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Conserved domains on  [gi|2035341191|ref|NP_001381823|]
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NACHT, LRR and PYD domains-containing protein 11 isoform 1 [Homo sapiens]

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 ...
 679-954 1.86e-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: 129.01  E-value: 1.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  679 EDLLKALARNRSLTYLSInctsiSLNMFSLLHDILHEP------TCQISHLSLMKCDLRASECEEIASLLiSGGSLRKLT 752
Cdd:cd00116     41 KALASALRPQPSLKELCL-----SLNETGRIPRGLQSLlqgltkGCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELK 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  753 LSSNPLRSDGMNILCDALLHPNCTLISLVLVFCCLTENCCSALGRVLLFSPTLRQLDLCVNRLKNYGVlHVTFPLLFPTC 832
Cdd:cd00116    115 LNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI-RALAEGLKANC 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  833 QLEELHLSGCFFSSDICQYIAIVIATNEKLRSLEIGSNKIEDAGMQLLCGGLRHPNCMLVNIGLEECMLTSACCRSLASV 912
Cdd:cd00116    194 NLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEV 273

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2035341191  913 LTTNKTLERLNLLQNHLGNDGVAKLLESLISPDCVLKVVGLP 954
Cdd:cd00116    274 LAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-91 4.29e-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: 108.48  E-value: 4.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191   11 LLWYLENLSDKEFQSFKKYLARKILDFKLPQFPLIQMTK---EELANVLPISYEGQYIWNMLFSIFSMMRKEDLCRKIIG 87
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKadgEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                   ....
gi 2035341191   88 RRNR 91
Cdd:cd08320     81 EMNE 84
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 149-315 4.25e-15

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member pfam05729:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 166  Bit Score: 73.88  E-value: 4.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  149 VFLMGERASGKTIVINLAVLRWIKGEMWQNMiSYVVHLTAHEINQMTN-SSLAELIAKDWPDGQAPI----ADILSDPKK 223
Cdd:pfam05729    3 VILQGEAGSGKTTLLQKLALLWAQGKLPQGF-DFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVsevwAVILELPER 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  224 LLFILEDLDNIRFELNVNESALcsnstqkvPIPVLLVSLLKRKMAPGCWFLISSRPTRGNNVKTFLKEVDCCTTLQLSNG 303
Cdd:pfam05729   82 LLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                          170
                   ....*....|..
gi 2035341191  304 KREIYFNSFFKD 315
Cdd:pfam05729  154 DRKQYVRKYFSD 165
NLRC4_HD2 super family cl39284
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 450-559 1.61e-11

NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein and NOD2 protein.


The actual alignment was detected with superfamily member pfam17776:

Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 62.31  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  450 HLNVQEFCTAIAFLM--------AVPNYLIPSGSREYKEK-----REQYSDFNQVFTFIFGLLNANRRKILETSFGYQLP 516
Cdd:pfam17776    1 HLSFQEFFAALFYVLsfkeeksnPLKEFFGLRKRESLKSLldkalKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2035341191  517 mvDSFKWYSVGYMKHLDRDPEKLTHHMPLFYCLYENREEEFVK 559
Cdd:pfam17776   81 --SEIKQELLQWIKSLIQKELSSERFLNLFHCLYELQDESFVK 121
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 679-954 1.86e-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: 129.01  E-value: 1.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  679 EDLLKALARNRSLTYLSInctsiSLNMFSLLHDILHEP------TCQISHLSLMKCDLRASECEEIASLLiSGGSLRKLT 752
Cdd:cd00116     41 KALASALRPQPSLKELCL-----SLNETGRIPRGLQSLlqgltkGCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELK 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  753 LSSNPLRSDGMNILCDALLHPNCTLISLVLVFCCLTENCCSALGRVLLFSPTLRQLDLCVNRLKNYGVlHVTFPLLFPTC 832
Cdd:cd00116    115 LNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI-RALAEGLKANC 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  833 QLEELHLSGCFFSSDICQYIAIVIATNEKLRSLEIGSNKIEDAGMQLLCGGLRHPNCMLVNIGLEECMLTSACCRSLASV 912
Cdd:cd00116    194 NLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEV 273

