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Conserved domains on  [gi|685156911|ref|NP_001165635|]
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NLR family, pyrin domain containing 4 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-92 6.81e-34

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: 124.66  E-value: 6.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  10 LMWYLEELNKKEFVKFKEFLKQEILQLRLKQISWTKVKKASREDLANLLLKHYEEKQAWDMTFKIFQKMNRKDLIERAGR 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ...
gi 685156911  90 EIA 92
Cdd:cd08320   81 EMN 83
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 689-953 9.29e-33

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


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 129.78  E-value: 9.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 689 NQRLQHLNLSLTFLSHSD--VKLLCDVLnQAECNIEKLMIAACNLSPDDCKVFASVLiSSKMLKHLNLSSNNLDKGISS- 765
Cdd:cd00116   50 QPSLKELCLSLNETGRIPrgLQSLLQGL-TKGCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRl 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 766 LCKALCHPDCILKHLVLANCSLSEQCWDYLSEVVRRNKTLSHLDISSNDLKDEGLKVLCGALTlPDSGLISLSVRHCLIT 845
Cdd:cd00116  128 LAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLK-ANCNLEVLDLNNNGLT 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 846 TSGCQDLAEVLRHNQNLRSLQVSNNKIEDAGVKLLCDAIKQPNCHLENIGLEACELTGACCKDLASAFVHCKTLWGINLL 925
Cdd:cd00116  207 DEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286

                        250       260
                 ....*....|....*....|....*...
gi 685156911 926 ENALDHSGLVVLFEALKQQKCTLHVLGL 953
Cdd:cd00116  287 GNKFGEEGAQLLAESLLEPGNELESLWV 314
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 148-317 2.65e-29

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: 114.71  E-value: 2.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  148 HMVFLQGVAGIGKSLMLTKLMLAWSEGIVFQnKFSYIFYFCCQDVKQLKRA-SLAELISREWPNASAP----TAEILSQP 222
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPvsevWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  223 EKLLFIIDSLEVMECNMSERESElcdnctekQPVSLLLSSLLRRKMLPESSFLISATPETFEKMEDRIECTNVKIITGFN 302
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 685156911  303 ENNIKMYFRSLFQDK 317
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 451-564 8.90e-19

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: 83.11  E-value: 8.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  451 HPSLQEVCAAVFYLLKSHLDHP--------SQDVKSVEALLFTFLKKAKVQWIFLGCFLFGLLHESEQEKLEMFFGHQLS 522
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 685156911  523 QEIKHQLYQCLETISVNEELQEqiDGMKLFYCLFEMEDEAFL 564
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFV 120
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 393-449 4.84e-13

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


:

Pssm-ID: 465501  Cd Length: 57  Bit Score: 64.51  E-value: 4.84e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 685156911  393 DQLQGLCSLAAEGMWTDTFVFSEEALRRNGILDSDIPTLLDRRILERSKESESCYIF 449
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
 
Name Accession Description Interval E-value
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-92 6.81e-34

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: 124.66  E-value: 6.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  10 LMWYLEELNKKEFVKFKEFLKQEILQLRLKQISWTKVKKASREDLANLLLKHYEEKQAWDMTFKIFQKMNRKDLIERAGR 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ...
gi 685156911  90 EIA 92
Cdd:cd08320   81 EMN 83
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 689-953 9.29e-33

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 129.78  E-value: 9.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 689 NQRLQHLNLSLTFLSHSD--VKLLCDVLnQAECNIEKLMIAACNLSPDDCKVFASVLiSSKMLKHLNLSSNNLDKGISS- 765
Cdd:cd00116   50 QPSLKELCLSLNETGRIPrgLQSLLQGL-TKGCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRl 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 766 LCKALCHPDCILKHLVLANCSLSEQCWDYLSEVVRRNKTLSHLDISSNDLKDEGLKVLCGALTlPDSGLISLSVRHCLIT 845
Cdd:cd00116  128 LAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLK-ANCNLEVLDLNNNGLT 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 846 TSGCQDLAEVLRHNQNLRSLQVSNNKIEDAGVKLLCDAIKQPNCHLENIGLEACELTGACCKDLASAFVHCKTLWGINLL 925
Cdd:cd00116  207 DEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286

