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Conserved domains on  [gi|33519450|ref|NP_789790|]
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NACHT, LRR and PYD domains-containing protein 9 [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 ...
 622-897 3.62e-38

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: 145.58  E-value: 3.62e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 622 LCSMFITNKNFQILDM--ENTSLDDPSLAILCKALaQPVCKLRKLIFTSVYFGHD-SELFKAVLHNPHLKLLSLYGTSLS 698
Cdd:cd00116  43 LASALRPQPSLKELCLslNETGRIPRGLQSLLQGL-TKGCGLQELDLSDNALGPDgCGVLESLLRSSSLQELKLNNNGLG 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 699 QSDIRHLCETLKHPMCKIEELILGKCDISSEVCEDIASVLACNSKLKHLSLVENPLRDEGMTLLCEALKHShCALERLML 778
Cdd:cd00116 122 DRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDL 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 779 MYCCLTSVSCDSISEVLLCSKSLSLLDLGSNALEDNGVASLCAALKHPGCSIRELWLMGCFLTSDSCKDIAAVLICNGKL 858
Cdd:cd00116 201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 33519450 859 KTLKLGHNEIGDTGVRQLCAALQHPHCKLECLGLQTCPI 897
Cdd:cd00116 281 LELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-93 9.04e-36

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: 130.05  E-value: 9.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450  11 LLWYLKELRKEEFWKFKELLKQPLEKFELKPIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDLWTKAQE 90
Cdd:cd08320   1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                ...
gi 33519450  91 EMR 93
Cdd:cd08320  81 EMN 83
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 146-314 3.73e-34

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: 128.58  E-value: 3.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   146 HTVVLEGPDGIGKTTLLRKVMLDWAEGNLWKDrFTFVFFLNVCEMNGI-AETSLLELLSRDWPES----SEKIEDIFSQP 220
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSgNARSLADLLFSQWPEPaapvSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   221 ERILFIMDGFEqlkfnlQLKADLSDDwRQRQPMPIILSSLLQKKMLPESSLLI-----ALGKLAMQkhyfmLRHPKLIKL 295
Cdd:pfam05729  80 ERLLLILDGLD------ELVSDLGQL-DGPCPVLTLLSSLLRKKLLPGASLLLtvrpdALRDLRRG-----LEEPRYLEV 147

                         170
                  ....*....|....*....
gi 33519450   296 LGFSESEKKSYFSYFFGEK 314
Cdd:pfam05729 148 RGFSESDRKQYVRKYFSDE 166
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 445-560 7.70e-23

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: 94.67  E-value: 7.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   445 HLCIQEFCAAMFYLLKRPKDDPNPAI--------GSITQLVRASVVQPQTLLTQVGIFMFGISTEEIVSMLETSFGFPLS 516
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 33519450   517 KDLKQEITQCLESLSQCEADREaiAFQELFIGLFETQEKEFVTK 560
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFVKE 122
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 392-440 5.43e-08

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: 50.26  E-value: 5.43e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 33519450   392 LKSLCALAAEGIWTYTFVFSHGDLRRNGLSESEGVMWVGMRLLQRRGDC 440
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGC 51
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 622-897 3.62e-38

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: 145.58  E-value: 3.62e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 622 LCSMFITNKNFQILDM--ENTSLDDPSLAILCKALaQPVCKLRKLIFTSVYFGHD-SELFKAVLHNPHLKLLSLYGTSLS 698
Cdd:cd00116  43 LASALRPQPSLKELCLslNETGRIPRGLQSLLQGL-TKGCGLQELDLSDNALGPDgCGVLESLLRSSSLQELKLNNNGLG 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 699 QSDIRHLCETLKHPMCKIEELILGKCDISSEVCEDIASVLACNSKLKHLSLVENPLRDEGMTLLCEALKHShCALERLML 778
Cdd:cd00116 122 DRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDL 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 779 MYCCLTSVSCDSISEVLLCSKSLSLLDLGSNALEDNGVASLCAALKHPGCSIRELWLMGCFLTSDSCKDIAAVLICNGKL 858
Cdd:cd00116 201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 33519450 859 KTLKLGHNEIGDTGVRQLCAALQHPHCKLECLGLQTCPI 897
Cdd:cd00116 281 LELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-93 9.04e-36

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: 130.05  E-value: 9.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450  11 LLWYLKELRKEEFWKFKELLKQPLEKFELKPIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDLWTKAQE 90
Cdd:cd08320   1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                ...
gi 33519450  91 EMR 93
Cdd:cd08320  81 EMN 83
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 146-314 3.73e-34

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: 128.58  E-value: 3.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   146 HTVVLEGPDGIGKTTLLRKVMLDWAEGNLWKDrFTFVFFLNVCEMNGI-AETSLLELLSRDWPES----SEKIEDIFSQP 220
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSgNARSLADLLFSQWPEPaapvSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   221 ERILFIMDGFEqlkfnlQLKADLSDDwRQRQPMPIILSSLLQKKMLPESSLLI-----ALGKLAMQkhyfmLRHPKLIKL 295
Cdd:pfam05729  80 ERLLLILDGLD------ELVSDLGQL-DGPCPVLTLLSSLLRKKLLPGASLLLtvrpdALRDLRRG-----LEEPRYLEV 147

                         170
                  ....*....|....*....
gi 33519450   296 LGFSESEKKSYFSYFFGEK 314
Cdd:pfam05729 148 RGFSESDRKQYVRKYFSDE 166
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 3.59e-26

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: 102.67  E-value: 3.59e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33519450    10 GLLWYLKELRKEEFWKFKELLKQpLEKFELKPIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDLW 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLED-EPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 445-560 7.70e-23

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: 94.67  E-value: 7.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   445 HLCIQEFCAAMFYLLKRPKDDPNPAI--------GSITQLVRASVVQPQTLLTQVGIFMFGISTEEIVSMLETSFGFPLS 516
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 33519450   517 KDLKQEITQCLESLSQCEADREaiAFQELFIGLFETQEKEFVTK 560
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 590-882 6.93e-21

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: 96.78  E-value: 6.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 590 HLTTLRMCVENIFPDDSGcISDYNEKLVYWRELC------SMFITNKNFQILDMENTSLDDPSLAILCKALAQPVcKLRK 663
Cdd:COG5238 135 LALPRRINLIQVLKDPLG-GNAVHLLGLAARLGLlaaismAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTT 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 664 LIFTSVYFGHDS--ELFKAVLHNPHLKLLSLYGTSLSQSDIRHLCETLKHPMcKIEELILGKCDISSEVCEDIASVLACN 741
Cdd:COG5238 213 LWLKRNPIGDEGaeILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGN 291

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 742 SKLKHLSLVENPLRDEGMTLLCEALKHSHcALERLMLMYCCLTSVSCDSISEVLLCSKSLSLLDLGSNALEDNGVASLCA 821
Cdd:COG5238 292 TTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAK 370

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33519450 822 ALKHPGcSIRELWLMGCFLTSDSCKDIAAVLICNgKLKTLKLGHNEIGDTGVRQLCAALQH 882
Cdd:COG5238 371 YLEGNT-TLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLEQLLER 429
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 392-440 5.43e-08

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: 50.26  E-value: 5.43e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 33519450   392 LKSLCALAAEGIWTYTFVFSHGDLRRNGLSESEGVMWVGMRLLQRRGDC 440
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGC 51
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
855-882 1.81e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.31  E-value: 1.81e-04
                           10        20
                   ....*....|....*....|....*...
gi 33519450    855 NGKLKTLKLGHNEIGDTGVRQLCAALQH 882
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 ...
 622-897 3.62e-38

