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Conserved domains on  [gi|755519588|ref|XP_011248869|]
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NACHT, LRR and PYD domains-containing protein 4A isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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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 ...
 148-316 2.32e-33

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: 125.50  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  148 QVVFLSGGAGVGKTLMLKRLMLAWIESPVFlHKFSYIFYFCCREVKQLKTA-SLAELISREWPGPSAPIEE----ILSKP 222
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLP-QGFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  223 EKLLFIIDSLEGMeCDLFKWESELCdnctekqPVNVLLSSLLRRKMLPESSLLISATPESFEKMENRIEYTHVKIIKGLK 302
Cdd:pfam05729  80 ERLLLILDGLDEL-VSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....
gi 755519588  303 ERNIKMSFHRLFQD 316
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-91 4.54e-32

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.


:

Pssm-ID: 260032  Cd Length: 84  Bit Score: 118.88  E-value: 4.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  10 LMWYLEELNKKEFVKFKEFLKQEVLQLGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIERAKR 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ..
gi 755519588  90 EI 91
Cdd:cd08320   81 EM 82
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 451-564 2.05e-21

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: 90.04  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  451 HPSVQEVCAAIFYLLKSHVDHP--------SQEVKSIEKLMFAFLKKVKVQWIFFGSFIFGLLHESEQKKLEAFFGHQLS 522
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755519588  523 QEIKRQLYQCLETISGNEELQEqiDGMKLFYCLFEMDDDTFL 564
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFV 120
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 393-449 4.91e-09

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: 52.57  E-value: 4.91e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755519588  393 DQLQGLCSLAAEGMWTDTFVFGEEALRRNGIMDSDIPILLDIGMLINIRESEKSYIF 449
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 148-316 2.32e-33

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: 125.50  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  148 QVVFLSGGAGVGKTLMLKRLMLAWIESPVFlHKFSYIFYFCCREVKQLKTA-SLAELISREWPGPSAPIEE----ILSKP 222
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLP-QGFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  223 EKLLFIIDSLEGMeCDLFKWESELCdnctekqPVNVLLSSLLRRKMLPESSLLISATPESFEKMENRIEYTHVKIIKGLK 302
Cdd:pfam05729  80 ERLLLILDGLDEL-VSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....
gi 755519588  303 ERNIKMSFHRLFQD 316
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-91 4.54e-32

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.


Pssm-ID: 260032  Cd Length: 84  Bit Score: 118.88  E-value: 4.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  10 LMWYLEELNKKEFVKFKEFLKQEVLQLGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIERAKR 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ..
gi 755519588  90 EI 91
Cdd:cd08320   81 EM 82
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 9-85 5.49e-25

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 98.43  E-value: 5.49e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755519588    9 GLMWYLEELNKKEFVKFKEFLKQEVlQLGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIE 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 451-564 2.05e-21

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: 90.04  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  451 HPSVQEVCAAIFYLLKSHVDHP--------SQEVKSIEKLMFAFLKKVKVQWIFFGSFIFGLLHESEQKKLEAFFGHQLS 522
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755519588  523 QEIKRQLYQCLETISGNEELQEqiDGMKLFYCLFEMDDDTFL 564
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFV 120
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
122-534 4.38e-13

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 72.53  E-value: 4.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 122 LKEKFTEDDY-DCFENLFQSKGTESKPQVVFLSGGAGVGKTLMLKRLMLAWIESPVFLHKFsYIFYFCCREVKqlKTASL 200
Cdd:COG5635  154 LDDLYVPLNLlERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLA--EEASL 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 201 AELISREW----PGPSAPIEEILSKPeKLLFIIDSLEgmecdlfkwesELCDNCTEKQPVNvLLSSLLRRkmLPESSLLI 276
Cdd:COG5635  231 EDLLAEALekrgGEPEDALERLLRNG-RLLLLLDGLD-----------EVPDEADRDEVLN-QLRRFLER--YPKARVII 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 277 SATPESFEkmENRIEYTHVKIIKGLKERNIKMSFHRLFQDRNRAHEAF-SLVRENEQLFTVCQVPVLCWMVATCLKEEIE 355
Cdd:COG5635  296 TSRPEGYD--SSELEGFEVLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRERGE 373

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 356 KGRDPVSICR-CTTSLYTTHIFNlfipQNAHSPSKKSQDQLQGLCSLAAEGMWT-DTFVFGEEALRR------NGIMDSD 427
Cdd:COG5635  374 LPDTRAELYEqFVELLLERWDEQ----RGLTIYRELSREELRELLSELALAMQEnGRTEFAREELEEilreylGRRKDAE 449

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 428 I---PILLDIGMLinIRESEKSYIFLHPSVQEVCAA----------IFYLLKSHVDHPS-QEVKsieKLMFAFLKKVKvq 493
Cdd:COG5635  450 AlldELLLRTGLL--VERGEGRYSFAHRSFQEYLAAralveeldeeLLELLAEHLEDPRwREVL---LLLAGLLDDVK-- 522

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 755519588 494 wiFFGSFIFGLLHESEQKKLEAFFGHQLSQEIKRQLYQCLE 534
Cdd:COG5635  523 --QIKELIDALLARDDAAALALAAALLLALLLALALLALLA 561
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 393-449 4.91e-09

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: 52.57  E-value: 4.91e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755519588  393 DQLQGLCSLAAEGMWTDTFVFGEEALRRNGIMDSDIPILLDIGMLINIRESEKSYIF 449
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 148-316 2.32e-33

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: 125.50  E-value: 2.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  148 QVVFLSGGAGVGKTLMLKRLMLAWIESPVFlHKFSYIFYFCCREVKQLKTA-SLAELISREWPGPSAPIEE----ILSKP 222
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLP-QGFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  223 EKLLFIIDSLEGMeCDLFKWESELCdnctekqPVNVLLSSLLRRKMLPESSLLISATPESFEKMENRIEYTHVKIIKGLK 302
Cdd:pfam05729  80 ERLLLILDGLDEL-VSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....
gi 755519588  303 ERNIKMSFHRLFQD 316
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-91 4.54e-32

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.


