| 000 | 01813 a2200529 4500 | ||
|---|---|---|---|
| 005 | 20250513043417.0 | ||
| 264 | 0 | _c19950720 | |
| 008 | 199507s 0 0 eng d | ||
| 022 | _a0022-2844 | ||
| 024 | 7 |
_a10.1007/BF00166618 _2doi |
|
| 040 |
_aNLM _beng _cNLM |
||
| 100 | 1 | _aEriani, G | |
| 245 | 0 | 0 |
_aThe class II aminoacyl-tRNA synthetases and their active site: evolutionary conservation of an ATP binding site. _h[electronic resource] |
| 260 |
_bJournal of molecular evolution _cMay 1995 |
||
| 300 |
_a499-508 p. _bdigital |
||
| 500 | _aPublication Type: Comparative Study; Journal Article | ||
| 650 | 0 | 4 |
_aAdenosine Triphosphate _xmetabolism |
| 650 | 0 | 4 | _aAllosteric Site |
| 650 | 0 | 4 | _aAmino Acid Sequence |
| 650 | 0 | 4 |
_aAmino Acyl-tRNA Synthetases _xchemistry |
| 650 | 0 | 4 |
_aAspartate-tRNA Ligase _xchemistry |
| 650 | 0 | 4 |
_aBacterial Proteins _xchemistry |
| 650 | 0 | 4 | _aBinding Sites |
| 650 | 0 | 4 | _aBiological Evolution |
| 650 | 0 | 4 | _aConsensus Sequence |
| 650 | 0 | 4 |
_aFungal Proteins _xchemistry |
| 650 | 0 | 4 | _aModels, Molecular |
| 650 | 0 | 4 | _aMolecular Sequence Data |
| 650 | 0 | 4 | _aProtein Binding |
| 650 | 0 | 4 | _aProtein Conformation |
| 650 | 0 | 4 |
_aRNA, Transfer _xmetabolism |
| 650 | 0 | 4 |
_aRNA, Transfer, Asp _xmetabolism |
| 650 | 0 | 4 |
_aSaccharomyces cerevisiae _xenzymology |
| 650 | 0 | 4 | _aSequence Alignment |
| 650 | 0 | 4 | _aSequence Homology, Amino Acid |
| 650 | 0 | 4 | _aSpecies Specificity |
| 650 | 0 | 4 | _aStructure-Activity Relationship |
| 700 | 1 | _aCavarelli, J | |
| 700 | 1 | _aMartin, F | |
| 700 | 1 | _aAdor, L | |
| 700 | 1 | _aRees, B | |
| 700 | 1 | _aThierry, J C | |
| 700 | 1 | _aGangloff, J | |
| 700 | 1 | _aMoras, D | |
| 773 | 0 |
_tJournal of molecular evolution _gvol. 40 _gno. 5 _gp. 499-508 |
|
| 856 | 4 | 0 |
_uhttps://doi.org/10.1007/BF00166618 _zAvailable from publisher's website |
| 999 |
_c7782591 _d7782591 |
||