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Conserved domains on  [gi|2462523376|ref|XP_054223863|]
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NACHT, LRR and PYD domains-containing protein 6 isoform X1 [Homo sapiens]

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 ...
 197-350 4.06e-45

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: 159.39  E-value: 4.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 197 TVVLQGPAGIGKTMAAKKILYDWAAGKLYQGqVDFAFFMPCGELLERAGTRSLADLILDQCPDRGAPVPQ----MLAQPQ 272
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523376 273 RLLFILDGADELPALGGPEAAPCtdpfeaaSGARVLGGLLSKALLPTALLLVTTRAAAPGRLQGRLCSPQCAEVRGFS 350
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 501-636 5.06e-22

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: 91.97  E-value: 5.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 501 SFQEFLAALSYLL---EDGGVPRTAAGGVGT-------LLRGDAQPHSHLVLTTRFLFGLLSAERMRDIERHFGCMVSER 570
Cdd:pfam17776   3 SFQEFFAALFYVLsfkEEKSNPLKEFFGLRKreslkslLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLSSE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523376 571 VKQEALRWVQGQGQgcpgvapevtegakgledteepeeeeEGEEPNYPLELLYCLYETQEDAFVRQ 636
Cdd:pfam17776  83 IKQELLQWIKSLIQ--------------------------KELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 31-99 2.13e-21

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: 88.74  E-value: 2.13e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376  31 QEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQE 99
Cdd:cd08321    13 EEELKKFKWKLRDIPLEGyPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEKLQK 82
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 442-497 1.57e-06

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: 45.63  E-value: 1.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523376 442 LRNLCRLAREGVLGRRAQFAEKELEQLELRGSKVQTLFLSKKELPgVLETEVTYQF 497
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK-DLGCEKVYSF 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 ...
 197-350 4.06e-45

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: 159.39  E-value: 4.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 197 TVVLQGPAGIGKTMAAKKILYDWAAGKLYQGqVDFAFFMPCGELLERAGTRSLADLILDQCPDRGAPVPQ----MLAQPQ 272
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523376 273 RLLFILDGADELPALGGPEAAPCtdpfeaaSGARVLGGLLSKALLPTALLLVTTRAAAPGRLQGRLCSPQCAEVRGFS 350
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 501-636 5.06e-22

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: 91.97  E-value: 5.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 501 SFQEFLAALSYLL---EDGGVPRTAAGGVGT-------LLRGDAQPHSHLVLTTRFLFGLLSAERMRDIERHFGCMVSER 570
Cdd:pfam17776   3 SFQEFFAALFYVLsfkEEKSNPLKEFFGLRKreslkslLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLSSE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523376 571 VKQEALRWVQGQGQgcpgvapevtegakgledteepeeeeEGEEPNYPLELLYCLYETQEDAFVRQ 636
Cdd:pfam17776  83 IKQELLQWIKSLIQ--------------------------KELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 31-99 2.13e-21

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: 88.74  E-value: 2.13e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376  31 QEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQE 99
Cdd:cd08321    13 EEELKKFKWKLRDIPLEGyPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEKLQK 82
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 30-95 5.38e-17

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: 76.09  E-value: 5.38e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523376  30 SQEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAA 95
Cdd:pfam02758  10 SEEEFKKFKSLLEDEPEEGlRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
35-682 1.27e-16

