SCOPe 2.08: Domain d1yjka1: 1yjk A:50-198

Lineage for d1yjka1 (1yjk A:50-198)

1. Root: SCOPe 2.08

2. Class b: All beta proteins [48724] (180 folds)

3. Fold b.121: Nucleoplasmin-like/VP (viral coat and capsid proteins) [88632] (7 superfamilies)
   sandwich; 8 strands in 2 sheets; jelly-roll; some members can have additional 1-2 strands
   characteristic interaction between the domains of this fold allows the formation of five-fold and pseudo six-fold assemblies

4. Superfamily b.121.1: PHM/PNGase F [49742] (2 families)
   members of this superfamily bind peptide substrates
   duplication: consists of two domains of this fold packed together like the adjacent nucleoplasmin subunits

5. Family b.121.1.2: Peptidylglycine alpha-hydroxylating monooxygenase, PHM [49746] (1 protein)

6. Protein Peptidylglycine alpha-hydroxylating monooxygenase, PHM [63402] (1 species)

7. Species Norway rat (Rattus norvegicus) [TaxId:10116] [49748] (26 PDB entries)

8. Domain d1yjka1: 1yjk A:50-198 [123423]
   automated match to d3miha1
   complexed with cu, gol

Details for d1yjka1

PDB Entry: 1yjk, 2 Å

PDB Description: Reduced Peptidylglycine Alpha-Hydroxylating Monooxygenase (PHM) in a New Crystal Form

PDB Compounds: (A:) Peptidyl-glycine alpha-amidating monooxygenase

SCOPe Domain Sequences for d1yjka1:

Sequence; same for both SEQRES and ATOM records:

>d1yjka1 b.121.1.2 (A:50-198) Peptidylglycine alpha-hydroxylating monooxygenase, PHM {Norway rat (Rattus norvegicus) [TaxId: 10116]}
tigpvtpldasdfaldirmpgvtpkesdtyfcmsmrlpvdeeafvidfkprasmdtvhhm
llfgcnmpsstgsywfcdegtctdkanilyawarnapptrlpkgvgfrvggetgskyfvl
qvhygdisafrdnhkdcsgvsvhltrvpq

Timeline for d1yjka1:

• d1yjka1 first appeared in SCOP 1.73
  
• d1yjka1 appears in SCOPe 2.07