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2035341191  913 LTTNKTLERLNLLQNHLGNDGVAKLLESLISPDCVLKVVGLP 954
Cdd:cd00116    274 LAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-91 4.29e-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: 108.48  E-value: 4.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191   11 LLWYLENLSDKEFQSFKKYLARKILDFKLPQFPLIQMTK---EELANVLPISYEGQYIWNMLFSIFSMMRKEDLCRKIIG 87
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKadgEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                   ....
gi 2035341191   88 RRNR 91
Cdd:cd08320     81 EMNE 84
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 680-941 8.04e-19

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: 90.62  E-value: 8.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  680 DLLKALARNRSLTYLSINCTSISLNMFSLLHDilhEPTCQISHLSLMKCDLRASECEEIASLLiSGGSLRKLTLSSNPLR 759
Cdd:COG5238    118 DLRRIMAKTLEDSLILYLALPRRINLIQVLKD---PLGGNAVHLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIG 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  760 SDGMNILCDALLHPNcTLISLVLVFCCLTENCCSALGRVLLFSPTLRQLDLCVNRLKNYGVLHVTFPLLFPTcQLEELHL 839
Cdd:COG5238    194 DEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYL 271

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  840 SGCFFSSDICQYIAIVIATNEKLRSLEIGSNKIEDAGMQLLCGGLRHpNCMLVNIGLEECMLTSACCRSLASVLTTNKTL 919
Cdd:COG5238    272 SGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTL 350

                          250       260
                   ....*....|....*....|..
gi 2035341191  920 ERLNLLQNHLGNDGVAKLLESL 941
Cdd:COG5238    351 HSLDLSDNQIGDEGAIALAKYL 372
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 149-315 4.25e-15

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: 73.88  E-value: 4.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  149 VFLMGERASGKTIVINLAVLRWIKGEMWQNMiSYVVHLTAHEINQMTN-SSLAELIAKDWPDGQAPI----ADILSDPKK 223
Cdd:pfam05729    3 VILQGEAGSGKTTLLQKLALLWAQGKLPQGF-DFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVsevwAVILELPER 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  224 LLFILEDLDNIRFELNVNESALcsnstqkvPIPVLLVSLLKRKMAPGCWFLISSRPTRGNNVKTFLKEVDCCTTLQLSNG 303
Cdd:pfam05729   82 LLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                          170
                   ....*....|..
gi 2035341191  304 KREIYFNSFFKD 315
Cdd:pfam05729  154 DRKQYVRKYFSD 165
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-82 6.25e-15

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: 70.70  E-value: 6.25e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035341191   10 DLLWYLENLSDKEFQSFKKYL--ARKILDFKLPQFPLIQMTKEELANVLPISYEGQYIWNMLFSIFSMMRKEDLC 82
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLedEPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 450-559 1.61e-11

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: 62.31  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  450 HLNVQEFCTAIAFLM--------AVPNYLIPSGSREYKEK-----REQYSDFNQVFTFIFGLLNANRRKILETSFGYQLP 516
Cdd:pfam17776    1 HLSFQEFFAALFYVLsfkeeksnPLKEFFGLRKRESLKSLldkalKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2035341191  517 mvDSFKWYSVGYMKHLDRDPEKLTHHMPLFYCLYENREEEFVK 559
Cdd:pfam17776   81 --SEIKQELLQWIKSLIQKELSSERFLNLFHCLYELQDESFVK 121
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 679-954 1.86e-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: 129.01  E-value: 1.86e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  679 EDLLKALARNRSLTYLSInctsiSLNMFSLLHDILHEP------TCQISHLSLMKCDLRASECEEIASLLiSGGSLRKLT 752
Cdd:cd00116     41 KALASALRPQPSLKELCL-----SLNETGRIPRGLQSLlqgltkGCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELK 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  753 LSSNPLRSDGMNILCDALLHPNCTLISLVLVFCCLTENCCSALGRVLLFSPTLRQLDLCVNRLKNYGVlHVTFPLLFPTC 832
Cdd:cd00116    115 LNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI-RALAEGLKANC 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  833 QLEELHLSGCFFSSDICQYIAIVIATNEKLRSLEIGSNKIEDAGMQLLCGGLRHPNCMLVNIGLEECMLTSACCRSLASV 912
Cdd:cd00116    194 NLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEV 273

