ID S6I0B4_9GAMM Unreviewed; 375 AA.
AC S6I0B4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Ribosomal RNA large subunit methyltransferase G {ECO:0000256|HAMAP-Rule:MF_01859};
DE EC=2.1.1.174 {ECO:0000256|HAMAP-Rule:MF_01859};
DE AltName: Full=23S rRNA m2G1835 methyltransferase {ECO:0000256|HAMAP-Rule:MF_01859};
DE AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmG {ECO:0000256|HAMAP-Rule:MF_01859};
GN Name=rlmG {ECO:0000256|HAMAP-Rule:MF_01859};
GN ORFNames=OFPI_10300 {ECO:0000313|EMBL:EPJ53589.1};
OS Osedax symbiont Rs2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae.
OX NCBI_TaxID=1330035 {ECO:0000313|EMBL:EPJ53589.1, ECO:0000313|Proteomes:UP000014830};
RN [1] {ECO:0000313|EMBL:EPJ53589.1, ECO:0000313|Proteomes:UP000014830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rs2 {ECO:0000313|Proteomes:UP000014830};
RA Yi H., Goffredi S.;
RT "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT Osedax worms: functional variation and environmental selection.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Specifically methylates the guanine in position 1835
CC (m2G1835) of 23S rRNA. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01859};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01859}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmG family.
CC {ECO:0000256|HAMAP-Rule:MF_01859}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPJ53589.1}.
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; ASZI01000070; EPJ53589.1; -; Genomic_DNA.
DR AlphaFoldDB; S6I0B4; -.
DR PATRIC; fig|1330035.3.peg.988; -.
DR Proteomes; UP000014830; Unassembled WGS sequence.
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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR HAMAP; MF_01859; 23SrRNA_methyltr_G; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR017237; rRNA_m2G-MeTrfase_RlmG.
DR InterPro; IPR046977; RsmC/RlmG.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR PANTHER; PTHR47816:SF5; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE G; 1.
DR PANTHER; PTHR47816; RIBOSOMAL RNA SMALL SUBUNIT METHYLTRANSFERASE C; 1.
DR Pfam; PF05175; MTS; 1.
DR PIRSF; PIRSF037565; RRNA_m2G_Mtase_RsmD_prd; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01859};
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01859};
KW Reference proteome {ECO:0000313|Proteomes:UP000014830};
KW rRNA processing {ECO:0000256|HAMAP-Rule:MF_01859};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01859};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01859}.
FT DOMAIN 200..371
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 375 AA; 42039 MW; 4528FBD536BF846A CRC64;
MQTTLTLERG AFSLKRFPIK KNEQLQAWDA ADQLVLNHLA DEADNRELRV LIINDQFGAL
SVALSNTQAC MLSDSYIAQQ ATQANLTLNN LPPITLLNST EALTGQYDLV IIKVQKSLAQ
LEDQLHKLRP HLHSNSKIIG CAMVKMIHNS TLSFFEKIIG PTKTSLAKKK ARLIFSQFDR
ELQVAANPYP QSYTLEPDGL QILNHANVFS RAKLDLGCRY FIEHIPSSDE ALEIIDLGCG
NGIVGIIAAQ RNPKAKIHFC DESHMAVASA QHNYHQAFKD SSQATFQVTD CLGDREKASA
DLILNNPPFH QQNAIGDFIA WQMFSQALQV LKKHGQLWVI GNRHLDYQNK LLKLFGNCQQ
VQSNKKFVIL KSVKK
//