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RLMKL_SHESM
ID   RLMKL_SHESM             Reviewed;         713 AA.
AC   Q0HJZ9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Shewmr4_1540;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-2006) 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; CP000446; ABI38618.1; -; Genomic_DNA.
DR   RefSeq; WP_011622322.1; NC_008321.1.
DR   AlphaFoldDB; Q0HJZ9; -.
DR   SMR; Q0HJZ9; -.
DR   KEGG; she:Shewmr4_1540; -.
DR   HOGENOM; CLU_014042_2_0_6; -.
DR   OMA; WIRGYEA; -.
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; 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..713
FT                   /note="Ribosomal RNA large subunit methyltransferase K/L"
FT                   /id="PRO_0000366832"
FT   DOMAIN          43..154
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ   SEQUENCE   713 AA;  80033 MW;  25DE38B271A0FF93 CRC64;
     MLNFFAAAPK GFEYSLAQEL TEFGATEIKE SVAGVYFTAP LALAYRITLW TRLASRIVLV
     IYKGPCESAE QLYNAAYCID WSSHFSNRNT FSIDFHGTGG FINNTQFGAL KIKDAIVDRF
     RDDGDARPNV ARIDADIKID AHFRNGVITI AMNFSGPSLH QRGYRSTTGE APLKENLAAN
     MLVRSGWKAA PTTLLDPFCG SGTVLIEAAL MAADIAPGLQ RSRFGFEHWR RHDKATWHEI
     LEEAKARASL GVKRCDVKFY GSDIDSRLVA LAKRNAQNAG VLELIDFKVA NALNVEPPAG
     EGYLITNPPY GERLGSVSEL LQLYYQLGDK FKKEFGGWKV AMLCSDIELI SALKLKADKQ
     MKMFNGALEC AFNLYTLHAQ STRRDTPVLP EGVDIADIAP AFANRIKKNA KQLEKWAKKE
     GIDSYRLYDA DIPEYNVAVD RYLDHIVVQE YMAPASIPEA VTKRRLSDVL LALPAAIGVD
     PHKITMKTRE RQKGTNQYQK LDERKLELIT TEYGAKFKLN LTGYLDTGLF LDHRLTRRLV
     GQKSKGRRVL NLFSYTGSAS VHAALGGAKS VTTVDMSNTY LAWAKENFAL NDLSGKQYEF
     VQADCLQWIR DSALDKSAQY DLIFIDPPTF SNSKRMEDSF DVQRDHVNLL GMLIKLLSPN
     GEIVFSNNKR KFKMDTETLA KMKIKVENID DLTLPMDYKR NPHIHNTWLI THA
 
 
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