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Conserved domains on  [gi|34878693|ref|NP_004886|]
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NACHT, LRR and PYD domains-containing protein 3 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
575-951 1.37e-67

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: 229.55  E-value: 1.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  575 FVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQE-EDFVQRAMDYFPKi 653
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  654 eINLSTRMDHMVSSFCIENCHRVESLSLGFlhnmpkeeeeeekegrhldmvqcvlpssshaacshglvnshltssfcrgl 733
Cdd:cd00116   80 -GCGLQELDLSDNALGPDGCGVLESLLRSS-------------------------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  734 fsvlstsqSLTELDLSDNSLGDPGMRVLCETLQHPGCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDF 813
Cdd:cd00116  109 --------SLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDA 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  814 GIRLLCVGLKHlLCNLKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSGVAILCEKAKNPQCNLQKLGLVN 893
Cdd:cd00116  181 GIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSC 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34878693  894 SGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNC 951
Cdd:cd00116  260 NDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDD 317
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
220-389 5.52e-56

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


:

Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 190.98  E-value: 5.52e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693    220 HTVVFQGAAGIGKTILARKMMLDWASGTLYQDrFDYLFYIHCREVSLVT-QRSLGDLIMSCCPDPNPPIHK----IVRKP 294
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693    295 SRILFLMDGFDELQGAFDEHIGPLctdwqkaeRGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFS 374
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151
                          170
                   ....*....|....*
gi 34878693    375 EAKRKEYFFKYFSDE 389
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
10-93 8.83e-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: 107.33  E-value: 8.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693   10 LARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKR 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80

                 ....
gi 34878693   90 DEPK 93
Cdd:cd08320   81 EMNE 84
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
222-562 1.18e-23

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 107.97  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  222 VVFQGAAGIGKTILARKMMLDWASGTLYQDRFdYLFYIHCREvsLVTQRSLGDLI----MSCCPDPNPPIHKIVRKPsRI 297
Cdd:COG5635  183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRD--LAEEASLEDLLaealEKRGGEPEDALERLLRNG-RL 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  298 LFLMDGFDELQgafdehigplctdwQKAERGDIL--LSSLIRKklLPEASLLITTRPVALEklQHLLDHPRHVEILGFSE 375
Cdd:COG5635  259 LLLLDGLDEVP--------------DEADRDEVLnqLRRFLER--YPKARVIITSRPEGYD--SSELEGFEVLELAPLSD 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  376 AKRKEYFFKYF-SDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCtglkQQMESGKSLAQTSkttTAVYVFFLSSLLQPR 454
Cdd:COG5635  321 EQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLA----LLLRERGELPDTR---AELYEQFVELLLERW 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  455 GGSQEHGLCAHLWG------LCSLAADGIWNQKILFEESDLR----NHGLQKADVSAFL-----RMNLFQKEVdcEKFYS 519
Cdd:COG5635  394 DEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEeilrEYLGRRKDAEALLdelllRTGLLVERG--EGRYS 471
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 34878693  520 FIHMTFQEFFAAmYYLLEEEKEGRTNVPGSRLKLPSRDVTVLL 562
Cdd:COG5635  472 FAHRSFQEYLAA-RALVEELDEELLELLAEHLEDPRWREVLLL 513
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
144-210 2.51e-19

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


:

Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 83.05  E-value: 2.51e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34878693    144 VRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKT-KTCESPVSPIKMELLFD 210
Cdd:pfam14484    5 LKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
885-1031 8.88e-12

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: 67.38  E-value: 8.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  885 NLQKLGLVNSGLTSVCCSALSSVLSTNQNLT------------------------------------------------- 915
Cdd:cd00116   24 CLQVLRLEGNTLGEEAAKALASALRPQPSLKelclslnetgriprglqsllqgltkgcglqeldlsdnalgpdgcgvles 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  916 --------HLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVM 987
Cdd:cd00116  104 llrssslqELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIR 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 34878693  988 MFCEVLKqQSCLLQNLGLSEMYFNYETKSALETLQEEKPELTVV 1031
Cdd:cd00116  184 ALAEGLK-ANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVL 226
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
575-951 1.37e-67

