ID F8GG95_NITSI Unreviewed; 246 AA.
AC F8GG95;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=Nit79A3_2602 {ECO:0000313|EMBL:AEJ02369.1};
OS Nitrosomonas sp. (strain Is79A3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=261292 {ECO:0000313|EMBL:AEJ02369.1};
RN [1] {ECO:0000313|EMBL:AEJ02369.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Is79A3 {ECO:0000313|EMBL:AEJ02369.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Bollmann A., Norton J.,
RA Suwa Y., Klotz M., Stein L., Laanbroek H., Arp D., Woyke T.;
RT "Complete sequence of Nitrosomonas sp. Is79A3.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
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; CP002876; AEJ02369.1; -; Genomic_DNA.
DR AlphaFoldDB; F8GG95; -.
DR STRING; 261292.Nit79A3_2602; -.
DR KEGG; nii:Nit79A3_2602; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_0_1_4; -.
DR OrthoDB; 9785673at2; -.
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};
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 6..82
FT /note="RNA 2-O ribose methyltransferase substrate binding"
FT /evidence="ECO:0000259|SMART:SM00967"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
SQ SEQUENCE 246 AA; 26920 MW; 49709038428B4B62 CRC64;
MSSTRLIFGF HAVTSRLRQN PDSIKEIFID ATRDDQRARG LIKLAEDQKI RLITCEGPRL
TSMAGTDRHQ GVVANIDITR SYVDISDVLD TLTEPARLLV LDGIQDPHNL GACLRVADAF
GVHAVIAPKD RAVGLTSTVY KVSSGAADTV PYIAVTNLSR TLKQLKKQGI WIIGTAEDAD
HDLTHFQIQG PVAWVFGSEE KGLRRLTRES CDQLVRIPML GSIESLNVAV SAGICLFETL
RQQSSA
//
