RSMG_HAES1
ID RSMG_HAES1 Reviewed; 212 AA.
AC Q0I5W5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_00074};
DE EC=2.1.1.170 {ECO:0000255|HAMAP-Rule:MF_00074};
DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
DE Short=16S rRNA m7G methyltransferase {ECO:0000255|HAMAP-Rule:MF_00074};
GN Name=rsmG {ECO:0000255|HAMAP-Rule:MF_00074}; OrderedLocusNames=HS_1704;
OS Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Histophilus.
OX NCBI_TaxID=205914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129Pt;
RX PubMed=17172329; DOI=10.1128/jb.01422-06;
RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA Xie G., Inzana T.J.;
RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT influenzae Rd.";
RL J. Bacteriol. 189:1890-1898(2007).
CC -!- FUNCTION: Specifically methylates the N7 position of guanine in
CC position 527 of 16S rRNA. {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42732, Rhea:RHEA-COMP:10209, Rhea:RHEA-COMP:10210,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.170; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00074};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00074}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA
CC methyltransferase RsmG family. {ECO:0000255|HAMAP-Rule:MF_00074}.
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DR EMBL; CP000436; ABI25972.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0I5W5; -.
DR SMR; Q0I5W5; -.
DR STRING; 205914.HS_1704; -.
DR EnsemblBacteria; ABI25972; ABI25972; HS_1704.
DR KEGG; hso:HS_1704; -.
DR eggNOG; COG0357; Bacteria.
DR HOGENOM; CLU_065341_2_0_6; -.
DR OMA; ICFPHLH; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1.
DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31760; PTHR31760; 1.
DR Pfam; PF02527; GidB; 1.
DR PIRSF; PIRSF003078; GidB; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00138; rsmG_gidB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..212
FT /note="Ribosomal RNA small subunit methyltransferase G"
FT /id="PRO_0000335358"
FT BINDING 72
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 77
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 123..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
FT BINDING 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00074"
SQ SEQUENCE 212 AA; 24282 MW; 42F51A4BAF24E83A CRC64;
MEKLNFLLKN TALLPTNLQK ERLVQLVLLL NKWNKAYNLT SVRDPMEMLV KHILDSIVVS
PYLQGNIFID VGTGPGLPGL PLAIINPDKK FFLLDSLGKR ISFIRNAVRE LELTNVEPVL
SRVEEFKPDH QFDGVLSRAF ASLKDMTEWC QHLLTDQGFF YALKGQYNME EVSALSAQFS
VEKIIEMNVP ELVGKRHLVL LKKIRINLMN YL
