RLMKL_PSEPG
ID RLMKL_PSEPG Reviewed; 730 AA.
AC B0KG92;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=PputGB1_1608;
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000926; ABY97513.1; -; Genomic_DNA.
DR RefSeq; WP_012271277.1; NC_010322.1.
DR AlphaFoldDB; B0KG92; -.
DR SMR; B0KG92; -.
DR STRING; 76869.PputGB1_1608; -.
DR EnsemblBacteria; ABY97513; ABY97513; PputGB1_1608.
DR KEGG; ppg:PputGB1_1608; -.
DR eggNOG; COG0116; Bacteria.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_2_0_6; -.
DR OMA; WIRGYEA; -.
DR Proteomes; UP000002157; 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.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; RNA-binding; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..730
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366792"
FT DOMAIN 46..157
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
FT REGION 395..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 730 AA; 82307 MW; 09F9970DA9B1B239 CRC64;
MSDRFELYLT CPKGLEGLLA EEAKGLGLEE VREHTSAIRG AADMETAYRL CVWSRLANRV
LLVLKRFSMK NADDLYDGVN AVDWADHLAA DGTLAVEFSG HGSGIDNTHF GALKVKDAIV
DKLRNREGLR PSVEKIDPDV RVHLRLDRGE AILSLDLSGH SLHQRGYRLQ QGAAPLKENL
AAAVLIRSGW PRIAAEGGAL ADPMCGVGTF LVEAAMIAAD IAPNLKRERW GFSAWLGHVP
ALWRKVHDEA QARAQAGLAK PPLWIRGYEA DPRLIQPGRN NVERAGLGDW VKIYQGEVST
FEPRPDQNQK GLVISNPPYG ERLGDEASLL YLYQNLGERL RQACMGWEAA VFTGAPQLGK
RMGIRSHKQY AFWNGALPCK LLLFKVQPDQ FVTGERREAQ PEGTEVRQQA PQASEPARLS
EGAQMFANRL QKNLKQLGKW ARREQIDCYR LYDADMPEYA LAVDLYQDWV HVQEYAAPRS
IDPDKAQARL LDALAAIPQA LGISPQRVVL KRRERQSGTR QYERQATEGR FQEVNEGGVK
LLVNLTDYLD TGLFLDHRPM RMRIQREAAG KRFLNLFCYT ATATVHAAKG GARSTTSVDL
SKTYLDWARR NLALNGYSER NRLEQSDVMA WLEGNRDSYD LIFIDPPTFS NSKRMEGVFD
VQRDHVQLLD LAMARLAPGG VLYFSNNFRK FQLDEHLMAR YAVEEITAQT LDPDFARNNR
IHRAWRLQLR
