RLMKL_FRATN
ID RLMKL_FRATN Reviewed; 718 AA.
AC A0Q621;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=FTN_0798;
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112;
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(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; CP000439; ABK89686.1; -; Genomic_DNA.
DR RefSeq; WP_003038988.1; NZ_CP009633.1.
DR AlphaFoldDB; A0Q621; -.
DR SMR; A0Q621; -.
DR EnsemblBacteria; ABK89686; ABK89686; FTN_0798.
DR GeneID; 60807011; -.
DR KEGG; ftn:FTN_0798; -.
DR OMA; WIRGYEA; -.
DR OrthoDB; 307177at2; -.
DR BioCyc; FTUL401614:G1G75-833-MON; -.
DR Proteomes; UP000000762; 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..718
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366755"
FT DOMAIN 44..155
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ SEQUENCE 718 AA; 83680 MW; 98D7D1B3DEDF30AB CRC64;
MQKFTFFVSC AKGIELLLKD ELERLGISSQ EKLAGVEFEG SIKDAYKVCI YSYLASQVML
KVATDKVINQ QDLYEFISSI NWMDYFAVDK TFKIIISGKH YDFNNTMFVS QKTKDAIVDQ
FRNVTNQRPN IDTENPDNVI KLHLHKQFVN VFLCLNIDSL HKRSYRQFQG QAPLKESLAA
AILIKAGWLE ELKKHQPILI DPMCGSGTIL IEAALMAKNI APVLLNKEFK IFNSKFHNKE
LWDNLLEIAK NSQKVTNAII CGFDIDNNVL DKAQRNIYQA GVEDVVTVKR QDIRDLENEF
ESEGLIVTNP PYGERLYGDQ LDELLDIFNG FGDRLSQDFY GWKVAVLTSF ADSIKEMQLR
TTKRNKFYNG AIETILYQFE INEHAKFKHE TQLEKNIRIA EASVQKSDEH IDFANKLKKN
LKSLKPWLKQ TGLECYRLYD ADIPTFAVAV DVYGEHIFLQ EYRADATIDQ NIAKQRFYQA
IYQIHKTLDI KYENIHTRVR QRQKGKEQYQ KENDKNKFHI INEFDAKFYV NFDDYLDTGI
FLDHRKIRQL VAKAAKNKTL LNLFSYTCTA SVHAALKGAK TTSVDMSNTY LEWGKNNFEL
NKLDIKKHSF IQADCISWLK TNKDKFDVIF LDPPTFSNSK RMDDILDIQR DHELLINLAM
DSLKKDGILY FSNNYRRFKM SPQILEKFNC ENIDKICLSR DFLSNKNIHN CWEIKYKK
