NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|768011997|ref|XP_011525782|]
View 

NACHT, LRR and PYD domains-containing protein 12 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 212-381 8.03e-61

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: 204.46  E-value: 8.03e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   212 TVVMQGAAGIGKSMLAHKVMLDWADGKLFQGrFDYLFYINCREMNQSATECSMQDLIFSCWPEPSAPLQE----LIRVPE 287
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   288 RLLFIIDGFDELKPSFHDPQGPWclcweekrPTELLLNSLIRKKLLPELSLLITTRPTALEKLHRLLEHPRHVEILGFSE 367
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|....
gi 768011997   368 AERKEYFYKYFHNA 381
Cdd:pfam05729  153 SDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 688-979 1.76e-43

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


:

Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 160.98  E-value: 1.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  688 LVQLRPERTVLLDAYSEHLAAALCTNPNLIELSLYRNALGS--RGVKLLCQGLRHpNCKLQNLRLKRCRISSSACEDLSA 765
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRipRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVLES 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  766 ALiANKNLTRMDLSGNGVGFPGMMLLCEGLRHPQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGL 845
Cdd:cd00116   104 LL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  846 RLLCQGLRHpVCRLRTLWLKICRLTAAACDELASTLSVNQSLRELDLSLNELGDLGVLLLCEGLRHPTCKLQTLRLDSCG 925
Cdd:cd00116   183 RALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCND 261

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768011997  926 LTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHPGCKLRVLWLF 979
Cdd:cd00116   262 ITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 514-628 1.22e-34

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: 128.56  E-value: 1.22e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   514 HLSFQEFFAAMYYILDEGEG---------GAGPDQDVTRLLTEYAFSERSFLALTSRFLFGLLNEETRSHLEKSLCWKVS 584
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEksnplkeffGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 768011997   585 PHIKMDLLQWIQSKAQSDGStlQQGSLEFFSCLYEIQEEEFIQQ 628
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELS--SERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 13-92 5.92e-28

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: 107.71  E-value: 5.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   13 LSTYLEELEAVELKKFKLYLGTAT-ELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWERGQR 91
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESlEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  .
gi 768011997   92 E 92
Cdd:cd08320    81 E 81
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 459-512 1.83e-17

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: 77.22  E-value: 1.83e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 768011997   459 RGLCSLAADGLWNQKILFEEQDLRKHGLDGEDVSAFLNMNIFQKDINCERYYSF 512
Cdd:pfam17779    4 LKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 129-200 1.50e-13

Fish-specific NACHT associated domain; This domain is frequently found associated with the NACHT domain (pfam05729) in fish and other vertebrates.


:

Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 66.48  E-value: 1.50e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768011997   129 YRDYVRRKFRLMEDRNARLGECVNLSHRYTRLLLVKEHSNPMQVQQQLLDTGRGHaRTVGHQASPIKIETLF 200
Cdd:pfam14484    1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAS-KKPESEETPIRCEDIF 71
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 212-381 8.03e-61

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: 204.46  E-value: 8.03e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   212 TVVMQGAAGIGKSMLAHKVMLDWADGKLFQGrFDYLFYINCREMNQSATECSMQDLIFSCWPEPSAPLQE----LIRVPE 287
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   288 RLLFIIDGFDELKPSFHDPQGPWclcweekrPTELLLNSLIRKKLLPELSLLITTRPTALEKLHRLLEHPRHVEILGFSE 367
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|....
gi 768011997   368 AERKEYFYKYFHNA 381
Cdd:pfam05729  153 SDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 688-979 1.76e-43

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 160.98  E-value: 1.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  688 LVQLRPERTVLLDAYSEHLAAALCTNPNLIELSLYRNALGS--RGVKLLCQGLRHpNCKLQNLRLKRCRISSSACEDLSA 765
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRipRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVLES 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  766 ALiANKNLTRMDLSGNGVGFPGMMLLCEGLRHPQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGL 845
Cdd:cd00116   104 LL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  846 RLLCQGLRHpVCRLRTLWLKICRLTAAACDELASTLSVNQSLRELDLSLNELGDLGVLLLCEGLRHPTCKLQTLRLDSCG 925
Cdd:cd00116   183 RALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCND 261