                        250       260
                 ....*....|....*....|....*...
gi 685156911 926 ENALDHSGLVVLFEALKQQKCTLHVLGL 953
Cdd:cd00116  287 GNKFGEEGAQLLAESLLEPGNELESLWV 314
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 148-317 2.65e-29

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: 114.71  E-value: 2.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  148 HMVFLQGVAGIGKSLMLTKLMLAWSEGIVFQnKFSYIFYFCCQDVKQLKRA-SLAELISREWPNASAP----TAEILSQP 222
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPvsevWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  223 EKLLFIIDSLEVMECNMSERESElcdnctekQPVSLLLSSLLRRKMLPESSFLISATPETFEKMEDRIECTNVKIITGFN 302
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 685156911  303 ENNIKMYFRSLFQDK 317
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 9-85 1.78e-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: 103.44  E-value: 1.78e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685156911    9 GLMWYLEELNKKEFVKFKEFLKQEIlQLRLKQISWTKVKKASREDLANLLLKHYEEKQAWDMTFKIFQKMNRKDLIE 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 752-973 3.92e-23

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: 103.72  E-value: 3.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 752 LNLSSNNL-DKGISSLCKALCHPDCiLKHLVLANCSLSEQCWDYLSEVVRRNKTLSHLDISSNDLKDEGLKVLCGALTLP 830
Cdd:COG5238  185 VYLGCNQIgDEGIEELAEALTQNTT-VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 831 DSgLISLSVRHCLITTSGCQDLAEVLRHNQNLRSLQVSNNKIEDAGVKLLCDAIKQpNCHLENIGLEACELTGACCKDLA 910
Cdd:COG5238  264 TT-VETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALA 341

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685156911 911 SAFVHCKTLWGINLLENALDHSGLVVLFEALKQQKcTLHVLGLRITDFDKETQEFLIAEEEKN 973
Cdd:COG5238  342 KALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLGKNNIGKQGAEALIDALQTN 403
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 451-564 8.90e-19

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: 83.11  E-value: 8.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  451 HPSLQEVCAAVFYLLKSHLDHP--------SQDVKSVEALLFTFLKKAKVQWIFLGCFLFGLLHESEQEKLEMFFGHQLS 522
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 685156911  523 QEIKHQLYQCLETISVNEELQEqiDGMKLFYCLFEMEDEAFL 564
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFV 120
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 393-449 4.84e-13

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


Pssm-ID: 465501  Cd Length: 57  Bit Score: 64.51  E-value: 4.84e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 685156911  393 DQLQGLCSLAAEGMWTDTFVFSEEALRRNGILDSDIPTLLDRRILERSKESESCYIF 449
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
83-512 2.43e-10

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 64.83  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  83 LIERAGREIAGHSKLYQAHLKKKLTHDYARKFNIKAQDLFKQKFTQDDCDRFENLLVSKATGKKphmVFLQGVAGIGKSL 162
Cdd:COG5635  119 LSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRLELLEAKKKR---LLILGEPGSGKTT 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 163 MLTKLMLAWSEGIVFQNKFsYIFYFCCQDVKqlKRASLAELISREWPNASAPTAEILS---QPEKLLFIIDSLEvmECNM 239
Cdd:COG5635  196 LLRYLALELAERYLDAEDP-IPILIELRDLA--EEASLEDLLAEALEKRGGEPEDALErllRNGRLLLLLDGLD--EVPD 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 240 SERESELCDNCTEKQpvslllssllrrKMLPESSFLISATPETFEkmEDRIECTNVKIITGFNENNIKMYFRSLFQDKNR 319
Cdd:COG5635  271 EADRDEVLNQLRRFL------------ERYPKARVIITSRPEGYD--SSELEGFEVLELAPLSDEQIEEFLKKWFEATER 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 320 TLEAF-SLVRENEQLFNVCQVPVLCWMVATCIKkeiEKGRDPvficRRTTSLYTTHIFNLFTPQNAQ-----YPSKKSQD 393
Cdd:COG5635  337 KAERLlEALEENPELRELARNPLLLTLLALLLR---ERGELP----DTRAELYEQFVELLLERWDEQrgltiYRELSREE 409

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 394 QLQGLCSLAAEGMWTDTFVFSEEALRRngILDSDIPTLLD-----RRILERS----KESESCYIFLHPSLQEVCAAVFyl 464
Cdd:COG5635  410 LRELLSELALAMQENGRTEFAREELEE--ILREYLGRRKDaeallDELLLRTgllvERGEGRYSFAHRSFQEYLAARA-- 485

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 685156911 465 LKSHLDhpsqdvKSVEALLFTFLKKAKVQWIFLgcFLFGLLHESEQEK 512
Cdd:COG5635  486 LVEELD------EELLELLAEHLEDPRWREVLL--LLAGLLDDVKQIK 525
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
859-886 8.45e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.39  E-value: 8.45e-04
                           10        20
                   ....*....|....*....|....*...
gi 685156911   859 NQNLRSLQVSNNKIEDAGVKLLCDAIKQ 886
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
858-881 5.23e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 35.29  E-value: 5.23e-03
                          10        20
                  ....*....|....*....|....
gi 685156911  858 HNQNLRSLQVSNNKIEDAGVKLLC 881
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
Name Accession Description Interval E-value
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-92 6.81e-34

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: 124.66  E-value: 6.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  10 LMWYLEELNKKEFVKFKEFLKQEILQLRLKQISWTKVKKASREDLANLLLKHYEEKQAWDMTFKIFQKMNRKDLIERAGR 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ...
gi 685156911  90 EIA 92
Cdd:cd08320   81 EMN 83
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 689-953 9.29e-33

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 129.78  E-value: 9.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 689 NQRLQHLNLSLTFLSHSD--VKLLCDVLnQAECNIEKLMIAACNLSPDDCKVFASVLiSSKMLKHLNLSSNNLDKGISS- 765
Cdd:cd00116   50 QPSLKELCLSLNETGRIPrgLQSLLQGL-TKGCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRl 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 766 LCKALCHPDCILKHLVLANCSLSEQCWDYLSEVVRRNKTLSHLDISSNDLKDEGLKVLCGALTlPDSGLISLSVRHCLIT 845
Cdd:cd00116  128 LAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLK-ANCNLEVLDLNNNGLT 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 846 TSGCQDLAEVLRHNQNLRSLQVSNNKIEDAGVKLLCDAIKQPNCHLENIGLEACELTGACCKDLASAFVHCKTLWGINLL 925
Cdd:cd00116  207 DEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286

                        250       260
                 ....*....|....*....|....*...
gi 685156911 926 ENALDHSGLVVLFEALKQQKCTLHVLGL 953
Cdd:cd00116  287 GNKFGEEGAQLLAESLLEPGNELESLWV 314
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 681-892 7.80e-30

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: 120.92  E-value: 7.80e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 681 HLFFELIQNQRLQHLNLSLTFLSHSDVKLLCDVLNQAECNIEKLMIAACNLSPDDCKVFASVLISSKMLKHLNLSSNNL- 759
Cdd:cd00116   99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIg 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 760 DKGISSLCKALCHpDCILKHLVLANCSLSEQCWDYLSEVVRRNKTLSHLDISSNDLKDEGLKVLCGALTLPDSGLISLSV 839
Cdd:cd00116  179 DAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 685156911 840 RHCLITTSGCQDLAEVLRHNQNLRSLQVSNNKIEDAGVKLLCDAIKQPNCHLE 892
Cdd:cd00116  258 SCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELE 310
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 148-317 2.65e-29

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: 114.71  E-value: 2.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  148 HMVFLQGVAGIGKSLMLTKLMLAWSEGIVFQnKFSYIFYFCCQDVKQLKRA-SLAELISREWPNASAP----TAEILSQP 222
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQ-GFDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPvsevWAVILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  223 EKLLFIIDSLEVMECNMSERESElcdnctekQPVSLLLSSLLRRKMLPESSFLISATPETFEKMEDRIECTNVKIITGFN 302
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGP--------CPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 685156911  303 ENNIKMYFRSLFQDK 317
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 9-85 1.78e-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: 103.44  E-value: 1.78e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685156911    9 GLMWYLEELNKKEFVKFKEFLKQEIlQLRLKQISWTKVKKASREDLANLLLKHYEEKQAWDMTFKIFQKMNRKDLIE 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 729-953 1.86e-26

