RLMKL_XANOM
ID RLMKL_XANOM Reviewed; 711 AA.
AC Q2P309;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=XOO2313;
OS Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=342109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 311018;
RA Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT large numbers of effector genes and insertion sequences to its race
RT diversity.";
RL Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE69068.1; -; Genomic_DNA.
DR RefSeq; WP_011408610.1; NC_007705.1.
DR AlphaFoldDB; Q2P309; -.
DR SMR; Q2P309; -.
DR KEGG; xom:XOO2313; -.
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..711
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366859"
FT DOMAIN 42..153
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ SEQUENCE 711 AA; 78145 MW; A074BCDAF66CDCEA CRC64;
MKFFASCAKG LEYLLADELL ALGASKATAT ISGVNVEGEL RDAQRAVLWS RLASRVLWPL
SEFDCPDEDA LYAGVAELPW DAHLSVGHTL SVDAHVSGTA ITHARYAAQR IKDAVVDTMR
RQGLERPSVD VESPDLRLNL SLRKGRATIS VDLGGGPLHR RGWRMAQNEA PLKENLAAAV
LMRGGWPRAY ADGGGLLDPM CGSGTLLIEG ALMAADVAPG LQRYGSDLPS RWRGFDRNGW
QQLVSEARER DSVGRAALKQ VIHGSDMDPH AIRAAKENAQ VAGVAEAIWF GVCEVGELQT
PPQATGVVVC NPPYDERLAA DAALYRRLGD TLQCAVPQWR ASLLCGNAEL AYATGLRAGK
KYQLFNGAIE CALIVCDPIA VPRRTPLAAP TALSEGAQMV ANRLRKNLQK FKKWRAREGV
ECFRAYDADL PEYSAAIDVY QQADGDRRIF LHVQEYAAPA TIPEADVRRR LNELLAAARE
VFEVPAERVA LKSRERGKGG SKYGRFEQRN EIVHVREHGA LLRVNLFDYL DTGLFLDHRP
LRGTMAQQSR GRRFLNLFCY TGVASVEAAV AGAASTTSVD LSGTYLQWCA DNLALNGLAG
SKHKLVQADA LAWLEAERAH FDVIFCDPPT FSNSARAEDF DIQRAHVRLL RAAVARLAPG
GVLYFSNNFR RFKLDEEGVA EFAQCEDISP RTIDPDFERH ARIHRAWRLT A