RLMKL_ALTMD
ID RLMKL_ALTMD Reviewed; 699 AA.
AC B4RZ48; F2G293;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=MADE_1010175;
OS Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS ecotype).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1774373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA Johnson J., Friedman R., Rodriguez-Valera F.;
RT "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT Alteromonas macleodii suggests alternative lifestyles associated with
RT different kinds of particulate organic matter.";
RL ISME J. 2:1194-1212(2008).
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; CP001103; AEA98173.1; -; Genomic_DNA.
DR RefSeq; WP_012518498.1; NC_011138.3.
DR AlphaFoldDB; B4RZ48; -.
DR SMR; B4RZ48; -.
DR EnsemblBacteria; AEA98173; AEA98173; MADE_1010175.
DR KEGG; amc:MADE_1010175; -.
DR HOGENOM; CLU_014042_2_0_6; -.
DR OMA; WIRGYEA; -.
DR Proteomes; UP000001870; 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..699
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366727"
FT DOMAIN 44..155
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ SEQUENCE 699 AA; 78010 MW; 458E6107109EAF3F CRC64;
MNTILVTTSR GLDELLKQEV LTLCPDAQIK QGPGTIQFEG SKEDAYKLCL WSRLANRVIW
VLASGKAGDA EALYNTAMGI DWQMQMDSRH TLSVQFIGTN FAIKNTQFGA VRVKDAIVDS
FVEQGLPRPS VERKTPDISV YARLHRDNVI LGIDLAGASL HQRAYRQETG DAPLKEHIAS
AMLMRSGWTE NTDAPLVDLM CGSGTIAIEA AYIARNIAPG IKRSYWGFTK WLGHEATLWD
SLLEDAISVQ KPSCGGGIYA GDFSRKMVAI AKANADFAGV FNDISFSQQD ATKSSPPVAT
PGYVVSNPPY GERLGELTSL IPLFSDWGKR FKEAWKGWHV SLLSSNRDLL RVLKLRATKD
YAMNNGKLEC RLANYVLDEQ NTVQFSEDAG NHEFANRLKK NLKRMKGWVK SANTNCYRIY
DADLPDYNVA VDRYGDWLVV QEYAPPKTVS EDKARKRLQE VLLHLPAVTG VSPKNIALKV
RAQQKGSKQY EKINQSGEMM EVFENGARFL VNLTDYLDTG LFLDHRNTRQ KVKALSQGKD
VLNLFSYTGS VSVFAAMGGA KSVTTVDMSN TYLDWAKKNV ALNKLSGPHA FIQADCTTWL
GTHKGKYDLI FIDPPSFSNS KRMQNTWDVQ RDHVKMLTDA KACLKEQGTI IFSNNKRGFK
LDETAVTALG LQVENITKET IPEDFARKGK IHQCWVLRS