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 84.47  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376  35 KRFRHKLRDVGPDGRSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRAD-ARDVAAQLQERRLQRLGLGSGTLL 113
Cdd:COG5635    23 TRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALsALLLVLLLLESLLLLLLLLLLLAE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 114 SVSEYKKKYREHVLQLHARVKERNARSVKITKRFTKLLIAPESAAPEEALGPAEEPEPGRARRSDThTFNRLFRRDEEGR 193
Cdd:COG5635   103 ALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIE-SLKRLELLEAKKK 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 194 RpltVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVdFAFFMPCGELlerAGTRSLADLILDQCPDRGAPVPQM---LAQ 270
Cdd:COG5635   182 R---LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDL---AEEASLEDLLAEALEKRGGEPEDAlerLLR 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 271 PQRLLFILDGADELPalggpeaapctDPFEAASGARVLGGLLSKalLPTALLLVTTRAAA--PGRLQGRlcspQCAEVRG 348
Cdd:COG5635   255 NGRLLLLLDGLDEVP-----------DEADRDEVLNQLRRFLER--YPKARVIITSRPEGydSSELEGF----EVLELAP 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 349 FSDKDKKK-YFYKFFRDERRAERAYRFVKENETLFALCFVPFVCWIVCTVLRQQLELGRDLSRtsktttsVYLLFITSVL 427
Cdd:COG5635   318 LSDEQIEEfLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE-------LYEQFVELLL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 428 SSAPVADGPRLQGDL------RNLCRLAREGVLGRRAQFAEKELEQL---ELRGSKVQTLFLSKKELPGVL---ETEVTY 495
Cdd:COG5635   391 ERWDEQRGLTIYRELsreelrELLSELALAMQENGRTEFAREELEEIlreYLGRRKDAEALLDELLLRTGLlveRGEGRY 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 496 QFIDQSFQEFLAALsYLLEDGGVPRTAAggvgtLLRGDAQPHSHLVLttRFLFGLLSaeRMRDIERHFGCMVSERVKQEA 575
Cdd:COG5635   471 SFAHRSFQEYLAAR-ALVEELDEELLEL-----LAEHLEDPRWREVL--LLLAGLLD--DVKQIKELIDALLARDDAAAL 540

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 576 LRWVQGQGQGCPGVAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDAFVRQALCRFPELALQRVRFCRMD 655
Cdd:COG5635   541 ALAAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLLLLALAL 620

                         650       660
                  ....*....|....*....|....*..
gi 2462523376 656 VAVLSYCVRCCPAGQALRLISCRLVAA 682
Cdd:COG5635   621 LLALLLLLLLLLLAELLLLALLALVLL 647
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 442-497 1.57e-06

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: 45.63  E-value: 1.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523376 442 LRNLCRLAREGVLGRRAQFAEKELEQLELRGSKVQTLFLSKKELPgVLETEVTYQF 497
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK-DLGCEKVYSF 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 ...
 197-350 4.06e-45

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: 159.39  E-value: 4.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 197 TVVLQGPAGIGKTMAAKKILYDWAAGKLYQGqVDFAFFMPCGELLERAGTRSLADLILDQCPDRGAPVPQ----MLAQPQ 272
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462523376 273 RLLFILDGADELPALGGPEAAPCtdpfeaaSGARVLGGLLSKALLPTALLLVTTRAAAPGRLQGRLCSPQCAEVRGFS 350
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 501-636 5.06e-22

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: 91.97  E-value: 5.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 501 SFQEFLAALSYLL---EDGGVPRTAAGGVGT-------LLRGDAQPHSHLVLTTRFLFGLLSAERMRDIERHFGCMVSER 570
Cdd:pfam17776   3 SFQEFFAALFYVLsfkEEKSNPLKEFFGLRKreslkslLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLSSE 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523376 571 VKQEALRWVQGQGQgcpgvapevtegakgledteepeeeeEGEEPNYPLELLYCLYETQEDAFVRQ 636
Cdd:pfam17776  83 IKQELLQWIKSLIQ--------------------------KELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 31-99 2.13e-21

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: 88.74  E-value: 2.13e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376  31 QEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQE 99
Cdd:cd08321    13 EEELKKFKWKLRDIPLEGyPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEKLQK 82
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 30-95 5.38e-17

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: 76.09  E-value: 5.38e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523376  30 SQEQLKRFRHKLRDVGPDG-RSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAA 95
Cdd:pfam02758  10 SEEEFKKFKSLLEDEPEEGlRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
35-682 1.27e-16

