ID   RLMKL_PASMU             Reviewed;         719 AA.
AC   Q9CNW9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=PM0304;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02388.1; -; Genomic_DNA.
DR   RefSeq; WP_010906576.1; NC_002663.1.
DR   AlphaFoldDB; Q9CNW9; -.
DR   SMR; Q9CNW9; -.
DR   STRING; 747.DR93_1080; -.
DR   EnsemblBacteria; AAK02388; AAK02388; PM0304.
DR   KEGG; pmu:PM0304; -.
DR   PATRIC; fig|272843.6.peg.316; -.
DR   HOGENOM; CLU_014042_2_0_6; -.
DR   OMA; WIRGYEA; -.
DR   Proteomes; UP000000809; 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; Reference proteome; RNA-binding;
KW   rRNA processing; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..719
FT                   /note="Ribosomal RNA large subunit methyltransferase K/L"
FT                   /id="PRO_0000366778"
FT   DOMAIN          43..154
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ   SEQUENCE   719 AA;  81746 MW;  7339F637772A47B6 CRC64;
     MKQLFATTAR GFEELLKVEL TDLGAMDCQI TQGGVHFHAD EETQYRVLLW TRLASRILLP
     IVTCKVYSDL DLYSAVVGQN WLDYFDEKAH FMVDFNGTNR EIRHTQFGAM RVKDGIVDYF
     ERVGKPRPNV DKSQPDIRIH AYLNREELVI SLDLSGDALH MRGYREDTGK APLRETLAAA
     IVLRSGWQLG TPLMDPMCGS GTLLIEAAQM QANIAPQLHR LHWGFDFWKG HNQQAWDKVK
     GEAIELAEQT FNQNQKANFY GCDLDHRVLQ KAKRNAQNAG VAHLIQWQQG DVAALKNPFV
     EAKGTVICNP PYGERLGTTP ALIALYSVFG QRLKQQFADW NVSIFSGEPA LLDCLRLRSH
     RQFKAKNGPL DCVQKNYHIS ARATASDENT QNSPEIDRTL TSSQVAVDFA NRLQKNSKKI
     EKWAKQQGIN AYRLYDADLP EYNLAVDRYD DHIVVQEYAA PKNIDENKAR QRLLDAVTAT
     LQVTGVETNK LILKVRQKQK GTNQYEKLAN KGDYFYVNEY GAKLWVNLTD YLDTGLFLDH
     RLTRKMLGEM AKGKDVLNLF AYTGSATVHM ALGGAKSTTT VDMSNTYLNW AEQNLLLNDL
     EGKQHKLIQA DCLQWLARCD RQFDLIFVDP PTFSNSKRME DSWDVQRDHI KLMTQLKRIL
     RPNGTIVFSN NKRGFKMDVE GLAALGLSAV EISAKTLPLD FERNKQIHNC WVVRLKADL