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768011997  926 LTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHPGCKLRVLWLF 979
Cdd:cd00116   262 ITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 514-628 1.22e-34

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: 128.56  E-value: 1.22e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   514 HLSFQEFFAAMYYILDEGEG---------GAGPDQDVTRLLTEYAFSERSFLALTSRFLFGLLNEETRSHLEKSLCWKVS 584
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEksnplkeffGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 768011997   585 PHIKMDLLQWIQSKAQSDGStlQQGSLEFFSCLYEIQEEEFIQQ 628
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELS--SERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 13-92 5.92e-28

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: 107.71  E-value: 5.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   13 LSTYLEELEAVELKKFKLYLGTAT-ELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWERGQR 91
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESlEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  .
gi 768011997   92 E 92
Cdd:cd08320    81 E 81
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 12-87 7.18e-27

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: 104.59  E-value: 7.18e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768011997    12 RLSTYLEELEAVELKKFKLYLGTATELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWE 87
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLEDEPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 742-966 2.86e-25

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 109.88  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  742 NCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVGFPGMmllceglrhpqcrlqmiqlrkcqlesgacQEMA 821
Cdd:COG5238   179 NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGA-----------------------------EILA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  822 SVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVcRLRTLWLKICRLTAAACDELASTLSVNQSLRELDLSLNELGDLG 901
Cdd:COG5238   230 EALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEG 308

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768011997  902 VLLLCEGLRHpTCKLQTLRLDSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRL 966
Cdd:COG5238   309 AIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL 372
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
213-569 5.05e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 102.58  E-value: 5.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  213 VVMQGAAGIGKSMLAHKVMLDWADGKLFQGRFdYLFYINCREMnqsATECSMQDLI----FSCWPEPSAPLQELIRvPER 288
Cdd:COG5635   183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDL---AEEASLEDLLaealEKRGGEPEDALERLLR-NGR 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  289 LLFIIDGFDELKPSFHDPQgpwCLCWeekrptellLNSLIRKklLPELSLLITTRPTALEKlhRLLEHPRHVEILGFSEA 368
Cdd:COG5635   258 LLLLLDGLDEVPDEADRDE---VLNQ---------LRRFLER--YPKARVIITSRPEGYDS--SELEGFEVLELAPLSDE 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  369 ERKEYFYKYF-HNAEQAGQVFNYVRDNEPLFTMCFVPLVCWVVCTCLQQQlegggllRQTSRTTTAVYMLYLLSLMQ--- 444
Cdd:COG5635   322 QIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLALLLRER-------GELPDTRAELYEQFVELLLErwd 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  445 ---PKPGAPRLQPPPNQRGLCSLAADGLWNQKILFEEQDLRKHGLD----GEDVSAFLNMNIFQKDINCER---YYSFIH 514
Cdd:COG5635   395 eqrGLTIYRELSREELRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDELLLRTGLLVERgegRYSFAH 474

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768011997  515 LSFQEFFAAmYYILDEGEggAGPDQDVTRLLTEYAFSErsflalTSRFLFGLLNE 569
Cdd:COG5635   475 RSFQEYLAA-RALVEELD--EELLELLAEHLEDPRWRE------VLLLLAGLLDD 520
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 459-512 1.83e-17

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: 77.22  E-value: 1.83e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 768011997   459 RGLCSLAADGLWNQKILFEEQDLRKHGLDGEDVSAFLNMNIFQKDINCERYYSF 512
Cdd:pfam17779    4 LKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 129-200 1.50e-13

Fish-specific NACHT associated domain; This domain is frequently found associated with the NACHT domain (pfam05729) in fish and other vertebrates.


