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Conserved domains on  [gi|140972011|ref|NP_780499|]
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NACHT, LRR and PYD domains-containing protein 4F [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 636-926 9.53e-36

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: 138.26  E-value: 9.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 636 QELRIKDTNFNEPAIRVLYESLKYPSftlnklvannvsfgdnhvlfeliqnsSLQYLDLSCSFLSHNEVKLLCDILN-QA 714
Cdd:cd00116   26 QVLRLEGNTLGEEAAKALASALRPQP--------------------------SLKELCLSLNETGRIPRGLQSLLQGlTK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 715 ECNIEKLMIAHCKLSPDDCKIFGSILmSSKSLKVLNLASNNL-NQGISSLCKALCHPHCTLEYLVLSNCSLSEQCWDYLS 793
Cdd:cd00116   80 GCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 794 EVLRQNKTLSHLDISSNDLKDEGLKILCRSLiLPYCVLESLCLSCCGITERGCQDLAEVLKNNQNLKYLHVSYNKLKDTG 873
Cdd:cd00116  159 KALRANRDLKELNLANNGIGDAGIRALAEGL-KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 140972011 874 VMLLCDAIKHPNCHLKDLQLEACEITDASNEELCYAFMQCETLQTLNLMGNAF 926
Cdd:cd00116  238 AAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKF 290
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 147-315 1.73e-33

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


:

Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 126.65  E-value: 1.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  147 HMVFLKGMAGVGKTLMLKNLMLAWSKGLVFQnKFSYAFYFCCQDVKQLKTA-SLAELISREWPSPSAPIEE----ILSQP 221
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  222 EKLLFIIDSLEGMEWDLtkqeselcDDCMEKQPVSTLLSSLLRRKMLPESSLLLSTTPETFEKMEDRIQCTDVKTATAFD 301
Cdd:pfam05729  80 ERLLLILDGLDELVSDL--------GQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....
gi 140972011  302 ERSMKIYFHRLFQD 315
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-88 1.01e-26

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: 104.25  E-value: 1.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  10 LIWYLRELNKKEFMKFKDFLIQEILELKLKQVSSTKVKKASREDLANLLLK-CGENQAWDMTFRILQKINRKDLTERATG 88
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEhYPEQQAWDVALSIFEKMNRTDLCEKARA 80
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 450-563 4.20e-15

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: 72.32  E-value: 4.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  450 HPSVQEVCAAIFYMLKRHVEHP--------SQDVKNIETVLFMFLKKVKTQWIFLGCFIFGLLQKSEQEKLGVFFGHRLS 521
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 140972011  522 KNIHHKLYQCLETLsgnaeLQEQIDGMR---LFSCLFEMEDEAFL 563
Cdd:pfam17776  81 SEIKQELLQWIKSL-----IQKELSSERflnLFHCLYELQDESFV 120
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 392-448 1.45e-09

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


:

Pssm-ID: 465501  Cd Length: 57  Bit Score: 54.49  E-value: 1.45e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 140972011  392 DQLQGLCSLAAEGMWTDTFVFGKEALRRNGIFDSDIPTLLDIGMLGKIREFENSYIF 448
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 636-926 9.53e-36

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: 138.26  E-value: 9.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 636 QELRIKDTNFNEPAIRVLYESLKYPSftlnklvannvsfgdnhvlfeliqnsSLQYLDLSCSFLSHNEVKLLCDILN-QA 714
Cdd:cd00116   26 QVLRLEGNTLGEEAAKALASALRPQP--------------------------SLKELCLSLNETGRIPRGLQSLLQGlTK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 715 ECNIEKLMIAHCKLSPDDCKIFGSILmSSKSLKVLNLASNNL-NQGISSLCKALCHPHCTLEYLVLSNCSLSEQCWDYLS 793
Cdd:cd00116   80 GCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 794 EVLRQNKTLSHLDISSNDLKDEGLKILCRSLiLPYCVLESLCLSCCGITERGCQDLAEVLKNNQNLKYLHVSYNKLKDTG 873
Cdd:cd00116  159 KALRANRDLKELNLANNGIGDAGIRALAEGL-KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 140972011 874 VMLLCDAIKHPNCHLKDLQLEACEITDASNEELCYAFMQCETLQTLNLMGNAF 926
Cdd:cd00116  238 AAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKF 290
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 147-315 1.73e-33

