RLMKL_PSEA7
ID RLMKL_PSEA7 Reviewed; 725 AA.
AC A6V328;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=PSPA7_2090;
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7;
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) 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; CP000744; ABR81760.1; -; Genomic_DNA.
DR RefSeq; WP_012075110.1; NC_009656.1.
DR AlphaFoldDB; A6V328; -.
DR SMR; A6V328; -.
DR PRIDE; A6V328; -.
DR EnsemblBacteria; ABR81760; ABR81760; PSPA7_2090.
DR KEGG; pap:PSPA7_2090; -.
DR HOGENOM; CLU_014042_2_0_6; -.
DR OMA; WIRGYEA; -.
DR OrthoDB; 307177at2; -.
DR Proteomes; UP000001582; 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..725
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366786"
FT DOMAIN 46..157
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
FT REGION 393..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 81095 MW; E0C34472B27C0642 CRC64;
MADVYELFLT CPKGLESLLL EEAQGLGLSE ARAQVSAVRG QGSLEVAYRL CLWSRLANRV
LLVLARFPVE NAESMYLAVH AVNWEDHLDA GGTLAVEFSG KGSGIDNTHF GALKVKDAIV
DNLRERSGRR PSVDKVNPDV RVHLHLDRGQ ATLSLDLSGH SLHQRGYRLQ QGAAPLKENL
AAAVLIRAGW PKIAAEGGAL ADPMCGVGTF LVEAALMAAD IAPNLRRERW GFSNWLGHVP
ALWRKLHEEA QQRAAAGLAR APLWIRGYEA DPRLIQPARN NIERAGVADW VKIYQGELAT
FEPRPDKGQA GLVICNPPYG ERLGDEASLL YLYQNLGERL RQSCIGWSAG VFTGAPELGK
RMGIRSHKQY AFWNGALACK LLMIQVEPRQ FVTGERGERN DDGQARAPSE PARLSEGGQM
FANRLQKNLR QLGKWARRDK VECYRLYDAD MPEYALAVDI YGDWVHVQEY AAPKSVDPAK
AQARLFDALA AIPQALGVAQ ERVVVKRRER QAGKKQYERQ SSEGKFLEVG EGGVRLLVNL
TDYLDTGLFL DHRPMRLRIQ KEAAGKRFLN LFCYTATATV HAARGGARST TSVDLSKTYL
DWARRNLSLN GFSDRQRLVH SDVMEWLRED DGQYELIFID PPTFSNSKRM EGVFDVQRDQ
VELLDLAMAR LAPGGVLYFS NNFRKFELDE SVQARYAVEE ITGETLDPDF ARNPKIHRAW
RITVR
