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Conserved domains on  [gi|1784638299|ref|NP_899632|]
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NACHT, LRR and PYD domains-containing protein 3 isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 573-920 2.86e-77

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: 254.59  E-value: 2.86e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 573 FVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQE-EDFVQRAMDYFPKI 651
Cdd:cd00116     1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 652 eiNLSTRMDHMVSSFCIENCHRVESLSLGF-LHNMPKEEEEEEkeGRHLDMVQCVLPSSSHAACSHGLGRCGLSHECCFD 730
Cdd:cd00116    81 --CGLQELDLSDNALGPDGCGVLESLLRSSsLQELKLNNNGLG--DRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 731 ISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLlCNLKKLWLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGD 810
Cdd:cd00116   157 LAKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 811 KGIKLLCEGLLHPdcklqvleldncnltshccwdlstlltsSQSLRKLSLGNNDLGDLGVMMFCEVLKQQsCLLQNLGLS 890
Cdd:cd00116   236 AGAAALASALLSP----------------------------NISLLTLSLSCNDITDDGAKDLAEVLAEK-ESLLELDLR 286

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1784638299 891 EMYFNYE--TKSALETLQE-EKPELTVVFEPSW 920
Cdd:cd00116   287 GNKFGEEgaQLLAESLLEPgNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 2.39e-56

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: 191.36  E-value: 2.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 218 HTVVFQGAAGIGKTILARKMMLDWASGTLYQDrFDYLFYIHCREVSLVT-QRSLGDLIMSCCPDPNPPIHK----IVRKP 292
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 293 SRILFLMDGFDELQGAFDEHIGPLctdwqkaeRGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 1784638299 373 EAKRKEYFFKYFSDE 387
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 8-91 1.40e-27

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: 106.56  E-value: 1.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299   8 LARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKR 87
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  ....
gi 1784638299  88 DEPK 91
Cdd:cd08320    81 EMNE 84
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
220-560 2.75e-23

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 106.43  E-value: 2.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 220 VVFQGAAGIGKTILARKMMLDWASGTLYQDRFdYLFYIHCREvsLVTQRSLGDLI----MSCCPDPNPPIHKIVRKPsRI 295
Cdd:COG5635   183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRD--LAEEASLEDLLaealEKRGGEPEDALERLLRNG-RL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 296 LFLMDGFDELQgafdehigplctdwQKAERGDIL--LSSLIRKklLPEASLLITTRPVALEklQHLLDHPRHVEILGFSE 373
Cdd:COG5635   259 LLLLDGLDEVP--------------DEADRDEVLnqLRRFLER--YPKARVIITSRPEGYD--SSELEGFEVLELAPLSD 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 374 AKRKEYFFKYF-SDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCtglkQQMESGKSLAQTSkttTAVYVFFLSSLLQPR 452
Cdd:COG5635   321 EQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLA----LLLRERGELPDTR---AELYEQFVELLLERW 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 453 GGSQEHGLCAHLWG------LCSLAADGIWNQKILFEESDLR----NHGLQKADVSAFL-----RMNLFQKEVdcEKFYS 517
Cdd:COG5635   394 DEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEeilrEYLGRRKDAEALLdelllRTGLLVERG--EGRYS 471

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1784638299 518 FIHMTFQEFFAAmYYLLEEEKEGRTNVPGSRLKLPSRDVTVLL 560
Cdd:COG5635   472 FAHRSFQEYLAA-RALVEELDEELLELLAEHLEDPRWREVLLL 513
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 142-208 4.06e-19

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: 82.28  E-value: 4.06e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1784638299 142 VRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKT-KTCESPVSPIKMELLFD 208
Cdd:pfam14484   5 LKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 573-920 2.86e-77