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 66.48  E-value: 1.50e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768011997   129 YRDYVRRKFRLMEDRNARLGECVNLSHRYTRLLLVKEHSNPMQVQQQLLDTGRGHaRTVGHQASPIKIETLF 200
Cdd:pfam14484    1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAS-KKPESEETPIRCEDIF 71
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
884-911 7.50e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.47  E-value: 7.50e-05
                            10        20
                    ....*....|....*....|....*...
gi 768011997    884 NQSLRELDLSLNELGDLGVLLLCEGLRH 911
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
883-906 3.61e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 35.67  E-value: 3.61e-03
                           10        20
                   ....*....|....*....|....
gi 768011997   883 VNQSLRELDLSLNELGDLGVLLLC 906
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 212-381 8.03e-61

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: 204.46  E-value: 8.03e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   212 TVVMQGAAGIGKSMLAHKVMLDWADGKLFQGrFDYLFYINCREMNQSATECSMQDLIFSCWPEPSAPLQE----LIRVPE 287
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   288 RLLFIIDGFDELKPSFHDPQGPWclcweekrPTELLLNSLIRKKLLPELSLLITTRPTALEKLHRLLEHPRHVEILGFSE 367
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                          170
                   ....*....|....
gi 768011997   368 AERKEYFYKYFHNA 381
Cdd:pfam05729  153 SDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 688-979 1.76e-43

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 160.98  E-value: 1.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  688 LVQLRPERTVLLDAYSEHLAAALCTNPNLIELSLYRNALGS--RGVKLLCQGLRHpNCKLQNLRLKRCRISSSACEDLSA 765
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRipRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVLES 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  766 ALiANKNLTRMDLSGNGVGFPGMMLLCEGLRHPQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGL 845
Cdd:cd00116   104 LL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  846 RLLCQGLRHpVCRLRTLWLKICRLTAAACDELASTLSVNQSLRELDLSLNELGDLGVLLLCEGLRHPTCKLQTLRLDSCG 925
Cdd:cd00116   183 RALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCND 261

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768011997  926 LTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHPGCKLRVLWLF 979
Cdd:cd00116   262 ITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 705-924 1.99e-40

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 152.12  E-value: 1.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  705 HLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHPNCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVG 784
Cdd:cd00116    99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  785 FPGMMLLCEGLRHpQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCRLRTLWL 864
Cdd:cd00116   179 DAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  865 KICRLTAAACDELASTLSVNQSLRELDLSLNELGDLGVLLLCEGLRHPTCKLQTLRLDSC 924
Cdd:cd00116   258 SCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDD 317
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 718-983 1.73e-37

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 143.65  E-value: 1.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  718 ELSLYRNALGSRGVKLLCQGLRHpnckLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGN-------GVGFPGMML 790
Cdd:cd00116     2 QLSLKGELLKTERATELLPKLLC----LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNetgriprGLQSLLQGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  791 LceglrhPQCRLQMIQLRKCQLESGACQEMASVLgTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCRLRTLWLKICRLT 870
Cdd:cd00116    78 T------KGCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  871 AAACDELASTLSVNQSLRELDLSLNELGDLGVLLLCEGLRHpTCKLQTLRLDSCGLTAKACENLYFTLGINQTLTDLYLT 950
Cdd:cd00116   151 GASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLG 229

                         250       260       270
                  ....*....|....*....|....*....|...
gi 768011997  951 NNALGDTGVRLLCKRLSHPGCKLRVLWLFGMDL 983
Cdd:cd00116   230 DNNLTDAGAAALASALLSPNISLLTLSLSCNDI 262
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 514-628 1.22e-34

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: 128.56  E-value: 1.22e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   514 HLSFQEFFAAMYYILDEGEG---------GAGPDQDVTRLLTEYAFSERSFLALTSRFLFGLLNEETRSHLEKSLCWKVS 584
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEksnplkeffGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 768011997   585 PHIKMDLLQWIQSKAQSDGStlQQGSLEFFSCLYEIQEEEFIQQ 628
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELS--SERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 13-92 5.92e-28

