ID   RLMKL_LEGPA             Reviewed;         707 AA.
AC   Q5X969;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=lpp0022;
OS   Legionella pneumophila (strain Paris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(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; CR628336; CAH11170.1; -; Genomic_DNA.
DR   RefSeq; WP_011212667.1; NC_006368.1.
DR   AlphaFoldDB; Q5X969; -.
DR   SMR; Q5X969; -.
DR   KEGG; lpp:lpp0022; -.
DR   LegioList; lpp0022; -.
DR   HOGENOM; CLU_014042_2_0_6; -.
DR   OMA; WIRGYEA; -.
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; 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..707
FT                   /note="Ribosomal RNA large subunit methyltransferase K/L"
FT                   /id="PRO_0000366771"
FT   DOMAIN          44..155
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ   SEQUENCE   707 AA;  80183 MW;  CE692BD232197F8D CRC64;
     MNYSLFISCS KGLEYLLEDE LKGLGLHVTQ VSPQGVYGEA SLPVIYNLCL WSRLANRIQL
     ILFSGHAAKE QAVHQLCTDF HWQTVFTHDK TIAIEFHGAS EQIRNTMFGA QIVKDGIVDH
     FRRLNGSRPS VDKEKPQILI HAHLKNDILT VSFDLVGYSL HQRGYRKKAG KAPLKENVAA
     AMLLRAKWPE LAAQGYGLHD PFCGSGTLVI EAAMMAAHIA PGLLRQDQSL QYWARHQSSL
     WEKLRTQALQ QVKPLAVKLV GTDADGKIIT LARSNAERAG VLPLVEFNTL PLNACRPGTK
     RGLVVCNPPY GERLGEVTQL VPLYQQLGTT LHTCYQGWQA AILTSSPVLA KALGLRADKQ
     YTLYNGPLEC KLYCLTLSAA NKLKNTPDAP LSDNAQMLFN RLEKNRNHLQ KWARKNQITC
     YRIYDADLPE YAYAIDIYND YAVLQEYAPP ASIPVHKAEK RSLEMLQVVP RALGIHPEKL
     IVKQRKQQKG SEQYQKIGKT SQRLIVTEGK AKLIVNLYDY LDTGLFLDHR LMRLKFAQLE
     PGTRFLNCFC YTASASVHAA LAGALTTNVD LSKTYLLWAE DNFRLNDINL SKHQFLQYDC
     KEWMKTTRDK FDVIFLDPPS FSNSKRMSDI LDIQRDHVSL INMAMRLLNP DGVLYFSTNL
     RQFKLEPMLK EKYAVQDITP QTIDQDFKRN SKIHHCFKIV MPHFADN