SMART: Pfam domain UQ

The domain within your query sequence starts at position 5 and ends at position 45; the E-value for the UQ_con domain shown below is 8.3e-7.

RINKELSDLARDPPAQCSAGPVGDDMFHWQATIMGPLNESE

UQ_con

PFAM accession number:	PF00179
Interpro abstract (IPR000608):	Ubiquitin-conjugating enzymes (UBC or E2 enzymes) [ (PUBMED:2193438) (PUBMED:1647207) (PUBMED:1656558) ] catalyse the covalent attachment of ubiquitin to target proteins. Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1, IPR000011 ), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3, IPR000569 IPR003613 ), which work sequentially in a cascade [ (PUBMED:14998368) ]. The E1 enzyme mediates an ATP-dependent transfer of a thioester-linked ubiquitin molecule to a cysteine residue on the E2 enzyme. The E2 enzyme ( EC 6.3.2.19 ) then either transfers the ubiquitin moiety directly to a substrate, or to an E3 ligase, which can also ubiquitinylate a substrate. There are several different E2 enzymes (over 30 in humans), which are broadly grouped into four classes, all of which have a core catalytic domain (containing the active site cysteine), and some of which have short N- and C-terminal amino acid extensions: class I enzymes consist of just the catalytic core domain (UBC), class II possess a UBC and a C-terminal extension, class III possess a UBC and an N-terminal extension, and class IV possess a UBC and both N- and C-terminal extensions. These extensions appear to be important for some subfamily function, including E2 localisation and protein-protein interactions [ (PUBMED:15545318) ]. In addition, there are proteins with an E2-like fold that are devoid of catalytic activity (such as protein crossbronx from flies), but which appear to assist in poly-ubiquitin chain formation.

PFAM accession number:

PF00179

Interpro abstract (IPR000608):

Ubiquitin-conjugating enzymes (UBC or E2 enzymes) [ (PUBMED:2193438) (PUBMED:1647207) (PUBMED:1656558) ] catalyse the covalent attachment of ubiquitin to target proteins. Ubiquitinylation is an ATP-dependent process that involves the action of at least three enzymes: a ubiquitin-activating enzyme (E1, IPR000011 ), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3, IPR000569 IPR003613 ), which work sequentially in a cascade [ (PUBMED:14998368) ]. The E1 enzyme mediates an ATP-dependent transfer of a thioester-linked ubiquitin molecule to a cysteine residue on the E2 enzyme. The E2 enzyme ( EC 6.3.2.19 ) then either transfers the ubiquitin moiety directly to a substrate, or to an E3 ligase, which can also ubiquitinylate a substrate.

There are several different E2 enzymes (over 30 in humans), which are broadly grouped into four classes, all of which have a core catalytic domain (containing the active site cysteine), and some of which have short N- and C-terminal amino acid extensions: class I enzymes consist of just the catalytic core domain (UBC), class II possess a UBC and a C-terminal extension, class III possess a UBC and an N-terminal extension, and class IV possess a UBC and both N- and C-terminal extensions. These extensions appear to be important for some subfamily function, including E2 localisation and protein-protein interactions [ (PUBMED:15545318) ]. In addition, there are proteins with an E2-like fold that are devoid of catalytic activity (such as protein crossbronx from flies), but which appear to assist in poly-ubiquitin chain formation.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry UQ_con