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: 229.55  E-value: 1.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  575 FVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQE-EDFVQRAMDYFPKi 653
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  654 eINLSTRMDHMVSSFCIENCHRVESLSLGFlhnmpkeeeeeekegrhldmvqcvlpssshaacshglvnshltssfcrgl 733
Cdd:cd00116   80 -GCGLQELDLSDNALGPDGCGVLESLLRSS-------------------------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  734 fsvlstsqSLTELDLSDNSLGDPGMRVLCETLQHPGCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDF 813
Cdd:cd00116  109 --------SLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDA 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  814 GIRLLCVGLKHlLCNLKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSGVAILCEKAKNPQCNLQKLGLVN 893
Cdd:cd00116  181 GIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSC 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34878693  894 SGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNC 951
Cdd:cd00116  260 NDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDD 317
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
220-389 5.52e-56

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


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 190.98  E-value: 5.52e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693    220 HTVVFQGAAGIGKTILARKMMLDWASGTLYQDrFDYLFYIHCREVSLVT-QRSLGDLIMSCCPDPNPPIHK----IVRKP 294
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693    295 SRILFLMDGFDELQGAFDEHIGPLctdwqkaeRGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFS 374
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151
                          170
                   ....*....|....*
gi 34878693    375 EAKRKEYFFKYFSDE 389
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
522-645 8.33e-38

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


Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 137.42  E-value: 8.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693    522 HMTFQEFFAAMYYLLEEEKEGRTNVPGSRLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKIS 601
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 34878693    602 QQIRLELLKWIEVKAKAKKLqiQPSQLELFYCLYEMQEEDFVQR 645
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELS--SERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
10-93 8.83e-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: 107.33  E-value: 8.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693   10 LARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKR 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80

                 ....
gi 34878693   90 DEPK 93
Cdd:cd08320   81 EMNE 84
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
714-1024 8.97e-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: 108.72  E-value: 8.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  714 AACSHGLVNSHLTSSFCRGlfsvlstsQSLTELDLSDNSLGDPGMRVLCETLQHpGCNIRRLWLGRCGLSHECCFDISLV 793
Cdd:COG5238  161 LAARLGLLAAISMAKALQN--------NSVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEA 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  794 LSSNQKLVELDLSDNALGDFGIRLLcvgLKHLLCN--LKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSG 871
Cdd:COG5238  232 LKGNKSLTTLDLSNNQIGDEGVIAL---AEALKNNttVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEG 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  872 VAILCEKAKNPQcNLQKLGLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEgllhpdcklqvleldnc 951
Cdd:COG5238  309 AIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAK----------------- 370
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34878693  952 nltshccwdlstLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSclLQNLGLSEMYFNYETKSALETLQEE 1024
Cdd:COG5238  371 ------------YLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR--LHTLILDGNLIGAEAQQRLEQLLER 429
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
222-562 1.18e-23

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 107.97  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  222 VVFQGAAGIGKTILARKMMLDWASGTLYQDRFdYLFYIHCREvsLVTQRSLGDLI----MSCCPDPNPPIHKIVRKPsRI 297
Cdd:COG5635  183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRD--LAEEASLEDLLaealEKRGGEPEDALERLLRNG-RL 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  298 LFLMDGFDELQgafdehigplctdwQKAERGDIL--LSSLIRKklLPEASLLITTRPVALEklQHLLDHPRHVEILGFSE 375
Cdd:COG5635  259 LLLLDGLDEVP--------------DEADRDEVLnqLRRFLER--YPKARVIITSRPEGYD--SSELEGFEVLELAPLSD 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  376 AKRKEYFFKYF-SDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCtglkQQMESGKSLAQTSkttTAVYVFFLSSLLQPR 454
Cdd:COG5635  321 EQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLA----LLLRERGELPDTR---AELYEQFVELLLERW 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  455 GGSQEHGLCAHLWG------LCSLAADGIWNQKILFEESDLR----NHGLQKADVSAFL-----RMNLFQKEVdcEKFYS 519
Cdd:COG5635  394 DEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEeilrEYLGRRKDAEALLdelllRTGLLVERG--EGRYS 471
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 34878693  520 FIHMTFQEFFAAmYYLLEEEKEGRTNVPGSRLKLPSRDVTVLL 562
Cdd:COG5635  472 FAHRSFQEYLAA-RALVEELDEELLELLAEHLEDPRWREVLLL 513
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
10-85 3.47e-23

