ID   RLMKL_FRATF             Reviewed;         717 AA.
AC   A7NCY2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=FTA_1360;
OS   Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=458234;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FTNF002-00 / FTA;
RX   PubMed=19756146; DOI=10.1371/journal.pone.0007041;
RA   Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D., Jay J.J.,
RA   Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H., Zhou L.W.,
RA   Lion C., Dempsey M.P.;
RT   "Complete genome sequence of Francisella tularensis subspecies holarctica
RT   FTNF002-00.";
RL   PLoS ONE 4:E7041-E7041(2009).
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; CP000803; ABU61835.1; -; Genomic_DNA.
DR   RefSeq; WP_003016450.1; NC_009749.1.
DR   AlphaFoldDB; A7NCY2; -.
DR   SMR; A7NCY2; -.
DR   KEGG; fta:FTA_1360; -.
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; 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..717
FT                   /note="Ribosomal RNA large subunit methyltransferase K/L"
FT                   /id="PRO_0000366751"
FT   DOMAIN          44..155
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ   SEQUENCE   717 AA;  83482 MW;  E2F7874A05847BF5 CRC64;
     MQKFTFFVSC AKGIELLLKD ELERLGISSQ EKLAGVEFEG SIKDAYKVCI YSYLASQVML
     KVATDKVINQ QDLYEFISSI NWMDYFAVDK TFKIIISGKH YDFNNTMFVS QKTKDAIVDQ
     FRNVINQRPN IDTENPDNVI KLHLHKQFVN VFLCLNIDSL HKRSYRQFQG QAPLKESLAA
     AILIKAGWLE ELKKHQPILI DPMCGSGTIL IEAALMAKNI APVLLNKEFK IFNSKFHNQE
     LWDNLLEIAK NSQKVTNAII CGFDIDNNVL DKAQRNIYQA GVEDVVTVKR QDIRDLENEF
     ESEGLIVTNP PYGERLYGDQ LDELLDIFNG FGDRLSQDFY GWKVAVLTSF ADSIKEMQLR
     TTERNKFYNG AIETILYQFK INEHAKFKHE TQLEKNIRIA EASAQKSDEH IDFANKLKKN
     LKSLKPWLKQ TGLECYRLYD ADIPTFAVAV DVYSEHIFLQ EYRADATIDQ NIAKQRFYQA
     IYQIHKTLDI KYENIHTRVR QRQKGKEQYQ KENDKNKFHI INEFDAKFYV NFDDYLDTGI
     FLDHRKIRQL VAKAAKNKTL LNLFSYTCTA SVHAALKGAK TTSVDMSNTY LEWGKNNFTL
     NNIDAKKHSF IQADCISWLK TNKDKFDVIF LDPPTFSNSK RMDDILDIQR DHELLINLAM
     DSLKKDGILY FSNNYRRFKM SPQILEKFNC ENIDKICLSR DFLSNKNIHN CWEIKYK