Tag | Content |
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CPLM ID | CPLM-015043 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ribosomal RNA large subunit methyltransferase E |
Protein Synonyms/Alias | 23S rRNA Um2552 methyltransferase; rRNA (uridine-2'-O-)-methyltransferase |
Gene Name | rlmE |
Gene Synonyms/Alias | ftsJ; rrmJ; RPA2197 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
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85 | WSQVAAKKVGAADGR | acetylation | [1] | 210 | VKPAASRKDSSERYL | acetylation | [1] |
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Reference | [1] System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases. Crosby HA, Pelletier DA, Hurst GB, Escalante-Semerena JC. J Biol Chem. 2012 May 4;287(19):15590-601. [ PMID: 22416131] |
Functional Description | Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit (By similarity). |
Sequence Annotation | ACT_SITE 179 179 Proton acceptor (By similarity). BINDING 76 76 S-adenosyl-L-methionine; via amide BINDING 78 78 S-adenosyl-L-methionine; via amide BINDING 99 99 S-adenosyl-L-methionine (By similarity). BINDING 115 115 S-adenosyl-L-methionine (By similarity). BINDING 139 139 S-adenosyl-L-methionine (By similarity). |
Keyword | Complete proteome; Cytoplasm; Methyltransferase; rRNA processing; S-adenosyl-L-methionine; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 237 AA |
Protein Sequence | MAKDTTGRMR VTVKSGGRMK LSSKLWLERQ LNDPYVAQAK RDGYRSRAAY KLTEIDDKFR 60 LLKSGMAVVD LGAAPGGWSQ VAAKKVGAAD GRGKVVAIDL LEMGEVPGVT FAQLDFLDPS 120 APERLREMLG GGADIVMSDM AANTTGHRKT DQLRIVGLVE TAAMFASEVL KPGGTFLAKV 180 FQSGADASLM TELKRDYASV KHVKPAASRK DSSERYLLAT GFRGGAARDA EAAAETE 237 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:HAMAP. |
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