ID A0A560HMS2_9PROT Unreviewed; 202 AA. AC A0A560HMS2; DT 16-OCT-2019, integrated into UniProtKB/TrEMBL. DT 16-OCT-2019, sequence version 1. DT 13-SEP-2023, entry version 12. DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_00074}; DE EC=2.1.1.170 {ECO:0000256|HAMAP-Rule:MF_00074}; DE AltName: Full=16S rRNA 7-methylguanosine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074}; DE Short=16S rRNA m7G methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074}; GN Name=rsmG {ECO:0000256|HAMAP-Rule:MF_00074}; GN ORFNames=FBZ92_13635 {ECO:0000313|EMBL:TWB47221.1}; OS Nitrospirillum amazonense. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales; OC Azospirillaceae; Nitrospirillum. OX NCBI_TaxID=28077 {ECO:0000313|EMBL:TWB47221.1, ECO:0000313|Proteomes:UP000318050}; RN [1] {ECO:0000313|EMBL:TWB47221.1, ECO:0000313|Proteomes:UP000318050} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BR 11140 {ECO:0000313|EMBL:TWB47221.1, RC ECO:0000313|Proteomes:UP000318050}; RA Whitman W.; RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing RT to study the core and pangenomes of soil and plant-associated RT prokaryotes."; RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Specifically methylates the N7 position of guanine in CC position 527 of 16S rRNA. {ECO:0000256|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:0000256|HAMAP- CC Rule:MF_00074}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00074}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA CC methyltransferase RsmG family. {ECO:0000256|HAMAP-Rule:MF_00074}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00074}. 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:TWB47221.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; VITT01000036; TWB47221.1; -; Genomic_DNA. DR RefSeq; WP_040845177.1; NZ_VITT01000036.1. DR AlphaFoldDB; A0A560HMS2; -. DR OrthoDB; 9808773at2; -. DR Proteomes; UP000318050; Unassembled WGS sequence. 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; Vaccinia Virus protein VP39; 1. DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1. DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR00138; rsmG_gidB; 1. DR PANTHER; PTHR31760; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1. DR PANTHER; PTHR31760:SF0; S-ADENOSYL-L-METHIONINE-DEPENDENT METHYLTRANSFERASES SUPERFAMILY PROTEIN; 1. DR Pfam; PF02527; GidB; 1. DR PIRSF; PIRSF003078; GidB; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00074}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074, KW ECO:0000313|EMBL:TWB47221.1}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_00074}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00074}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00074, ECO:0000313|EMBL:TWB47221.1}. FT BINDING 71 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074" FT BINDING 76 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074" FT BINDING 120..121 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074" FT BINDING 134 FT /ligand="S-adenosyl-L-methionine" FT /ligand_id="ChEBI:CHEBI:59789" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074" SQ SEQUENCE 202 AA; 21877 MW; 0B28D926663D8840 CRC64; MTPADFASRF HVSRETLDRL TLYAQLLAKW NPAINLVAKS TVPDVWDRHM ADSAQLYALL PPGTRTQVDM GSGAGFPGLV MAILGVPDVH LIESDTRKAT FLREMARATG TPVTVHAQRI EQAPEIAADV VTARALAALP ELLDWGYRFL KPGATCLFLK GRTAPEELTL AAQSWTMTVS QVPSITDASG TILILGEIAR AR //