Tag | Content |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Glutamate--tRNA ligase |
Protein Synonyms/Alias | GluRS |
Gene Name | gltX |
Gene Synonyms/Alias | SSO0093; ORFNames=C04029, C05_017 |
Created Date | 3-June-2014 |
Organism | Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) |
NCBI Taxa ID | 273057 |
Phosphorylation | Position | Peptide | Code | Type | References | 14 | LRETIYKYALQNAVK | Y | HTP | [1] | |
Reference | [1]Change of carbon source causes dramatic effects in the phospho-proteome of the archaeon Sulfolobus solfataricus. Esser D,Pham TK,Reimann J,Albers SV,Siebers B,Wright PC J. Proteome Res. 2012, Oct, 5;11(10):4823-33. [ PMID:22639831] |
Functional Description From UniProt | FUNCTION: 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) |
| |
| Aminoacyl-tRNAsynthetase; ATP-binding; Completeproteome; Cytoplasm; Ligase; Nucleotide-binding; Proteinbiosynthesis; Referenceproteome |
Protein Sequence | MMELNELRET IYKYALQNAV KHNGKAETGP VMSKIIAERP ELRSNAREIV KIIKEIIEQV 60 NSLTLEQQLT EIKAKYPELL EEKKHEEKRK VLPPLPNVKG QVVTRFAPNP DGPLHLGNAR 120 SAILSYEYAK MYNGKFILRF DDTDPKVKRP ILDAYDWIKE DLKWLGIKWE QELYASERLE 180 LYYKYARYLI EKGYAYVDTC DSSIFRKFRD SRGKMKEPEC LHRSSSPESN LELFEKMLGG 240 KFKEGEAVVR LKTDLSDPDP SQIDWVMLRI IDTAKNPHPR VGSKYWVWPT YNFASIIDDH 300 ELGITHVLRA KEHMSNTEKQ RYISEYMGWE FPEVLQFGRL RLEGFMMSKS KIRGMLEKGT 360 NRDDPRLPTL AGLRRRGILP DTIKDVIIDV GVKVTDATIS FENIAAINRK KLDPVAKRIM 420 FVKDAEEFSV ELPESLNAKI PLIPSKQEMN RTIIVNPGDK ILIESNDAED NSILRLMELC 480 NVKVDKHNRK LIFHSKTLDE AKKVNAKIVQ WVKSNEKVPV MVEKAERDEI KMINGYAEKI 540 AADLEIDEIV QFYRFGFVRV DRKDENMLRV VFSHD 575 |
| GO:0005737 C:cytoplasm IEA:UniProtKB-SubCell GO:0005524 F:ATP binding IEA:UniProtKB-HAMAP GO:0004818 F:glutamate-tRNA ligase activity IEA:UniProtKB-HAMAP GO:0006424 P:glutamyl-tRNA aminoacylation IEA:UniProtKB-HAMAP |
| |
| |
| |
| |
| |