ID   RLMKL_XYLF2             Reviewed;         724 AA.
AC   B2IA87;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 70.
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=XfasM23_2125;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACB93523.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001011; ACB93523.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011098330.1; NC_010577.1.
DR   AlphaFoldDB; B2IA87; -.
DR   SMR; B2IA87; -.
DR   EnsemblBacteria; ACB93523; ACB93523; XfasM23_2125.
DR   GeneID; 58017541; -.
DR   KEGG; xfn:XfasM23_2125; -.
DR   HOGENOM; CLU_014042_2_0_6; -.
DR   Proteomes; UP000001698; 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; 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..724
FT                   /note="Ribosomal RNA large subunit methyltransferase K/L"
FT                   /id="PRO_0000366863"
FT   DOMAIN          42..153
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ   SEQUENCE   724 AA;  78819 MW;  67EB78D61125BC39 CRC64;
     MRFFVSCAKG LEYLLVDEVL ALGAAGATAT VAGVNVEGGL CDAQRLVLWS RLASRVLWPL
     AAFACADEDA LYAGVAALPW VEHVLPGQTL AVDAHVSGEA ITHARYAAQR VKDAVVDTLR
     DAGVVRPSVD VEHPDVRLNL SLRKGRATLS VDLGGRALHH RGWRQAPHAA SLKEHLAAAV
     LLRAGWAKVY AEGGGLLDPM CGSGTLLIEG ALMVADVAPG LSRYADPDAM SHVSVAERPV
     LLPSRWRGFD VVAWEALVVD AQQRARRGLA ELRPVLHGSD IDPRALGAAF ANARAAGVQD
     AIEFVVAGID VLPAVSEPHG VVVCNAPYDV RLAADPGLYR HLGDALRRVV PRWRAALVCG
     SSTLAFATGL RADKKYQFFN GALECVLIVC DPVVPLAREA GGAQALSEGA QMAANRLRKN
     VQRLKKWRIR AGVECYRVYD ADLPEYAAAI DVYQEVDGAR RLFLHVQEYA APASIPEGDV
     RRRRHELLAA VRAVFDVSVA QVALKTRQRG KGGSQYGCFA QRGEFFHVCE HGALLRVNLF
     DYLDTGLFLD HRPLRGRMAR EAVGKRFLNV FCYTGVASVE AAVAGAAATT SVDLSSTYLH
     WCTDNFALNG QGGVRHRLVQ ADALAWLEAE RGQYDVIFCD PPTFSNSARA DDFDVQRDHV
     RLLRAAVARL TPGGVLYFSN NFRRFRLDVD AVAAFAQCEE ISPVTIDLDF SRNTRIHRTW
     LLWR