Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. 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 and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559  10 LMWYLEELNKKEFVKFKEFLKQEVLQLGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIERAKR 89
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80

                  ..
gi 1720422559  90 EI 91
Cdd:cd08320    81 EM 82

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720422559 406 DQLQGLCSLAAEGMWTDTFVFGEEALRRNGIMDSDIPILLDIGMLINIRESEKSYIF 462
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. 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 and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559  10 LMWYLEELNKKEFVKFKEFLKQEVLQLGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIERAKR 89
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80

                  ..
gi 1720422559  90 EI 91
Cdd:cd08320    81 EM 82

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559 464 HPSVQEVCAAIFYLLKSHVDHP--------SQEVKSIEKLMFAFLKKVKVQWIFFGSFIFGLLHESEQKKLEAFFGHQLS 535
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720422559 536 QEIKRQLYQCLETISGNEELQEqiDGMKLFYCLFEMDDDTFL 577
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFV 120

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720422559 406 DQLQGLCSLAAEGMWTDTFVFGEEALRRNGIMDSDIPILLDIGMLINIRESEKSYIF 462
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. 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 and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559  10 LMWYLEELNKKEFVKFKEFLKQEVLQLGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIERAKR 89
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80

                  ..
gi 1720422559  90 EI 91
Cdd:cd08320    81 EM 82

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559 464 HPSVQEVCAAIFYLLKSHVDHP--------SQEVKSIEKLMFAFLKKVKVQWIFFGSFIFGLLHESEQKKLEAFFGHQLS 535
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720422559 536 QEIKRQLYQCLETISGNEELQEqiDGMKLFYCLFEMDDDTFL 577
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFV 120

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559   4 FFSDFGLMWYLEELNKKEFVKFKEFLKQEVLQLGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDL 83
Cdd:COG5635    19 DLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559  84 IERAKREIDDIFQSSPLVLTDSGCPKLYRAHMKTKMTHDSSRAFTISIQNFLKEKFTE-----DDYDCFENLFQSKGTES 158
Cdd:COG5635    99 LLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDlyvplNLLERIESLKRLELLEA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559 159 KPQVVFLSGGAGVGKTLMLKRLMLAWIESPVFLHKFsYIFYFCCREVKqlKTASLAELISREW----PGPSAPIEEILSK 234
Cdd:COG5635   179 KKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLA--EEASLEDLLAEALekrgGEPEDALERLLRN 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559 235 PeKLLFIIDSLEgmecdlfkwesELCDNCTEKQPVNvLLSSLLRRkmLPESSLLISATPESFEkmENRIEYTHVKIIKGL 314
Cdd:COG5635   256 G-RLLLLLDGLD-----------EVPDEADRDEVLN-QLRRFLER--YPKARVIITSRPEGYD--SSELEGFEVLELAPL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559 315 KERNIKMSFHRLFQDRNRAHEAF-SLVRENEQLFTVCQVPVLCWMVATCLKEEIEKGRDPVSICR-CTTSLYTTHIFNlf 392
Cdd:COG5635   319 SDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRERGELPDTRAELYEqFVELLLERWDEQ-- 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559 393 ipQNAHSPSKKSQDQLQGLCSLAAEGMWT-DTFVFGEEALRR------NGIMDSDI---PILLDIGMLinIRESEKSYIF 462
Cdd:COG5635   397 --RGLTIYRELSREELRELLSELALAMQEnGRTEFAREELEEilreylGRRKDAEAlldELLLRTGLL--VERGEGRYSF 472

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720422559 463 LHPSVQEVCAA----------IFYLLKSHVDHPS-QEVKsieKLMFAFLKKVKvqwiFFGSFIFGLLHESEQKKLEAFFG 531
Cdd:COG5635   473 AHRSFQEYLAAralveeldeeLLELLAEHLEDPRwREVL---LLLAGLLDDVK----QIKELIDALLARDDAAALALAAA 545

                         570
                  ....*....|....*.
gi 1720422559 532 HQLSQEIKRQLYQCLE 547
Cdd:COG5635   546 LLLALLLALALLALLA 561

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. 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 Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720422559  10 LMWYLEELNKKEFVKFKEFLKQEVLQLGLKQVSWTevkkasRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIERAK 88
Cdd:cd08305     1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYD------RIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73