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: 111.29  E-value: 1.86e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 729 CNLSPDDCKVFASVLISSKMLKHLNLSSNNLDKGISSLCKALCH--PDCILKHLVLANCSLS-EQCWDYlsEVVRRNKTL 805
Cdd:cd00116   33 NTLGEEAAKALASALRPQPSLKELCLSLNETGRIPRGLQSLLQGltKGCGLQELDLSDNALGpDGCGVL--ESLLRSSSL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 806 SHLDISSNDLKDEGLKVLCGALTLPDSGLISLSVRHCLITTSGCQDLAEVLRHNQNLRSLQVSNNKIEDAGVKLLCDAIK 885
Cdd:cd00116  111 QELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLK 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685156911 886 QpNCHLENIGLEACELTGACCKDLASAFVHCKTLWGINLLENALDHSGLVVLFEALKQQKCTLHVLGL 953
Cdd:cd00116  191 A-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 752-973 3.92e-23

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: 103.72  E-value: 3.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 752 LNLSSNNL-DKGISSLCKALCHPDCiLKHLVLANCSLSEQCWDYLSEVVRRNKTLSHLDISSNDLKDEGLKVLCGALTLP 830
Cdd:COG5238  185 VYLGCNQIgDEGIEELAEALTQNTT-VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 831 DSgLISLSVRHCLITTSGCQDLAEVLRHNQNLRSLQVSNNKIEDAGVKLLCDAIKQpNCHLENIGLEACELTGACCKDLA 910
Cdd:COG5238  264 TT-VETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALA 341

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 685156911 911 SAFVHCKTLWGINLLENALDHSGLVVLFEALKQQKcTLHVLGLRITDFDKETQEFLIAEEEKN 973
Cdd:COG5238  342 KALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLGKNNIGKQGAEALIDALQTN 403
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 627-966 3.14e-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: 97.55  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 627 MCSVLISS-KDIHVLQVkdtNLNETAFWVLYN-----HLKYPSCTLKVLVVNNVTflcdnhlffELIQNQRLQHLNLSLT 700
Cdd:COG5238  123 MAKTLEDSlILYLALPR---RINLIQVLKDPLggnavHLLGLAARLGLLAAISMA---------KALQNNSVETVYLGCN 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 701 FLSHSDVKLLCDVLNQaECNIEKLMIAACNLSPDDCKVFASVLISSKMLKHLNLSSNNL-DKGISSLCKALCHPDCIlKH 779
Cdd:COG5238  191 QIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIgDEGVIALAEALKNNTTV-ET 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 780 LVLANCSLSEQCWDYLSEVVRRNKTLSHLDISSNDLKDEGLKVLCGALTlPDSGLISLSVRHCLITTSGCQDLAEVLRHN 859
Cdd:COG5238  269 LYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQ-GNKTLHTLNLAYNGIGAQGAIALAKALQEN 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 860 QNLRSLQVSNNKIEDAGVKLLCDAIKQPnchlenigleaceltgacckdlasafvhcKTLWGINLLENALDHSGLVVLFE 939
Cdd:COG5238  348 TTLHSLDLSDNQIGDEGAIALAKYLEGN-----------------------------TTLRELNLGKNNIGKQGAEALID 398

                        330       340
                 ....*....|....*....|....*..
gi 685156911 940 ALkqQKCTLHVLGLRITDFDKETQEFL 966
Cdd:COG5238  399 AL--QTNRLHTLILDGNLIGAEAQQRL 423
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 777-954 6.68e-20

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: 91.65  E-value: 6.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 777 LKHLVLANCSLSEQCWDYLSEVVRRNKTLSHLDISSNDL--KDEGLKVLCGALTlPDSGLISLSVRHCLITTSGCQDLaE 854
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETgrIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVL-E 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 855 VLRHNQNLRSLQVSNNKIEDAGVKLLCDAIKQPNCHLENIGLEACELTGACCKDLASAFVHCKTLWGINLLENALDHSGL 934
Cdd:cd00116  103 SLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI 182

                        170       180
                 ....*....|....*....|
gi 685156911 935 VVLFEALKQQkCTLHVLGLR 954
Cdd:cd00116  183 RALAEGLKAN-CNLEVLDLN 201
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 451-564 8.90e-19

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: 83.11  E-value: 8.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  451 HPSLQEVCAAVFYLLKSHLDHP--------SQDVKSVEALLFTFLKKAKVQWIFLGCFLFGLLHESEQEKLEMFFGHQLS 522
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSnplkeffgLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 685156911  523 QEIKHQLYQCLETISVNEELQEqiDGMKLFYCLFEMEDEAFL 564
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELSSE--RFLNLFHCLYELQDESFV 120
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 575-844 1.79e-18

