Tag | Content |
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CPLM ID | CPLM-026633 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Elongation factor G, EF-G |
Protein Synonyms/Alias | |
Gene Name | RPA4328 |
Gene Synonyms/Alias | |
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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364 | GDVVALGKLDTIKTG | 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 | |
Sequence Annotation | |
Keyword | Complete proteome; Elongation factor; GTP-binding; Hydrolase; Nucleotide-binding; Protein biosynthesis. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 683 AA |
Protein Sequence | MGQDVRSPRG PRCIALVGPF QSGKTTLLEA ILARTGAIPR AGSVDAGTSH GDSSPEARQH 60 KMGLSLTAVT TQFMGESYTF LDCPGSVEFA HDMRAALPAV DAAVVVCEAD ERKLPQLQLI 120 LRELEDLGIP RFLFLNKIDR ANKRIREVLD SLQPASRIPL VLRQIPIWNG DLIAGYVDLA 180 LERAFVYREH KPSEVIDLEG GNLDREKEAR FSMLEKLADH DDALMEQLLD DIQPPRDAVF 240 DDLARELREG VICPVLLGSA LRENGVLRLL KALRHEAPDV TETAARLGVT AGKDAVGYVF 300 KTQHLQHGGK LSLARLFAGT LADGDNVQSS SGEASRVSGM QAVGGGHDSK RSSATAGDVV 360 ALGKLDTIKT GDTFGNGKTA PASLVEVTAA PPVLAMALAA ADRKDDVKLG QALQRLNEED 420 PSLTIVHDPQ SHEMVLWGQG EMHLRVALER LHDRYGVTVK SHAPGIGYRE TIRKPVTQRG 480 RHKKQSGGHG QFGDVVLDIK PLARGEGFAF AETVVGGAVP RNYMGAVEEG VIDALRAGPL 540 GFPVVDVHVT LTDGSYHSVD SSDQAFRTAA RIGITEALPQ CQPVLLEPIH TVEIVCPTEA 600 TAKVNAILSG RRGQILGFDT RDGWPGWDMV RATMPEAEIG DLIVELRSAT AGAGSFTRSF 660 DHMAEVSGRT ADQIVAAHRQ AAA 683 |
Gene Ontology | GO:0005525; F:GTP binding; IEA:UniProtKB-KW. GO:0003924; F:GTPase activity; IEA:InterPro. GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. GO:0006184; P:GTP catabolic process; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |