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Conserved domains on  [gi|564372211|ref|XP_006246519|]
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NACHT, LRR and PYD domains-containing protein 3 isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 575-940 3.75e-61

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: 210.67  E-value: 3.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 575 FVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQE-EDFVQSAMGHFPKI 653
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 654 eiNLSTRMDHVVSSFCIKNCHRvktlslgflhnspkeeeeekrgsqpldqvqcvfpdphvacssrlvnccltssfcrglF 733
Cdd:cd00116   81 --CGLQELDLSDNALGPDGCGV---------------------------------------------------------L 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 734 SSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFG 813
Cdd:cd00116  102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 814 VRLLCVGLKHlLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQCNLQKLGLVNS 893
Cdd:cd00116  182 IRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCN 260

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 564372211 894 GLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPDC 940
Cdd:cd00116  261 DITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGN 307
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 2.03e-56

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


:

Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 191.75  E-value: 2.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  218 HTVVFQGAAGIGKTILARKIMLDWALGKLFKDkFDYLFFIHCREVSLRAPK-SLADLIISCWPDPNPPVCK----ILCKP 292
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  293 SRILFLMDGFDELQGAFDEHIEEVctdwqkavRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 564372211  373 EAKRKEYFFKYFSNE 387
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-90 6.78e-28

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260032  Cd Length: 84  Bit Score: 107.71  E-value: 6.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKK 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 .
gi 564372211  90 D 90
Cdd:cd08320   81 E 81
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 138-208 1.76e-16

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


:

Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 74.57  E-value: 1.76e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564372211  138 YRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRT-KMWDRPMSSLKLELLFE 208
Cdd:pfam14484   1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 466-518 4.63e-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: 4.63e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564372211  466 GLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSF 518
Cdd:pfam17779   5 KLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 575-940 3.75e-61

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: 210.67  E-value: 3.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 575 FVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQE-EDFVQSAMGHFPKI 653
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 654 eiNLSTRMDHVVSSFCIKNCHRvktlslgflhnspkeeeeekrgsqpldqvqcvfpdphvacssrlvnccltssfcrglF 733
Cdd:cd00116   81 --CGLQELDLSDNALGPDGCGV---------------------------------------------------------L 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 734 SSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFG 813
Cdd:cd00116  102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 814 VRLLCVGLKHlLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQCNLQKLGLVNS 893
Cdd:cd00116  182 IRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCN 260

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 564372211 894 GLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPDC 940
Cdd:cd00116  261 DITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGN 307
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 2.03e-56

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


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 191.75  E-value: 2.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  218 HTVVFQGAAGIGKTILARKIMLDWALGKLFKDkFDYLFFIHCREVSLRAPK-SLADLIISCWPDPNPPVCK----ILCKP 292
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  293 SRILFLMDGFDELQGAFDEHIEEVctdwqkavRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 564372211  373 EAKRKEYFFKYFSNE 387
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 520-645 1.62e-30

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: 116.62  E-value: 1.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  520 HMTFQEFFAAMYYLLEEEEEGVTVRKGPEGCSdlLNRDVKVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCK 599
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR--KRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 564372211  600 ISQQVRLELLKWIevKAKAKKLQRQPSQLELFYCLYEMQEEDFVQS 645
Cdd:pfam17776  79 LSSEIKQELLQWI--KSLIQKELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-90 6.78e-28

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260032  Cd Length: 84  Bit Score: 107.71  E-value: 6.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKK 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 .
gi 564372211  90 D 90
Cdd:cd08320   81 E 81
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 2.08e-25

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: 100.36  E-value: 2.08e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372211   10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCvPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWE 85
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEPEEGLR-SIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
199-529 9.74e-24

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 107.97  E-value: 9.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 199 SSLKLELLFEPEDEHLepvhtvVFQGAAGIGKTILARKIMLDWALGKLFKDkfDYL-FFIHCREvsLRAPKSLADLI--- 274
Cdd:COG5635  168 ESLKRLELLEAKKKRL------LILGEPGSGKTTLLRYLALELAERYLDAE--DPIpILIELRD--LAEEASLEDLLaea 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 275 ISCWPDPNPPVCKILCKPSRILFLMDGFDELqgAFDEHIEEVCTDwqkavrgdilLSSLIRKklLPKASLLITTRPVALE 354
Cdd:COG5635  238 LEKRGGEPEDALERLLRNGRLLLLLDGLDEV--PDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYD 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 355 klQHLLDHPRHVEILGFSEAKRKEYFFKYF-SNELQAREAFRLIQENEILFTMCFIPLVCWIVCTGLKQQMETGKSLAQt 433
Cdd:COG5635  304 --SSELEGFEVLELAPLSDEQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE- 380

