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Database: UniProt
Entry: Q0K5G8_CUPNH
LinkDB: Q0K5G8_CUPNH
Original site: Q0K5G8_CUPNH 
ID   Q0K5G8_CUPNH            Unreviewed;       466 AA.
AC   Q0K5G8;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   SubName: Full=tRNA and rRNA cytosine-C5-methylase {ECO:0000313|EMBL:CAJ94753.1};
GN   Name=sun2 {ECO:0000313|EMBL:CAJ94753.1};
GN   OrderedLocusNames=H16_A3697 {ECO:0000313|EMBL:CAJ94753.1};
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ94753.1, ECO:0000313|Proteomes:UP000008210};
RN   [1] {ECO:0000313|EMBL:CAJ94753.1, ECO:0000313|Proteomes:UP000008210}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier
RC   337 {ECO:0000313|Proteomes:UP000008210};
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA   Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I.,
RA   Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT   eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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; AM260479; CAJ94753.1; -; Genomic_DNA.
DR   RefSeq; WP_011616263.1; NZ_CP039287.1.
DR   AlphaFoldDB; Q0K5G8; -.
DR   STRING; 381666.H16_A3697; -.
DR   GeneID; 57645829; -.
DR   KEGG; reh:H16_A3697; -.
DR   PATRIC; fig|381666.6.peg.4086; -.
DR   eggNOG; COG0144; Bacteria.
DR   HOGENOM; CLU_005316_0_4_4; -.
DR   OrthoDB; 9810297at2; -.
DR   Proteomes; UP000008210; Chromosome 1.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008649; F:rRNA methyltransferase activity; IEA:InterPro.
DR   CDD; cd02440; AdoMet_MTases; 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:UP000008210};
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          188..465
FT                   /note="SAM-dependent MTase RsmB/NOP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51686"
FT   REGION          429..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        396
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         276..282
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
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         324
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
FT   BINDING         343
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01023"
SQ   SEQUENCE   466 AA;  50242 MW;  3358E700B956F381 CRC64;
     MRLPPDSLAF QMLGAAAAVR AVSEGTALPQ AIEDAAAQLR LDRVQDAATR GALQDIAYRT
     MRQFGTARAL VTKLVTRPPG AQVDSLLAVA LALLLEHAPG PRDKQDGADA GRPGYSTFTV
     VDQAVSAAAS EPKTAHARGL VNAVLRRFLR ERKALLAEVN RDEQARWNLP PWWLRMLREA
     YPDQWMALAA SANVRPPMTV RVNTARVSVQ QYQTDLANAG LAGHVVGPQA VRLVRAVPVT
     QLPGFAEGVV SVQDAGAQLA APLLEVADGM RVLDACAAPG GKTGHLLELA DIEVTAVESD
     PQRTTRIAEN LARLGKQARI VVGDASRPAD WWDGQPFDRI LADVPCSASG IVRRHPDIRW
     LRRETDIAKL VTEQRRIVSQ LWPLLKPGGI LVYVTCSIFP TEGEEQARWF GAQLADAIRL
     QAPGQLLPGT HATQAAGANG EKDATAGTSL PSDHDGFFYA RFQKRA
//
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