RLMKL_VIBCH
ID RLMKL_VIBCH Reviewed; 708 AA.
AC Q9KRZ5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=VC_1488;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF94643.1; -; Genomic_DNA.
DR PIR; A82195; A82195.
DR RefSeq; NP_231129.1; NC_002505.1.
DR RefSeq; WP_001077794.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KRZ5; -.
DR SMR; Q9KRZ5; -.
DR STRING; 243277.VC_1488; -.
DR DNASU; 2613994; -.
DR EnsemblBacteria; AAF94643; AAF94643; VC_1488.
DR GeneID; 57740149; -.
DR KEGG; vch:VC_1488; -.
DR PATRIC; fig|243277.26.peg.1416; -.
DR eggNOG; COG0116; Bacteria.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_2_0_6; -.
DR OMA; WIRGYEA; -.
DR BioCyc; VCHO:VC1488-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central.
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; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..708
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366846"
FT DOMAIN 43..154
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ SEQUENCE 708 AA; 79833 MW; 80C9C366AA5ADB8F CRC64;
MNQYLAVTSN GLENLLVEEL TQLGINDAKP VQAGVKFKAT NEQIYRCCLW SRLASRFVRI
VAEFKCQNDL DLYLSTTSVN WVNYFHSSKK LVVDFNGTNR EIRNSQYGAM KVKDAIVDCF
TKKNLPRPSI SKDLADLHIH VRLHKENALL GIDMVGSGLH ARGYRTEAGK APLRETLAAA
IILRSGWDAS KPLLDPMCGS GTLLIEAAMM AANIAPGLQR KKWGFEALED FEPELWASVK
SEASVQGKRG VKKVETHFYG VDNDNRVLQT AKDNARRAGV EELISFTLGD AAKVKRPENF
AEGIVICNPP YGERLGTHPG LIALYTAFGA QLKAEFGGCH ASIFSSSDEL LSCLRMRADK
QFKLNNGALP CHQKNYTIAM REQNSVSNEG TQEILIAPDF ANRLKKNFNK IGKWAKREGL
DCFRLYDADL PEYNVAIDVY QDHLMIQEYA APKDIPEEKA KRRLTDIIRA AIQVLDVDAN
NVVLKVRERQ KGTSQYEKLG QQAQTMQITE YGVKLIVNLY DYLDTGLFLD HKITRRRLGQ
MAQGKDFLNL FAYTGSATVH AACGGAKSTT TVDMSKTYLE WAKENMQLNG QVGRQHQYVQ
ADCLQWLANA QSQYDLIFID PPTFSNSKRM EQTFDVQRDH VTLMTNLKRL LRPEGTIVFS
NNKRHFKMDM EALHALGLNA QNISHQTLPL DFERNKQIHN CWLITHQS