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: 145.58  E-value: 3.62e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 622 LCSMFITNKNFQILDM--ENTSLDDPSLAILCKALaQPVCKLRKLIFTSVYFGHD-SELFKAVLHNPHLKLLSLYGTSLS 698
Cdd:cd00116  43 LASALRPQPSLKELCLslNETGRIPRGLQSLLQGL-TKGCGLQELDLSDNALGPDgCGVLESLLRSSSLQELKLNNNGLG 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 699 QSDIRHLCETLKHPMCKIEELILGKCDISSEVCEDIASVLACNSKLKHLSLVENPLRDEGMTLLCEALKHShCALERLML 778
Cdd:cd00116 122 DRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKAN-CNLEVLDL 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 779 MYCCLTSVSCDSISEVLLCSKSLSLLDLGSNALEDNGVASLCAALKHPGCSIRELWLMGCFLTSDSCKDIAAVLICNGKL 858
Cdd:cd00116 201 NNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESL 280

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 33519450 859 KTLKLGHNEIGDTGVRQLCAALQHPHCKLECLGLQTCPI 897
Cdd:cd00116 281 LELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-93 9.04e-36

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: 130.05  E-value: 9.04e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450  11 LLWYLKELRKEEFWKFKELLKQPLEKFELKPIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDLWTKAQE 90
Cdd:cd08320   1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                ...
gi 33519450  91 EMR 93
Cdd:cd08320  81 EMN 83
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 146-314 3.73e-34

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: 128.58  E-value: 3.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   146 HTVVLEGPDGIGKTTLLRKVMLDWAEGNLWKDrFTFVFFLNVCEMNGI-AETSLLELLSRDWPES----SEKIEDIFSQP 220
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSgNARSLADLLFSQWPEPaapvSEVWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   221 ERILFIMDGFEqlkfnlQLKADLSDDwRQRQPMPIILSSLLQKKMLPESSLLI-----ALGKLAMQkhyfmLRHPKLIKL 295
Cdd:pfam05729  80 ERLLLILDGLD------ELVSDLGQL-DGPCPVLTLLSSLLRKKLLPGASLLLtvrpdALRDLRRG-----LEEPRYLEV 147

                         170
                  ....*....|....*....
gi 33519450   296 LGFSESEKKSYFSYFFGEK 314
Cdd:pfam05729 148 RGFSESDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 688-949 7.75e-28

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: 115.15  E-value: 7.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 688 KLLSLYGTSLSQSDIRHLCETLKHPmckiEELILGKCDISSEVCEDIASVLACNSKLKHLSLVENPLR--DEGMTLLCEA 765
Cdd:cd00116   1 LQLSLKGELLKTERATELLPKLLCL----QVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 766 LKhSHCALERLMLMYCCLTSVSCDSIsEVLLCSKSLSLLDLGSNALEDNGVASLCAALKHPGCSIRELWLMGCFLTSDSC 845
Cdd:cd00116  77 LT-KGCGLQELDLSDNALGPDGCGVL-ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASC 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 846 KDIAAVLICNGKLKTLKLGHNEIGDTGVRQLCAALQHpHCKLECLGLQTCPITRACCDDIAAALIACKTLRSLNLDWIAL 925
Cdd:cd00116 155 EALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNL 233

                       250       260
                ....*....|....*....|....
gi 33519450 926 DADAVVVLCEALSHPDCALQMLGL 949
Cdd:cd00116 234 TDAGAAALASALLSPNISLLTLSL 257
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 3.59e-26

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: 102.67  E-value: 3.59e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 33519450    10 GLLWYLKELRKEEFWKFKELLKQpLEKFELKPIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDLW 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLED-EPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 445-560 7.70e-23

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: 94.67  E-value: 7.70e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   445 HLCIQEFCAAMFYLLKRPKDDPNPAI--------GSITQLVRASVVQPQTLLTQVGIFMFGISTEEIVSMLETSFGFPLS 516
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 33519450   517 KDLKQEITQCLESLSQCEADREaiAFQELFIGLFETQEKEFVTK 560
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 590-882 6.93e-21

