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Database: UniProt
Entry: A0A1S2K7T4_9ACTN
LinkDB: A0A1S2K7T4_9ACTN
Original site: A0A1S2K7T4_9ACTN 
ID   A0A1S2K7T4_9ACTN        Unreviewed;       426 AA.
AC   A0A1S2K7T4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=BJP40_21335 {ECO:0000313|EMBL:OII64145.1};
OS   Streptomyces sp. CC53.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII64145.1, ECO:0000313|Proteomes:UP000179639};
RN   [1] {ECO:0000313|EMBL:OII64145.1, ECO:0000313|Proteomes:UP000179639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC53 {ECO:0000313|EMBL:OII64145.1,
RC   ECO:0000313|Proteomes:UP000179639};
RA   Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT   "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT   transport.";
RL   Submitted (OCT-2016) 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:OII64145.1}.
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DR   EMBL; MKXB01000104; OII64145.1; -; Genomic_DNA.
DR   RefSeq; WP_071279996.1; NZ_MKXB01000104.1.
DR   AlphaFoldDB; A0A1S2K7T4; -.
DR   STRING; 1906740.BJP40_21335; -.
DR   Proteomes; UP000179639; 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:OII64145.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000179639};
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          222..392
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
FT   REGION          394..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  44977 MW;  62A445628EE196CD CRC64;
     MNGLTTPWGT YALTRHPEHP RDPLRAWDAA DAYLLGRFAE PGAPELTGTV AVAGDRWGAL
     TTALAGRRAG AAGPGGAPAA RLVQITDSHL GREATRANLA RAGLADAPAL DLLTTRDTPP
     DRVDVLLVRV PKSLALLEDQ LHRLAPALHE GSTVIGTGMV KEIHTSTLDL FERLVGPTRT
     SLAVRKARLV FSTPDPALPR PANPWPLTYA LPEDAPGVGG RTVVTHAGVF CADRLDIGTR
     LFLRHLPQGL GAARVVDLGC GNGVVGLAVA VADPDAEVVF TDESYQAVAS AEETFRASAP
     PAAKARFTVG DGMAELPDDS VDVVLCNPPF HSHQALTDAT ARRMFMGARR ALKAGGELRV
     VGNRHLGYHV TLKRIFGNCD VVAGDPKFVV LRAVKSPPGK QARAGTAPPR RQGRPRRPAG
     RNHPGA
//
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