| Tag | Content |
|---|
| CPLM ID | CPLM-015037 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glutamate--tRNA ligase |
Protein Synonyms/Alias | Glutamyl-tRNA synthetase; GluRS |
Gene Name | gltX |
Gene Synonyms/Alias | RPA2906 |
Created Date | July 27, 2013 |
Organism | Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) |
NCBI Taxa ID | 258594 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 113 | ELTAMRDKARAEGRA | acetylation | [1] |
|
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 | Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (By similarity). |
Sequence Annotation | MOTIF 11 21 "HIGH" region.
MOTIF 240 244 "KMSKS" region.
BINDING 243 243 ATP (By similarity). |
Keyword | Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; Protein biosynthesis. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 473 AA |
Protein Sequence | MTRPVVTRFA PSPTGFLHIG GGRTALFNWL YARKHGGTML LRIEDTDRQR STQEAIDAIL 60
DGLKWLGIDW DGDTVYQFAR AARHREVAEQ LLAAGKAYRC YATAEELTAM RDKARAEGRA 120
KLYDGSWRDR DPSEAPAGVK PTIRLKAPLT GETVIEDQVQ GRVAWQNENL DDLVLLRGDG 180
TPTYMLAVVV DDHDMGVTHV IRGDDHLINA ARQKQIYDAM EWELPVMAHI PLIHGPDGSK 240
LSKRHGALGV DAYRAMGYLP AALRNYLVRL GWSHGDQEIF TTQEMIDAFD LPAIGRSAAR 300
FDFAKLESLN GHYIRQSDDH SLVTLLEDLL KYIPQGPAIA TKFDDSIRAK LTQAMPGLKE 360
RAKTLIELLD NAGFIFADRP LALDPKAQAV LTPETRQLIG RLRAALEDVS PWTAATTEAA 420
MRAFAEQAGL KLGAVAQPLR VALTGRTTSP GIFDVLAVLG RDECLSRLAD QSA 473 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |