Tag | Content |
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CPLM ID | CPLM-015029 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | 50S ribosomal protein L1 |
Protein Synonyms/Alias | RRP-L1 |
Gene Name | rplA |
Gene Synonyms/Alias | RPA3272 |
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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36 | VKERAISKFDETIEV | acetylation | [1] | 128 | PLVGRLGKVLGPRGM | 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 | Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release (By similarity). |
Sequence Annotation | |
Keyword | Complete proteome; Repressor; Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Translation regulation; tRNA-binding. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 229 AA |
Protein Sequence | MAIGKRLKKI REGIDRTKLY PLDEAVKLVK ERAISKFDET IEVAINLGVD PRHADQMVRG 60 VVMLPNGTGR TVRVGVFARG AKADEAKAAG ADVVGAEDLV EQVQAGNINF DRCIATPDMM 120 PLVGRLGKVL GPRGMMPNPK IGTVTMDVAG AVKGAKGGSV EFRVEKAGII QAGVGKASFD 180 ADKLVENIKA LADAVNKAKP SGAKGTYIQR VAVSSTMGPG VKVEPGTVH 229 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |