The domain within your query sequence starts at position 4 and ends at position 89; the E-value for the CARD domain shown below is 4.91e-19.



Caspase recruitment domain
SMART accession number:SM00114
Description: Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.
Interpro abstract (IPR001315):

The caspase recruitment domain (CARD domain) is a homotypic protein interaction module composed of a bundle of six alpha-helices. CARD is related in sequence and structure to the death domain (DD, see IPR000488 ) and the death effector domain (DED, see IPR001875 ), which work in similar pathways and show similar interaction properties [ (PUBMED:11504623) ]. The CARD domain typically associates with other CARD-containing proteins, forming either dimers or trimers. CARD domains can be found in isolation, or in combination with other domains. Domains associated with CARD include: NACHT ( IPR007111 ) (in Nal1 and Bir1), NB-ARC ( IPR002182 ) (in Apaf-1), pyrin/dapin domains ( IPR004020 ) (in Nal1), leucine-rich repeats ( IPR001611 ) (in Nal1), WD repeats ( IPR001680 ) (in Apaf1), Src homology domains ( IPR001452 ), PDZ ( IPR001478 ), RING, kinase and DD domains [ (PUBMED:15226512) ].

CARD-containing proteins are involved in apoptosis through their regulation of caspases that contain CARDs in their N-terminal pro-domains, including human caspases 1, 2, 9, 11 and 12 [ (PUBMED:9175472) ]. CARD-containing proteins are also involved in inflammation through their regulation of NF-kappaB [ (PUBMED:12101092) ]. The mechanisms by which CARDs activate caspases and NF-kappaB involve the assembly of multi-protein complexes, which can facilitate dimerisation or serve as scaffolds on which proteases and kinases are assembled and activated.

GO process:regulation of apoptotic process (GO:0042981)
Family alignment:
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There are 5205 CARD domains in 5027 proteins in SMART's nrdb database.

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