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 126.65  E-value: 1.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  147 HMVFLKGMAGVGKTLMLKNLMLAWSKGLVFQnKFSYAFYFCCQDVKQLKTA-SLAELISREWPSPSAPIEE----ILSQP 221
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  222 EKLLFIIDSLEGMEWDLtkqeselcDDCMEKQPVSTLLSSLLRRKMLPESSLLLSTTPETFEKMEDRIQCTDVKTATAFD 301
Cdd:pfam05729  80 ERLLLILDGLDELVSDL--------GQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....
gi 140972011  302 ERSMKIYFHRLFQD 315
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-88 1.01e-26

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: 104.25  E-value: 1.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  10 LIWYLRELNKKEFMKFKDFLIQEILELKLKQVSSTKVKKASREDLANLLLK-CGENQAWDMTFRILQKINRKDLTERATG 88
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEhYPEQQAWDVALSIFEKMNRTDLCEKARA 80
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 744-925 2.22e-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: 110.26  E-value: 2.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 744 KSLKVLNLASNNL-NQGISSLCKALCHPHcTLEYLVLSNCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDEGLKILCR 822
Cdd:COG5238  180 NSVETVYLGCNQIgDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAE 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 823 SLILPYCVlESLCLSCCGITERGCQDLAEVLKNNQNLKYLHVSYNKLKDTGVMLLCDAIKHpNCHLKDLQLEACEITDAS 902
Cdd:COG5238  259 ALKNNTTV-ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQG 336

                        170       180
                 ....*....|....*....|...
gi 140972011 903 NEELCYAFMQCETLQTLNLMGNA 925
Cdd:COG5238  337 AIALAKALQENTTLHSLDLSDNQ 359
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 9-84 6.95e-21

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: 87.26  E-value: 6.95e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 140972011    9 GLIWYLRELNKKEFMKFKdFLIQEILELKLKQVSSTKVKKASREDLANLLL-KCGENQAWDMTFRILQKINRKDLTE 84
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFK-SLLEDEPEEGLRSIPRGKLEKADRLDLADLLVeHYGEDAAVDVTIEILKKINLKDLAE 76
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 450-563 4.20e-15

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: 72.32  E-value: 4.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  450 HPSVQEVCAAIFYMLKRHVEHP--------SQDVKNIETVLFMFLKKVKTQWIFLGCFIFGLLQKSEQEKLGVFFGHRLS 521
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 140972011  522 KNIHHKLYQCLETLsgnaeLQEQIDGMR---LFSCLFEMEDEAFL 563
Cdd:pfam17776  81 SEIKQELLQWIKSL-----IQKELSSERflnLFHCLYELQDESFV 120
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 392-448 1.45e-09

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 54.49  E-value: 1.45e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 140972011  392 DQLQGLCSLAAEGMWTDTFVFGKEALRRNGIFDSDIPTLLDIGMLGKIREFENSYIF 448
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 636-926 9.53e-36

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: 138.26  E-value: 9.53e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 636 QELRIKDTNFNEPAIRVLYESLKYPSftlnklvannvsfgdnhvlfeliqnsSLQYLDLSCSFLSHNEVKLLCDILN-QA 714
Cdd:cd00116   26 QVLRLEGNTLGEEAAKALASALRPQP--------------------------SLKELCLSLNETGRIPRGLQSLLQGlTK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 715 ECNIEKLMIAHCKLSPDDCKIFGSILmSSKSLKVLNLASNNL-NQGISSLCKALCHPHCTLEYLVLSNCSLSEQCWDYLS 793
Cdd:cd00116   80 GCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLgDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 794 EVLRQNKTLSHLDISSNDLKDEGLKILCRSLiLPYCVLESLCLSCCGITERGCQDLAEVLKNNQNLKYLHVSYNKLKDTG 873
Cdd:cd00116  159 KALRANRDLKELNLANNGIGDAGIRALAEGL-KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAG 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 140972011 874 VMLLCDAIKHPNCHLKDLQLEACEITDASNEELCYAFMQCETLQTLNLMGNAF 926
Cdd:cd00116  238 AAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKF 290
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 147-315 1.73e-33

NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in MHC transcription activation. This family is closely related to pfam00931.