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 2035341191  913 LTTNKTLERLNLLQNHLGNDGVAKLLESLISPDCVLKVVGLP 954
Cdd:cd00116    274 LAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-91 4.29e-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: 108.48  E-value: 4.29e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191   11 LLWYLENLSDKEFQSFKKYLARKILDFKLPQFPLIQMTK---EELANVLPISYEGQYIWNMLFSIFSMMRKEDLCRKIIG 87
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKadgEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                   ....
gi 2035341191   88 RRNR 91
Cdd:cd08320     81 EMNE 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 625-901 1.33e-23

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: 102.82  E-value: 1.33e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  625 ICSLFYTMESLRELHIFDNDLNGISE--RILSKALEhSSCKLRTLKLSyvSTASGFED--LLKALARNRSLTYLSINCTS 700
Cdd:cd00116     43 LASALRPQPSLKELCLSLNETGRIPRglQSLLQGLT-KGCGLQELDLS--DNALGPDGcgVLESLLRSSSLQELKLNNNG 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  701 ISLNMFSLLHDILHEPTCQISHLSLMKCDLRASECEEIASLLISGGSLRKLTLSSNPLRSDGMNILCDALLHpNCTLISL 780
Cdd:cd00116    120 LGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVL 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  781 VLVFCCLTENCCSALGRVLLFSPTLRQLDLCVNRLKNYGVLHVTFPLLFPTCQLEELHLSGCFFSSDICQYIAIVIATNE 860
Cdd:cd00116    199 DLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKE 278

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2035341191  861 KLRSLEIGSNKIEDAGMQLLCGGLRHPNCMLVNIGLEECML 901
Cdd:cd00116    279 SLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 680-941 8.04e-19

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: 90.62  E-value: 8.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  680 DLLKALARNRSLTYLSINCTSISLNMFSLLHDilhEPTCQISHLSLMKCDLRASECEEIASLLiSGGSLRKLTLSSNPLR 759
Cdd:COG5238    118 DLRRIMAKTLEDSLILYLALPRRINLIQVLKD---PLGGNAVHLLGLAARLGLLAAISMAKAL-QNNSVETVYLGCNQIG 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  760 SDGMNILCDALLHPNcTLISLVLVFCCLTENCCSALGRVLLFSPTLRQLDLCVNRLKNYGVLHVTFPLLFPTcQLEELHL 839
Cdd:COG5238    194 DEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYL 271

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  840 SGCFFSSDICQYIAIVIATNEKLRSLEIGSNKIEDAGMQLLCGGLRHpNCMLVNIGLEECMLTSACCRSLASVLTTNKTL 919
Cdd:COG5238    272 SGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTL 350

                          250       260
                   ....*....|....*....|..
gi 2035341191  920 ERLNLLQNHLGNDGVAKLLESL 941
Cdd:COG5238    351 HSLDLSDNQIGDEGAIALAKYL 372
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 777-981 4.16e-18

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: 86.64  E-value: 4.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  777 LISLVLVFCCLTENCCSALGRVLLFSPTLRQLDLCVNRLKNYG-VLHVTFPLLFPTCQLEELHLSGCFFSSDICQYIaIV 855
Cdd:cd00116     25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRIPrGLQSLLQGLTKGCGLQELDLSDNALGPDGCGVL-ES 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  856 IATNEKLRSLEIGSNKIEDAGMQLLCGGLRHPNCMLVNIGLEECMLTSACCRSLASVLTTNKTLERLNLLQNHLGNDGVA 935
Cdd:cd00116    104 LLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIR 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2035341191  936 KLLESLISpDCVLKVVGLPLTGLNTQ-TQQLLMTVkerkPSLIFLSE 981
Cdd:cd00116    184 ALAEGLKA-NCNLEVLDLNNNGLTDEgASALAETL----ASLKSLEV 225
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 149-315 4.25e-15

