SCOPe 2.08: Domain d1nyla2: 1nyl A:8-338

Lineage for d1nyla2 (1nyl A:8-338)

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 Glutaminyl-tRNA synthetase (GlnRS) [52380] (2 species)

7. Species Escherichia coli [TaxId:562] [52381] (17 PDB entries)

8. Domain d1nyla2: 1nyl A:8-338 [80742]
   Other proteins in same PDB: d1nyla1

Details for d1nyla2

PDB Entry: 1nyl, 2.6 Å

PDB Description: Unliganded glutaminyl-tRNA synthetase

PDB Compounds: (A:) glutaminyl-tRNA synthetase

SCOPe Domain Sequences for d1nyla2:

Sequence, based on SEQRES records:

>d1nyla2 c.26.1.1 (A:8-338) Glutaminyl-tRNA synthetase (GlnRS) {Escherichia coli [TaxId: 562]}
tnfirqiidedlasgkhttvhtrfppepngylhighaksiclnfgiaqdykgqcnlrfdd
tnpvkedieyvesikndvewlgfhwsgnvryssdyfdqlhayaielinkglayvdeltpe
qireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivmrd
pvlyrikfaehhqtgnkwciypmydfthcisdalegithslctlefqdnrrlydwvldni
tipvhprqyefsrlnleytvmskrklnllvtdkhvegwddprmptisglrrrgytaasir
efckrigvtkqdntiemaslesciredlnen

Sequence, based on observed residues (ATOM records):

>d1nyla2 c.26.1.1 (A:8-338) Glutaminyl-tRNA synthetase (GlnRS) {Escherichia coli [TaxId: 562]}
tnfirqiidedlasgkhttvhtrfppepngylhighaksiclnfgiaqdykgqcnlrfdd
tnpkedieyvesikndvewlgfhwsgnvryssdyfdqlhayaielinkglayvdeltpeq
ireyrgtltqpgknspyrdrsveenlalfekmraggfeegkaclrakidmaspfivmrdp
vlyrikfaehhqtgnkwciypmydfthcisdalegithslctlefqdnrrlydwvldnit
ipvhprqyefsrlnleytvmskrklnllvtdkhvegwddprmptisglrrrgytaasire
fckrigvkqdntiemaslesciredlnen

Timeline for d1nyla2:

• d1nyla2 first appeared in SCOP 1.63
  
• d1nyla2 appears in SCOPe 2.07