SCOPe 2.08: Domain d1r6ta2: 1r6t A:82-466

Lineage for d1r6ta2 (1r6t A:82-466)

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 Tryptophanyl-tRNA synthetase (TrpRS) [52378] (5 species)
   overall structure is similar to TyrRS

7. Species Human (Homo sapiens) [TaxId:9606] [102256] (13 PDB entries)
   Uniprot P23381 94-471

8. Domain d1r6ta2: 1r6t A:82-466 [97161]
   Other proteins in same PDB: d1r6ta1, d1r6ta3, d1r6tb2
   complexed with gol, tym

Details for d1r6ta2

PDB Entry: 1r6t, 2.1 Å

PDB Description: crystal structure of human tryptophanyl-trna synthetase

PDB Compounds: (A:) Tryptophanyl-tRNA synthetase

SCOPe Domain Sequences for d1r6ta2:

Sequence; same for both SEQRES and ATOM records:

>d1r6ta2 c.26.1.1 (A:82-466) Tryptophanyl-tRNA synthetase (TrpRS) {Human (Homo sapiens) [TaxId: 9606]}
edfvdpwtvqtssakgidydklivrfgsskidkelinrieratgqrphhflrrgiffshr
dmnqvldayenkkpfylytgrgpsseamhvghlipfiftkwlqdvfnvplviqmtddeky
lwkdltldqaygdavenakdiiacgfdinktfifsdldymgmssgfyknvvkiqkhvtfn
qvkgifgftdsdcigkisfpaiqaapsfsnsfpqifrdrtdiqclipcaidqdpyfrmtr
dvaprigypkpallhstffpalqgaqtkmsasdpnssifltdtakqiktkvnkhafsggr
dtieehrqfggncdvdvsfmyltffledddkleqirkdytsgamltgelkkalievlqpl
iaehqarrkevtdeivkefmtprkl

Timeline for d1r6ta2:

• d1r6ta2 first appeared in SCOP 1.67
  
• d1r6ta2 appears in SCOPe 2.07