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Conserved domains on  [gi|157502191|ref|NP_877439|]
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metastasis-associated in colon cancer protein 1 [Homo sapiens]

Protein Classification

death domain-containing protein( domain architecture ID 10109012)

death domain-containing protein may be involved in protein-protein interactions, similar to Drosophila melanogaster protein immune deficiency (IMD), which functions as an adapter protein that transduces immunity signals from the activation of pathogen recognition receptors (PRRs) by bacterial infection to the IMD/NF-kappa-B signaling pathway

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
743-818 7.53e-04

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: 38.80  E-value: 7.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502191 743 AVKLGKGWRELAEKLvRLTKQQMEAYEIPHRGNTGDVAVEMmwkpaydfLYTWSAHYGNNYRdvLQDLQSALDRMK 818
Cdd:cd01670    6 AEELGRDWKKLARKL-GLSEGDIDQIEEDNRDDLKEQAYQM--------LERWREREGDEAT--LGRLIQALREIG 70
 
Name Accession Description Interval E-value
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
743-818 7.53e-04

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: 38.80  E-value: 7.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502191 743 AVKLGKGWRELAEKLvRLTKQQMEAYEIPHRGNTGDVAVEMmwkpaydfLYTWSAHYGNNYRdvLQDLQSALDRMK 818
Cdd:cd01670    6 AEELGRDWKKLARKL-GLSEGDIDQIEEDNRDDLKEQAYQM--------LERWREREGDEAT--LGRLIQALREIG 70
 
Name Accession Description Interval E-value
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
743-818 7.53e-04

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: 38.80  E-value: 7.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157502191 743 AVKLGKGWRELAEKLvRLTKQQMEAYEIPHRGNTGDVAVEMmwkpaydfLYTWSAHYGNNYRdvLQDLQSALDRMK 818
Cdd:cd01670    6 AEELGRDWKKLARKL-GLSEGDIDQIEEDNRDDLKEQAYQM--------LERWREREGDEAT--LGRLIQALREIG 70
 
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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