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Database: UniProt
Entry: G4SX43_META2
LinkDB: G4SX43_META2
Original site: G4SX43_META2 
ID   G4SX43_META2            Unreviewed;       248 AA.
AC   G4SX43;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=23S rRNA (guanosine-2'-O-)-methyltransferase RlmB {ECO:0000256|HAMAP-Rule:MF_01887};
DE            EC=2.1.1.185 {ECO:0000256|HAMAP-Rule:MF_01887};
DE   AltName: Full=23S rRNA (guanosine2251 2'-O)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01887};
DE   AltName: Full=23S rRNA Gm2251 2'-O-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01887};
GN   Name=rlmB {ECO:0000256|HAMAP-Rule:MF_01887,
GN   ECO:0000313|EMBL:CCE23098.1};
GN   OrderedLocusNames=MEALZ_1410 {ECO:0000313|EMBL:CCE23098.1};
OS   Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS   B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylotuvimicrobium.
OX   NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE23098.1, ECO:0000313|Proteomes:UP000008315};
RN   [1] {ECO:0000313|Proteomes:UP000008315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC   {ECO:0000313|Proteomes:UP000008315};
RX   PubMed=22207753; DOI=10.1128/JB.06392-11;
RA   Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA   Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA   Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA   Trotsenko Y.A., Kalyuzhnaya M.G.;
RT   "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT   Methylomicrobium alcaliphilum 20Z.";
RL   J. Bacteriol. 194:551-552(2012).
CC   -!- FUNCTION: Specifically methylates the ribose of guanosine 2251 in 23S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01887}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2251) in 23S rRNA + S-adenosyl-L-methionine = 2'-O-
CC         methylguanosine(2251) in 23S rRNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:24140, Rhea:RHEA-COMP:10239, Rhea:RHEA-COMP:10241,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74445; EC=2.1.1.185;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01887};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01887}.
CC   -!- SIMILARITY: Belongs to the class IV-like SAM-binding methyltransferase
CC       superfamily. RNA methyltransferase TrmH family. RlmB subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01887}.
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DR   EMBL; FO082060; CCE23098.1; -; Genomic_DNA.
DR   RefSeq; WP_014147894.1; NC_016112.1.
DR   AlphaFoldDB; G4SX43; -.
DR   STRING; 1091494.MEALZ_1410; -.
DR   KEGG; mah:MEALZ_1410; -.
DR   PATRIC; fig|271065.3.peg.1448; -.
DR   HOGENOM; CLU_021322_0_1_6; -.
DR   OMA; QVPPYEY; -.
DR   Proteomes; UP000008315; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0070039; F:rRNA (guanosine-2'-O-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd18103; SpoU-like_RlmB; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_01887; 23SrRNA_methyltr_B; 1.
DR   InterPro; IPR024915; 23S_rRNA_MeTrfase_RlmB.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR004441; rRNA_MeTrfase_TrmH.
DR   InterPro; IPR001537; SpoU_MeTrfase.
DR   InterPro; IPR013123; SpoU_subst-bd.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   NCBIfam; TIGR00186; rRNA_methyl_3; 1.
DR   PANTHER; PTHR46429; 23S RRNA (GUANOSINE-2'-O-)-METHYLTRANSFERASE RLMB; 1.
DR   PANTHER; PTHR46429:SF1; 23S RRNA (GUANOSINE-2'-O-)-METHYLTRANSFERASE RLMB; 1.
DR   Pfam; PF00588; SpoU_methylase; 1.
DR   Pfam; PF08032; SpoU_sub_bind; 1.
DR   SMART; SM00967; SpoU_sub_bind; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
DR   SUPFAM; SSF55315; L30e-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01887};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP-
KW   Rule:MF_01887}; Reference proteome {ECO:0000313|Proteomes:UP000008315};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW   Rule:MF_01887};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW   Rule:MF_01887};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01887}.
FT   DOMAIN          5..81
FT                   /note="RNA 2-O ribose methyltransferase substrate binding"
FT                   /evidence="ECO:0000259|SMART:SM00967"
FT   BINDING         198
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT   BINDING         218
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT   BINDING         227
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
SQ   SEQUENCE   248 AA;  27260 MW;  8502BD5DE8F1948E CRC64;
     MSRVKIYGIH SVQAALDYSP QHIHQAWVDS HRQDRRLSQL LEDLKKIGIN PEKVDRKKLD
     RLADGNNHQS IVLEIELPSA QSEDALKQAV SSLTGMPLFL VLDNVQDPHN LGACLRTADA
     TGVHGVIITK DNAVGITPTV CKVASGAAET VPVYQVTNLA RTLRWLKDQG VWIFGAAGEA
     EQTLYQCDFK LPMALVIGAE GKGMRRLTRE QCDWLVKLPM QGSVSSLNLS VATGAMLYEV
     VRQRSIPS
//
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