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


Pssm-ID: 460678  Cd Length: 76  Bit Score: 94.19  E-value: 3.47e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34878693     10 LARYLEDLEDVDLKKFKMHLEDYPpQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYE 85
Cdd:pfam02758    2 LLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
144-210 2.51e-19

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


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 83.05  E-value: 2.51e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34878693    144 VRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKT-KTCESPVSPIKMELLFD 210
Cdd:pfam14484    5 LKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
466-520 3.42e-14

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


Pssm-ID: 465501  Cd Length: 57  Bit Score: 67.98  E-value: 3.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 34878693    466 LWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSF 520
Cdd:pfam17779    3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
885-1031 8.88e-12

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: 67.38  E-value: 8.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  885 NLQKLGLVNSGLTSVCCSALSSVLSTNQNLT------------------------------------------------- 915
Cdd:cd00116   24 CLQVLRLEGNTLGEEAAKALASALRPQPSLKelclslnetgriprglqsllqgltkgcglqeldlsdnalgpdgcgvles 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  916 --------HLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVM 987
Cdd:cd00116  104 llrssslqELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIR 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 34878693  988 MFCEVLKqQSCLLQNLGLSEMYFNYETKSALETLQEEKPELTVV 1031
Cdd:cd00116  184 ALAEGLK-ANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVL 226
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
797-824 1.34e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 42.78  E-value: 1.34e-05
                            10        20
                    ....*....|....*....|....*...
gi 34878693     797 NQKLVELDLSDNALGDFGIRLLCVGLKH 824
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
968-995 1.06e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.08  E-value: 1.06e-04
                            10        20
                    ....*....|....*....|....*...
gi 34878693     968 SQSLRKLSLGNNDLGDLGVMMFCEVLKQ 995
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
575-951 1.37e-67

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: 229.55  E-value: 1.37e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  575 FVVRFLFGLVNQERTSYLEKKLSCKISQQIRLELLKWIEVKAKAKKLQIQPSQLELFYCLYEMQE-EDFVQRAMDYFPKi 653
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  654 eINLSTRMDHMVSSFCIENCHRVESLSLGFlhnmpkeeeeeekegrhldmvqcvlpssshaacshglvnshltssfcrgl 733
Cdd:cd00116   80 -GCGLQELDLSDNALGPDGCGVLESLLRSS-------------------------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  734 fsvlstsqSLTELDLSDNSLGDPGMRVLCETLQHPGCNIRRLWLGRCGLSHECCFDISLVLSSNQKLVELDLSDNALGDF 813
Cdd:cd00116  109 --------SLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDA 180
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  814 GIRLLCVGLKHlLCNLKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSGVAILCEKAKNPQCNLQKLGLVN 893
Cdd:cd00116  181 GIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSC 259
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 34878693  894 SGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNC 951
Cdd:cd00116  260 NDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDD 317
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
220-389 5.52e-56

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


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 190.98  E-value: 5.52e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693    220 HTVVFQGAAGIGKTILARKMMLDWASGTLYQDrFDYLFYIHCREVSLVT-QRSLGDLIMSCCPDPNPPIHK----IVRKP 294
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693    295 SRILFLMDGFDELQGAFDEHIGPLctdwqkaeRGDILLSSLIRKKLLPEASLLITTRPVALEKLQHLLDHPRHVEILGFS 374
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151
                          170
                   ....*....|....*
gi 34878693    375 EAKRKEYFFKYFSDE 389
Cdd:pfam05729  152 ESDRKQYVRKYFSDE 166
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
522-645 8.33e-38

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


Pssm-ID: 465499 [Multi-domain]  Cd Length: 122  Bit Score: 137.42  E-value: 8.33e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693    522 HMTFQEFFAAMYYLLEEEKEGRTNVPGSRLKLPSRDVTVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCKIS 601
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 34878693    602 QQIRLELLKWIEVKAKAKKLqiQPSQLELFYCLYEMQEEDFVQR 645
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELS--SERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
10-93 8.83e-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: 107.33  E-value: 8.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693   10 LARYLEDLEDVDLKKFKMHLEDYPPQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAKR 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80

                 ....
gi 34878693   90 DEPK 93
Cdd:cd08320   81 EMNE 84
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
714-1024 8.97e-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: 108.72  E-value: 8.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  714 AACSHGLVNSHLTSSFCRGlfsvlstsQSLTELDLSDNSLGDPGMRVLCETLQHpGCNIRRLWLGRCGLSHECCFDISLV 793
Cdd:COG5238  161 LAARLGLLAAISMAKALQN--------NSVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEA 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  794 LSSNQKLVELDLSDNALGDFGIRLLcvgLKHLLCN--LKKLWLVSCCLTSACCQDLASVLSTSHSLTRLYVGENALGDSG 871
Cdd:COG5238  232 LKGNKSLTTLDLSNNQIGDEGVIAL---AEALKNNttVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEG 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  872 VAILCEKAKNPQcNLQKLGLVNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEgllhpdcklqvleldnc 951
Cdd:COG5238  309 AIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAK----------------- 370
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34878693  952 nltshccwdlstLLTSSQSLRKLSLGNNDLGDLGVMMFCEVLKQQSclLQNLGLSEMYFNYETKSALETLQEE 1024
Cdd:COG5238  371 ------------YLEGNTTLRELNLGKNNIGKQGAEALIDALQTNR--LHTLILDGNLIGAEAQQRLEQLLER 429
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
222-562 1.18e-23

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 107.97  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  222 VVFQGAAGIGKTILARKMMLDWASGTLYQDRFdYLFYIHCREvsLVTQRSLGDLI----MSCCPDPNPPIHKIVRKPsRI 297
Cdd:COG5635  183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRD--LAEEASLEDLLaealEKRGGEPEDALERLLRNG-RL 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  298 LFLMDGFDELQgafdehigplctdwQKAERGDIL--LSSLIRKklLPEASLLITTRPVALEklQHLLDHPRHVEILGFSE 375
Cdd:COG5635  259 LLLLDGLDEVP--------------DEADRDEVLnqLRRFLER--YPKARVIITSRPEGYD--SSELEGFEVLELAPLSD 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  376 AKRKEYFFKYF-SDEAQARAAFSLIQENEVLFTMCFIPLVCWIVCtglkQQMESGKSLAQTSkttTAVYVFFLSSLLQPR 454
Cdd:COG5635  321 EQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLA----LLLRERGELPDTR---AELYEQFVELLLERW 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  455 GGSQEHGLCAHLWG------LCSLAADGIWNQKILFEESDLR----NHGLQKADVSAFL-----RMNLFQKEVdcEKFYS 519
Cdd:COG5635  394 DEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEeilrEYLGRRKDAEALLdelllRTGLLVERG--EGRYS 471
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 34878693  520 FIHMTFQEFFAAmYYLLEEEKEGRTNVPGSRLKLPSRDVTVLL 562
Cdd:COG5635  472 FAHRSFQEYLAA-RALVEELDEELLELLAEHLEDPRWREVLLL 513
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
10-85 3.47e-23

