RLMKL_XANC8
ID RLMKL_XANC8 Reviewed; 711 AA.
AC Q4UT85;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=XC_2689;
OS Xanthomonas campestris pv. campestris (strain 8004).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=314565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8004;
RX PubMed=15899963; DOI=10.1101/gr.3378705;
RA Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT "Comparative and functional genomic analyses of the pathogenicity of
RT phytopathogen Xanthomonas campestris pv. campestris.";
RL Genome Res. 15:757-767(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY49738.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000050; AAY49738.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_011036729.1; NC_007086.1.
DR AlphaFoldDB; Q4UT85; -.
DR SMR; Q4UT85; -.
DR EnsemblBacteria; AAY49738; AAY49738; XC_2689.
DR KEGG; xcb:XC_2689; -.
DR HOGENOM; CLU_014042_2_0_6; -.
DR OrthoDB; 307177at2; -.
DR Proteomes; UP000000420; 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_0000366855"
FT DOMAIN 42..153
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ SEQUENCE 711 AA; 78407 MW; 556D6F0321A20E5E CRC64;
MKFFASCAKG LEYLLADELL ALGASKATAT ISGVNVEGAL RDAQRAVLWS RLASRVLWPL
TEFDCPDEDA LYAGVAELPW HEHLSTGHTL SVDAHVSGTA ITHARYAAQR IKDAVVDTIR
RQGLERPSVD VESPDLRLNL SLRKGRATIS VDLGGGPLHR RGWRMAQNEA PLKENLAAAV
LLRAGWPRAY ADGGGLLDPM CGSGTLLIEG ALMAADVAPG LQRYGSDIPS RWRGFDRDSW
QQLVTEARER DSVGRAALKQ VIHGSDMDPH AIRAAKENAQ VAGVAEAIWF GVREVGDLQT
RPQATGVVVC NPPYDERLAA DAALYRKLGD TLQRVVPQWR ASLLCGNAEL AYATGLRAGK
KYQLFNGAIE CALIVCDPIA VPRRTPLAAP TALSEGAQMV ANRLRKNLQK FKKWRAREGI
ECFRVYDADL PEYSAAIDVY QQADGDRRIF LHVQEYAAPA TIPEADVRRR LGELLAAARE
VFEVPAERVA LKSRERGKGG SKYGRFEQRN EIVNVREHGA LLRVNLFDYL DTGLFLDHRP
LRGTMAQQSK GRRFLNLFCY TGVASVQAAV AGASATTSVD LSGTYLQWCA DNLALNGQAG
SKHKLVQADA LAWLEAERAH FDVIFCDPPT FSNSARAEDF DIQREHVRLL RAAVARLAPG
GVLYFSNNFR RFKLDEEAVS EFAQCEEISP RTIDPDFERH ARIHRAWRLT A