ID C0DUN5_EIKCO Unreviewed; 248 AA.
AC C0DUN5;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 62.
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=EIKCOROL_01071 {ECO:0000313|EMBL:EEG24433.1};
OS Eikenella corrodens ATCC 23834.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Eikenella.
OX NCBI_TaxID=546274 {ECO:0000313|EMBL:EEG24433.1, ECO:0000313|Proteomes:UP000005837};
RN [1] {ECO:0000313|EMBL:EEG24433.1, ECO:0000313|Proteomes:UP000005837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23834 {ECO:0000313|EMBL:EEG24433.1,
RC ECO:0000313|Proteomes:UP000005837};
RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEG24433.1}.
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DR EMBL; ACEA01000017; EEG24433.1; -; Genomic_DNA.
DR RefSeq; WP_003823039.1; NZ_EQ973317.1.
DR AlphaFoldDB; C0DUN5; -.
DR GeneID; 60769034; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_0_1_4; -.
DR Proteomes; UP000005837; 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};
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 248 AA; 27160 MW; 15B938FB67BC9E48 CRC64;
MSNRRLIYGF HAVNARLWQN PKSLTELYAL SGRHDTRMQQ ALEKAAQENI PVHFVEAARL
DNLCRHARHQ GIAGFIDASH NHVHLDDVLD NLTEPPLLLI LDGITDPHNL GACLRVADAM
GVHAVIAPKN RSVGLNATVS KVACGAAETV PYIAVTNLAR TLRELKERDI WIVGTDMGGE
ADLFHYDIPA AVAWVMGNEG EGMRRLTREH CDALVSIPML GTVESLNVSV STGMVLAETR
RQRALKAG
//
