RLMB_CHRVO
ID RLMB_CHRVO Reviewed; 248 AA.
AC Q7NYX3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=23S rRNA (guanosine-2'-O-)-methyltransferase RlmB {ECO:0000255|HAMAP-Rule:MF_01887};
DE EC=2.1.1.185 {ECO:0000255|HAMAP-Rule:MF_01887};
DE AltName: Full=23S rRNA (guanosine2251 2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887};
DE AltName: Full=23S rRNA Gm2251 2'-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01887};
GN Name=rlmB {ECO:0000255|HAMAP-Rule:MF_01887}; OrderedLocusNames=CV_1149;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
CC -!- FUNCTION: Specifically methylates the ribose of guanosine 2251 in 23S
CC rRNA. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01887};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01887}.
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DR EMBL; AE016825; AAQ58824.1; -; Genomic_DNA.
DR RefSeq; WP_011134704.1; NC_005085.1.
DR AlphaFoldDB; Q7NYX3; -.
DR SMR; Q7NYX3; -.
DR STRING; 243365.CV_1149; -.
DR EnsemblBacteria; AAQ58824; AAQ58824; CV_1149.
DR KEGG; cvi:CV_1149; -.
DR eggNOG; COG0566; Bacteria.
DR HOGENOM; CLU_021322_0_1_4; -.
DR OMA; QVPPYEY; -.
DR OrthoDB; 1422015at2; -.
DR Proteomes; UP000001424; 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 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; L30e-like.
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 PANTHER; PTHR46429; PTHR46429; 1.
DR Pfam; PF00588; SpoU_methylase; 1.
DR Pfam; PF08032; SpoU_sub_bind; 1.
DR SMART; SM00967; SpoU_sub_bind; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR SUPFAM; SSF75217; SSF75217; 1.
DR TIGRFAMs; TIGR00186; rRNA_methyl_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..248
FT /note="23S rRNA (guanosine-2'-O-)-methyltransferase RlmB"
FT /id="PRO_0000159783"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
FT BINDING 217
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
FT BINDING 226
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01887"
SQ SEQUENCE 248 AA; 26769 MW; C76F78C4B48F6914 CRC64;
MSNKRLIHGF HAINARLWQN PKSLIEIWLA GGRHDARAKA VLDKAGAENV KLHIVDKERL
DSMSGNARHQ GVVAMIDASM NYVDLDDVLE NLSEPPLLLI LDGVTDPHNL GACLRVADAM
GAHAVIAPKD RSATLNATVS KVACGAAEVV PYITVTNLAR TLRDLKDAGV WIAGTTMEAD
TDLYHFDASG PLAWVMGAEG EGMRRLTREH CDVLVSIPMF GTVESLNVSV SSGMVLSESR
RQRVLKAG
