|EMBL:ABF09750.1};
GN   OrderedLocusNames=Rmet_2877 {ECO:0000313|EMBL:ABF09750.1};
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:ABF09750.1, 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|PROSITE-ProRule:PRU01023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01023}.
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DR   EMBL; CP000352; ABF09750.1; -; Genomic_DNA.
DR   RefSeq; WP_011517429.1; NC_007973.1.
DR   AlphaFoldDB; Q1LJC6; -.
DR   STRING; 266264.Rmet_2877; -.
DR   KEGG; rme:Rmet_2877; -.
DR   eggNOG; COG0144; Bacteria.
DR   HOGENOM; CLU_005316_0_2_4; -.
DR   Proteomes; UP000002429; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008173; F:RNA methyltransferase activity; IEA:InterPro.
DR   GO; GO:0001510; P:RNA methylation; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR049560; MeTrfase_RsmB-F_NOP2_cat.
DR   InterPro; IPR001678; MeTrfase_RsmB-F_NOP2_dom.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR22807; NOP2 YEAST -RELATED NOL1/NOP2/FMU SUN DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR22807:SF77; SUN PROTEIN; 1.
DR   Pfam; PF01189; Methyltr_RsmB-F; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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          184..465
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        398
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         298
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         325
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         345
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   466 AA;  50648 MW;  F1B472DB4AE36F9B CRC64;
     MSRNPATSQD NRQRSRPSKG KASPIRKSPN ARQQGADGAP RTPGGLQAFH LQHIDRLLGK
     VLLFARPSDA VVSHYFRENS KLGHRDRGII AEAIFAVLRR RVEFGQFAES GTGSATRRLG
     LLGLAATLGR DVLSPFLHPD EAVWLDRLTT IERSSLAPRV RANLPEWLYD DLVARHGEAF
     TAALGDAWLR PAPLDLRVNT AKLSREEALA ELQTAGIAAE LAPMAPAGIR LKGKPALNQL
     PLFINGGVEV QDEGSQLLCH LLAPRRGEMV VDFCAGAGGK TLALGVAMRS TGRLYAFDVS
     EKRLANLKPR LARSGLSNVH PVLIDSERDA KVKRLAGKID RVLVDAPCSG LGTLRRNPDL
     KWRQTPESVV ELTAKQAAIL DAAAKLVKGG GRVVYATCSV LEAENEAIIR DFLASHENFR
     LVPVSEVLAE QKIEVPELPA EGGMLALYPH IHQTDGFFAA VLERTR
//
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