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 434 sktttaVYVFFLSSLLQSRGGIEEHLFSAYLPG------LCSLAADGIWNQKILFEECDLRKHGLQ----KTDVSAFL-- 501
Cdd:COG5635  381 ------LYEQFVELLLERWDEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLde 454

                        330       340       350
                 ....*....|....*....|....*....|.
gi 564372211 502 ---RMNVFQKEVdcERFYSFSHMTFQEFFAA 529
Cdd:COG5635  455 lllRTGLLVERG--EGRYSFAHRSFQEYLAA 483
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 731-937 8.19e-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: 102.56  E-value: 8.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 731 GLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHpGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALG 810
Cdd:COG5238  227 ILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 811 DFGVRLLCVGLKHlLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQcNLQKLGL 890
Cdd:COG5238  306 DEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNL 383

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564372211 891 VNSGLTSLCCSALTSVLKTNQnLTHLYLRSNALGDMGLKLLCEGLLH 937
Cdd:COG5238  384 GKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGAEAQQRLEQLLER 429
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 138-208 1.76e-16

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


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 74.57  E-value: 1.76e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564372211  138 YRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRT-KMWDRPMSSLKLELLFE 208
Cdd:pfam14484   1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 466-518 4.63e-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: 4.63e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564372211  466 GLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSF 518
Cdd:pfam17779   5 KLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
739-766 3.98e-07

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 47.02  E-value: 3.98e-07
                           10        20
                   ....*....|....*....|....*...
gi 564372211   739 NQSLTELDLSDNTLGDPGMRVLCEALQH 766
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 575-940 3.75e-61

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: 210.67  E-value: 3.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 575 FVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQE-EDFVQSAMGHFPKI 653
Cdd:cd00116    1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 654 eiNLSTRMDHVVSSFCIKNCHRvktlslgflhnspkeeeeekrgsqpldqvqcvfpdphvacssrlvnccltssfcrglF 733
Cdd:cd00116   81 --CGLQELDLSDNALGPDGCGV---------------------------------------------------------L 101

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 734 SSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFG 813
Cdd:cd00116  102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 814 VRLLCVGLKHlLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQCNLQKLGLVNS 893
Cdd:cd00116  182 IRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCN 260

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 564372211 894 GLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPDC 940
Cdd:cd00116  261 DITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGN 307
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 2.03e-56

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


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 191.75  E-value: 2.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  218 HTVVFQGAAGIGKTILARKIMLDWALGKLFKDkFDYLFFIHCREVSLRAPK-SLADLIISCWPDPNPPVCK----ILCKP 292
Cdd:pfam05729   1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  293 SRILFLMDGFDELQGAFDEHIEEVctdwqkavRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729  80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                         170
                  ....*....|....*
gi 564372211  373 EAKRKEYFFKYFSNE 387
Cdd:pfam05729 152 ESDRKQYVRKYFSDE 166
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 520-645 1.62e-30

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: 116.62  E-value: 1.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  520 HMTFQEFFAAMYYLLEEEEEGVTVRKGPEGCSdlLNRDVKVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCK 599
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR--KRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCK 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 564372211  600 ISQQVRLELLKWIevKAKAKKLQRQPSQLELFYCLYEMQEEDFVQS 645
Cdd:pfam17776  79 LSSEIKQELLQWI--KSLIQKELSSERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 10-90 6.78e-28

Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and PYD domains) proteins including NALP1 (CARD7, NLRP1), NALP3 (NLRP3, Cryopyrin, CIAS1), and NALP12 (NLRP12, Monarch-1), among others. Mammals contains at least 14 NALP proteins, named NALP1-14 (or NLRP1-14). NALPs are members of the NBS-LRR family of proteins possessing a tripartite domain structure including a C-terminal LRR (leucine-rich repeats), a central nucleotide-binding site (NBS) domain or NACHT (for neuronal apoptosis inhibitor protein, CIITA, HET-E and TP1), and an N-terminal protein-protein interaction domain, which is a Pyrin domain in the case of NALPs. The NBS-LRR family is also referred to as the NLR (Nod-like Receptor) or CATERPILLAR (for CARD, transcription enhancer, R-(purine)-binding, pyrin, lots of LRRs) family. NALP1 contains an additional Caspase activation and recruitment domain (CARD) at the C-terminus. NALP1 and NALP3 are both involved in the assembly of the 'inflammasome', a multiprotein platform which is formed in response to infection or injury and is responsible for caspase-1 activation and regulation of IL-1beta maturation. NALP1-inflammasomes recognize specific substances while NALP3-inflammasomes responds to many diverse triggers. Mutations in the NALP3 gene are associated with a broad spectrum of autoinflammatory disorders including Muckle-Wells Syndrome (MWS), familial cold autoinflammatory syndrome (FCAS), and chronic neurologic cutaneous and articular syndrome (CINCA). NALP12 functions as a negative regulator of inflammation. In general, Pyrin is a subfamily of the Death Domain (DD) superfamily and functions in several signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260032  Cd Length: 84  Bit Score: 107.71  E-value: 6.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211  10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKK 89
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 .
gi 564372211  90 D 90
Cdd:cd08320   81 E 81
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 2.08e-25

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: 100.36  E-value: 2.08e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372211   10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCvPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWE 85
Cdd:pfam02758   2 LLWYLEELSEEEFKKFKSLLEDEPEEGLR-SIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
199-529 9.74e-24

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 107.97  E-value: 9.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 199 SSLKLELLFEPEDEHLepvhtvVFQGAAGIGKTILARKIMLDWALGKLFKDkfDYL-FFIHCREvsLRAPKSLADLI--- 274
Cdd:COG5635  168 ESLKRLELLEAKKKRL------LILGEPGSGKTTLLRYLALELAERYLDAE--DPIpILIELRD--LAEEASLEDLLaea 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 275 ISCWPDPNPPVCKILCKPSRILFLMDGFDELqgAFDEHIEEVCTDwqkavrgdilLSSLIRKklLPKASLLITTRPVALE 354
Cdd:COG5635  238 LEKRGGEPEDALERLLRNGRLLLLLDGLDEV--PDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYD 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 355 klQHLLDHPRHVEILGFSEAKRKEYFFKYF-SNELQAREAFRLIQENEILFTMCFIPLVCWIVCTGLKQQMETGKSLAQt 433
Cdd:COG5635  304 --SSELEGFEVLELAPLSDEQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE- 380

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 434 sktttaVYVFFLSSLLQSRGGIEEHLFSAYLPG------LCSLAADGIWNQKILFEECDLRKHGLQ----KTDVSAFL-- 501
Cdd:COG5635  381 ------LYEQFVELLLERWDEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLde 454

                        330       340       350
                 ....*....|....*....|....*....|.
gi 564372211 502 ---RMNVFQKEVdcERFYSFSHMTFQEFFAA 529
Cdd:COG5635  455 lllRTGLLVERG--EGRYSFAHRSFQEYLAA 483
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 731-937 8.19e-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: 102.56  E-value: 8.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 731 GLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHpGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALG 810
Cdd:COG5238  227 ILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 811 DFGVRLLCVGLKHlLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQcNLQKLGL 890
Cdd:COG5238  306 DEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNL 383

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564372211 891 VNSGLTSLCCSALTSVLKTNQnLTHLYLRSNALGDMGLKLLCEGLLH 937
Cdd:COG5238  384 GKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGAEAQQRLEQLLER 429
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 739-935 4.45e-22

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: 100.25  E-value: 4.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 739 NQSLTELDLSDNTLGDPGMRVLCEALQHpGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFGVRLLc 818
Cdd:COG5238  179 NNSVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIAL- 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 819 vgLKHLLCN--LQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQcNLQKLGLVNSGLT 896
Cdd:COG5238  257 --AEALKNNttVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIG 333

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564372211 897 SLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGL 935
Cdd:COG5238  334 AQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL 372
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 7-86 5.78e-22

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: 90.66  E-value: 5.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211   7 RCKLAQYLEDLEDVDLKKFKMHLEDYPPEkGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEK 86
Cdd:cd08321    1 RDLLLDALEDLGEEELKKFKWKLRDIPLE-GYPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEK 79
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 138-208 1.76e-16

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


Pssm-ID: 464185 [Multi-domain]  Cd Length: 72  Bit Score: 74.57  E-value: 1.76e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564372211  138 YRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRT-KMWDRPMSSLKLELLFE 208
Cdd:pfam14484   1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
732-939 7.74e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 77.67  E-value: 7.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 732 LFSSLSTNQSLTELDLSDNTLGDpgmrvLCEALqhPGC-NIQRLWLGRCGLThqccfNISSVLSSSQKLVELDLSDNALG 810
Cdd:COG4886  128 LPEELANLTNLKELDLSNNQLTD-----LPEPL--GNLtNLKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQIT 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 811 DFGVRLLCvglkhlLCNLQKLWLVSCCLTsaccqDLALVLSSNHSLTRLYIGENALGDsgVQVLCeKMKdpqcNLQKLGL 890
Cdd:COG4886  196 DLPEPLGN------LTNLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTD--LPELG-NLT----NLEELDL 257