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 126.65  E-value: 1.73e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  147 HMVFLKGMAGVGKTLMLKNLMLAWSKGLVFQnKFSYAFYFCCQDVKQLKTA-SLAELISREWPSPSAPIEE----ILSQP 221
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  222 EKLLFIIDSLEGMEWDLtkqeselcDDCMEKQPVSTLLSSLLRRKMLPESSLLLSTTPETFEKMEDRIQCTDVKTATAFD 301
Cdd:pfam05729  80 ERLLLILDGLDELVSDL--------GQLDGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....
gi 140972011  302 ERSMKIYFHRLFQD 315
Cdd:pfam05729 152 ESDRKQYVRKYFSD 165
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-88 1.01e-26

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: 104.25  E-value: 1.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  10 LIWYLRELNKKEFMKFKDFLIQEILELKLKQVSSTKVKKASREDLANLLLK-CGENQAWDMTFRILQKINRKDLTERATG 88
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEhYPEQQAWDVALSIFEKMNRTDLCEKARA 80
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 744-925 2.22e-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: 110.26  E-value: 2.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 744 KSLKVLNLASNNL-NQGISSLCKALCHPHcTLEYLVLSNCSLSEQCWDYLSEVLRQNKTLSHLDISSNDLKDEGLKILCR 822
Cdd:COG5238  180 NSVETVYLGCNQIgDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAE 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 823 SLILPYCVlESLCLSCCGITERGCQDLAEVLKNNQNLKYLHVSYNKLKDTGVMLLCDAIKHpNCHLKDLQLEACEITDAS 902
Cdd:COG5238  259 ALKNNTTV-ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQG 336

                        170       180
                 ....*....|....*....|...
gi 140972011 903 NEELCYAFMQCETLQTLNLMGNA 925
Cdd:COG5238  337 AIALAKALQENTTLHSLDLSDNQ 359
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 586-924 2.87e-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: 2.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 586 AAYCLKHCSTLKKLSFST--ENVLNEGDQSYMEE------LLICWNNMCSV-----------------FVRSK--DIQEL 638
Cdd:COG5238   50 ARYLQSRSSITQYLRFEGqgDPGLNPVALEKAAEafptqlLVVDWEGAEEVspvalaetatavatpppDLRRImaKTLED 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 639 RIKDTN---FNEPAIRVLYESLKYPSFTLNKLVANNVSFGDNHVLFELiQNSSLQYLDLSCSFLSHNEVKLLCDILNQaE 715
Cdd:COG5238  130 SLILYLalpRRINLIQVLKDPLGGNAVHLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDEGIEELAEALTQ-N 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 716 CNIEKLMIAHCKLSPDDCKIFGSILMSSKSLKVLNLASNNL-NQGISSLCKALCHPHcTLEYLVLSNCSLSEQCWDYLSE 794
Cdd:COG5238  208 TTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIgDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAK 286

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 795 VLRQNKTLSHLDISSNDLKDEGLKILCRSLILPYcVLESLCLSCCGITERGCQDLAEVLKNNQNLKYLHVSYNKLKDTGV 874
Cdd:COG5238  287 ALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGA 365

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 140972011 875 MLLCDAIK-HPNchLKDLQLEACEITDASNEELCyAFMQCETLQTLNLMGN 924
Cdd:COG5238  366 IALAKYLEgNTT--LRELNLGKNNIGKQGAEALI-DALQTNRLHTLILDGN 413
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 9-84 6.95e-21

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: 87.26  E-value: 6.95e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 140972011    9 GLIWYLRELNKKEFMKFKdFLIQEILELKLKQVSSTKVKKASREDLANLLL-KCGENQAWDMTFRILQKINRKDLTE 84
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFK-SLLEDEPEEGLRSIPRGKLEKADRLDLADLLVeHYGEDAAVDVTIEILKKINLKDLAE 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 629-834 3.69e-19