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 87.41  E-value: 1.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 575 NFVAKDYSDVIVAAYCLKHCSTLKKLSFSTqNILSEEQEHSYtekllicwhhmcSVLISSKDIHVLQVKDTNLNETAFWV 654
Cdd:cd00116   61 NETGRIPRGLQSLLQGLTKGCGLQELDLSD-NALGPDGCGVL------------ESLLRSSSLQELKLNNNGLGDRGLRL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 655 LYNHLKYPSCTLKVLVV--NNVTFLCDNHLFFELIQNQRLQHLNLSLTFLSHSDVKLLCDVLnQAECNIEKLMIAACNLS 732
Cdd:cd00116  128 LAKGLKDLPPALEKLVLgrNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGL-KANCNLEVLDLNNNGLT 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 733 PDDCKVFASVLISSKMLKHLNLSSNNL-DKGISSLCKALCHPDCILKHLVLANCSLSEQCWDYLSEVVRRNKTLSHLDIS 811
Cdd:cd00116  207 DEGASALAETLASLKSLEVLNLGDNNLtDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLR 286

                        250       260       270
                 ....*....|....*....|....*....|...
gi 685156911 812 SNDLKDEGLKVLCGALTLPDSGLISLSVRHCLI 844
Cdd:cd00116  287 GNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 802-979 3.61e-18

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: 88.31  E-value: 3.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 802 NKTLSHLDISSNDLKDEGLKVLCGALTLPDSgLISLSVRHCLITTSGCQDLAEVLRHNQNLRSLQVSNNKIEDAGVKLLC 881
Cdd:COG5238  179 NNSVETVYLGCNQIGDEGIEELAEALTQNTT-VTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 882 DAIKQpNCHLENIGLEACELTGACCKDLASAFVHCKTLWGINLLENALDHSGLVVLFEALKQQKcTLHVLGLRITDFDKE 961
Cdd:COG5238  258 EALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQ 335

                        170
                 ....*....|....*...
gi 685156911 962 TQEFLIAEEEKNPYLSIL 979
Cdd:COG5238  336 GAIALAKALQENTTLHSL 353
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 10-86 3.26e-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: 3.26e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 685156911  10 LMWYLEELNKKEFVKFKEFLKqEILQLRLKQISWTKVKKASREDLANLLLKHYEEKQAWDMTFKIFQKMNRKDLIER 86
Cdd:cd08321    4 LLDALEDLGEEELKKFKWKLR-DIPLEGYPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEK 79
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 393-449 4.84e-13

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


Pssm-ID: 465501  Cd Length: 57  Bit Score: 64.51  E-value: 4.84e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 685156911  393 DQLQGLCSLAAEGMWTDTFVFSEEALRRNGILDSDIPTLLDRRILERSKESESCYIF 449
Cdd:pfam17779   1 KLLLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
83-512 2.43e-10

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 64.83  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911  83 LIERAGREIAGHSKLYQAHLKKKLTHDYARKFNIKAQDLFKQKFTQDDCDRFENLLVSKATGKKphmVFLQGVAGIGKSL 162
Cdd:COG5635  119 LSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLNLLERIESLKRLELLEAKKKR---LLILGEPGSGKTT 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 163 MLTKLMLAWSEGIVFQNKFsYIFYFCCQDVKqlKRASLAELISREWPNASAPTAEILS---QPEKLLFIIDSLEvmECNM 239
Cdd:COG5635  196 LLRYLALELAERYLDAEDP-IPILIELRDLA--EEASLEDLLAEALEKRGGEPEDALErllRNGRLLLLLDGLD--EVPD 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 240 SERESELCDNCTEKQpvslllssllrrKMLPESSFLISATPETFEkmEDRIECTNVKIITGFNENNIKMYFRSLFQDKNR 319
Cdd:COG5635  271 EADRDEVLNQLRRFL------------ERYPKARVIITSRPEGYD--SSELEGFEVLELAPLSDEQIEEFLKKWFEATER 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 320 TLEAF-SLVRENEQLFNVCQVPVLCWMVATCIKkeiEKGRDPvficRRTTSLYTTHIFNLFTPQNAQ-----YPSKKSQD 393
Cdd:COG5635  337 KAERLlEALEENPELRELARNPLLLTLLALLLR---ERGELP----DTRAELYEQFVELLLERWDEQrgltiYRELSREE 409

