nucleotide-binding oligomerization domain-containing protein 2 isoform X5 [Homo sapiens]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| NACHT | pfam05729 | NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
266-436 | 2.17e-43 | ||||||||
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931. : Pssm-ID: 428606 [Multi-domain] Cd Length: 166 Bit Score: 154.39 E-value: 2.17e-43
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| CARD_NOD2_1_CARD15 | cd08787 | Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and ... |
7-92 | 3.97e-43 | ||||||||
Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 1. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found 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. : Pssm-ID: 176765 Cd Length: 87 Bit Score: 150.84 E-value: 3.97e-43
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| CARD_NOD2_2_CARD15 | cd08788 | Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ... |
107-187 | 1.07e-39 | ||||||||
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 2. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found 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. : Pssm-ID: 260056 Cd Length: 81 Bit Score: 141.08 E-value: 1.07e-39
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| NACHT | COG5635 | Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
96-604 | 8.88e-21 | ||||||||
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; : Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 97.95 E-value: 8.88e-21
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| NLRC4_HD2 super family | cl39284 | NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ... |
576-730 | 3.33e-14 | ||||||||
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein. The actual alignment was detected with superfamily member pfam17776: Pssm-ID: 465499 [Multi-domain] Cd Length: 122 Bit Score: 69.63 E-value: 3.33e-14
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| Name | Accession | Description | Interval | E-value | ||||||||
| NACHT | pfam05729 | NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
266-436 | 2.17e-43 | ||||||||
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931. Pssm-ID: 428606 [Multi-domain] Cd Length: 166 Bit Score: 154.39 E-value: 2.17e-43
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| CARD_NOD2_1_CARD15 | cd08787 | Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and ... |
7-92 | 3.97e-43 | ||||||||
Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 1. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found 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. Pssm-ID: 176765 Cd Length: 87 Bit Score: 150.84 E-value: 3.97e-43
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| CARD_NOD2_2_CARD15 | cd08788 | Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ... |
107-187 | 1.07e-39 | ||||||||
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 2. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found 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. Pssm-ID: 260056 Cd Length: 81 Bit Score: 141.08 E-value: 1.07e-39
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| NACHT | COG5635 | Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
96-604 | 8.88e-21 | ||||||||
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 97.95 E-value: 8.88e-21
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
4-94 | 2.23e-14 | ||||||||
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: 69.13 E-value: 2.23e-14
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| NLRC4_HD2 | pfam17776 | NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ... |
576-730 | 3.33e-14 | ||||||||
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein. Pssm-ID: 465499 [Multi-domain] Cd Length: 122 Bit Score: 69.63 E-value: 3.33e-14
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| NOD2_WH | pfam17779 | NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ... |
519-574 | 5.27e-08 | ||||||||
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known. Pssm-ID: 465501 Cd Length: 57 Bit Score: 49.87 E-value: 5.27e-08
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| AAA | smart00382 | ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
267-366 | 3.19e-03 | ||||||||
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment. Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 3.19e-03
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
107-188 | 6.11e-03 | ||||||||
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: 36.38 E-value: 6.11e-03
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| Name | Accession | Description | Interval | E-value | ||||||||
| NACHT | pfam05729 | NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ... |
266-436 | 2.17e-43 | ||||||||
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931. Pssm-ID: 428606 [Multi-domain] Cd Length: 166 Bit Score: 154.39 E-value: 2.17e-43
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| CARD_NOD2_1_CARD15 | cd08787 | Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and ... |
7-92 | 3.97e-43 | ||||||||
Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 1. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found 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. Pssm-ID: 176765 Cd Length: 87 Bit Score: 150.84 E-value: 3.97e-43
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| CARD_NOD2_2_CARD15 | cd08788 | Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and ... |
107-187 | 1.07e-39 | ||||||||
Caspase activation and recruitment domain of NOD2, repeat 2; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 2. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. In general, CARDs are death domains (DDs) found 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. Pssm-ID: 260056 Cd Length: 81 Bit Score: 141.08 E-value: 1.07e-39
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| NACHT | COG5635 | Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
96-604 | 8.88e-21 | ||||||||
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 97.95 E-value: 8.88e-21
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
4-94 | 2.23e-14 | ||||||||
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: 69.13 E-value: 2.23e-14
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| NLRC4_HD2 | pfam17776 | NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ... |
576-730 | 3.33e-14 | ||||||||
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein. Pssm-ID: 465499 [Multi-domain] Cd Length: 122 Bit Score: 69.63 E-value: 3.33e-14
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| CARD | cd01671 | Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
8-82 | 1.91e-08 | ||||||||
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: 51.75 E-value: 1.91e-08
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| NOD2_WH | pfam17779 | NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ... |
519-574 | 5.27e-08 | ||||||||
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known. Pssm-ID: 465501 Cd Length: 57 Bit Score: 49.87 E-value: 5.27e-08
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| CARD | cd01671 | Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ... |
107-187 | 1.08e-07 | ||||||||
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: 49.82 E-value: 1.08e-07
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| CARD_BIRC2_BIRC3 | cd08329 | Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ... |
107-183 | 1.29e-04 | ||||||||
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found 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. Pssm-ID: 260038 Cd Length: 94 Bit Score: 41.66 E-value: 1.29e-04
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| AAA | smart00382 | ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
267-366 | 3.19e-03 | ||||||||
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment. Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 3.19e-03
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| CARD | pfam00619 | Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ... |
107-188 | 6.11e-03 | ||||||||
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: 36.38 E-value: 6.11e-03
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| Blast search parameters | ||||
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