SCOP 1.73: Domain d1f4la2: 1f4l A:4-140,A:176-388

Lineage for d1f4la2 (1f4l A:4-140,A:176-388)

1. Root: SCOP 1.73

2. Class c: Alpha and beta proteins (a/b) [51349] (141 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] (5 families)

5. Family c.26.1.1: Class I aminoacyl-tRNA synthetases (RS), catalytic domain [52375] (12 proteins)
   contains a conserved all-alpha subdomain at the C-terminal extension

6. Protein Methionyl-tRNA synthetase (MetRS) [52384] (3 species)

7. Species Escherichia coli [TaxId:562] [52386] (9 PDB entries)

8. Domain d1f4la2: 1f4l A:4-140,A:176-388 [59649]
   Other proteins in same PDB: d1f4la1, d1f4la3
   complexed with met, zn

Details for d1f4la2

PDB Entry: 1f4l, 1.85 Å

PDB Description: crystal structure of the e.coli methionyl-trna synthetase complexed with methionine

PDB Compounds: (A:) Methionyl-tRNA synthetase

SCOP Domain Sequences for d1f4la2:

Sequence; same for both SEQRES and ATOM records:

>d1f4la2 c.26.1.1 (A:4-140,A:176-388) Methionyl-tRNA synthetase (MetRS) {Escherichia coli [TaxId: 562]}
akkilvtcalpyangsihlghmlehiqadvwvryqrmrghevnficaddahgtpimlkaq
qlgitpeqmigemsqehqtdfagfnisydnyhsthseenrqlseliysrlkengfiknrt
isqlydpekgmflpdrfXvvsgatpvmrdsehfffdlpsfsemlqawtrsgalqeqvank
mqewfesglqqwdisrdapyfgfeipnapgkyfyvwldapigymgsfknlcdkrgdsvsf
deywkkdstaelyhfigkdivyfhslfwpamlegsnfrkpsnlfvhgyvtvngakmsksr
gtfikastwlnhfdadslryyytaklssriddidlnledfvqrvnadivnk

Timeline for d1f4la2:

• d1f4la2 first appeared in SCOP 1.57
  
• d1f4la2 appears in SCOP 1.71
  
• d1f4la2 appears in SCOP 1.75
  
• d1f4la2 appears in the current release, SCOPe 2.08