ID B7RW81_9GAMM Unreviewed; 251 AA.
AC B7RW81;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
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 ORFNames=GPB2148_2505 {ECO:0000313|EMBL:EEB79573.1};
OS marine gamma proteobacterium HTCC2148.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB79573.1, ECO:0000313|Proteomes:UP000002793};
RN [1] {ECO:0000313|Proteomes:UP000002793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2148 {ECO:0000313|Proteomes:UP000002793};
RX PubMed=20472793; DOI=10.1128/jb.00511-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT OM60/NOR5 clade of the Gammaproteobacteria.";
RL J. Bacteriol. 192:3842-3843(2010).
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; DS999224; EEB79573.1; -; Genomic_DNA.
DR AlphaFoldDB; B7RW81; -.
DR STRING; 247634.GPB2148_2505; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_0_1_6; -.
DR OrthoDB; 9785673at2; -.
DR Proteomes; UP000002793; Unassembled WGS sequence.
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:UP000002793};
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 3..78
FT /note="RNA 2-O ribose methyltransferase substrate binding"
FT /evidence="ECO:0000259|SMART:SM00967"
FT BINDING 204
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT BINDING 224
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT BINDING 233
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
SQ SEQUENCE 251 AA; 27340 MW; 8232044CADB95009 CRC64;
MQYIYGIHAV DSLLRQNPKS VQRLWVQQGR EDKRIASLLE LAQNQGVPMA RESRKDLDDM
VKGRHQGVVA ETLSDPVHGD TQQANLWQES DLLRMVDEKD SPVLILVLDG VTDPHNLGAC
LRSADAAGVD AVVVPKDKSA DLSPTVRKVA CGAGEIVPFV RVTNISRTLD ALKERQVWIF
GAAGEAEKSI YDNDLTGSMA LVMGAEGAGL RRLTREHCDF LIKLPMAGSV SSLNVSVATG
VCLFEVIRQR G
//