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: 96.78  E-value: 6.93e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 590 HLTTLRMCVENIFPDDSGcISDYNEKLVYWRELC------SMFITNKNFQILDMENTSLDDPSLAILCKALAQPVcKLRK 663
Cdd:COG5238 135 LALPRRINLIQVLKDPLG-GNAVHLLGLAARLGLlaaismAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTT 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 664 LIFTSVYFGHDS--ELFKAVLHNPHLKLLSLYGTSLSQSDIRHLCETLKHPMcKIEELILGKCDISSEVCEDIASVLACN 741
Cdd:COG5238 213 LWLKRNPIGDEGaeILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGN 291

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 742 SKLKHLSLVENPLRDEGMTLLCEALKHSHcALERLMLMYCCLTSVSCDSISEVLLCSKSLSLLDLGSNALEDNGVASLCA 821
Cdd:COG5238 292 TTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAK 370

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 33519450 822 ALKHPGcSIRELWLMGCFLTSDSCKDIAAVLICNgKLKTLKLGHNEIGDTGVRQLCAALQH 882
Cdd:COG5238 371 YLEGNT-TLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAEAQQRLEQLLER 429
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 682-939 7.15e-17

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: 84.46  E-value: 7.15e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 682 LHNPHLKLLSLYGTSLSQSDIRHLCETLKHPMcKIEELILGKCDISSEVCEDIASVLACNSKLKHLSLVENPLRDEGMTL 761
Cdd:COG5238 177 LQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 762 LCEALKHSHcALERLMLMYCCLTSVSCDSISEVLLCSKSLSLLDLGSNALEDNGVASLCAALKHPGcSIRELWLMGCFLT 841
Cdd:COG5238 256 LAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIG 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 842 SDSCKDIAAVLICNGKLKTLKLGHNEIGDTGVRQLCAALQHpHCKLECLGLQTCPITraccDDIAAALIA---CKTLRSL 918
Cdd:COG5238 334 AQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG-NTTLRELNLGKNNIG----KQGAEALIDalqTNRLHTL 408

                       250       260
                ....*....|....*....|.
gi 33519450 919 NLDWIALDADAVVVLCEALSH 939
Cdd:COG5238 409 ILDGNLIGAEAQQRLEQLLER 429
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 815-962 3.55e-16

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: 80.86  E-value: 3.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 815 GVASLCAALKHpGCSIRELWLMGCFLTSDSCKDIAAVLIcNGKLKTLKLGHNEIGDTGVRQLCAALQHPHCKLECLGLQT 894
Cdd:cd00116  69 GLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVLESLLR-SSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGR 146

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 33519450 895 CPITRACCDDIAAALIACKTLRSLNLDWIALDADAVVVLCEALSHpDCALQMLGLHKSGFDEETQKIL 962
Cdd:cd00116 147 NRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASAL 213
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
5-454 3.81e-14

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 77.15  E-value: 3.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450   5 FFSDFGLLWYLKELRKEEFWKFKELLKQPLEKFELKPIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDL 84
Cdd:COG5635  48 LDLLLADLGALLALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAEALLALLELAALLKAVLLSLSGGSDL 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450  85 WTKAQEEMRNKLNPYrkhmketfqLIWEKETCLHVPEHFYKETMKNEYKELNDAYTAAARRHT-VVLEGPDGIGKTTLLR 163
Cdd:COG5635 128 VLLLSESDLLLALLI---------LLLDADGLLVSLDDLYVPLNLLERIESLKRLELLEAKKKrLLILGEPGSGKTTLLR 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 164 KVMLDWAEGNLWKDRFTFVFFlnvcEMNGIAE-TSLLELLS----RDWPESSEKIEDIFSQPeRILFIMDGFEQLKfnlq 238
Cdd:COG5635 199 YLALELAERYLDAEDPIPILI----ELRDLAEeASLEDLLAealeKRGGEPEDALERLLRNG-RLLLLLDGLDEVP---- 269

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 239 lkadlsdDWRQRQPMPIILSSLLQKkmLPESSLLIALGKLAMQKHYFmlRHPKLIKLLGFSESEKKSYFS-YFFGEKSKA 317
Cdd:COG5635 270 -------DEADRDEVLNQLRRFLER--YPKARVIITSRPEGYDSSEL--EGFEVLELAPLSDEQIEEFLKkWFEATERKA 338

