nucleolar protein 3 isoform C [Homo sapiens]
List of domain hits
Name | Accession | Description | Interval | E-value | |||
DD super family | cl14633 | Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) ... |
5-58 | 7.91e-11 | |||
Death Domain Superfamily of protein-protein interaction domains; The Death Domain (DD) superfamily includes the DD, Pyrin, CARD (Caspase activation and recruitment domain) and DED (Death Effector Domain) families. 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. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. They are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways including those that impact innate immunity, inflammation, differentiation, and cancer. The actual alignment was detected with superfamily member smart00114: Pssm-ID: 472698 Cd Length: 88 Bit Score: 55.81 E-value: 7.91e-11
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metallo-dependent_hydrolases super family | cl00281 | Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
30-115 | 9.23e-04 | |||
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others. The actual alignment was detected with superfamily member PRK13404: Pssm-ID: 469705 [Multi-domain] Cd Length: 477 Bit Score: 38.91 E-value: 9.23e-04
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Name | Accession | Description | Interval | E-value | |||
CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
5-58 | 7.91e-11 | |||
Caspase recruitment domain; 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. Pssm-ID: 128424 Cd Length: 88 Bit Score: 55.81 E-value: 7.91e-11
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CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
10-58 | 1.27e-06 | |||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold. Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 44.47 E-value: 1.27e-06
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CARD | cd01671 | Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
12-58 | 3.08e-04 | |||
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260018 [Multi-domain] Cd Length: 79 Bit Score: 37.88 E-value: 3.08e-04
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PRK13404 | PRK13404 | dihydropyrimidinase; Provisional |
30-115 | 9.23e-04 | |||
dihydropyrimidinase; Provisional Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 38.91 E-value: 9.23e-04
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Name | Accession | Description | Interval | E-value | |||
CARD | smart00114 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ... |
5-58 | 7.91e-11 | |||
Caspase recruitment domain; 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. Pssm-ID: 128424 Cd Length: 88 Bit Score: 55.81 E-value: 7.91e-11
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CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
10-58 | 1.27e-06 | |||
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold. Pssm-ID: 459874 [Multi-domain] Cd Length: 85 Bit Score: 44.47 E-value: 1.27e-06
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CARD | cd01671 | Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
12-58 | 3.08e-04 | |||
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes. Pssm-ID: 260018 [Multi-domain] Cd Length: 79 Bit Score: 37.88 E-value: 3.08e-04
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PRK13404 | PRK13404 | dihydropyrimidinase; Provisional |
30-115 | 9.23e-04 | |||
dihydropyrimidinase; Provisional Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 38.91 E-value: 9.23e-04
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Blast search parameters | ||||
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