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: 89.72  E-value: 3.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 629 FVRSKDIQELRIKDTNFNEPAIRVLYESLKYPSFTLNKLVA--NNVSFGDNHVLFE-LIQNSSLQYLDLSCSFLSHNEVK 705
Cdd:cd00116  104 LLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLgrNRLEGASCEALAKaLRANRDLKELNLANNGIGDAGIR 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 706 LLCDILnQAECNIEKLMIAHCKLSPDDCKIFGSILMSSKSLKVLNLASNNL-NQGISSLCKALCHPHCTLEYLVLSNCSL 784
Cdd:cd00116  184 ALAEGL-KANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLtDAGAAALASALLSPNISLLTLSLSCNDI 262

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 140972011 785 SEQCWDYLSEVLRQNKTLSHLDISSNDLKDEGLKILCRSLILPYCVLESL 834
Cdd:cd00116  263 TDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESL 312
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 450-563 4.20e-15

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: 72.32  E-value: 4.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011  450 HPSVQEVCAAIFYMLKRHVEHP--------SQDVKNIETVLFMFLKKVKTQWIFLGCFIFGLLQKSEQEKLGVFFGHRLS 521
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 140972011  522 KNIHHKLYQCLETLsgnaeLQEQIDGMR---LFSCLFEMEDEAFL 563
Cdd:pfam17776  81 SEIKQELLQWIKSL-----IQKELSSERflnLFHCLYELQDESFV 120
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 726-927 6.07e-15

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: 77.01  E-value: 6.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 726 CKLSPDDCKIFGSILMSSKSLKVLNLASNNLNQGISSLCKALCH--PHCTLEYLVLSNCSLS-EQCWDYlsEVLRQNKTL 802
Cdd:cd00116   33 NTLGEEAAKALASALRPQPSLKELCLSLNETGRIPRGLQSLLQGltKGCGLQELDLSDNALGpDGCGVL--ESLLRSSSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 803 SHLDISSNDLKDEGLKILCRSLILPYCVLESLCLSCCGITERGCQDLAEVLKNNQNLKYLHVSYNKLKDTGVMLLCDAIK 882
Cdd:cd00116  111 QELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLK 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 140972011 883 HpNCHLKdlqleaceitdasneelcyafmqcetlqTLNLMGNAFE 927
Cdd:cd00116  191 A-NCNLE----------------------------VLDLNNNGLT 206
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 774-924 7.86e-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: 73.54  E-value: 7.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 774 LEYLVLSNCSLSEQCWDYLSEVLRQNKTLSHLDISS-------------------------------------------- 809
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLnetgriprglqsllqgltkgcglqeldlsdnalgpdgcgvlesl 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 810 -------------NDLKDEGLKILCRSLILPYCVLESLCLSCCGITERGCQDLAEVLKNNQNLKYLHVSYNKLKDTGVML 876
Cdd:cd00116  105 lrssslqelklnnNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRA 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 140972011 877 LCDAIKHpNCHLKDLQLEACEITDASNEELCYAFMQCETLQTLNLMGN 924
Cdd:cd00116  185 LAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDN 231
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
144-485 2.74e-12

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 70.99  E-value: 2.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 144 RKPHMVFLkGMAGVGKTLMLKNLMLAWSKGLVFQNKFsYAFYFCCQDVKqlKTASLAELISREW----PSPSAPIEEILS 219
Cdd:COG5635  179 KKKRLLIL-GEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDLA--EEASLEDLLAEALekrgGEPEDALERLLR 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 220 QPeKLLFIIDSLEgmEWDLTKQESELCDDcmekqpvstlLSSLLRRkmLPESSLLLSTTPETFEKMEDRiQCTDVKTAtA 299
Cdd:COG5635  255 NG-RLLLLLDGLD--EVPDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYDSSELE-GFEVLELA-P 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 300 FDERSMKIYFHRLFQDRKRAQEAF-SLVRENKQLFTICQVPLLCWMVATCLKEEIEKGGDPVSLCRR-TTSLYTTHIFSL 377
Cdd:COG5635  318 LSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLLTLLALLLRERGELPDTRAELYEQfVELLLERWDEQR 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 378 FIPQsaqYPSKKSQDQLQGLCSLAAEGMWTDTFVFGKEALRR------NGIFDSDI---PTLLDIGMLgkIREFENSYIF 448
Cdd:COG5635  398 GLTI---YRELSREELRELLSELALAMQENGRTEFAREELEEilreylGRRKDAEAlldELLLRTGLL--VERGEGRYSF 472