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: 107.71  E-value: 5.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997   13 LSTYLEELEAVELKKFKLYLGTAT-ELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWERGQR 91
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESlEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  .
gi 768011997   92 E 92
Cdd:cd08320    81 E 81
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 12-87 7.18e-27

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: 104.59  E-value: 7.18e-27
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768011997    12 RLSTYLEELEAVELKKFKLYLGTATELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWE 87
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLEDEPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 742-966 2.86e-25

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 109.88  E-value: 2.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  742 NCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVGFPGMmllceglrhpqcrlqmiqlrkcqlesgacQEMA 821
Cdd:COG5238   179 NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGA-----------------------------EILA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  822 SVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVcRLRTLWLKICRLTAAACDELASTLSVNQSLRELDLSLNELGDLG 901
Cdd:COG5238   230 EALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEG 308

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768011997  902 VLLLCEGLRHpTCKLQTLRLDSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRL 966
Cdd:COG5238   309 AIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL 372
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 705-966 4.06e-24

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 106.41  E-value: 4.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  705 HLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHPNcKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVG 784
Cdd:COG5238   171 ISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIG 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  785 FPGMMLLCEGLRHPQcRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVcRLRTLWL 864
Cdd:COG5238   250 DEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNL 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  865 KICRLTAAACDELASTLSVNQSLRELDLSLNELGDLGVLLLCEGL-RHPTckLQTLRLDSCGLTAKACENLYFTLGINQt 943
Cdd:COG5238   328 AYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLeGNTT--LRELNLGKNNIGKQGAEALIDALQTNR- 404

                         250       260
                  ....*....|....*....|....*.
gi 768011997  944 LTDLYLTNNALGDTGVRLL---CKRL 966
Cdd:COG5238   405 LHTLILDGNLIGAEAQQRLeqlLERI 430
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
213-569 5.05e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 102.58  E-value: 5.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  213 VVMQGAAGIGKSMLAHKVMLDWADGKLFQGRFdYLFYINCREMnqsATECSMQDLI----FSCWPEPSAPLQELIRvPER 288
Cdd:COG5635   183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDL---AEEASLEDLLaealEKRGGEPEDALERLLR-NGR 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  289 LLFIIDGFDELKPSFHDPQgpwCLCWeekrptellLNSLIRKklLPELSLLITTRPTALEKlhRLLEHPRHVEILGFSEA 368
Cdd:COG5635   258 LLLLLDGLDEVPDEADRDE---VLNQ---------LRRFLER--YPKARVIITSRPEGYDS--SELEGFEVLELAPLSDE 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  369 ERKEYFYKYF-HNAEQAGQVFNYVRDNEPLFTMCFVPLVCWVVCTCLQQQlegggllRQTSRTTTAVYMLYLLSLMQ--- 444
Cdd:COG5635   322 QIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLALLLRER-------GELPDTRAELYEQFVELLLErwd 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  445 ---PKPGAPRLQPPPNQRGLCSLAADGLWNQKILFEEQDLRKHGLD----GEDVSAFLNMNIFQKDINCER---YYSFIH 514
Cdd:COG5635   395 eqrGLTIYRELSREELRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDELLLRTGLLVERgegRYSFAH 474

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 768011997  515 LSFQEFFAAmYYILDEGEggAGPDQDVTRLLTEYAFSErsflalTSRFLFGLLNE 569
Cdd:COG5635   475 RSFQEYLAA-RALVEELD--EELLELLAEHLEDPRWRE------VLLLLAGLLDD 520
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 11-88 4.05e-19

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: 82.57  E-value: 4.05e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768011997   11 CRLSTYLEELEAVELKKFKLYLGTATELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWER 88
Cdd:cd08321     2 DLLLDALEDLGEEELKKFKWKLRDIPLEGYPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEK 79
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 703-930 4.26e-18

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 88.31  E-value: 4.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  703 SEHLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHpNCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNG 782
Cdd:COG5238   225 AEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNR 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  783 VGFPGMMLLCEGLRHpqcrlqmiqlrkcqlesgacqemasvlgtNPHLVELDLTGNALEDLGLRLLCQGLR-HPvcRLRT 861
Cdd:COG5238   304 IGDEGAIALAEGLQG-----------------------------NKTLHTLNLAYNGIGAQGAIALAKALQeNT--TLHS 352

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768011997  862 LWLKICRLTAAACDELASTLSVNQSLRELDLSLNELGDLGVLLLCEGLRHPtcKLQTLRLDSCGLTAKA 930
Cdd:COG5238   353 LDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTN--RLHTLILDGNLIGAEA 419
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 459-512 1.83e-17

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: 77.22  E-value: 1.83e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 768011997   459 RGLCSLAADGLWNQKILFEEQDLRKHGLDGEDVSAFLNMNIFQKDINCERYYSF 512
Cdd:pfam17779    4 LKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 809-968 1.97e-16

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 82.92  E-value: 1.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  809 KCQLESGACQEMASVLgTNPHLVELDLTGNALEDLGLRLLCQGLRHPVcRLRTLWLKICRLTAAACDELASTLSVNQSLR 888
Cdd:COG5238   162 AARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLT 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  889 ELDLSLNELGDLGVLLLCEGLRHPTcKLQTLRLDSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSH 968
Cdd:COG5238   240 TLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG 318
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 677-802 5.90e-14

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 73.93  E-value: 5.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  677 RARCSAGAH-TLLVQLRPERTVLLDAYSEHLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHPNCKLQNLRLKRCRI 755
Cdd:cd00116   183 RALAEGLKAnCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDI 262

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 768011997  756 SSSACEDLSAALIANKNLTRMDLSGNGVGFPGMMLLCEGLRHPQCRL 802
Cdd:cd00116   263 TDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNEL 309
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 129-200 1.50e-13

Fish-specific NACHT associated domain; This domain is frequently found associated with the NACHT domain (pfam05729) in fish and other vertebrates.


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 66.48  E-value: 1.50e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768011997   129 YRDYVRRKFRLMEDRNARLGECVNLSHRYTRLLLVKEHSNPMQVQQQLLDTGRGHaRTVGHQASPIKIETLF 200
Cdd:pfam14484    1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAS-KKPESEETPIRCEDIF 71
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 682-854 2.75e-13

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 73.29  E-value: 2.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  682 AGAHTLLVQLRPERTV-LLDAYSEH--------LAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHpNCKLQNLRLKR 752
Cdd:COG5238   251 EGVIALAEALKNNTTVeTLYLSGNQigaegaiaLAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAY 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  753 CRISSSACEDLSAALIANKNLTRMDLSGNGVGFPGMMLLCEGL-RHPQcrLQMIQLRKCQLESGACQEMASVLGTNpHLV 831
Cdd:COG5238   330 NGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLeGNTT--LRELNLGKNNIGKQGAEALIDALQTN-RLH 406

                         170       180
                  ....*....|....*....|...
gi 768011997  832 ELDLTGNALEDLGLRLLCQGLRH 854
Cdd:COG5238   407 TLILDGNLIGAEAQQRLEQLLER 429
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
715-962 5.40e-09

