RLMG_SERP5
ID RLMG_SERP5 Reviewed; 379 AA.
AC A8GJW6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase G {ECO:0000255|HAMAP-Rule:MF_01859};
DE EC=2.1.1.174 {ECO:0000255|HAMAP-Rule:MF_01859};
DE AltName: Full=23S rRNA m2G1835 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01859};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmG {ECO:0000255|HAMAP-Rule:MF_01859};
GN Name=rlmG {ECO:0000255|HAMAP-Rule:MF_01859}; OrderedLocusNames=Spro_4312;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the guanine in position 1835
CC (m2G1835) of 23S rRNA. {ECO:0000255|HAMAP-Rule:MF_01859}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(1835) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC N(2)-methylguanosine(1835) in 23S rRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42744, Rhea:RHEA-COMP:10217, Rhea:RHEA-COMP:10218,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.174;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01859};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01859}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmG family.
CC {ECO:0000255|HAMAP-Rule:MF_01859}.
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DR EMBL; CP000826; ABV43406.1; -; Genomic_DNA.
DR RefSeq; WP_012147009.1; NC_009832.1.
DR AlphaFoldDB; A8GJW6; -.
DR SMR; A8GJW6; -.
DR STRING; 399741.Spro_4312; -.
DR EnsemblBacteria; ABV43406; ABV43406; Spro_4312.
DR KEGG; spe:Spro_4312; -.
DR eggNOG; COG2813; Bacteria.
DR HOGENOM; CLU_040288_4_0_6; -.
DR OMA; DFLAWRM; -.
DR OrthoDB; 1027015at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052916; F:23S rRNA (guanine(1835)-N(2))-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR Gene3D; 3.40.50.150; -; 2.
DR HAMAP; MF_01859; 23SrRNA_methyltr_G; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR017237; rRNA_m2G-MeTrfase_RsmD.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR PANTHER; PTHR47816:SF5; PTHR47816:SF5; 1.
DR Pfam; PF05175; MTS; 1.
DR PIRSF; PIRSF037565; RRNA_m2G_Mtase_RsmD_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..379
FT /note="Ribosomal RNA large subunit methyltransferase G"
FT /id="PRO_0000366503"
SQ SEQUENCE 379 AA; 42282 MW; EDE09A80FEDFFB6D CRC64;
MSQLDLGTQQ LELERYPQQE ESTQLQAWEA ADEYLLQQLE NVNIGDRPVL IFNDNFGTLA
CALHSHQPYS ISDSYMSQLA TRHNLKLNEL DPQQVTLLDT LAELPASPAV VLIRIPKALA
LLEQQLRALR DVVAPDTVII AGAKARDVHT STMQLFEKVL GPTRTSLAWK KARLIHCEVA
DIVPPAAPVT TNWVLDGTDW VIHNHANVFS RSNLDIGARL FLDHLPHDIE GHIIDLGCGN
GVIGMAALMQ NPQAQVSFVD ESYMAVASSE LNVEHNLPQD MDRCQFEVNN SLAGIERESV
QAVLCNPPFH QQHAITDHTA WQMFCDAKRC LQVGGELRIV GNRHLDYHQK LKRLFGNCTL
IASNKKFVIL KAVKSGARY
