Function and Biology Details
Reactions catalysed:
ATP + H(2)O = ADP + phosphate
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- Butyrophylin-like, SPRY domain
- Helicase, C-terminal domain-like
- P-loop containing nucleoside triphosphate hydrolase
- SPRY domain
- RIG-I-like receptor, C-terminal regulatory domain
- Helicase superfamily 1/2, ATP-binding domain
- Concanavalin A-like lectin/glucanase domain superfamily
- E3 ubiquitin-protein ligase TRIM65, PRY/SPRY domain
5 more domains
Structure analysis Details
Assembly composition:
hetero octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180178 (preferred)
Entry contents:
2 distinct polypeptide molecules
2 distinct RNA molecules
2 distinct RNA molecules
Macromolecules (4 distinct):
Interferon-induced helicase C domain-containing protein 1
Molecule details ›
Chains: A, C, E
Length: 739 amino acids
Theoretical weight: 84.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 739 amino acids
Theoretical weight: 84.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9BYX4 (Residues: 287-1025; Coverage: 72%)
Sequence domains:
E3 ubiquitin-protein ligase TRIM65
Molecule details ›
Chains: B, D, F
Length: 191 amino acids
Theoretical weight: 21.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: SPRY domain
Length: 191 amino acids
Theoretical weight: 21.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q6PJ69 (Residues: 312-502; Coverage: 37%)
Sequence domains: SPRY domain