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: 254.59  E-value: 2.86e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 573 FVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQE-EDFVQRAMDYFPKI 651
Cdd:cd00116     1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 652 eiNLSTRMDHMVSSFCIENCHRVESLSLGF-LHNMPKEEEEEEkeGRHLDMVQCVLPSSSHAACSHGLGRCGLSHECCFD 730
Cdd:cd00116    81 --CGLQELDLSDNALGPDGCGVLESLLRSSsLQELKLNNNGLG--DRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 731 ISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLlCNLKKLWLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGD 810
Cdd:cd00116   157 LAKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 811 KGIKLLCEGLLHPdcklqvleldncnltshccwdlstlltsSQSLRKLSLGNNDLGDLGVMMFCEVLKQQsCLLQNLGLS 890
Cdd:cd00116   236 AGAAALASALLSP----------------------------NISLLTLSLSCNDITDDGAKDLAEVLAEK-ESLLELDLR 286

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1784638299 891 EMYFNYE--TKSALETLQE-EKPELTVVFEPSW 920
Cdd:cd00116   287 GNKFGEEgaQLLAESLLEPgNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 2.39e-56

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: 191.36  E-value: 2.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 218 HTVVFQGAAGIGKTILARKMMLDWASGTLYQDrFDYLFYIHCREVSLVT-QRSLGDLIMSCCPDPNPPIHK----IVRKP 292
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 293 SRILFLMDGFDELQGAFDEHIGPLctdwqkaeRGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 1784638299 373 EAKRKEYFFKYFSDE 387
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 520-643 8.05e-38

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: 137.42  E-value: 8.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 520 HMTFQEFFAAMYYLLEEEKEGRTNVPGSRLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKIS 599
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1784638299 600 QQIRLELLKWIEVKAKAKKLqiQPSQLELFYCLYEMQEEDFVQR 643
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 ...
 8-91 1.40e-27

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: 106.56  E-value: 1.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299   8 LARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKR 87
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  ....
gi 1784638299  88 DEPK 91
Cdd:cd08320    81 EMNE 84
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
220-560 2.75e-23

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 106.43  E-value: 2.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 220 VVFQGAAGIGKTILARKMMLDWASGTLYQDRFdYLFYIHCREvsLVTQRSLGDLI----MSCCPDPNPPIHKIVRKPsRI 295
Cdd:COG5635   183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRD--LAEEASLEDLLaealEKRGGEPEDALERLLRNG-RL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 296 LFLMDGFDELQgafdehigplctdwQKAERGDIL--LSSLIRKklLPEASLLITTRPVALEklQHLLDHPRHVEILGFSE 373
Cdd:COG5635   259 LLLLDGLDEVP--------------DEADRDEVLnqLRRFLER--YPKARVIITSRPEGYD--SSELEGFEVLELAPLSD 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 374 AKRKEYFFKYF-SDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCtglkQQMESGKSLAQTSkttTAVYVFFLSSLLQPR 452
Cdd:COG5635   321 EQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLA----LLLRERGELPDTR---AELYEQFVELLLERW 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 453 GGSQEHGLCAHLWG------LCSLAADGIWNQKILFEESDLR----NHGLQKADVSAFL-----RMNLFQKEVdcEKFYS 517
Cdd:COG5635   394 DEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEeilrEYLGRRKDAEALLdelllRTGLLVERG--EGRYS 471

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1784638299 518 FIHMTFQEFFAAmYYLLEEEKEGRTNVPGSRLKLPSRDVTVLL 560
Cdd:COG5635   472 FAHRSFQEYLAA-RALVEELDEELLELLAEHLEDPRWREVLLL 513
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-83 5.73e-23

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: 93.42  E-value: 5.73e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1784638299   8 LARYLEDLEDVDLKKFKMHLEDYPpQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYE 83
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 142-208 4.06e-19

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: 82.28  E-value: 4.06e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1784638299 142 VRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKT-KTCESPVSPIKMELLFD 208
Cdd:pfam14484   5 LKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 464-518 3.00e-14

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: 67.98  E-value: 3.00e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1784638299 464 LWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSF 518
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 721-890 1.57e-12