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


Pssm-ID: 460678  Cd Length: 76  Bit Score: 94.19  E-value: 3.47e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34878693     10 LARYLEDLEDVDLKKFKMHLEDYPpQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYE 85
Cdd:pfam02758    2 LLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
7-86 2.43e-20

Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated speck-like protein containing a CARD) and similar proteins. ASC is an adaptor molecule that functions in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. ASC contains two domains from the Death Domain (DD) superfamily, an N-terminal pyrin-like domain and a C-terminal Caspase activation and recruitment domain (CARD). Through these 2 domains, ASC serves as an adaptor for inflammasome integrity and oligomerizes to form supramolecular assemblies. Included in this family is human PYNOD (also known as NLRP10 or NOD8) which via its Pyrin domain suppresses oligomerization of ASC, and ASC-mediated NF-kappaB activation. Other members of this subfamily are associated with ATPase domains and their function remains unknown. In general, Pyrin is a subfamily of the DD superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and Death Effector Domain (DED). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260033  Cd Length: 82  Bit Score: 86.04  E-value: 2.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693    7 RCKLARYLEDLEDVDLKKFKMHLEDYPpQKGCIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEK 86
Cdd:cd08321    1 RDLLLDALEDLGEEELKKFKWKLRDIP-LEGYPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEK 79
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
144-210 2.51e-19

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


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 83.05  E-value: 2.51e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34878693    144 VRSRFQCIEDRNARLGESVSLNKRYTRLRLIKEHRSQQEREQELLAIGKT-KTCESPVSPIKMELLFD 210
Cdd:pfam14484    5 LKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
466-520 3.42e-14

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


Pssm-ID: 465501  Cd Length: 57  Bit Score: 67.98  E-value: 3.42e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 34878693    466 LWGLCSLAADGIWNQKILFEESDLRNHGLQKADVSAFLRMNLFQKEVDCEKFYSF 520
Cdd:pfam17779    3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
720-984 5.14e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 72.27  E-value: 5.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  720 LVNSHLTSsfcrgLFSVLSTSQSLTELDLSDNSLGDpgmrvLCETLqhPGC-NIRRLWLGRCGLSheccfDISLVLSSNQ 798
Cdd:COG4886  120 LSGNQLTD-----LPEELANLTNLKELDLSNNQLTD-----LPEPL--GNLtNLKSLDLSNNQLT-----DLPEELGNLT 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  799 KLVELDLSDNALGDFGIRLLCvglkhlLCNLKKLWLVSCCLTsaccqDLASVLSTSHSLTRLYVGENALGDsgvaiLCEK 878
Cdd:COG4886  183 NLKELDLSNNQITDLPEPLGN------LTNLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTD-----LPEL 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  879 AKNPqcNLQKLGLVNSGLTSVccsalsSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCC 958
Cdd:COG4886  247 GNLT--NLEELDLSNNQLTDL------PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLL 318
                        250       260
                 ....*....|....*....|....*.
gi 34878693  959 WDLSTLLTSSQSLRKLSLGNNDLGDL 984
Cdd:COG4886  319 LLTTLLLLLLLLKGLLVTLTTLALSL 344
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
737-985 9.38e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.50  E-value: 9.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  737 LSTSQSLTELDLSDNSLGDpgmrvLCETLQHPGcNIRRLWLGRCGLSheccfDISLVLSSNQKLVELDLSDNALGDFGIR 816
Cdd:COG4886  109 LSNLTNLESLDLSGNQLTD-----LPEELANLT-NLKELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQLTDLPEE 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  817 LLcvGLKhllcNLKKLWLVSCCLTsaccqDLASVLSTSHSLTRLYVGENALGDSGVAIlcekaknPQC-NLQKLGLVNSG 895
Cdd:COG4886  178 LG--NLT----NLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTDLPEPL-------ANLtNLETLDLSNNQ 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  896 LTSVccsalsSVLSTNQNLTHLYLRGNTLGDkgikLLCEGLLHpdcKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLS 975
Cdd:COG4886  240 LTDL------PELGNLTNLEELDLSNNQLTD----LPPLANLT---NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLL 306
                        250
                 ....*....|
gi 34878693  976 LGNNDLGDLG 985
Cdd:COG4886  307 LLNLLELLIL 316
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
885-1031 8.88e-12

