ID A2TZP3_9FLAO Unreviewed; 209 AA.
AC A2TZP3;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 78.
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=rsmG {ECO:0000256|HAMAP-Rule:MF_00074};
GN Synonyms=gidB {ECO:0000313|EMBL:EAQ42328.1};
GN ORFNames=MED152_06400 {ECO:0000313|EMBL:EAQ42328.1};
OS Polaribacter sp. MED152.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ42328.1, ECO:0000313|Proteomes:UP000006470};
RN [1] {ECO:0000313|EMBL:EAQ42328.1, ECO:0000313|Proteomes:UP000006470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED152 {ECO:0000313|EMBL:EAQ42328.1};
RX PubMed=17215843; DOI=10.1038/nature05381;
RA Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA Neutze R., Pedros-Alio C., Pinhassi J.;
RT "Light stimulates growth of proteorhodopsin-containing marine
RT Flavobacteria.";
RL Nature 445:210-213(2007).
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; CP004349; EAQ42328.1; -; Genomic_DNA.
DR RefSeq; WP_015481040.1; NC_020830.1.
DR AlphaFoldDB; A2TZP3; -.
DR STRING; 313598.MED152_06400; -.
DR KEGG; pom:MED152_06400; -.
DR eggNOG; COG0357; Bacteria.
DR HOGENOM; CLU_065341_2_2_10; -.
DR OrthoDB; 9808773at2; -.
DR Proteomes; UP000006470; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000006470};
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}.
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 122..123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ SEQUENCE 209 AA; 23803 MW; 0B24A27EB4816859 CRC64;
MDILLKYFTD LTETQKEQFS KLQDLYKDWN LKINVVSRKD IDELYLRHVL HSLGIAKVMP
FKPGAKVMDV GTGGGFPGIP LAILFPETQF HLVDSIGKKI KVVNEVAEGL GLENVTTTHG
RVEEVEDTYD FIVSRAVAQM ETFVRWTKGK IAKKQNHDLK NGILYLKGGD LTEELQKYTS
ATIYDLPNYF DEPFFETKKV VHLGMKFKG
//