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: 70.59  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 721 CGLSHECCFDISLVLSsNQKLVELDLSDNALGDFGIRLLCvglKHLLCN--LKKLWLVNSGLTSVCCSALSSVLSTNQNL 798
Cdd:COG5238   163 ARLGLLAAISMAKALQ-NNSVETVYLGCNQIGDEGIEELA---EALTQNttVTTLWLKRNPIGDEGAEILAEALKGNKSL 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 799 THLYLRGNTLGDKGIKLLCEGLLHPDcKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLk 878
Cdd:COG5238   239 TTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL- 316

                         170
                  ....*....|..
gi 1784638299 879 QQSCLLQNLGLS 890
Cdd:COG5238   317 QGNKTLHTLNLA 328
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
738-765 8.03e-06

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 43.16  E-value: 8.03e-06
                           10        20
                   ....*....|....*....|....*...
gi 1784638299  738 NQKLVELDLSDNALGDFGIRLLCVGLKH 765
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 573-920 2.86e-77

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: 254.59  E-value: 2.86e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 573 FVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQE-EDFVQRAMDYFPKI 651
Cdd:cd00116     1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTKG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 652 eiNLSTRMDHMVSSFCIENCHRVESLSLGF-LHNMPKEEEEEEkeGRHLDMVQCVLPSSSHAACSHGLGRCGLSHECCFD 730
Cdd:cd00116    81 --CGLQELDLSDNALGPDGCGVLESLLRSSsLQELKLNNNGLG--DRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 731 ISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLlCNLKKLWLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGD 810
Cdd:cd00116   157 LAKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTD 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 811 KGIKLLCEGLLHPdcklqvleldncnltshccwdlstlltsSQSLRKLSLGNNDLGDLGVMMFCEVLKQQsCLLQNLGLS 890
Cdd:cd00116   236 AGAAALASALLSP----------------------------NISLLTLSLSCNDITDDGAKDLAEVLAEK-ESLLELDLR 286

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1784638299 891 EMYFNYE--TKSALETLQE-EKPELTVVFEPSW 920
Cdd:cd00116   287 GNKFGEEgaQLLAESLLEPgNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 2.39e-56

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: 191.36  E-value: 2.39e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 218 HTVVFQGAAGIGKTILARKMMLDWASGTLYQDrFDYLFYIHCREVSLVT-QRSLGDLIMSCCPDPNPPIHK----IVRKP 292
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 293 SRILFLMDGFDELQGAFDEHIGPLctdwqkaeRGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 1784638299 373 EAKRKEYFFKYFSDE 387
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 520-643 8.05e-38

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: 137.42  E-value: 8.05e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 520 HMTFQEFFAAMYYLLEEEKEGRTNVPGSRLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKIS 599
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1784638299 600 QQIRLELLKWIEVKAKAKKLqiQPSQLELFYCLYEMQEEDFVQR 643
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 ...
 8-91 1.40e-27

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: 106.56  E-value: 1.40e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299   8 LARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKR 87
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  ....
gi 1784638299  88 DEPK 91
Cdd:cd08320    81 EMNE 84
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
220-560 2.75e-23

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 106.43  E-value: 2.75e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 220 VVFQGAAGIGKTILARKMMLDWASGTLYQDRFdYLFYIHCREvsLVTQRSLGDLI----MSCCPDPNPPIHKIVRKPsRI 295
Cdd:COG5635   183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRD--LAEEASLEDLLaealEKRGGEPEDALERLLRNG-RL 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 296 LFLMDGFDELQgafdehigplctdwQKAERGDIL--LSSLIRKklLPEASLLITTRPVALEklQHLLDHPRHVEILGFSE 373
Cdd:COG5635   259 LLLLDGLDEVP--------------DEADRDEVLnqLRRFLER--YPKARVIITSRPEGYD--SSELEGFEVLELAPLSD 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 374 AKRKEYFFKYF-SDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCtglkQQMESGKSLAQTSkttTAVYVFFLSSLLQPR 452
Cdd:COG5635   321 EQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLA----LLLRERGELPDTR---AELYEQFVELLLERW 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 453 GGSQEHGLCAHLWG------LCSLAADGIWNQKILFEESDLR----NHGLQKADVSAFL-----RMNLFQKEVdcEKFYS 517
Cdd:COG5635   394 DEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEeilrEYLGRRKDAEALLdelllRTGLLVERG--EGRYS 471

