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IID90030
 UniprotP19508
ProteinProtein Vpx
Genevpx
OrganismSimian immunodeficiency virus (isolate PBj14/BCL-3)
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
112
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-112 Hetero trimer : IID00743Complex,Q9Y3Z3
 Evidence X-RAY 4cc9 B Reference
       Region 4cc9 B 1-4 disorder
       Region 4cc9 B 5-90 order
       Region 4cc9 B 91-99 disorder
       Region 4cc9 B 100-111 order
       Region 4cc9 B 112-112 disorder
SeqProS predicted 100-111 The unbound state of this region is predicted to be disordered by DICHOT and MobiDB. Hetero trimer : IID00743Complex,Q9Y3Z3
       Region 4cc9 B 100-111 order
 
Prediction
NeProc
Disorder 1-18,92-112
Order 19-91
ProS 13-18,92-100,109-112
AlphaFold
Disorder 1-1,9-16,90-105
Order 2-8,17-89,106-112
Pfam Hmmer
PF00522 5-99 3e-56
SEG 101-110
Function
Function in SwissProt
Plays a role in nuclear translocation of the viral pre-integration complex (PIC), thus is required for the virus to infect non-dividing cells. Targets specific host proteins for degradation by the 26S proteasome. Acts by associating with the cellular CUL4A-DDB1 E3 ligase complex through direct interaction with host VPRPB/DCAF-1. This change in the E3 ligase substrate specificity results in the degradation of host SAMHD1. In turn, SAMHD1 depletion allows viral replication in host myeloid cells by preventing SAMHD1-mediated hydrolysis of intracellular dNTPs necessary for reverse transcription.