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 140972011 449 LHPSVQEVCAA----------IFYMLKRHVEHPSQDvkniETVLFMF 485
Cdd:COG5635  473 AHRSFQEYLAAralveeldeeLLELLAEHLEDPRWR----EVLLLLA 515
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
682-906 1.23e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.57  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 682 ELIQNSSLQYLDLScsflsHNEVKLLCDILNQAEcNIEKLMIAHCKLSPddckiFGSILMSSKSLKVLNLASNNlnqgIS 761
Cdd:COG4886  108 ELSNLTNLESLDLS-----GNQLTDLPEELANLT-NLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQ----LT 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 762 SLCKALCHphCT-LEYLVLSNCSLSEqcwdyLSEVLRQNKTLSHLDISSNDLKD--EGLKILCRslilpycvLESLCLSC 838
Cdd:COG4886  173 DLPEELGN--LTnLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTDlpEPLANLTN--------LETLDLSN 237

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 140972011 839 CGITergcqDLAEvLKNNQNLKYLHVSYNKLKDtgvmlLCDAIKHPNchLKDLQLEACEITDASNEEL 906
Cdd:COG4886  238 NQLT-----DLPE-LGNLTNLEELDLSNNQLTD-----LPPLANLTN--LKTLDLSNNQLTDLKLKEL 292
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
744-927 3.59e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 63.03  E-value: 3.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 744 KSLKVLNLASNNlnqgISSLCKALCHPHcTLEYLVLSNCSLSEqcwdyLSEVLRQNKTLSHLDISSNDLKDeglkiLCRS 823
Cdd:COG4886  113 TNLESLDLSGNQ----LTDLPEELANLT-NLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD-----LPEE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 824 LI-LPYcvLESLCLSCCGITergcqDLAEVLKNNQNLKYLHVSYNKLKDtgvmlLCDAIKhpNC-HLKDLQLEACEITDA 901
Cdd:COG4886  178 LGnLTN--LKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTD-----LPEPLA--NLtNLETLDLSNNQLTDL 243

                        170       180
                 ....*....|....*....|....*.
gi 140972011 902 SNeelcyaFMQCETLQTLNLMGNAFE 927
Cdd:COG4886  244 PE------LGNLTNLEELDLSNNQLT 263
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 392-448 1.45e-09

NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular function is not known.


Pssm-ID: 465501  Cd Length: 57  Bit Score: 54.49  E-value: 1.45e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 140972011  392 DQLQGLCSLAAEGMWTDTFVFGKEALRRNGIFDSDIPTLLDIGMLGKIREFENSYIF 448
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 10-85 3.57e-09

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: 54.45  E-value: 3.57e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 140972011  10 LIWYLRELNKKEFMKFKDFLIQEILELKlKQVSSTKVKKASREDLANLLLKC-GENQAWDMTFRILQKINRKDLTER 85
Cdd:cd08321    4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYyGEDYAVEVTVEVLRAINQNDLAEK 79
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 698-810 9.49e-07

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.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 50.55  E-value: 9.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 140972011 698 FLSHNEVKLLCDILNQaeCNIEKLMIAHCKLSPDDCKIF--GSILMSSKSLKVLNLASNNLnQGISSLcKALCHphctLE 775
Cdd:cd21340   74 YLGGNRISVVEGLENL--TNLEELHIENQRLPPGEKLTFdpRSLAALSNSLRVLNISGNNI-DSLEPL-APLRN----LE 145

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 140972011 776 YLVLSNCSLSEqcWDYLSEVLRQNKTLSHLDISSN 810
Cdd:cd21340  146 QLDASNNQISD--LEELLDLLSSWPSLRELDLTGN 178
 
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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