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Conserved domains on  [gi|1958656985|ref|XP_038941325|]
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NACHT, LRR and PYD domains-containing protein 3 isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 2.07e-57

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: 193.29  E-value: 2.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 218 HTVVFQGAAGIGKTILARKIMLDWALGKLFKDkFDYLFFIHCREVSLRAPK-SLADLIISCWPDPNPPVCK----ILCKP 292
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 293 SRILFLMDGFDELQGAFDEHIEEVctdwqkavRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 1958656985 373 EAKRKEYFFKYFSNE 387
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 575-785 2.87e-32

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 127.86  E-value: 2.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 575 FVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQE-EDFVQSAMGHFPKi 653
Cdd:cd00116     1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 654 eINLSTRMDHVVSSFCIKNCHRVKTLSLGF-LHNSPKEEEEEkrGSQPLDQVQCVFPD-PHVACSSRLVNCCLTSSFCRG 731
Cdd:cd00116    80 -GCGLQELDLSDNALGPDGCGVLESLLRSSsLQELKLNNNGL--GDRGLRLLAKGLKDlPPALEKLVLGRNRLEGASCEA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958656985 732 LFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHpGCNIQRLcsSLWFTKICS 785
Cdd:cd00116   157 LAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVL--DLNNNGLTD 207
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-90 5.83e-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: 5.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985  10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKK 89
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  .
gi 1958656985  90 D 90
Cdd:cd08320    81 E 81
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 138-208 3.62e-16

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: 73.80  E-value: 3.62e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656985 138 YRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRT-KMWDRPMSSLKLELLFE 208
Cdd:pfam14484   1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 466-518 2.38e-13

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: 65.28  E-value: 2.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958656985 466 GLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSF 518
Cdd:pfam17779   5 KLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 2.07e-57

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: 193.29  E-value: 2.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 218 HTVVFQGAAGIGKTILARKIMLDWALGKLFKDkFDYLFFIHCREVSLRAPK-SLADLIISCWPDPNPPVCK----ILCKP 292
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 293 SRILFLMDGFDELQGAFDEHIEEVctdwqkavRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 1958656985 373 EAKRKEYFFKYFSNE 387
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 575-785 2.87e-32

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: 127.86  E-value: 2.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 575 FVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQE-EDFVQSAMGHFPKi 653
Cdd:cd00116     1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 654 eINLSTRMDHVVSSFCIKNCHRVKTLSLGF-LHNSPKEEEEEkrGSQPLDQVQCVFPD-PHVACSSRLVNCCLTSSFCRG 731
Cdd:cd00116    80 -GCGLQELDLSDNALGPDGCGVLESLLRSSsLQELKLNNNGL--GDRGLRLLAKGLKDlPPALEKLVLGRNRLEGASCEA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958656985 732 LFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHpGCNIQRLcsSLWFTKICS 785
Cdd:cd00116   157 LAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVL--DLNNNGLTD 207
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 520-645 6.35e-31

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: 117.39  E-value: 6.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 520 HMTFQEFFAAMYYLLEEEEEGVTVRKGPEGCSdlLNRDVKVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCK 599
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR--KRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958656985 600 ISQQVRLELLKWIevKAKAKKLQRQPSQLELFYCLYEMQEEDFVQS 645
Cdd:pfam17776  79 LSSEIKQELLQWI--KSLIQKELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-90 5.83e-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: 5.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985  10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKK 89
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  .
gi 1958656985  90 D 90
Cdd:cd08320    81 E 81
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 1.40e-25

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


Pssm-ID: 460678  Cd Length: 76  Bit Score: 100.36  E-value: 1.40e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656985  10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCvPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWE 85
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEPEEGLR-SIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
199-529 6.77e-24

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 107.97  E-value: 6.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 199 SSLKLELLFEPEDEHLepvhtvVFQGAAGIGKTILARKIMLDWALGKLFKDkfDYL-FFIHCREvsLRAPKSLADLI--- 274
Cdd:COG5635   168 ESLKRLELLEAKKKRL------LILGEPGSGKTTLLRYLALELAERYLDAE--DPIpILIELRD--LAEEASLEDLLaea 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 275 ISCWPDPNPPVCKILCKPSRILFLMDGFDELqgAFDEHIEEVCTDwqkavrgdilLSSLIRKklLPKASLLITTRPVALE 354
Cdd:COG5635   238 LEKRGGEPEDALERLLRNGRLLLLLDGLDEV--PDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYD 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 355 klQHLLDHPRHVEILGFSEAKRKEYFFKYFSNELQAREAF-RLIQENEILFTMCFIPLVCWIVCTGLKQQMETGKSLAQt 433
Cdd:COG5635   304 --SSELEGFEVLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE- 380

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 434 sktttaVYVFFLSSLLQSRGGIEEHLFSAYLPG------LCSLAADGIWNQKILFEECDLRKHGLQ----KTDVSAFL-- 501
Cdd:COG5635   381 ------LYEQFVELLLERWDEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLde 454

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958656985 502 ---RMNVFQKEVdcERFYSFSHMTFQEFFAA 529
Cdd:COG5635   455 lllRTGLLVERG--EGRYSFAHRSFQEYLAA 483
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 138-208 3.62e-16

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: 73.80  E-value: 3.62e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656985 138 YRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRT-KMWDRPMSSLKLELLFE 208
Cdd:pfam14484   1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 466-518 2.38e-13

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: 65.28  E-value: 2.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958656985 466 GLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSF 518
Cdd:pfam17779   5 KLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
739-766 7.57e-08