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: 67.38  E-value: 8.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  885 NLQKLGLVNSGLTSVCCSALSSVLSTNQNLT------------------------------------------------- 915
Cdd:cd00116   24 CLQVLRLEGNTLGEEAAKALASALRPQPSLKelclslnetgriprglqsllqgltkgcglqeldlsdnalgpdgcgvles 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  916 --------HLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSLRKLSLGNNDLGDLGVM 987
Cdd:cd00116  104 llrssslqELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIR 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 34878693  988 MFCEVLKqQSCLLQNLGLSEMYFNYETKSALETLQEEKPELTVV 1031
Cdd:cd00116  184 ALAEGLK-ANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVL 226
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
733-1024 5.97e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 59.56  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  733 LFSVLSTSQSLTELDLSDNSLGDpgmrvLCETLQhpGC-NIRRLWLGRCGLSheccfDISLVLSSNQKLVELDLSDNALG 811
Cdd:COG4886  151 LPEPLGNLTNLKSLDLSNNQLTD-----LPEELG--NLtNLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLT 218
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  812 DFGIRLlcVGLKhllcNLKKLWLVSCCLTsaccqDLASvLSTSHSLTRLYVGENALGDsgvaiLCEKAKNPqcNLQKLGL 891
Cdd:COG4886  219 DLPEPL--ANLT----NLETLDLSNNQLT-----DLPE-LGNLTNLEELDLSNNQLTD-----LPPLANLT--NLKTLDL 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34878693  892 VNSGLTSVCCSALSSVLSTNQNLTHLYLRGNTLGDKGIKLLCEGLLHPDCKLQVLELDNCNLTSHCCWDLSTLLTSSQSL 971
Cdd:COG4886  280 SNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLL 359
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 34878693  972 RKLSLGNNDLGDLGVMMFCEVLKQQSCLLQNLGLSEMYFNYETKSALETLQEE 1024
Cdd:COG4886  360 SLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVN 412
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
797-824 1.34e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 42.78  E-value: 1.34e-05
                            10        20
                    ....*....|....*....|....*...
gi 34878693     797 NQKLVELDLSDNALGDFGIRLLCVGLKH 824
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
10-88 1.60e-05

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


Pssm-ID: 260019  Cd Length: 73  Bit Score: 43.83  E-value: 1.60e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34878693   10 LARYLEDLEDVDLKKFKMHLEDYppqkgcIPLPRGQTEKADHVDLATLMIDFNGEEKAWAMAVWIFAAINRRDLYEKAK 88
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLASE------LKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
740-767 2.00e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 42.01  E-value: 2.00e-05
                            10        20
                    ....*....|....*....|....*...
gi 34878693     740 SQSLTELDLSDNSLGDPGMRVLCETLQH 767
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
968-995 1.06e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.08  E-value: 1.06e-04
                            10        20
                    ....*....|....*....|....*...
gi 34878693     968 SQSLRKLSLGNNDLGDLGVMMFCEVLKQ 995
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
911-938 2.74e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.93  E-value: 2.74e-04
                            10        20
                    ....*....|....*....|....*...
gi 34878693     911 NQNLTHLYLRGNTLGDKGIKLLCEGLLH 938
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
910-933 7.40e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 34.90  E-value: 7.40e-03
                           10        20
                   ....*....|....*....|....
gi 34878693    910 TNQNLTHLYLRGNTLGDKGIKLLC 933
Cdd:pfam13516    1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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