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 394 QLQGLCSLAAEGMWTDTFVFSEEALRRngILDSDIPTLLD-----RRILERS----KESESCYIFLHPSLQEVCAAVFyl 464
Cdd:COG5635  410 LRELLSELALAMQENGRTEFAREELEE--ILREYLGRRKDaeallDELLLRTgllvERGEGRYSFAHRSFQEYLAARA-- 485

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 685156911 465 LKSHLDhpsqdvKSVEALLFTFLKKAKVQWIFLgcFLFGLLHESEQEK 512
Cdd:COG5635  486 LVEELD------EELLELLAEHLEDPRWREVLL--LLAGLLDDVKQIK 525
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
631-874 1.69e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.47  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 631 LISSKDIHVLQVKDTNLNETAFWVLYNHLKYPSCTLKVLVVNNVTFLCDNHLFFELIQNQRLQHLnLSLTFLSHSDVKLL 710
Cdd:COG4886   31 LLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDL-TNLTELDLSGNEEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 711 CDVLNqaecnIEKLMIAACNLS--PDDckvfasvLISSKMLKHLNLSSNN---LDKGISSLCKalchpdciLKHLVLANC 785
Cdd:COG4886  110 SNLTN-----LESLDLSGNQLTdlPEE-------LANLTNLKELDLSNNQltdLPEPLGNLTN--------LKSLDLSNN 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 786 SLSEqcwdyLSEVVRRNKTLSHLDISSNDLKDegLKVLCGALTlpdsGLISLSVRHCLITtsgcqDLAEVLRHNQNLRSL 865
Cdd:COG4886  170 QLTD-----LPEELGNLTNLKELDLSNNQITD--LPEPLGNLT----NLEELDLSGNQLT-----DLPEPLANLTNLETL 233


                 ....*....
gi 685156911 866 QVSNNKIED 874
Cdd:COG4886  234 DLSNNQLTD 242
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-87 2.68e-06

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


Pssm-ID: 260019  Cd Length: 73  Bit Score: 45.76  E-value: 2.68e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685156911  10 LMWYLEELNKKEFVKFKEFLKQEILQLRLKQISWTKVKkasredLANLLLKHYEEKQAWDMTFKIFQKMNRKDLIERA 87
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLASELKLTRKMQEEYDRIE------IADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQL 72
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
859-886 8.45e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.39  E-value: 8.45e-04
                           10        20
                   ....*....|....*....|....*...
gi 685156911   859 NQNLRSLQVSNNKIEDAGVKLLCDAIKQ 886
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
858-881 5.23e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 35.29  E-value: 5.23e-03
                          10        20
                  ....*....|....*....|....
gi 685156911  858 HNQNLRSLQVSNNKIEDAGVKLLC 881
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
 748-919 5.59e-03

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 39.62  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 748 MLKHLNLSSNNLDKGISSLCKALchpdcilKHLVLANCSLSEQCWDYLSevvrRNKTLSHLDISSNDL-KDEGLKVLCga 826
Cdd:cd09293    8 LHKLGQITQSNISQLLRILHSGL-------EWLELYMCPISDPPLDQLS----NCNKLKKLILPGSKLiDDEGLIALA-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685156911 827 LTLPdsGLISLSVRHC-LITTSGCQDLAevlRHNQNLRSLQVSN----NKIEDAGVKllcdAIKQPNCHLENIGLEACEL 901
Cdd:cd09293   75 QSCP--NLQVLDLRACeNITDSGIVALA---TNCPKLQTINLGRhrngHLITDVSLS----ALGKNCTFLQTVGFAGCDV 145

                        170
                 ....*....|....*...
gi 685156911 902 TGACCKDLASafVHCKTL 919
Cdd:cd09293  146 TDKGVWELAS--GCSKSL 161
LRR_6 pfam13516
Leucine Rich repeat;
802-824 5.83e-03

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 34.90  E-value: 5.83e-03
                          10        20
                  ....*....|....*....|...
gi 685156911  802 NKTLSHLDISSNDLKDEGLKVLC 824
Cdd:pfam13516   2 NTHLTTLDLSDNDIGDEGAEALA 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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