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 48.56  E-value: 7.57e-08
                           10        20
                   ....*....|....*....|....*...
gi 1958656985  739 NQSLTELDLSDNTLGDPGMRVLCEALQH 766
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 730-766 3.56e-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: 44.01  E-value: 3.56e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958656985 730 RGLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQH 766
Cdd:COG5238   282 IALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG 318
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 2.07e-57

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: 193.29  E-value: 2.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 218 HTVVFQGAAGIGKTILARKIMLDWALGKLFKDkFDYLFFIHCREVSLRAPK-SLADLIISCWPDPNPPVCK----ILCKP 292
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 293 SRILFLMDGFDELQGAFDEHIEEVctdwqkavRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 1958656985 373 EAKRKEYFFKYFSNE 387
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 575-785 2.87e-32

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: 127.86  E-value: 2.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 575 FVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQE-EDFVQSAMGHFPKi 653
Cdd:cd00116     1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 654 eINLSTRMDHVVSSFCIKNCHRVKTLSLGF-LHNSPKEEEEEkrGSQPLDQVQCVFPD-PHVACSSRLVNCCLTSSFCRG 731
Cdd:cd00116    80 -GCGLQELDLSDNALGPDGCGVLESLLRSSsLQELKLNNNGL--GDRGLRLLAKGLKDlPPALEKLVLGRNRLEGASCEA 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958656985 732 LFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHpGCNIQRLcsSLWFTKICS 785
Cdd:cd00116   157 LAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVL--DLNNNGLTD 207
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 520-645 6.35e-31

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: 117.39  E-value: 6.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 520 HMTFQEFFAAMYYLLEEEEEGVTVRKGPEGCSdlLNRDVKVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCK 599
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR--KRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958656985 600 ISQQVRLELLKWIevKAKAKKLQRQPSQLELFYCLYEMQEEDFVQS 645
Cdd:pfam17776  79 LSSEIKQELLQWI--KSLIQKELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-90 5.83e-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: 5.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985  10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKK 89
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                  .
gi 1958656985  90 D 90
Cdd:cd08320    81 E 81
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 1.40e-25

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


Pssm-ID: 460678  Cd Length: 76  Bit Score: 100.36  E-value: 1.40e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656985  10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCvPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWE 85
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEPEEGLR-SIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
199-529 6.77e-24

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 107.97  E-value: 6.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 199 SSLKLELLFEPEDEHLepvhtvVFQGAAGIGKTILARKIMLDWALGKLFKDkfDYL-FFIHCREvsLRAPKSLADLI--- 274
Cdd:COG5635   168 ESLKRLELLEAKKKRL------LILGEPGSGKTTLLRYLALELAERYLDAE--DPIpILIELRD--LAEEASLEDLLaea 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 275 ISCWPDPNPPVCKILCKPSRILFLMDGFDELqgAFDEHIEEVCTDwqkavrgdilLSSLIRKklLPKASLLITTRPVALE 354
Cdd:COG5635   238 LEKRGGEPEDALERLLRNGRLLLLLDGLDEV--PDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYD 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 355 klQHLLDHPRHVEILGFSEAKRKEYFFKYFSNELQAREAF-RLIQENEILFTMCFIPLVCWIVCTGLKQQMETGKSLAQt 433
Cdd:COG5635   304 --SSELEGFEVLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE- 380

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985 434 sktttaVYVFFLSSLLQSRGGIEEHLFSAYLPG------LCSLAADGIWNQKILFEECDLRKHGLQ----KTDVSAFL-- 501
Cdd:COG5635   381 ------LYEQFVELLLERWDEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLde 454

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1958656985 502 ---RMNVFQKEVdcERFYSFSHMTFQEFFAA 529
Cdd:COG5635   455 lllRTGLLVERG--EGRYSFAHRSFQEYLAA 483
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 7-86 5.02e-22

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: 90.66  E-value: 5.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656985   7 RCKLAQYLEDLEDVDLKKFKMHLEDYPPEkGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEK 86
Cdd:cd08321     1 RDLLLDALEDLGEEELKKFKWKLRDIPLE-GYPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEK 79
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 138-208 3.62e-16

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: 73.80  E-value: 3.62e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656985 138 YRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRT-KMWDRPMSSLKLELLFE 208
Cdd:pfam14484   1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 466-518 2.38e-13

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: 65.28  E-value: 2.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958656985 466 GLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSF 518
Cdd:pfam17779   5 KLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
739-766 7.57e-08

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 48.56  E-value: 7.57e-08
                           10        20
                   ....*....|....*....|....*...
gi 1958656985  739 NQSLTELDLSDNTLGDPGMRVLCEALQH 766
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-88 5.71e-06

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: 44.60  E-value: 5.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656985  10 LAQYLEDLEDVDLKKFKMHLEDYppekgcVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAK 88
Cdd:cd08305     1 LLTGLENITDEEFKMFKSLLASE------LKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
LRR_6 pfam13516
Leucine Rich repeat;
738-761 1.19e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 39.53  E-value: 1.19e-04
                          10        20
                  ....*....|....*....|....
gi 1958656985 738 TNQSLTELDLSDNTLGDPGMRVLC 761
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 730-766 3.56e-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: 44.01  E-value: 3.56e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958656985 730 RGLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQH 766
Cdd:COG5238   282 IALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG 318
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 731-767 5.43e-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: 43.24  E-value: 5.43e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958656985 731 GLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHP 767
Cdd:COG5238   227 ILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN 263
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-765 6.46e-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: 42.85  E-value: 6.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1958656985 729 CRGLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQ 765
Cdd:COG5238   337 AIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLE 373
 
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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