ID L0RVL2_MYCC1 Unreviewed; 241 AA.
AC L0RVL2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Ribosomal RNA small subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_00074};
DE EC=2.1.1.- {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=MCYN0400 {ECO:0000313|EMBL:CCP24132.1};
GN Synonyms=rsmG {ECO:0000256|HAMAP-Rule:MF_00074};
GN OrderedLocusNames=MCYN_0400 {ECO:0000313|EMBL:CCP24132.1};
OS Mycoplasmopsis cynos (strain C142) (Mycoplasma cynos).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mycoplasmopsis.
OX NCBI_TaxID=1246955 {ECO:0000313|EMBL:CCP24132.1, ECO:0000313|Proteomes:UP000010466};
RN [1] {ECO:0000313|Proteomes:UP000010466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C142 {ECO:0000313|Proteomes:UP000010466};
RX PubMed=23409256; DOI=10.1128/genomeA.00196-12;
RA Walker C.A., Mannering S.A., Shields S., Blake D.P., Brownlie J.;
RT "Complete genome sequence of Mycoplasma cynos strain C142.";
RL Genome Announc. 1:E00196-E00196(2013).
CC -!- FUNCTION: Specifically methylates the N7 position of a guanine in 16S
CC rRNA. {ECO:0000256|HAMAP-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}.
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DR EMBL; HF559394; CCP24132.1; -; Genomic_DNA.
DR AlphaFoldDB; L0RVL2; -.
DR STRING; 1246955.MCYN_0400; -.
DR KEGG; mcy:MCYN_0400; -.
DR PATRIC; fig|1246955.3.peg.362; -.
DR eggNOG; COG0357; Bacteria.
DR HOGENOM; CLU_065341_0_1_14; -.
DR Proteomes; UP000010466; Chromosome.
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 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:CCP24132.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010466};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP-
KW Rule:MF_00074}; S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00074};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00074, ECO:0000313|EMBL:CCP24132.1}.
FT BINDING 78
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 130..131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 145
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ SEQUENCE 241 AA; 28576 MW; 0EA333A8B7375FB1 CRC64;
MCMEKYSKKY ELQRLCNENN WDFSLFQKYF DLIEEKNKVM NLTGFSGERL WEEGIFESLI
FMLKITENQE NKIILDIGAG AGFPSIPYAL TRPRNKLVIY EPIQKRVNFL NLVVHELNLN
DYVEVIRTRV EEVKEKNLFD IVTARAVASI KELLMSSFHL VKLNGSMLLL KSTKFQEELN
QAREILKLLK TEIKIIDMQN DFKHRNNKII KIKKLRSTPL QFPFSWKEIK LINRKEQNVK
N
//
