CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010199
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ribosomal RNA large subunit methyltransferase I 
Protein Synonyms/Alias
 23S rRNA m5C1962 methyltransferase; rRNA (cytosine-C(5)-)-methyltransferase RlmI 
Gene Name
 rlmI 
Gene Synonyms/Alias
 yccW; b0967; JW5898 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
48DIVDHQGKWLARGAYacetylation[1]
88RRLQQAQKWRDWLAQacetylation[1]
201VDIQHGHKTGYYLDQacetylation[1]
267RQNVELNKLDLSKAEacetylation[1]
272LNKLDLSKAEFVRDDacetylation[1]
282FVRDDVFKLLRTYRDacetylation[1]
293TYRDRGEKFDVIVMDacetylation[1]
303VIVMDPPKFVENKSQacetylation[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 cytosine at position 1962 (m5C1962) of 23S rRNA. Methylation occurs before assembly of 23S rRNA into 50S subunits. 
Sequence Annotation
 DOMAIN 2 81 PUA.  
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
 396 AA 
Protein Sequence
MSVRLVLAKG REKSLLRRHP WVFSGAVARM EGKASLGETI DIVDHQGKWL ARGAYSPASQ 60
IRARVWTFDP SESIDIAFFS RRLQQAQKWR DWLAQKDGLD SYRLIAGESD GLPGITIDRF 120
GNFLVLQLLS AGAEYQRAAL ISALQTLYPE CSIYDRSDVA VRKKEGMELT QGPVTGELPP 180
ALLPIEEHGM KLLVDIQHGH KTGYYLDQRD SRLATRRYVE NKRVLNCFSY TGGFAVSALM 240
GGCSQVVSVD TSQEALDIAR QNVELNKLDL SKAEFVRDDV FKLLRTYRDR GEKFDVIVMD 300
PPKFVENKSQ LMGACRGYKD INMLAIQLLN EGGILLTFSC SGLMTSDLFQ KIIADAAIDA 360
GRDVQFIEQF RQAADHPVIA TYPEGLYLKG FACRVM 396 
Gene Ontology
 GO:0005737; C:cytoplasm; IC:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0009383; F:rRNA (cytosine-C5-)-methyltransferase activity; IDA:EcoCyc.
 GO:0042710; P:biofilm formation; IMP:EcoCyc.
 GO:0070475; P:rRNA base methylation; IMP:EcoCyc. 
Interpro
 IPR002478; PUA.
 IPR015947; PUA-like_domain.
 IPR023542; rRNA_lsu_MeTfrase_I.
 IPR019614; SAM-dep_methyl-trfase. 
Pfam
 PF10672; Methyltrans_SAM 
SMART
 SM00359; PUA 
PROSITE
 PS50890; PUA 
PRINTS