SCOPe 2.04: Domain d1p16a2: 1p16 A:1-245

Lineage for d1p16a2 (1p16 A:1-245)

1. Root: SCOPe 2.04

2. Class d: Alpha and beta proteins (a+b) [53931] (380 folds)

3. Fold d.142: ATP-grasp [56058] (2 superfamilies)
   Consists of two subdomains with different alpha+beta folds
   shares functional and structural similarities with the PIPK and protein kinase superfamilies

4. Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain [56091] (6 families)
   has a circularly permuted topology

5. Family d.142.2.3: mRNA capping enzyme [56100] (2 proteins)
   automatically mapped to Pfam PF01331

6. Protein mRNA capping enzyme alpha subunit [90032] (1 species)

7. Species Yeast (Candida albicans) [TaxId:5476] [90033] (1 PDB entry)

8. Domain d1p16a2: 1p16 A:1-245 [87662]
   Other proteins in same PDB: d1p16a1, d1p16b1
   complexed with the phosphorylated carboxyl-terminal peptide of RNA polymerase II, chains C and D
   complexed with g, gtp, po4

Details for d1p16a2

PDB Entry: 1p16, 2.7 Å

PDB Description: structure of an mrna capping enzyme bound to the phosphorylated carboxyl-terminal domain of rna polymerase ii

PDB Compounds: (A:) mRNA capping enzyme alpha subunit

SCOPe Domain Sequences for d1p16a2:

Sequence; same for both SEQRES and ATOM records:

>d1p16a2 d.142.2.3 (A:1-245) mRNA capping enzyme alpha subunit {Yeast (Candida albicans) [TaxId: 5476]}
mvqleereipvipgnkldeeetkelrlmvaellgrrntgfpgsqpvsferrhleetlmqk
dyfvcektdglrcllflindpdkgegvflvtrendyyfipnihfplsvnetrekptyhhg
tlldgelvlenrnvsepvlryvifdalaihgkciidrplpkrlgyitenvmkpfdnfkkh
npdivnspefpfkvgfktmltsyhaddvlskmdklfhasdgliytcaetpyvfgtdqtll
kwkpa

Timeline for d1p16a2:

• d1p16a2 first appeared in SCOP 1.65
  
• d1p16a2 appears in SCOPe 2.03
  
• d1p16a2 appears in SCOPe 2.05
  
• d1p16a2 appears in the current release, SCOPe 2.08