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-NOV-2019, entry version 2. 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; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; 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 RT sequencing to study the core and pangenomes of soil and plant- RT associated 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 = CC N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L- CC homocysteine; Xref=Rhea:RHEA:42732, Rhea:RHEA-COMP:10209, CC Rhea:RHEA-COMP:10210, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; EC=2.1.1.170; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00074}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00074, CC ECO:0000256|SAAS:SAAS01091540}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RNA CC methyltransferase RsmG family. {ECO:0000256|HAMAP-Rule:MF_00074, CC ECO:0000256|SAAS:SAAS01091529}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00074}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Proteomes; UP000318050; Unassembled WGS sequence. DR HAMAP; MF_00074; 16SrRNA_methyltr_G; 1. DR InterPro; IPR003682; rRNA_ssu_MeTfrase_G. DR InterPro; IPR029063; SAM-dependent_MTases. 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 Complete proteome {ECO:0000313|Proteomes:UP000318050}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00074, KW ECO:0000256|SAAS:SAAS01091534}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00074, KW ECO:0000256|SAAS:SAAS01091532, ECO:0000313|EMBL:TWB47221.1}; KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_00074, KW ECO:0000256|SAAS:SAAS01091530}; KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00074, KW ECO:0000256|SAAS:SAAS01091525}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00074, KW ECO:0000256|SAAS:SAAS01091535, ECO:0000313|EMBL:TWB47221.1}. FT REGION 120 121 S-adenosyl-L-methionine binding. FT {ECO:0000256|HAMAP-Rule:MF_00074}. FT BINDING 71 71 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00074}. FT BINDING 76 76 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00074}. FT BINDING 134 134 S-adenosyl-L-methionine. FT {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 //