CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.30 | Roll | |
2.30.30 | SH3 type barrels. | |
2.30.30.30 |
Domain Context
CATH Clusters
Superfamily | 2.30.30.30 |
Functional Family | E3 ubiquitin-protein ligase UHRF1 |
Enzyme Information
2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q96T88
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.
-!- The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). -!- RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.
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UniProtKB Entries (2)
Q96T88 |
UHRF1_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase UHRF1
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Q3BDD9 |
Q3BDD9_9INSE
Siphlonella sp. EP083
Histone H3
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PDB Structure
PDB | 2L3R |
External Links | |
Method | SOLUTION NMR |
Organism | |
Primary Citation |
Recognition of Multivalent Histone States Associated with Heterochromatin by UHRF1 Protein.
J.Biol.Chem.
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