SCOPe 2.08: Domain d1e22a2: 1e22 A:161-502

Lineage for d1e22a2 (1e22 A:161-502)

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 folds)

3. Fold d.104: Class II aaRS and biotin synthetases [55680] (1 superfamily)
   contains large mixed beta-sheet

4. Superfamily d.104.1: Class II aaRS and biotin synthetases [55681] (5 families)

5. Family d.104.1.1: Class II aminoacyl-tRNA synthetase (aaRS)-like, catalytic domain [55682] (16 proteins)

6. Protein Lysyl-tRNA synthetase (LysRS) [55685] (3 species)
   contains an insertion of LEM/SAP-like HeH motif, residues 337-379

7. Species Escherichia coli, gene lysU [TaxId:562] [55686] (5 PDB entries)

8. Domain d1e22a2: 1e22 A:161-502 [40715]
   Other proteins in same PDB: d1e22a1
   protein/RNA complex; complexed with acp, gol, lys, mg
   has additional subdomain(s) that are not in the common domain

Details for d1e22a2

PDB Entry: 1e22, 2.43 Å

PDB Description: lysyl-trna synthetase (lysu) hexagonal form complexed with lysine and the non-hydrolysable atp analogue amp-pcp

PDB Compounds: (A:) lysyl-tRNA synthetase

SCOPe Domain Sequences for d1e22a2:

Sequence; same for both SEQRES and ATOM records:

>d1e22a2 d.104.1.1 (A:161-502) Lysyl-tRNA synthetase (LysRS) {Escherichia coli, gene lysU [TaxId: 562]}
dqevryrqryldliandksrqtfvvrskilaairqfmvargfmevetpmmqvipggasar
pfithhnaldldmylriapelylkrlvvggfervfeinrnfrnegisvrhnpeftmmely
mayadyhdlielteslfrtlaqevlgttkvtygehvfdfgkpfekltmreaikkyrpetd
madldnfdaakalaesigitvekswglgrivteifdevaeahliqptfiteypaevspla
rrndvnpeitdrfeffiggreigngfselndaedqaerfqeqvnakaagddeamfydedy
vtaleyglpptaglgigidrmimlftnshtirdvilfpamrp

Timeline for d1e22a2:

• d1e22a2 first appeared (with stable ids) in SCOP 1.55
  
• d1e22a2 appears in SCOPe 2.07