ID   RLMKL_HAEIG             Reviewed;         711 AA.
AC   A5UFS2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
GN   OrderedLocusNames=CGSHiGG_03160;
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; CP000672; ABQ99627.1; -; Genomic_DNA.
DR   RefSeq; WP_012054819.1; NC_009567.1.
DR   AlphaFoldDB; A5UFS2; -.
DR   SMR; A5UFS2; -.
DR   EnsemblBacteria; ABQ99627; ABQ99627; CGSHiGG_03160.
DR   KEGG; hiq:CGSHiGG_03160; -.
DR   HOGENOM; CLU_014042_2_0_6; -.
DR   OMA; WIRGYEA; -.
DR   Proteomes; UP000001990; 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..711
FT                   /note="Ribosomal RNA large subunit methyltransferase K/L"
FT                   /id="PRO_0000366762"
FT   DOMAIN          43..154
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ   SEQUENCE   711 AA;  81371 MW;  418BB4E407E703B9 CRC64;
     MKQLFATTSR GFEELLKVEL TELGAQEAKV VQGGVHYQAD DETLYRTLLW SRLASRILFP
     LIETKIYSDL DLYAAVSGFN WLAQFDERVT FFVDFNGTNQ EIRHTQFGAM RVKDGIVDYF
     ERQGKARPDV DKIQPDVRIH AYLNRENLVI SLDLSGEALH LRGYREDAGQ APLRETLAAA
     IVMRSGWQAG SPLVDPMCGS GTLLIEAAQI EAKIAPQLYR LHWGFDFWKA HNQSAWEKVK
     NEAIELAEEK QREIQPHFYG FDLDHRVLKK AQKNAQNAGV SHLIKWQQAD VAALKNPRLN
     EVGTVICNPP YGERLGTTPA LIALYSVFGQ RLKKEFCGWN VSVFSSESTL LDCLRMRASR
     QFKAKNGPLD CVQKNYQVSE RKSDAITDEK ELEFNRTSEV APDFANRLQK NIKKISKWAK
     QQELDAYRLY DADLPEYNLA VDRYADYIVV QEYAAPKNID ENKARQRLLD AVTATLQVTG
     VETNKLILKV RQKQKGTNQY EKLANKGEYF YVNEYGTQLW VNLTDYLDTG LFLDHRLTRK
     MIGELAKGKD FLNLFAYTGS ATVHAALGGA KSTTTVDMSN TYLNWAEQNL ILNDIEGKQH
     KLIQADCLQW LEKCDRQFDL IFVDPPTFSN SKRMEESWDV QRDHVKLMSN LKRVLSNNGT
     IVFSNNKRGF KMNLVALEEL GLSAVEISHK TLPLDFERNK QIHNCWMIQH I