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: 73.88  E-value: 4.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  149 VFLMGERASGKTIVINLAVLRWIKGEMWQNMiSYVVHLTAHEINQMTN-SSLAELIAKDWPDGQAPI----ADILSDPKK 223
Cdd:pfam05729    3 VILQGEAGSGKTTLLQKLALLWAQGKLPQGF-DFVFFLPCRELSRSGNaRSLADLLFSQWPEPAAPVsevwAVILELPER 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  224 LLFILEDLDNIRFELNVNESALcsnstqkvPIPVLLVSLLKRKMAPGCWFLISSRPTRGNNVKTFLKEVDCCTTLQLSNG 303
Cdd:pfam05729   82 LLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                          170
                   ....*....|..
gi 2035341191  304 KREIYFNSFFKD 315
Cdd:pfam05729  154 DRKQYVRKYFSD 165
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-82 6.25e-15

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: 70.70  E-value: 6.25e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2035341191   10 DLLWYLENLSDKEFQSFKKYL--ARKILDFKLPQFPLIQMTKEELANVLPISYEGQYIWNMLFSIFSMMRKEDLC 82
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLedEPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 450-559 1.61e-11

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: 62.31  E-value: 1.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  450 HLNVQEFCTAIAFLM--------AVPNYLIPSGSREYKEK-----REQYSDFNQVFTFIFGLLNANRRKILETSFGYQLP 516
Cdd:pfam17776    1 HLSFQEFFAALFYVLsfkeeksnPLKEFFGLRKRESLKSLldkalKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2035341191  517 mvDSFKWYSVGYMKHLDRDPEKLTHHMPLFYCLYENREEEFVK 559
Cdd:pfam17776   81 --SEIKQELLQWIKSLIQKELSSERFLNLFHCLYELQDESFVK 121
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 634-886 1.14e-10

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: 64.81  E-value: 1.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  634 SLRELHIFDNDLNGISERILSKALEHSScKLRTLKLSYVS-TASGFEDLLKALARNRSLT--YLSINctsislnmfsllh 710
Cdd:COG5238    209 TVTTLWLKRNPIGDEGAEILAEALKGNK-SLTTLDLSNNQiGDEGVIALAEALKNNTTVEtlYLSGN------------- 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  711 dilheptcQISHLSLmkcdlrasecEEIASLLISGGSLRKLTLSSNPLRSDGMNILCDALLHpNCTLISLVLVFCCLTEN 790
Cdd:COG5238    275 --------QIGAEGA----------IALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQ 335

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  791 CCSALGRVLLFSPTLRQLDLCVNRLKNYGV-LHVTFPLLFPTcqLEELHLSGCFFSSDICQYIAIVIATNeKLRSLEIGS 869
Cdd:COG5238    336 GAIALAKALQENTTLHSLDLSDNQIGDEGAiALAKYLEGNTT--LRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDG 412

                          250
                   ....*....|....*..
gi 2035341191  870 NKIEDAGMQLLCGGLRH 886
Cdd:COG5238    413 NLIGAEAQQRLEQLLER 429
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
157-500 9.50e-07

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 53.27  E-value: 9.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  157 SGKTIVI-NLAVLRWIKGEMWQNMISYVVHLTAHEinqmTNSSLAELIAKDWPDGQAPIADILSD---PKKLLFILEDLD 232
Cdd:COG5635    191 SGKTTLLrYLALELAERYLDAEDPIPILIELRDLA----EEASLEDLLAEALEKRGGEPEDALERllrNGRLLLLLDGLD 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  233 NIRFELNVNESAlcsnstqkvpipVLLVSLLKRkmAPGCWFLISSRPTRGNNVKtfLKEVDCCTTLQLSNGKREIYFNSF 312
Cdd:COG5635    267 EVPDEADRDEVL------------NQLRRFLER--YPKARVIITSRPEGYDSSE--LEGFEVLELAPLSDEQIEEFLKKW 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  313 FK-DRQRASAALQLVHEDEILVGLCRVAILCWITCTVLKRQMDKGRD----FQLCCQTPtdLHAHFLADALTSEAGLTAN 387
Cdd:COG5635    331 FEaTERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTraelYEQFVELL--LERWDEQRGLTIYRELSRE 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  388 QyhlgLLKRLCLLAAGGLFLSTLNFSGEDLR------CVGFTEADV---SVLQAANILLPSNthKDRYKFIHLNVQEFCT 458
Cdd:COG5635    409 E----LRELLSELALAMQENGRTEFAREELEeilreyLGRRKDAEAlldELLLRTGLLVERG--EGRYSFAHRSFQEYLA 482

