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Conserved domains on  [gi|218563746|ref|NP_001130008|]
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death domain-containing protein 1 isoform 2 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 10171980)

protein kinase family protein containing a Death domain (DD), may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 513-599 2.00e-38

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.


:

Pssm-ID: 260049  Cd Length: 86  Bit Score: 136.29  E-value: 2.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563746 513 WDNLLHWLAEELsEENAESLSSTLPLRRSTIQLIKLKNPDDLTEQIHEFLCFWKKSLPTFTDKLRLLARHLRKIGRSDLA 592
Cdd:cd08779    1 TDSNLLSLAKEL-GEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLA 79


                 ....*..
gi 218563746 593 EELKFKW 599
Cdd:cd08779   80 EELRDKL 86
 
Name Accession Description Interval E-value
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 513-599 2.00e-38

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.


Pssm-ID: 260049  Cd Length: 86  Bit Score: 136.29  E-value: 2.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563746 513 WDNLLHWLAEELsEENAESLSSTLPLRRSTIQLIKLKNPDDLTEQIHEFLCFWKKSLPTFTDKLRLLARHLRKIGRSDLA 592
Cdd:cd08779    1 TDSNLLSLAKEL-GEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLA 79


                 ....*..
gi 218563746 593 EELKFKW 599
Cdd:cd08779   80 EELRDKL 86
Death pfam00531
Death domain;
517-599 8.73e-10

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 55.45  E-value: 8.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563746  517 LHWLAEELSE--ENAESLSSTLPLRRSTIQLIKLKNPDdLTEQIHEFLCFWK-KSLPTFTdkLRLLARHLRKIGRSDLAE 593
Cdd:pfam00531   4 LDRLLDPPPPlgKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEqREGKNAT--VGTLLEALRKLGRRDAAE 80


                  ....*.
gi 218563746  594 ELKFKW 599
Cdd:pfam00531  81 KIQSIL 86
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 532-595 4.21e-03

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.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 36.62  E-value: 4.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218563746   532 LSSTLPLRRSTIQLIKLKNPDDLTEQIHEFLCFWKKSLPTFTDkLRLLARHLRKIGRSDLAEEL 595
Cdd:smart00005  23 LARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNAT-LGTLLEALRKMGRDDAVELL 85
 
Name Accession Description Interval E-value
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 513-599 2.00e-38

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.


Pssm-ID: 260049  Cd Length: 86  Bit Score: 136.29  E-value: 2.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563746 513 WDNLLHWLAEELsEENAESLSSTLPLRRSTIQLIKLKNPDDLTEQIHEFLCFWKKSLPTFTDKLRLLARHLRKIGRSDLA 592
Cdd:cd08779    1 TDSNLLSLAKEL-GEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPDKVGLLVTALSKSGRSDLA 79


                 ....*..
gi 218563746 593 EELKFKW 599
Cdd:cd08779   80 EELRDKL 86
Death pfam00531
Death domain;
517-599 8.73e-10

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 55.45  E-value: 8.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563746  517 LHWLAEELSE--ENAESLSSTLPLRRSTIQLIKLKNPDdLTEQIHEFLCFWK-KSLPTFTdkLRLLARHLRKIGRSDLAE 593
Cdd:pfam00531   4 LDRLLDPPPPlgKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEqREGKNAT--VGTLLEALRKLGRRDAAE 80


                  ....*.
gi 218563746  594 ELKFKW 599
Cdd:pfam00531  81 KIQSIL 86
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 517-596 3.05e-07

Death Domain: a protein-protein interaction domain; Death Domains (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. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 48.05  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563746 517 LHWLAEELSEEnAESLSSTLPLRRSTIQLIKLKNPDDLTEQIHEFLCFWK-KSLPTFTdkLRLLARHLRKIGRSDLAEEL 595
Cdd:cd01670    2 FDLVAEELGRD-WKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWReREGDEAT--LGRLIQALREIGRRDLAEKL 78


                 .
gi 218563746 596 K 596
Cdd:cd01670   79 E 79
DED cd00045
Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a ...
 516-596 1.10e-03

Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a subfamily of the Death Domain (DD) superfamily. DED-containing proteins include Fas-Associated via Death Domain (FADD), Astrocyte phosphoprotein PEA-15, the initiator caspases (caspase-8 and -10), and FLICE-inhibitory protein (FLIP), among others. These proteins are prominent components of the programmed cell death (apoptosis) pathway. Some members also have non-apoptotic functions such as regulation of insulin signaling (DEDD and PEA15) and cell cycle progression (DEDD). 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 CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260016  Cd Length: 77  Bit Score: 37.95  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563746 516 LLHWLAEELSEENAESLSStlplrrstiqLIKLKNPDDLTEQI---HEFLCFWKKSLPTFTDKLRLLARHLRKIGRSDLA 592
Cdd:cd00045    4 LLLKISDELTSEELRSLKF----------LCKDVIPAGKLERIsrgRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLL 73


                 ....
gi 218563746 593 EELK 596
Cdd:cd00045   74 EKVE 77
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 532-595 4.21e-03

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.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 36.62  E-value: 4.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 218563746   532 LSSTLPLRRSTIQLIKLKNPDDLTEQIHEFLCFWKKSLPTFTDkLRLLARHLRKIGRSDLAEEL 595
Cdd:smart00005  23 LARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNAT-LGTLLEALRKMGRDDAVELL 85
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 515-590 5.18e-03

Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. 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.


Pssm-ID: 260029  Cd Length: 84  Bit Score: 36.47  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218563746 515 NLLH--W--LAEEL--SEENaeslsstlplrrstIQLIKLKNPDDLTEQIHEFLCFW---KKSLPTFTDklrlLARHLRK 585
Cdd:cd08317   12 NLLGsdWpeLARELgvSEED--------------IDLIRSENPNSLAQQAMAMLRLWlerEGEKATGNA----LESALKK 73


                 ....*
gi 218563746 586 IGRSD 590
Cdd:cd08317   74 IGRDD 78
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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