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1784638299 518 FIHMTFQEFFAAmYYLLEEEKEGRTNVPGSRLKLPSRDVTVLL 560
Cdd:COG5635   472 FAHRSFQEYLAA-RALVEELDEELLELLAEHLEDPRWREVLLL 513
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-83 5.73e-23

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: 93.42  E-value: 5.73e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1784638299   8 LARYLEDLEDVDLKKFKMHLEDYPpQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYE 83
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 5-84 3.90e-20

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: 85.27  E-value: 3.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299   5 RCKLARYLEDLEDVDLKKFKMHLEDYPpQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEK 84
Cdd:cd08321     1 RDLLLDALEDLGEEELKKFKWKLRDIP-LEGYPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEK 79
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 142-208 4.06e-19

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: 82.28  E-value: 4.06e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1784638299 142 VRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKT-KTCESPVSPIKMELLFD 208
Cdd:pfam14484   5 LKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 464-518 3.00e-14

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: 67.98  E-value: 3.00e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1784638299 464 LWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSF 518
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 721-890 1.57e-12

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: 70.59  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 721 CGLSHECCFDISLVLSsNQKLVELDLSDNALGDFGIRLLCvglKHLLCN--LKKLWLVNSGLTSVCCSALSSVLSTNQNL 798
Cdd:COG5238   163 ARLGLLAAISMAKALQ-NNSVETVYLGCNQIGDEGIEELA---EALTQNttVTTLWLKRNPIGDEGAEILAEALKGNKSL 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 799 THLYLRGNTLGDKGIKLLCEGLLHPDcKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLk 878
Cdd:COG5238   239 TTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGL- 316

                         170
                  ....*....|..
gi 1784638299 879 QQSCLLQNLGLS 890
Cdd:COG5238   317 QGNKTLHTLNLA 328
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 735-908 1.73e-11

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: 67.51  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 735 LSSNQKLVELDLSDNALGDFGIRLLCVGLKHLlCNLKKLWLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIK 814
Cdd:COG5238   288 LQGNTTLTSLDLSVNRIGDEGAIALAEGLQGN-KTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAI 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 815 LLCEgllhpdcklqvleldncnltshccwdlstLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSclLQNLGLSEMYF 894
Cdd:COG5238   367 ALAK-----------------------------YLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR--LHTLILDGNLI 415

                         170
                  ....*....|....
gi 1784638299 895 NYETKSALETLQEE 908
Cdd:COG5238   416 GAEAQQRLEQLLER 429
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
730-913 1.24e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.57  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 730 DISLVLSSNQKLVELDLSDNALGDFGIRLLcvGLKhllcNLKKLWLVNSGLTSvccsaLSSVLSTNQNLTHLYLRGNTLG 809
Cdd:COG4886   150 DLPEPLGNLTNLKSLDLSNNQLTDLPEELG--NLT----NLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLT 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 810 DKGIKLlceGLLHpdcKLQVLELDNCNLTshccwDLSTlLTSSQSLRKLSLGNNDLGDLGvmmfcevlkqQSCLLQNLGL 889
Cdd:COG4886   219 DLPEPL---ANLT---NLETLDLSNNQLT-----DLPE-LGNLTNLEELDLSNNQLTDLP----------PLANLTNLKT 276

                         170       180
                  ....*....|....*....|....
gi 1784638299 890 SEMYFNYETKSALETLQEEKPELT 913
Cdd:COG4886   277 LDLSNNQLTDLKLKELELLLGLNS 300
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
735-868 2.09e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.80  E-value: 2.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 735 LSSNQKLVELDLSDNALGDFGIRLlcVGLKhllcNLKKLWLVNSGLTSvccsaLSSVLSTNQNLTHLYLRGNTLGDKGIK 814
Cdd:COG4886   109 LSNLTNLESLDLSGNQLTDLPEEL--ANLT----NLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTDLPEE 177

