Function and Biology

SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53 COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE

Source organisms:
Biochemical function: not assigned
Biological process: not assigned
Cellular component: not assigned

EC 2.7.12.1: Dual-specificity kinase

Reaction catalysed:
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Systematic name:
ATP:protein phosphotransferase (Ser/Thr- and Tyr-phosphorylating)
Alternative Name(s):
  • ADK1
  • Arabidopsis dual specificity kinase 1
  • CLK1
  • DDYRK2
  • Mps1p

GO terms

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF00498
Domain description: FHA domain
Occurring in:
  1. Serine/threonine-protein kinase RAD53
The deposited structure of PDB entry 1fhr contains 1 copy of Pfam domain PF00498 (FHA domain) in Serine/threonine-protein kinase RAD53. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR000253
Domain description: Forkhead-associated (FHA) domain
Occurring in:
  1. Serine/threonine-protein kinase RAD53
IPR008984
Domain description: SMAD/FHA domain superfamily
Occurring in:
  1. Serine/threonine-protein kinase RAD53

Structure domain

CATH CATH domain
2.60.200.20
Class: Mainly Beta
Architecture: Sandwich
Topology: Tumour Suppressor Smad4
Homology: Tumour Suppressor Smad4
Occurring in:
  1. Serine/threonine-protein kinase RAD53
The deposited structure of PDB entry 1fhr contains 1 copy of CATH domain 2.60.200.20 (Tumour Suppressor Smad4) in Serine/threonine-protein kinase RAD53. Showing 1 copy in chain A.
SCOP SCOP annotation
49885
Class: All beta proteins
Fold: SMAD/FHA domain
Superfamily: SMAD/FHA domain
Occurring in:
  1. Serine/threonine-protein kinase RAD53
The deposited structure of PDB entry 1fhr contains 1 copy of SCOP domain 49885 (FHA domain) in Serine/threonine-protein kinase RAD53. Showing 1 copy in chain A.