Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, 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 CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644407 477 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQTGQPGAVGHLVQALEQSDRQDVAE 556
Cdd:cd08779     1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80

                  ....*.
gi 1958644407 557 EVRAIL 562
Cdd:cd08779    81 ELRDKL 86

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644407  12 SFLVTPHGCSVTLA-CGVRLQFPAGATTTPITIHYRLWLP--EPGLVSLGPHDFLLSGVLELQPHGVAFQQNVSLWL 85
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGTRIECYLAVNrdESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEV 78

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, 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 CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644407 477 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQTGQPGAVGHLVQALEQSDRQDVAE 556
Cdd:cd08779     1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80

                  ....*.
gi 1958644407 557 EVRAIL 562
Cdd:cd08779    81 ELRDKL 86

Peptidase S68; This family of serine peptidases contains PIDD proteins. PIDD forms a complex with RAIDD and procaspase-2 that is known as the 'PIDDosome'. The PIDDosome forms when DNA damage occurs and either activates NF-kappaB, leading to cell survival, or caspase-2, which leads to apoptosis.

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1958644407 110 WNDLETHLEEEAPKRR-WARCQVPHFSWFLVVLR 142
Cdd:pfam10461   1 WSDLPTQLRRGSKSRKcVARCSVPHFSWFMVVSR 34

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958644407  12 SFLVTPHGCSVTLA-CGVRLQFPAGATTTPITIHYRLWLP--EPGLVSLGPHDFLLSGVLELQPHGVAFQQNVSLWL 85
Cdd:pfam00791   2 SGLVDSRGGRLVLPnSGVSLLIPPGAIPEGTRIECYLAVNrdESSRPPLEEGETLLSPVVECGPPGLKFLKPVILEV 78

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644407  164 GVKVTFPPGVTEEPRQVSMQVVHMAGLELRALLEESEAAVSPLLCLSQSGpPSFLQPVTVQLP 226
Cdd:smart00218  22 GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHG-ALFLRPVILEVP 83

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, 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 CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644407 477 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQTGQPGAVGHLVQALEQSDRQDVAE 556
Cdd:cd08779     1 TDSNLLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLAE 80

                  ....*.
gi 1958644407 557 EVRAIL 562
Cdd:cd08779    81 ELRDKL 86

Death domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644407 481 LLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDgQIRHMLFSWaESQTGQPGAVGHLVQALEQSDRQDVAEEVRA 560
Cdd:pfam00531   7 LLDPPPPLGKDWRELARKLGLSENEIDEIESENPRLRS-QTYELLRLW-EQREGKNATVGTLLEALRKLGRRDAAEKIQS 84

                  ..
gi 1958644407 561 IL 562
Cdd:pfam00531  85 IL 86

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958644407  488 LGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWaESQTGQPGAVGHLVQALEQSDRQDVAEEVR 559
Cdd:smart00005  16 LGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLW-EQREGKNATLGTLLEALRKMGRDDAVELLR 86

Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. In general, 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 CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958644407 477 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQtGQPGAVGHLVQALEQSD 550
Cdd:cd08319     1 TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQ-GKKATVQSLIQSLKAVE 73

Death domain of FAS or TNF receptor superfamily member 6; Death Domain (DD) found in the FS7-associated cell surface antigen (FAS). FAS, also known as TNFRSF6 (TNF receptor superfamily member 6), APT1, CD95, FAS1, or APO-1, together with FADD (Fas-associating via Death Domain) and caspase 8, is an integral part of the death inducing signalling complex (DISC), which plays an important role in the induction of apoptosis and is activated by binding of the ligand FasL to FAS. FAS also plays a critical role in self-tolerance by eliminating cell types (autoreactive T and B cells) that contribute to autoimmunity. 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644407 494 TVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQtGQPGAVGHLVQALEQSDRQDVAEEVRAILE 563
Cdd:cd08316    22 KFARKSGISETKIDEIQLDNPNDTAEQKVQLLRAWYQKH-GKKGAYRTLIKTLRKAGKRAKADKIQDIIK 90

Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix Protein P84 (also known as HPR1 or THOC1). HPR1/p84 resides in the nuclear matrix and is part of the THO complex, also called TREX (transcription/export) complex, which functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Mice lacking THOC1 have abnormal testis development and are sterile. In general, 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644407 476 LTQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEfRDDLDGQIRHMLFSWAEsQTGQPGAVGHLVQALEQSDRQDVA 555
Cdd:cd08318     5 VTSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIESD-SEDMKMRAKQLLVTWQD-REGAQATPEILMTALNAAGLNEIA 82

                  ...
gi 1958644407 556 EEV 558
Cdd:cd08318    83 ENL 85

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal DD, which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. In general, 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958644407 477 TQSNLLSVASRLGSDWPTVALHLGMPYRKLQRIRHEF-RDDLDGQIRHMLFSWAESQTGQPGAVGHLVQALEQSDRQDV 554
Cdd:cd08777     1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYeRDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDL 79

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. 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 CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958644407 488 LGSDWPTVALHLGMPYRKLQRIRHEFRDDLDGQIRHMLFSWAESQtGQPGAVGHLVQALEQSDRQDVAEEVRAIL 562
Cdd:cd08306    12 LGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIK-KAEATVADLIKALRDCQLNLVADLVEKKL 85