SCOPe 2.08: Domain d1ffya3: 1ffy A:1-200,A:395-644

Lineage for d1ffya3 (1ffy A:1-200,A:395-644)

1. Root: SCOPe 2.08

2. Class c: Alpha and beta proteins (a/b) [51349] (148 folds)

3. Fold c.26: Adenine nucleotide alpha hydrolase-like [52373] (3 superfamilies)
   core: 3 layers, a/b/a ; parallel beta-sheet of 5 strands, order 32145

4. Superfamily c.26.1: Nucleotidylyl transferase [52374] (6 families)

5. Family c.26.1.1: Class I aminoacyl-tRNA synthetases (RS), catalytic domain [52375] (13 proteins)
   contains a conserved all-alpha subdomain at the C-terminal extension

6. Protein Isoleucyl-tRNA synthetase (IleRS) [52387] (2 species)

7. Species Staphylococcus aureus [TaxId:1280] [52389] (3 PDB entries)

8. Domain d1ffya3: 1ffy A:1-200,A:395-644 [31593]
   Other proteins in same PDB: d1ffya1, d1ffya2
   protein/RNA complex; complexed with k, mg, mrc, zn

Details for d1ffya3

PDB Entry: 1ffy, 2.2 Å

PDB Description: insights into editing from an ile-trna synthetase structure with trna(ile) and mupirocin

PDB Compounds: (A:) isoleucyl-tRNA synthetase

SCOPe Domain Sequences for d1ffya3:

Sequence; same for both SEQRES and ATOM records:

>d1ffya3 c.26.1.1 (A:1-200,A:395-644) Isoleucyl-tRNA synthetase (IleRS) {Staphylococcus aureus [TaxId: 1280]}
mdyektllmpktdfpmrgglpnkepqiqekwdaedqyhkaleknkgnetfilhdgppyan
gnlhmghalnkilkdfivryktmqgfyapyvpgwdthglpieqaltkkgvdrkkmstaef
rekckefaleqielqkkdfrrlgvrgdfndpyitlkpeyeaaqirifgemadkgliykgk
kpvywspssesslaeaeieyXphdwrtkkpvifratpqwfasiskvrqdildaientnfk
vnwgktriynmvrdrgewvisrqrvwgvplpvfyaengeiimtketvnhvadlfaehgsn
iwfereakdllpegfthpgspngtftketdimdvwfdsgsshrgvletrpelsfpadmyl
egsdqyrgwfnssittsvatrgvspykfllshgfvmdgegkkmskslgnvivpdqvvkqk
gadiarlwvsstdyladvrisdeilkqtsdd

Timeline for d1ffya3:

• d1ffya3 first appeared (with stable ids) in SCOP 1.55
  
• d1ffya3 appears in SCOPe 2.07