Pssm-ID: 260032  Cd Length: 84  Bit Score: 118.88  E-value: 4.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  10 LMWYLEELNKKEFVKFKEFLKQEVLQLGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIERAKR 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ..
gi 755519588  90 EI 91
Cdd:cd08320   81 EM 82
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 9-85 5.49e-25

PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the same fold as the pfam00531 domain. This similarity may mean that this is a protein-protein interaction domain.


Pssm-ID: 460678  Cd Length: 76  Bit Score: 98.43  E-value: 5.49e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755519588    9 GLMWYLEELNKKEFVKFKEFLKQEVlQLGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIE 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 451-564 2.05e-21

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: 90.04  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588  451 HPSVQEVCAAIFYLLKSHVDHP--------SQEVKSIEKLMFAFLKKVKVQWIFFGSFIFGLLHESEQKKLEAFFGHQLS 522
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 755519588  523 QEIKRQLYQCLETISGNEELQEqiDGMKLFYCLFEMDDDTFL 564
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFV 120
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 10-86 1.10e-13

Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated speck-like protein containing a CARD) and similar proteins. ASC is an adaptor molecule that functions in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. ASC contains two domains from the Death Domain (DD) superfamily, an N-terminal pyrin-like domain and a C-terminal Caspase activation and recruitment domain (CARD). Through these 2 domains, ASC serves as an adaptor for inflammasome integrity and oligomerizes to form supramolecular assemblies. Included in this family is human PYNOD (also known as NLRP10 or NOD8) which via its Pyrin domain suppresses oligomerization of ASC, and ASC-mediated NF-kappaB activation. Other members of this subfamily are associated with ATPase domains and their function remains unknown. In general, Pyrin is a subfamily of the 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 Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260033  Cd Length: 82  Bit Score: 66.39  E-value: 1.10e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755519588  10 LMWYLEELNKKEFVKFKEFLKQEVLQlGLKQVSWTEVKKASRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIER 86
Cdd:cd08321    4 LLDALEDLGEEELKKFKWKLRDIPLE-GYPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEK 79
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
122-534 4.38e-13

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 72.53  E-value: 4.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 122 LKEKFTEDDY-DCFENLFQSKGTESKPQVVFLSGGAGVGKTLMLKRLMLAWIESPVFLHKFsYIFYFCCREVKqlKTASL 200
Cdd:COG5635  154 LDDLYVPLNLlERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLA--EEASL 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 201 AELISREW----PGPSAPIEEILSKPeKLLFIIDSLEgmecdlfkwesELCDNCTEKQPVNvLLSSLLRRkmLPESSLLI 276
Cdd:COG5635  231 EDLLAEALekrgGEPEDALERLLRNG-RLLLLLDGLD-----------EVPDEADRDEVLN-QLRRFLER--YPKARVII 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 277 SATPESFEkmENRIEYTHVKIIKGLKERNIKMSFHRLFQDRNRAHEAF-SLVRENEQLFTVCQVPVLCWMVATCLKEEIE 355
Cdd:COG5635  296 TSRPEGYD--SSELEGFEVLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRERGE 373

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 356 KGRDPVSICR-CTTSLYTTHIFNlfipQNAHSPSKKSQDQLQGLCSLAAEGMWT-DTFVFGEEALRR------NGIMDSD 427
Cdd:COG5635  374 LPDTRAELYEqFVELLLERWDEQ----RGLTIYRELSREELRELLSELALAMQEnGRTEFAREELEEilreylGRRKDAE 449

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755519588 428 I---PILLDIGMLinIRESEKSYIFLHPSVQEVCAA----------IFYLLKSHVDHPS-QEVKsieKLMFAFLKKVKvq 493
Cdd:COG5635  450 AlldELLLRTGLL--VERGEGRYSFAHRSFQEYLAAralveeldeeLLELLAEHLEDPRwREVL---LLLAGLLDDVK-- 522

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 755519588 494 wiFFGSFIFGLLHESEQKKLEAFFGHQLSQEIKRQLYQCLE 534
Cdd:COG5635  523 --QIKELIDALLARDDAAALALAAALLLALLLALALLALLA 561
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 393-449 4.91e-09

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: 52.57  E-value: 4.91e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755519588  393 DQLQGLCSLAAEGMWTDTFVFGEEALRRNGIMDSDIPILLDIGMLINIRESEKSYIF 449
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-88 9.20e-05

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.


Pssm-ID: 260019  Cd Length: 73  Bit Score: 41.14  E-value: 9.20e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755519588  10 LMWYLEELNKKEFVKFKEFLKQEVLQLGLKQVSWTevkkasRQDLASLLLKHYEEKPAWDMTFRFFQKINRKDLIERAK 88
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYD------RIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
 
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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