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.56  E-value: 5.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  715 NLIELSLYRNALGSRGVKLLCQGLRHPNCKLQNLRLKRCRISSSACEDLSAALianKNLTRMDLSGNGVGFPGMMLlcEG 794
Cdd:COG4886    60 LLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNL---TNLESLDLSGNQLTDLPEEL--AN 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  795 LRHpqcrLQMIQLRKCQLESgacqeMASVLGTNPHLVELDLTGNALEDLGLRLlcQGLRHpvcrLRTLWLKICRLTaaac 874
Cdd:COG4886   135 LTN----LKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTDLPEEL--GNLTN----LKELDLSNNQIT---- 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  875 dELASTLSVNQSLRELDLSLNELGDLGVLLlcEGLRhptcKLQTLRLDSCGLTA----KACENL-YFTLGINQ------- 942
Cdd:COG4886   196 -DLPEPLGNLTNLEELDLSGNQLTDLPEPL--ANLT----NLETLDLSNNQLTDlpelGNLTNLeELDLSNNQltdlppl 268

                         250       260
                  ....*....|....*....|....
gi 768011997  943 ----TLTDLYLTNNALGDTGVRLL 962
Cdd:COG4886   269 anltNLKTLDLSNNQLTDLKLKEL 292
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
704-997 2.60e-07

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.17  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  704 EHLAAALCTNPNLIELSLYRNALGSRGVKLlcqglrhPNCK-LQNLRLKRCRISssaceDLSAALIANKNLTRMDLSGNG 782
Cdd:COG4886   126 TDLPEELANLTNLKELDLSNNQLTDLPEPL-------GNLTnLKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQ 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  783 VGFPGMMLlcEGLRhpqcRLQMIQLRKCQLESgacqeMASVLGTNPHLVELDLTGNALEDL----GLRllcqglrhpvcR 858
Cdd:COG4886   194 ITDLPEPL--GNLT----NLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTDLpelgNLT-----------N 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  859 LRTLWLKICRLTAAacdelaSTLSVNQSLRELDLSLNELGDLGVLLLCEGLRHPTCKLQTLRLDS---CGLTAKACENLY 935
Cdd:COG4886   252 LEELDLSNNQLTDL------PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLlelLILLLLLTTLLL 325

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768011997  936 FTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHPGCKLRVLWLFGMDLNKMTHSRLAALRVT 997
Cdd:COG4886   326 LLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLL 387
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 793-994 4.63e-07

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 53.64  E-value: 4.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  793 EGLRHPQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRH--------PVCRLRTLWL 864
Cdd:COG5238    81 AAEAFPTQLLVVDWEGAEEVSPVALAETATAVATPPPDLRRIMAKTLEDSLILYLALPRRINliqvlkdpLGGNAVHLLG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768011997  865 KICRLTAAACDELASTLSvNQSLRELDLSLNELGDLGVLLLCEGLRHPTcKLQTLRLDSCGLTAKACENLYFTLGINQTL 944
Cdd:COG5238   161 LAARLGLLAAISMAKALQ-NNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSL 238

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 768011997  945 TDLYLTNNALGDTGVRLLCKRLSHpGCKLRVLWLFGmdlNKMTHSRLAAL 994
Cdd:COG5238   239 TTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSG---NQIGAEGAIAL 284
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 13-90 1.08e-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: 44.22  E-value: 1.08e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768011997   13 LSTYLEELEAVELKKFKLYLgtateLGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWERGQ 90
Cdd:cd08305     1 LLTGLENITDEEFKMFKSLL-----ASELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
884-911 7.50e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.47  E-value: 7.50e-05
                            10        20
                    ....*....|....*....|....*...
gi 768011997    884 NQSLRELDLSLNELGDLGVLLLCEGLRH 911
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
827-854 8.39e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.39  E-value: 8.39e-04
                            10        20
                    ....*....|....*....|....*...
gi 768011997    827 NPHLVELDLTGNALEDLGLRLLCQGLRH 854
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
770-797 3.13e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.85  E-value: 3.13e-03
                            10        20
                    ....*....|....*....|....*...
gi 768011997    770 NKNLTRMDLSGNGVGFPGMMLLCEGLRH 797
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
883-906 3.61e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 35.67  E-value: 3.61e-03
                           10        20
                   ....*....|....*....|....
gi 768011997   883 VNQSLRELDLSLNELGDLGVLLLC 906
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH