ID   RLMKL_MANSM             Reviewed;         715 AA.
AC   Q65UK6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Ribosomal RNA large subunit methyltransferase K/L {ECO:0000255|HAMAP-Rule:MF_01858};
DE   Includes:
DE     RecName: Full=23S rRNA m2G2445 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01858};
DE              EC=2.1.1.173 {ECO:0000255|HAMAP-Rule:MF_01858};
DE     AltName: Full=rRNA (guanine-N(2)-)-methyltransferase RlmL {ECO:0000255|HAMAP-Rule:MF_01858};
DE   Includes:
DE     RecName: Full=23S rRNA m7G2069 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01858};
DE              EC=2.1.1.264 {ECO:0000255|HAMAP-Rule:MF_01858};
DE     AltName: Full=rRNA (guanine-N(7)-)-methyltransferase RlmK {ECO:0000255|HAMAP-Rule:MF_01858};
GN   Name=rlmL {ECO:0000255|HAMAP-Rule:MF_01858}; OrderedLocusNames=MS0747;
OS   Mannheimia succiniciproducens (strain MBEL55E).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Basfia.
OX   NCBI_TaxID=221988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBEL55E;
RX   PubMed=15378067; DOI=10.1038/nbt1010;
RA   Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA   Jeong H., Hur C.G., Kim J.J.;
RT   "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT   succiniciproducens.";
RL   Nat. Biotechnol. 22:1275-1281(2004).
CC   -!- FUNCTION: Specifically methylates the guanine in position 2445
CC       (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA.
CC       {ECO:0000255|HAMAP-Rule:MF_01858}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2445) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(2445) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42740, Rhea:RHEA-COMP:10215, Rhea:RHEA-COMP:10216,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.173;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01858};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(2069) in 23S rRNA + S-adenosyl-L-methionine = H(+) +
CC         N(2)-methylguanosine(2069) in 23S rRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43772, Rhea:RHEA-COMP:10688, Rhea:RHEA-COMP:10689,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.264;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01858};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01858}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmKL family.
CC       {ECO:0000255|HAMAP-Rule:MF_01858}.
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DR   EMBL; AE016827; AAU37354.1; -; Genomic_DNA.
DR   RefSeq; WP_011199926.1; NC_006300.1.
DR   AlphaFoldDB; Q65UK6; -.
DR   SMR; Q65UK6; -.
DR   STRING; 221988.MS0747; -.
DR   PRIDE; Q65UK6; -.
DR   EnsemblBacteria; AAU37354; AAU37354; MS0747.
DR   KEGG; msu:MS0747; -.
DR   eggNOG; COG0116; Bacteria.
DR   eggNOG; COG1092; Bacteria.
DR   HOGENOM; CLU_014042_2_0_6; -.
DR   OMA; WIRGYEA; -.
DR   OrthoDB; 307177at2; -.
DR   Proteomes; UP000000607; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052915; F:23S rRNA (guanine(2445)-N(2))-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.150; -; 2.
DR   HAMAP; MF_01858; 23SrRNA_methyltr_KL; 1.
DR   InterPro; IPR017244; 23SrRNA_methyltr_KL.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR000241; RNA_methylase_dom.
DR   InterPro; IPR019614; SAM-dep_methyl-trfase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR004114; THUMP_dom.
DR   Pfam; PF10672; Methyltrans_SAM; 1.
DR   Pfam; PF02926; THUMP; 1.
DR   Pfam; PF01170; UPF0020; 1.
DR   PIRSF; PIRSF037618; RNA_Mtase_bacteria_prd; 1.
DR   SMART; SM00981; THUMP; 1.
DR   SUPFAM; SSF53335; SSF53335; 2.
DR   PROSITE; PS51165; THUMP; 1.
DR   PROSITE; PS01261; UPF0020; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; RNA-binding; rRNA processing;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..715
FT                   /note="Ribosomal RNA large subunit methyltransferase K/L"
FT                   /id="PRO_0000366774"
FT   DOMAIN          43..154
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ   SEQUENCE   715 AA;  81275 MW;  9B4EEF7EC847319C CRC64;
     MKELFATTAR GFEELLKLEL SSLGATECQV AQGGVHFMAD DETQYRALLW SRLSSRILLP
     IVKTKIYSDL DLYSAVVRQN WLAYFDERVR FLVDFNGTNR EIRHTQFGAM RVKDGIVDYF
     ERNGKARPNV DKDYPDIRIH AYLNRDDLVL SLDLSGEALH LRGYREDSGA APLRETLAAA
     IVLRSGWKQG TPLVDPMCGS GTLLIEAAQM EAKIAPQLHR MHWGFDFWRG HNQAAWEKVK
     REAVAMAEAE FNKNPNPHFY GFDLDHRVLQ KAQRNAQNAG VAHLIKWKQG DVAALKNPTP
     EDKGTVICNP PYGERLGTTP ALIALYSVFG QRLKEQFPGW NASIFSSEQG LLDCLRMRSH
     RQFKAKNGPL DCIQKNYQIS DRTLSPENKS AVENAGEFKP NANVATDFAN RLQKNIKKIE
     KWAKQEGIEA YRLYDADLPD YNLAVDHYGD HIVVQEYAAP KNIDENKARQ RLLDAVTATL
     AVTGVETNKL ILKVRQKQKG ANQYEKLANK GEYFYVNEYG AKLWVNLTDY LDTGLFLDHR
     LTRRMVGQMA KGKDFLNLFA YTGSATVHAA LGGAKSTTTV DMSNTYLNWA EQNLILNEAD
     GKQHKLIQAD CLQWLANCAQ QFDLIFVDPP TFSNSKRMED SWDVQRDHIK LMGNLKRILR
     PNGTIVFSNN KRGFKMDFEG LTRLGLKAEE ISAKTLPLDF ERNKQIHNCW IVEFV