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1784638299 815 LlceGLLHpdcKLQVLELDNCNLTshccwDLSTLLTSSQSLRKLSLGNNDLGDL 868
Cdd:COG4886   178 L---GNLT---NLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTDL 220
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
730-868 3.86e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.03  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 730 DISLVLSSNQKLVELDLSDNALGDfgirlLCVGLKHLLcNLKKLWLVNSGLTSvccsaLSSVLSTNQNLTHLYLRGNTLG 809
Cdd:COG4886   127 DLPEELANLTNLKELDLSNNQLTD-----LPEPLGNLT-NLKSLDLSNNQLTD-----LPEELGNLTNLKELDLSNNQIT 195

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1784638299 810 DkgIKLLCEGLlhpdCKLQVLELDNCNLTshccwDLSTLLTSSQSLRKLSLGNNDLGDL 868
Cdd:COG4886   196 D--LPEPLGNL----TNLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTDL 243
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 734-913 1.33e-09

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: 61.34  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 734 VLSSNQKLVELDLSDNALGDFGIRLLCVGLKHLlCNLKKLWLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGI 813
Cdd:COG5238   203 ALTQNTTVTTLWLKRNPIGDEGAEILAEALKGN-KSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGA 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 814 KLLCEgLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQScLLQNLGLSEMY 893
Cdd:COG5238   282 IALAK-ALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENT-TLHSLDLSDNQ 359

                         170       180
                  ....*....|....*....|
gi 1784638299 894 FNYETKSALETLQEEKPELT 913
Cdd:COG5238   360 IGDEGAIALAKYLEGNTTLR 379
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
730-869 6.43e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.63  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 730 DISLVLSSNQKLVELDLSDNALGDFGIRLlcVGLKhllcNLKKLWLVNSGLTSVccsalsSVLSTNQNLTHLYLRGNTLG 809
Cdd:COG4886   196 DLPEPLGNLTNLEELDLSGNQLTDLPEPL--ANLT----NLETLDLSNNQLTDL------PELGNLTNLEELDLSNNQLT 263

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 810 DkgikLLCEGLLHpdcKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLG 869
Cdd:COG4886   264 D----LPPLANLT---NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLIL 316
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
738-765 8.03e-06

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 43.16  E-value: 8.03e-06
                           10        20
                   ....*....|....*....|....*...
gi 1784638299  738 NQKLVELDLSDNALGDFGIRLLCVGLKH 765
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 8-86 1.92e-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: 43.45  E-value: 1.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1784638299   8 LARYLEDLEDVDLKKFKMHLEDYppqkgcIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAK 86
Cdd:cd08305     1 LLTGLENITDEEFKMFKSLLASE------LKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
852-879 6.36e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.47  E-value: 6.36e-05
                           10        20
                   ....*....|....*....|....*...
gi 1784638299  852 SQSLRKLSLGNNDLGDLGVMMFCEVLKQ 879
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 717-822 1.21e-04

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: 45.55  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1784638299 717 GLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDFGIRLLCVGLKhLLCNLKKLWLVNSGLTSVCCSALSSVLSTNQ 796
Cdd:COG5238   326 NLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLE-GNTTLRELNLGKNNIGKQGAEALIDALQTNR 404

                          90       100
                  ....*....|....*....|....*.
gi 1784638299 797 nLTHLYLRGNTLGDKGIKLLCEGLLH 822
Cdd:COG5238   405 -LHTLILDGNLIGAEAQQRLEQLLER 429
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
795-822 1.68e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.31  E-value: 1.68e-04
                           10        20
                   ....*....|....*....|....*...
gi 1784638299  795 NQNLTHLYLRGNTLGDKGIKLLCEGLLH 822
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
794-817 4.91e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 35.29  E-value: 4.91e-03
                          10        20
                  ....*....|....*....|....
gi 1784638299 794 TNQNLTHLYLRGNTLGDKGIKLLC 817
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.
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