RLMKL_ACTSZ
ID RLMKL_ACTSZ Reviewed; 676 AA.
AC A6VMR3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-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=Asuc_0890;
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z;
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(2010).
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; CP000746; ABR74260.1; -; Genomic_DNA.
DR RefSeq; WP_012072638.1; NC_009655.1.
DR AlphaFoldDB; A6VMR3; -.
DR SMR; A6VMR3; -.
DR STRING; 339671.Asuc_0890; -.
DR PRIDE; A6VMR3; -.
DR EnsemblBacteria; ABR74260; ABR74260; Asuc_0890.
DR KEGG; asu:Asuc_0890; -.
DR eggNOG; COG0116; Bacteria.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_2_0_6; -.
DR OMA; WIRGYEA; -.
DR OrthoDB; 307177at2; -.
DR Proteomes; UP000001114; 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; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..676
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366721"
FT DOMAIN 43..154
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ SEQUENCE 676 AA; 76855 MW; 548A4418057D54CE CRC64;
MKPLFATCAR GFEELLKTEL TELGAQDVRI AQGGVHFGAD DETQYKTLLW SRLASRILLP
IAQSKIYSDL DLYSTVVSQA WLEHFDERTH FFVDFNGTNR EIRHSQFGAM RVKDGIVDYF
ERHGKARPNV DKENPDVRIH AYLNRDDLIL SLDLSGEALH MRGYREDSGQ APLRETLAAA
LVLRSGWQKG TPLVDPMCGS GTLLIEAAQM EAQIAPQLHR SHWGFDFWKG HNQAVWEKVK
AEAVALAEAQ MEKNPLRNGE KGTVLCNPPY GERLGTTPAL IALYSVFGQR LKQQFGGWNV
SVFSSEQGLL DCLRMRSFRQ FKAKNGPLDC VQKNYRISDR SSVQTDERAA ENPAVSADSA
HTDVATDFAN RLQKNIKKIE KWAQQQGLDA YRLYDADLPD YNLAVDRYGD HIVVQEYAAP
KNIDENKTRQ RLLDAVTATL AVTGVETSKL ILKVRRKQKG SNQYEKLANK GEYFYVTEYG
AKLWVNLTDY LDTGLFLDHR LTRKMLGEMA KDKDFLNLFA YTGSATVHAA LGGAKSTTTV
DMSNTYLNWA EQNLILNDVD GKRHKLIQAD CLQWLMRCDK QFDLIFVDPP TFSNSKRMED
SWDVQRDHIK LMKNLKRILR PNGTIVFSNN KRGFKMDFDG LAQLGLNALE ISAKTLPLDF
ERNKQIHNCW LLTRKV
