ID Q5QXZ9_IDILO Unreviewed; 248 AA.
AC Q5QXZ9;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 113.
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=IL1942 {ECO:0000313|EMBL:AAV82774.1};
OS Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Idiomarina.
OX NCBI_TaxID=283942 {ECO:0000313|EMBL:AAV82774.1, ECO:0000313|Proteomes:UP000001171};
RN [1] {ECO:0000313|EMBL:AAV82774.1, ECO:0000313|Proteomes:UP000001171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-735 / DSM 15497 / L2-TR
RC {ECO:0000313|Proteomes:UP000001171};
RX PubMed=15596722; DOI=10.1073/pnas.0407638102;
RA Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y.,
RA Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S.,
RA Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S.,
RA Denery J., Aizawa S., Shibata S., Malahoff A., Alam M.;
RT "Genome sequence of the deep-sea gamma-proteobacterium Idiomarina
RT loihiensis reveals amino acid fermentation as a source of carbon and
RT energy.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004).
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; AE017340; AAV82774.1; -; Genomic_DNA.
DR RefSeq; WP_011235170.1; NC_006512.1.
DR AlphaFoldDB; Q5QXZ9; -.
DR STRING; 283942.IL1942; -.
DR KEGG; ilo:IL1942; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_0_1_6; -.
DR OrthoDB; 9785673at2; -.
DR Proteomes; UP000001171; 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:UP000001171};
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 199
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT BINDING 219
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
FT BINDING 228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01887"
SQ SEQUENCE 248 AA; 26548 MW; 93A389D07B307E44 CRC64;
MSQKVTVFGL HAVRAILKNH PDRLVELYVS KERQDDSVRD IVNQCHATGV RPQWVPKQAL
EKRAEGGNHQ GVVATVQSPP TLTEHDLPKL LEQSQQAGLF LILDGVTDPH NLGACLRTAD
AAGVTGVIVP KDKSAQITPT VRKVASGAAE NVPLVVVTNL ARALRDLQEL GVWAYGTAGE
ATQSVYDVDY RGPVALVMGA EGKGMRRLTR ETCDDLVSIP LSGSVSSLNV SVASGVCLFE
VVRQRNGS
//
