CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010196
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosomal RNA large subunit methyltransferase K/L 
Protein Synonyms/Alias
 23S rRNA m2G2445 methyltransferase; rRNA (guanine-N(2)-)-methyltransferase RlmL; 23S rRNA m7G2069 methyltransferase; rRNA (guanine-N(7)-)-methyltransferase RlmK 
Gene Name
 rlmL 
Gene Synonyms/Alias
 rlmK; rlmKL; ycbY; b0948; JW0931 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
113QYGAMKVKDAIVDAFacetylation[1]
174RAGIAPIKETLAAAIacetylation[1]
387AESTPDSKPAMVAEDacetylation[1]
408KNLKKFEKWARQEGIacetylation[1]
448VQEYAPPKTIDAHKAacetylation[1]
640RDHLALMKDLKRLLRacetylation[1]
670MDLDGLAKLGLKAQEacetylation[1]
681KAQEITQKTLSQDFAacetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Methylation occurs before assembly of 23S rRNA into 50S subunits. 
Sequence Annotation
 DOMAIN 43 154 THUMP.
 REGION 1 397 RlmL.
 REGION 398 702 RlmK.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 702 AA 
Protein Sequence
MNSLFASTAR GLEELLKTEL ENLGAVECQV VQGGVHFKGD TRLVYQSLMW SRLASRIMLP 60
LGECKVYSDL DLYLGVQAIN WTEMFNPGAT FAVHFSGLND TIRNSQYGAM KVKDAIVDAF 120
TRKNLPRPNV DRDAPDIRVN VWLHKETASI ALDLSGDGLH LRGYRDRAGI APIKETLAAA 180
IVMRSGWQPG TPLLDPMCGS GTLLIEAAML ATDRAPGLHR GRWGFSGWAQ HDEAIWQEVK 240
AEAQTRARKG LAEYSSHFYG SDSDARVIQR ARTNARLAGI GELITFEVKD VAQLTNPLPK 300
GPYGTVLSNP PYGERLDSEP ALIALHSLLG RIMKNQFGGW NLSLFSASPD LLSCLQLRAD 360
KQYKAKNGPL DCVQKNYHVA ESTPDSKPAM VAEDYTNRLR KNLKKFEKWA RQEGIECYRL 420
YDADLPEYNV AVDRYADWVV VQEYAPPKTI DAHKARQRLF DIIAATISVL GIAPNKLVLK 480
TRERQKGKNQ YQKLGEKGEF LEVTEYNAHL WVNLTDYLDT GLFLDHRIAR RMLGQMSKGK 540
DFLNLFSYTG SATVHAGLGG ARSTTTVDMS RTYLEWAERN LRLNGLTGRA HRLIQADCLA 600
WLREANEQFD LIFIDPPTFS NSKRMEDAFD VQRDHLALMK DLKRLLRAGG TIMFSNNKRG 660
FRMDLDGLAK LGLKAQEITQ KTLSQDFARN RQIHNCWLIT AA 702 
Gene Ontology
 GO:0005737; C:cytoplasm; IC:UniProtKB.
 GO:0052915; F:23S rRNA (guanine(2445)-N(2))-methyltransferase activity; IEA:HAMAP.
 GO:0003723; F:RNA binding; IEA:HAMAP.
 GO:0008990; F:rRNA (guanine-N2-)-methyltransferase activity; IDA:UniProtKB.
 GO:0070043; F:rRNA (guanine-N7-)-methyltransferase activity; IDA:EcoCyc. 
Interpro
 IPR017244; 23SrRNA_methyltr_KL.
 IPR002052; DNA_methylase_N6_adenine_CS.
 IPR002296; N12N6_MeTrfase.
 IPR000241; RNA_methylase_dom.
 IPR019614; SAM-dep_methyl-trfase.
 IPR004114; THUMP. 
Pfam
 PF10672; Methyltrans_SAM
 PF02926; THUMP
 PF01170; UPF0020 
SMART
 SM00981; THUMP 
PROSITE
 PS51165; THUMP
 PS01261; UPF0020 
PRINTS
 PR00507; N12N6MTFRASE.