3YGS


Conserved Protein Domain Family
CARD_CASP9

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cd08326: CARD_CASP9 
Click on image for an interactive view with Cn3D
Caspase activation and recruitment domain of Caspase-9
Caspase activation and recruitment domain (CARD) similar to that found in caspase-9 (CASP9, MCH6, APAF3), which interacts with the CARD of apoptotic protease-activating factor 1 (APAF-1). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-9 is the initiator caspase associated with the intrinsic or mitochondrial pathway of apoptosis, induced by many pro-apoptotic signals. Together with APAF-1, it forms the heptameric 'apoptosome' in response to the release of cytochrome c from mitochondria. Activated caspase-9 cleaves and activates downstream effector caspases, like caspase-3, caspase-6, and caspase-7, resulting in apoptosis. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.
Statistics
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PSSM-Id: 176740
View PSSM: cd08326
Aligned: 6 rows
Threshold Bit Score: 110.978
Threshold Setting Gi: 7767041
Created: 16-Nov-2009
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Caspase9-APAF1
Conserved site includes 9 residues -Click on image for an interactive view with Cn3D
Feature 1:Caspase9-APAF1 interaction site [polypeptide binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1             ## ##  #                                  #   #   #  #                     
3YGS_P         6 DRRLLRRCRLRLVEELQVDQLWDVLLSRELFRPHMIEDIQRAGSgsrRDQARQLIIDLETRGSQALPLFISCLEDTGqdM 85  human
NP_001079035   5 LRDILRRNRVRLVQSLQVKELWDLLVERGVFSNDMIEEIQREGTr--RDQARKLLVELETRGSQAFPLFLLCLKETAqhD 82  African clawed ...
AAH97103       5 HRQILQRHRLNLVKALNPEDVCDKLLSKGVFTQDMIDEIQSKATr--RDQARQLVKDLETRGSLAFPAFLDSLRETGhnD 82  zebrafish
XP_002190691   5 QRRALRRGRARLVAALRVEPLWEPLEQRGLFTRPMLEELQSAGSr--GEQARQLIIDLETRGKQAFPAFLSILRDTGqgH 82  zebra finch
XP_002586544   5 HRQILIENRVRLAKDMKPKFLYPILVEKKVFNDDMIEEIEAAGTr--FDQCNALLRDLPGRGKQAFQSFVEALDEAEqtD 82  Florida lancelet
XP_002731034   5 HKEILRRHRAKLAEEMTPKYVYPHLISNNIFKPFMIEDIEAAGSr--FDQNNQLLTSLESRGKHAFETFVNALFESGqtD 82  Saccoglossus ko...
Feature 1              
3YGS_P        86 LASFLR 91  human
NP_001079035  83 LADFLQ 88  African clawed frog
AAH97103      83 LAELLQ 88  zebrafish
XP_002190691  83 LAEMLM 88  zebra finch
XP_002586544  83 LADLLR 88  Florida lancelet
XP_002731034  83 LAELLR 88  Saccoglossus kowalevskii

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