RLMKL_PSYWF
ID RLMKL_PSYWF Reviewed; 807 AA.
AC A5WGC0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=PsycPRwf_1771;
OS Psychrobacter sp. (strain PRwf-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=349106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRwf-1;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL Submitted (MAY-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000713; ABQ94711.1; -; Genomic_DNA.
DR RefSeq; WP_011960988.1; NC_009524.1.
DR AlphaFoldDB; A5WGC0; -.
DR SMR; A5WGC0; -.
DR STRING; 349106.PsycPRwf_1771; -.
DR EnsemblBacteria; ABQ94711; ABQ94711; PsycPRwf_1771.
DR KEGG; prw:PsycPRwf_1771; -.
DR eggNOG; COG0116; Bacteria.
DR eggNOG; COG1092; Bacteria.
DR HOGENOM; CLU_014042_2_0_6; -.
DR OMA; WIRGYEA; -.
DR OrthoDB; 307177at2; -.
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; RNA-binding; rRNA processing;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..807
FT /note="Ribosomal RNA large subunit methyltransferase K/L"
FT /id="PRO_0000366801"
FT DOMAIN 67..182
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01858"
FT REGION 548..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 91670 MW; 08B956509E6E58B8 CRC64;
MSTPENTLVT PNTSDTIPTA SAAKRYDIVV TCADGLEAPL QTELSHMDIS HELKSTGRIA
VNATLEQIYK ICLWSRVASR VLLPIKKRNI NKEYDVAEQL NGLARTVDWT EWFELDNTFA
IRMSVDKRVQ VSQQFAMLRI KDAIADTFSE KLDARPDVDS NNPDFPIYAT VNEKQAEIFL
DLSGTSLHRR GYRVAMTDAP LKENLAAGLL YTVGWHKTKN SYSALIDPMC GSGTFIIEAL
LMHCDYPVGI DKAESQFGFY NWQEHDSELW QQCVVQAQER FHNGLQKAAA GKLPTILGFD
ADAGAIKAVH KNLIAAGLIE LIPHLTLEQR PLSQLKIALA KPLLDRKLKR PLVITNPPYG
ERLGESDFIK PLYQGLGLTL QEIFAKQKYQ PMLGLLAAHV EQADVLPIED PQTLRCHNGA
ITVYFRHGQL IRKEGESLIT RFEKTEIKVD EAQDFVNRLQ KNVNHLKKLA AKEDVTNLRV
YDADLPDYKV AIDVYGDYVH VQEWAPPKSI PPETARKRFN LALMGIREVF GINREQIFIK
TRARQVGNTQ YGNPEASAQS KESKNAPEPK KDNRNRYKGN KFQQAREEAK RQEAQRLAQK
KRKMHVVQED GAYFYVNFTD YLDTGLFIDH RNMRSMIRSA SRGADVLNLF AYTCTASVHA
ALGGAKSVTS VDLSQNYLDW GKQNFALNGL DVTTSRYQFI ASDIFDWIKD NTDQFDVIFI
DPPTFSNSKK FQGTFDVQRD HTALINRAMN RLANGGVIYF SNNFTKFELD EELYDRYEVT
EITSETIGFD FNPKKPIHHS FEIRHKL
