RLMKL_HAHCH
ID RLMKL_HAHCH Reviewed; 717 AA.
AC Q2SCH1;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=HCH_04964;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
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; CP000155; ABC31653.1; -; Genomic_DNA.
DR RefSeq; WP_011398718.1; NC_007645.1.
DR AlphaFoldDB; Q2SCH1; -.
DR SMR; Q2SCH1; -.
DR STRING; 349521.HCH_04964; -.
DR EnsemblBacteria; ABC31653; ABC31653; HCH_04964.
DR KEGG; hch:HCH_04964; -.
DR eggNOG; COG0116; Bacteria.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_2_0_6; -.
DR OMA; WIRGYEA; -.
DR OrthoDB; 307177at2; -.
DR Proteomes; UP000000238; 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 Pfam; PF10672; Methyltrans_SAM; 1.
DR Pfam; PF01170; UPF0020; 1.
DR PIRSF; PIRSF037618; RNA_Mtase_bacteria_prd; 1.
DR SUPFAM; SSF53335; SSF53335; 2.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW rRNA processing; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..717
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366765"
FT DOMAIN 45..142
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
SQ SEQUENCE 717 AA; 80840 MW; EC44005570644E16 CRC64;
MNEFSLFASC PKGLEYVLAD ELKTLGAEVL RTNPAGVEAK VDLAGAYRIC LGSRLANRVL
RLLQSTRTAT RDGLYQAASE VNWSEHLRPG ESYWIAAFGS SGDIRHSRFG AQVVKDAIND
HFRDRDLELP VIDKRSGVQT VQLNLAKTIT LGLDLAGRSL HQRGYRQEGA AAPLKENLAA
AILYRAGWPE ICGEDGCFVD PMCGSGTLVV EAAMIAMNIA PGLLNPHFLF EKAPWHDPEV
WRGVYEEAME KAVLGKRRWR GAIFGCDLNP AAIRTAKRNL SRAGLDRWVK LETASAMDFT
PDTEGCGQRL LVCNPPYGER LGQELELRSL YRALGRRLKT AYGEWKAGIF TSSVNLAKEI
GLRADKQYHL YNGPLATTLY LFDVYGNRPE AETPRKPQNA SLEGISEQAQ MFRNRLSKNL
AKWSKWAKKQ QLSAYRIYDA DMPEYAVAID WYDGGIIVQE YAPPKSVDEE KARQRLLDVL
EVTPAVLGID GGQLFLKQRK KQKGMLQYEK TDSSRKERTV EEHGCRFWVN LSDYLDSGLF
LDHRPTRYWI QKHSSGKRFL NLFCYTGAAS VHAAAGGAAT TTSVDMSQTY LSWAERNFHL
NKLSGPHRFV RANVLDWLKA EHNSYDLIFL DPPTFSNSKK MEDVLDIQRD HAGLIEDCMR
LLAPGGVLIF SCNYRRFKLD SGIEQRFAVE NHTAASIPED FKRNERIHQC WHIRHSA