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 318 LKVFNFVRDNGPLFILCHNPFTCWLVCtcvkQRLERGEDLEinsQNTTYLYASFLTTVFKAGSQS----FPPKVNRARLK 393
Cdd:COG5635 339 ERLLEALEENPELRELARNPLLLTLLA----LLLRERGELP---DTRAELYEQFVELLLERWDEQrgltIYRELSREELR 411

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 33519450 394 S-LCALAAEGIWTYTFVFSHGDLRR------NGLSESEGVMWVGMR---LLQRRG-DCFAFMHLCIQEFCAA 454
Cdd:COG5635 412 ElLSELALAMQENGRTEFAREELEEilreylGRRKDAEALLDELLLrtgLLVERGeGRYSFAHRSFQEYLAA 483
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 620-776 5.19e-14

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 74.31  E-value: 5.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 620 RELCSMFITNKNFQILDMENTSLDDPSLAILCKALAQpVCKLRKLIFTSVYFGH--DSELFKAVLHNPHLKLLSLYGTSL 697
Cdd:cd00116 155 EALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDegASALAETLASLKSLEVLNLGDNNL 233

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33519450 698 SQSDIRHLCETLKHPMCKIEELILGKCDISSEVCEDIASVLACNSKLKHLSLVENPLRDEGMTLLCEALKHSHCALERL 776
Cdd:cd00116 234 TDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESL 312
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 11-84 3.48e-13

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: 65.62  E-value: 3.48e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 33519450  11 LLWYLKELRKEEFWKFK-ELLKQPLEKFelKPIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDL 84
Cdd:cd08321   4 LLDALEDLGEEELKKFKwKLRDIPLEGY--PRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDL 76
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 809-957 7.03e-12

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 68.66  E-value: 7.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 809 NALEDNGVASLCAALKHpGCSIRELWLMGCFLTSDSCKDIAAVLICNGKLKTLKLGHNEIGDTGVRQLCAALQHPHcKLE 888
Cdd:COG5238 190 NQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVE 267

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33519450 889 CLGLQTCPITRACCDDIAAALIACKTLRSLNLDWIALDADAVVVLCEALSHpDCALQMLGLHKSGFDEE 957
Cdd:COG5238 268 TLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQ 335
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 392-440 5.43e-08

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: 50.26  E-value: 5.43e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 33519450   392 LKSLCALAAEGIWTYTFVFSHGDLRRNGLSESEGVMWVGMRLLQRRGDC 440
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGC 51
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
855-882 1.81e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.31  E-value: 1.81e-04
                           10        20
                   ....*....|....*....|....*...
gi 33519450    855 NGKLKTLKLGHNEIGDTGVRQLCAALQH 882
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
630-786 3.25e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.07  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 33519450 630 KNFQILDMENTSLDDpslaiLCKALAQpvckLRKLifTSVYFGHD--SELFKAVLHNPHLKLLSLYGTSLSqsDIRHLCE 707
Cdd:COG4886 113 TNLESLDLSGNQLTD-----LPEELAN----LTNL--KELDLSNNqlTDLPEPLGNLTNLKSLDLSNNQLT--DLPEELG 179

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33519450 708 TLKhpmcKIEELILGKCDISsevceDIASVLACNSKLKHLSLVENPLRDEGMTLlcEALKHshcaLERLMLMYCCLTSV 786
Cdd:COG4886 180 NLT----NLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLTDLPEPL--ANLTN----LETLDLSNNQLTDL 243
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 11-89 3.70e-03

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: 36.90  E-value: 3.70e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 33519450  11 LLWYLKELRKEEFWKFKELLKQplekfELKpIPWAELKKASKEDVAKLLDKHYPGKQAWEVTLNLFLQINRKDLWTKAQ 89
Cdd:cd08305   1 LLTGLENITDEEFKMFKSLLAS-----ELK-LTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
 
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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