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 84.47  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376  35 KRFRHKLRDVGPDGRSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRAD-ARDVAAQLQERRLQRLGLGSGTLL 113
Cdd:COG5635    23 TRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALsALLLVLLLLESLLLLLLLLLLLAE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 114 SVSEYKKKYREHVLQLHARVKERNARSVKITKRFTKLLIAPESAAPEEALGPAEEPEPGRARRSDThTFNRLFRRDEEGR 193
Cdd:COG5635   103 ALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIE-SLKRLELLEAKKK 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 194 RpltVVLQGPAGIGKTMAAKKILYDWAAGKLYQGQVdFAFFMPCGELlerAGTRSLADLILDQCPDRGAPVPQM---LAQ 270
Cdd:COG5635   182 R---LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDL---AEEASLEDLLAEALEKRGGEPEDAlerLLR 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 271 PQRLLFILDGADELPalggpeaapctDPFEAASGARVLGGLLSKalLPTALLLVTTRAAA--PGRLQGRlcspQCAEVRG 348
Cdd:COG5635   255 NGRLLLLLDGLDEVP-----------DEADRDEVLNQLRRFLER--YPKARVIITSRPEGydSSELEGF----EVLELAP 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 349 FSDKDKKK-YFYKFFRDERRAERAYRFVKENETLFALCFVPFVCWIVCTVLRQQLELGRDLSRtsktttsVYLLFITSVL 427
Cdd:COG5635   318 LSDEQIEEfLKKWFEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE-------LYEQFVELLL 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 428 SSAPVADGPRLQGDL------RNLCRLAREGVLGRRAQFAEKELEQL---ELRGSKVQTLFLSKKELPGVL---ETEVTY 495
Cdd:COG5635   391 ERWDEQRGLTIYRELsreelrELLSELALAMQENGRTEFAREELEEIlreYLGRRKDAEALLDELLLRTGLlveRGEGRY 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 496 QFIDQSFQEFLAALsYLLEDGGVPRTAAggvgtLLRGDAQPHSHLVLttRFLFGLLSaeRMRDIERHFGCMVSERVKQEA 575
Cdd:COG5635   471 SFAHRSFQEYLAAR-ALVEELDEELLEL-----LAEHLEDPRWREVL--LLLAGLLD--DVKQIKELIDALLARDDAAAL 540

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462523376 576 LRWVQGQGQGCPGVAPEVTEGAKGLEDTEEPEEEEEGEEPNYPLELLYCLYETQEDAFVRQALCRFPELALQRVRFCRMD 655
Cdd:COG5635   541 ALAAALLLALLLALALLALLALLLLLRLLLALLALLLLALLLLLLLALLLALLALDLGLAALLLLLLLLLLLLLLLALAL 620

                         650       660
                  ....*....|....*....|....*..
gi 2462523376 656 VAVLSYCVRCCPAGQALRLISCRLVAA 682
Cdd:COG5635   621 LLALLLLLLLLLLAELLLLALLALVLL 647
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 442-497 1.57e-06

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: 45.63  E-value: 1.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462523376 442 LRNLCRLAREGVLGRRAQFAEKELEQLELRGSKVQTLFLSKKELPgVLETEVTYQF 497
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQK-DLGCEKVYSF 57
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 30-101 4.67e-06

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: 45.31  E-value: 4.67e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462523376  30 SQEQLKRFRHKLRDVGPDGRS--IPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQERR 101
Cdd:cd08320     9 SKEELKKFKLLLKEESLEGGLkpIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARAEM 82
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 32-98 2.18e-04

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: 40.37  E-value: 2.18e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462523376  32 EQLKRFRHKLRDVGpdgrSIPWGRLERADAVDLAEQLAQFYGPEPALEVARKTLKRADARDVAAQLQ 98
Cdd:cd08305    11 EEFKMFKSLLASEL----KLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 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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