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Database: UniProt
Entry: A0A327WNP5_9ACTN
LinkDB: A0A327WNP5_9ACTN
Original site: A0A327WNP5_9ACTN 
ID   A0A327WNP5_9ACTN        Unreviewed;       398 AA.
AC   A0A327WNP5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=K377_00589 {ECO:0000313|EMBL:RAJ91820.1};
OS   Streptomyces sp. PsTaAH-137.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1305830 {ECO:0000313|EMBL:RAJ91820.1, ECO:0000313|Proteomes:UP000249376};
RN   [1] {ECO:0000313|EMBL:RAJ91820.1, ECO:0000313|Proteomes:UP000249376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PsTaAH-137 {ECO:0000313|EMBL:RAJ91820.1,
RC   ECO:0000313|Proteomes:UP000249376};
RA   Currie C.;
RT   "Biomass-degrading enzyme discovery via genome sequencing of insect-
RT   associated Streptomyces.";
RL   Submitted (JUN-2018) 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:RAJ91820.1}.
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DR   EMBL; QLLY01000001; RAJ91820.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327WNP5; -.
DR   Proteomes; UP000249376; 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   ECO:0000313|EMBL:RAJ91820.1};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_01859};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01859};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01859}.
FT   DOMAIN          217..385
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  42777 MW;  750D8CD8D38AA364 CRC64;
     MNRTDKAAPA PVLTTPWSDL ALTRHPEDPR DPLRAWDAAD AYLLKHLAEQ GVDLSGSVVV
     VGDRWGALGT ALAGTGGRAP TVISDSYLGL EATRTNLKRN GLSGPTLLTT QDTPPARADV
     LLVRVPKSLA LLEDQLHRLR PAVHAGTVVV GTGMVKEIHT STLQLFERII GPTRTSLAEK
     KARLIFTTPD PSLTPGPNPW PHRYALPDDI GPLAGRTVVN HAGVFCAEHL DIGTRFLLQH
     LPRATDARRI VDLGCGNGVV GTTAALTHPD AEVLFTDESY QAVASAEATY RENASGEARF
     RAADGLEGVP DGSVDLVLNN PPFHSHQATT DATAWRMFTQ ARAALAPGGE LWVVGNRHLG
     YHLKLRRLFG TSELVAGDPK FVILKAVKQA SRARGRRQ
//
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