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|..
gi 2035341191  459 AIAFLMAVPNYLIPSGSREYKEKReqysdFNQVFTFIFGLLN 500
Cdd:COG5635    483 ARALVEELDEELLELLAEHLEDPR-----WREVLLLLAGLLD 519
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 11-84 1.24e-05

Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or PAAD, is a subfamily of the Death Domain (DD) superfamily and it functions in several signaling pathways. The Pyrin domain is found at the N-terminus of a variety of proteins and serves as a linker that recruits other domains into signaling complexes. Pyrin-containing proteins include NALPs, ASC (Apoptosis-associated speck-like protein containing a CARD), and the interferon-inducible p200 (IFI-200) family of proteins which includes the human IFI-16, myeloid cell nuclear differentiation antigen (MNDA) and absent in melanoma (AIM) 2. NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. ASC and NALPs are involved in the regulation of inflammation. ASC, NALP1 and NALP3 are involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP12 functions as a negative regulator of inflammation. The p200 proteins are involved in the regulation of cell cycle and differentiation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including Caspase activation and recruitment domain (CARD) and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260019  Cd Length: 73  Bit Score: 44.22  E-value: 1.24e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2035341191   11 LLWYLENLSDKEFQSFKKYLARkilDFKLPQFPLIQMTKEELANVLPISYEGQYIWNMLFSIFSMMRKEDLCRK 84
Cdd:cd08305      1 LLTGLENITDEEFKMFKSLLAS---ELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQ 71
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 859-957 2.63e-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: 44.78  E-value: 2.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  859 NEKLRSLEIGSNKIEDAGMQLLCGGLRHPNC--MLV----NIGLEECmltsaccRSLASVLTTNKTLERLNLLQNHLGND 932
Cdd:COG5238    179 NNSVETVYLGCNQIGDEGIEELAEALTQNTTvtTLWlkrnPIGDEGA-------EILAEALKGNKSLTTLDLSNNQIGDE 251

                           90       100
                   ....*....|....*....|....*
gi 2035341191  933 GVAKLLESLISPDcvlKVVGLPLTG 957
Cdd:COG5238    252 GVIALAEALKNNT---TVETLYLSG 273
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
625-874 7.87e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 7.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  625 ICSLFYTMESLRELHIFDNDLNGISERILSKALEHSSCKLRTLKLSYVSTASGFEDLLKALARNRSLTYLSINCTSISLN 704
Cdd:COG4886     14 LLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLG 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  705 MFSLLHDILHEPTCQISHLS-LMKCDLRASECEEIASLLISGGSLRKLTLSSNPLRSdgmniLCDALlhPNCT-LISLVL 782
Cdd:COG4886     94 DLTNLTELDLSGNEELSNLTnLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTD-----LPEPL--GNLTnLKSLDL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035341191  783 VFCCLTEnccsaLGRVLLFSPTLRQLDLCVNRLKNygvlhvtFPLLFPTC-QLEELHLSGCFFSSdicqyIAIVIATNEK 861
Cdd:COG4886    167 SNNQLTD-----LPEELGNLTNLKELDLSNNQITD-------LPEPLGNLtNLEELDLSGNQLTD-----LPEPLANLTN 229

                          250
                   ....*....|...
gi 2035341191  862 LRSLEIGSNKIED 874
Cdd:COG4886    230 LETLDLSNNQLTD 242
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 11-45 9.16e-03

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: 36.35  E-value: 9.16e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2035341191   11 LLWYLENLSDKEFQSFKKYLarkiLDFKLPQFPLI 45
Cdd:cd08321      4 LLDALEDLGEEELKKFKWKL----RDIPLEGYPRI 34
 
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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