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Database: UniProt
Entry: F2N9E6_CORGP
LinkDB: F2N9E6_CORGP
Original site: F2N9E6_CORGP 
ID   F2N9E6_CORGP            Unreviewed;       251 AA.
AC   F2N9E6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
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   OrderedLocusNames=Corgl_1799 {ECO:0000313|EMBL:AEB07894.1};
OS   Coriobacterium glomerans (strain ATCC 49209 / DSM 20642 / JCM 10262 / PW2).
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae; Coriobacterium.
OX   NCBI_TaxID=700015 {ECO:0000313|EMBL:AEB07894.1, ECO:0000313|Proteomes:UP000006851};
RN   [1] {ECO:0000313|Proteomes:UP000006851}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 49209 / DSM 20642 / JCM 10262 / PW2
RC   {ECO:0000313|Proteomes:UP000006851};
RX   PubMed=23961308; DOI=10.4056/sigs.3507020;
RA   Stackebrandt E., Zeytun A., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Goodwin L.A., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Mavromatis K., Mikhailova N., Huntemann M., Pati A.,
RA   Chen A., Palaniappan K., Chang Y.J., Land M., Hauser L., Rohde M.,
RA   Pukall R., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Coriobacterium glomerans type strain (PW2(T))
RT   from the midgut of Pyrrhocoris apterus L. (red soldier bug).";
RL   Stand. Genomic Sci. 8:15-25(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; CP002628; AEB07894.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2N9E6; -.
DR   STRING; 700015.Corgl_1799; -.
DR   KEGG; cgo:Corgl_1799; -.
DR   eggNOG; COG0357; Bacteria.
DR   HOGENOM; CLU_065341_0_2_11; -.
DR   Proteomes; UP000006851; 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:AEB07894.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006851};
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         93
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         98
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         143..144
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
FT   BINDING         160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00074"
SQ   SEQUENCE   251 AA;  27705 MW;  004E8A34EEE78131 CRC64;
     MGRSFDPLPV DEDELNDLCI RLLLYCESCR LELFTDQAEL CVRHLLLVLK LNRTQNLTRI
     TDPNKGLILH VLDSLLLSRY IHSDEQASLL DMGTGPGFPG IPLHILTRYP TVLVDSVRKK
     IEAVTDIISA LDLSSVSAIH TRLEDFALSD YDGFPFVVAR ALAPLPTLLE LAAPLVPLGG
     RLVLTKGLPK PAEVTSGLRV ADIVGFALVD SDEFDLPENL GHRLIFVFQR TAESRVKLPR
     QNGLAKKNPL A
//
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