SCOPe 2.08: Domain d1yjla2: 1yjl A:199-355

Lineage for d1yjla2 (1yjl A:199-355)

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 d1yjla2: 1yjl A:199-355 [123426]
   automated match to d1yjla2

Details for d1yjla2

PDB Entry: 1yjl, 2.4 Å

PDB Description: reduced peptidylglycine alpha-hydroxylating monooxygenase in a new crystal form

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

SCOPe Domain Sequences for d1yjla2:

Sequence, based on SEQRES records:

>d1yjla2 b.121.1.2 (A:199-355) Peptidylglycine alpha-hydroxylating monooxygenase, PHM {Norway rat (Rattus norvegicus) [TaxId: 10116]}
pliagmylmmsvdtvippgekvvnadiscqykmypmhvfayrvhthhlgkvvsgyrvrng
qwtligrqnpqlpqafypvehpvdvtfgdilaarcvftgegrteathiggtssdeicnly
imyymeakyalsfmtctknvapdmfrtipaeanipip

Sequence, based on observed residues (ATOM records):

>d1yjla2 b.121.1.2 (A:199-355) Peptidylglycine alpha-hydroxylating monooxygenase, PHM {Norway rat (Rattus norvegicus) [TaxId: 10116]}
pliagmylmmsvdtvippgekvvnadiscqykmypmhvfayrvhthhlgkvvsgyrvrng
qwtligrqnpqlpqafypvehpvdvtfgdilaarcvfticnlyimyymeakyalsfmtct
knvapdmfrtipaeanipip

Timeline for d1yjla2:

• d1yjla2 first appeared in SCOP 1.73
  
• d1yjla2 appears in SCOPe 2.07