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564372211 891 VNSGLTSLccsaltSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPD 939
Cdd:COG4886  258 SNNQLTDL------PPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNS 300
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 466-518 4.63e-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: 4.63e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 564372211  466 GLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSF 518
Cdd:pfam17779   5 KLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 730-890 9.03e-13

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: 71.36  E-value: 9.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 730 RGLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGcNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNAL 809
Cdd:COG5238  282 IALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQI 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 810 GDFGVRLLCVGLKhllcnlqklwlvsccltsaccqdlalvlsSNHSLTRLYIGENALGDSGVQVLCEKMKDPQcnLQKLG 889
Cdd:COG5238  361 GDEGAIALAKYLE-----------------------------GNTTLRELNLGKNNIGKQGAEALIDALQTNR--LHTLI 409


                 .
gi 564372211 890 L 890
Cdd:COG5238  410 L 410
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
793-930 2.97e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.78  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 793 LSSSQKLVELDLSDNALGDFGVRLlcVGLKhllcNLQKLWLVSCCLTsaccqDLALVLSSNHSLTRLYIGENALgdSGVQ 872
Cdd:COG4886  109 LSNLTNLESLDLSGNQLTDLPEEL--ANLT----NLKELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQL--TDLP 175

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564372211 873 VLCEKMKdpqcNLQKLGLVNSGLTSlccsaLTSVLKTNQNLTHLYLRSNALGDMGLKL 930
Cdd:COG4886  176 EELGNLT----NLKELDLSNNQITD-----LPEPLGNLTNLEELDLSGNQLTDLPEPL 224
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
739-766 3.98e-07

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 47.02  E-value: 3.98e-07
                           10        20
                   ....*....|....*....|....*...
gi 564372211   739 NQSLTELDLSDNTLGDPGMRVLCEALQH 766
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
730-936 2.90e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.70  E-value: 2.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 730 RGLFSSLSTNQSLTELDLSDNTLGDpgmrvlcealqhpgcniqrlwlgrcglthqccfnISSVLSSSQKLVELDLSDNAL 809
Cdd:COG4886  172 TDLPEELGNLTNLKELDLSNNQITD----------------------------------LPEPLGNLTNLEELDLSGNQL 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 810 GDFGVRLlcVGLKhllcNLQKLWLVSCCLTsaccqDLAlVLSSNHSLTRLYIGENALGDSGVqvlCEKMKdpqcNLQKLG 889
Cdd:COG4886  218 TDLPEPL--ANLT----NLETLDLSNNQLT-----DLP-ELGNLTNLEELDLSNNQLTDLPP---LANLT----NLKTLD 278

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564372211 890 LVNSGLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLL 936
Cdd:COG4886  279 LSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLL 325
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-824 3.19e-06

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: 50.56  E-value: 3.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 729 CRGLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGcNIQRLWLGRCGLTHQccfNISSVLSSSQ--KLVELDLSD 806
Cdd:COG5238  337 AIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLGKNNIGKQ---GAEALIDALQtnRLHTLILDG 412

                         90
                 ....*....|....*...
gi 564372211 807 NALGDFGVRLLCVGLKHL 824
Cdd:COG5238  413 NLIGAEAQQRLEQLLERI 430
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 853-939 5.89e-06

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: 49.79  E-value: 5.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372211 853 NHSLTRLYIGENALGDSGVQVLCEKMKDPQcNLQKLGLVNSGLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLC 932
Cdd:COG5238  179 NNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALA 257


                 ....*..
gi 564372211 933 EGLLHPD 939
Cdd:COG5238  258 EALKNNT 264
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-88 8.06e-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: 44.60  E-value: 8.06e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564372211  10 LAQYLEDLEDVDLKKFKMHLEDYppekgcVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAK 88
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLASE------LKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
796-823 7.60e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.47  E-value: 7.60e-05
                           10        20
                   ....*....|....*....|....*...
gi 564372211   796 SQKLVELDLSDNALGDFGVRLLCVGLKH 823
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
738-761 3.91e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 38.37  E-value: 3.91e-04
                          10        20
                  ....*....|....*....|....
gi 564372211  738 TNQSLTELDLSDNTLGDPGMRVLC 761
Cdd:pfam13516   1 SNTHLTTLDLSDNDIGDEGAEALA 24
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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