NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958656977|ref|XP_038941323|]
View 

NACHT, LRR and PYD domains-containing protein 3 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 575-952 6.98e-62

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: 213.37  E-value: 6.98e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  575 FVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQE-EDFVQSAMGHFPKi 653
Cdd:cd00116      1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  654 eINLSTRMDHVVSSFCIKNCHRvktlslgflhnspkeeeeekrgsqpldqvqcvfpdphvacssrlvnccltssfcrglF 733
Cdd:cd00116     80 -GCGLQELDLSDNALGPDGCGV---------------------------------------------------------L 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  734 SSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFG 813
Cdd:cd00116    102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  814 VRLLCVGLKHlLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQCNLQKLGLVNS 893
Cdd:cd00116    182 IRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCN 260

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656977  894 GLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPDCKLQMLELDNCSL 952
Cdd:cd00116    261 DITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 3.72e-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: 191.36  E-value: 3.72e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  218 HTVVFQGAAGIGKTILARKIMLDWALGKLFKDkFDYLFFIHCREVSLRAPK-SLADLIISCWPDPNPPVCK----ILCKP 292
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  293 SRILFLMDGFDELQGAFDEHIEEVctdwqkavRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 1958656977  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 1.54e-27

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: 106.56  E-value: 1.54e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977   10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKK 89
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                   .
gi 1958656977   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 2.53e-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: 74.19  E-value: 2.53e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656977  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 6.52e-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: 64.12  E-value: 6.52e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958656977  466 GLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSF 518
Cdd:pfam17779    5 KLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 910-1024 5.93e-08

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


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 56.34  E-value: 5.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  910 NQNLTHLYLRSNALGDMGLKLLCEGLLHPDcKLQMLELDNCSLTSHSCWDLSTILTHNQSLRKLNLSNNDLGDLCVVTLC 989
Cdd:COG5238    179 NNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALA 257

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958656977  990 EVLkQQGCLLQSLQLGEMYLNCETKRTL-EALQEEK 1024
Cdd:COG5238    258 EAL-KNNTTVETLYLSGNQIGAEGAIALaKALQGNT 292
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 575-952 6.98e-62

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: 213.37  E-value: 6.98e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  575 FVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQE-EDFVQSAMGHFPKi 653
Cdd:cd00116      1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  654 eINLSTRMDHVVSSFCIKNCHRvktlslgflhnspkeeeeekrgsqpldqvqcvfpdphvacssrlvnccltssfcrglF 733
Cdd:cd00116     80 -GCGLQELDLSDNALGPDGCGV---------------------------------------------------------L 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  734 SSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFG 813
Cdd:cd00116    102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  814 VRLLCVGLKHlLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQCNLQKLGLVNS 893
Cdd:cd00116    182 IRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCN 260

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656977  894 GLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPDCKLQMLELDNCSL 952
Cdd:cd00116    261 DITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 3.72e-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: 191.36  E-value: 3.72e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  218 HTVVFQGAAGIGKTILARKIMLDWALGKLFKDkFDYLFFIHCREVSLRAPK-SLADLIISCWPDPNPPVCK----ILCKP 292
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  293 SRILFLMDGFDELQGAFDEHIEEVctdwqkavRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 1958656977  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 3.61e-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: 115.85  E-value: 3.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  520 HMTFQEFFAAMYYLLEEEEEGVTVRKGPEGCSdlLNRDVKVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCK 599
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR--KRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958656977  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 1.54e-27

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: 106.56  E-value: 1.54e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977   10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKK 89
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                   .
gi 1958656977   90 D 90
Cdd:cd08320     81 E 81
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 739-1023 4.04e-26

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: 112.58  E-value: 4.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  739 NQSLTELDLSDNTLGDPGMRVLCEALQHpGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFGVRLLc 818
Cdd:COG5238    179 NNSVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIAL- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  819 vgLKHLLCN--LQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQcNLQKLGLVNSGLT 896
Cdd:COG5238    257 --AEALKNNttVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIG 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  897 SLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEgllhpdcklqmleldncsltshscwdlstILTHNQSLRKLNLS 976
Cdd:COG5238    334 AQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAK-----------------------------YLEGNTTLRELNLG 384

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958656977  977 NNDLGDLCVVTLCEVLkqQGCLLQSLQLGEMYLNCETKRTLEALQEE 1023
Cdd:COG5238    385 KNNIGKQGAEALIDAL--QTNRLHTLILDGNLIGAEAQQRLEQLLER 429
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 4.53e-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: 99.59  E-value: 4.53e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656977   10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCvPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWE 85
Cdd:pfam02758    2 LLWYLEELSEEEFKKFKSLLEDEPEEGLR-SIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
199-529 2.05e-23

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 107.20  E-value: 2.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  199 SSLKLELLFEPEDEHLepvhtvVFQGAAGIGKTILARKIMLDWALGKLFKDkfDYL-FFIHCREvsLRAPKSLADLI--- 274
Cdd:COG5635    168 ESLKRLELLEAKKKRL------LILGEPGSGKTTLLRYLALELAERYLDAE--DPIpILIELRD--LAEEASLEDLLaea 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  275 ISCWPDPNPPVCKILCKPSRILFLMDGFDELqgAFDEHIEEVCTDwqkavrgdilLSSLIRKklLPKASLLITTRPVALE 354
Cdd:COG5635    238 LEKRGGEPEDALERLLRNGRLLLLLDGLDEV--PDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYD 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  355 klQHLLDHPRHVEILGFSEAKRKEYFFKYF-SNELQAREAFRLIQENEILFTMCFIPLVCWIVCTGLKQQMETGKSLAQt 433
Cdd:COG5635    304 --SSELEGFEVLELAPLSDEQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE- 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  434 sktttaVYVFFLSSLLQSRGGIEEHLFSAYLPG------LCSLAADGIWNQKILFEECDLRKHGLQ----KTDVSAFL-- 501
Cdd:COG5635    381 ------LYEQFVELLLERWDEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLde 454

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1958656977  502 ---RMNVFQKEVdcERFYSFSHMTFQEFFAA 529
Cdd:COG5635    455 lllRTGLLVERG--EGRYSFAHRSFQEYLAA 483
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 138-208 2.53e-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: 74.19  E-value: 2.53e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656977  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 6.52e-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: 64.12  E-value: 6.52e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958656977  466 GLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSF 518
Cdd:pfam17779    5 KLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 910-1024 5.93e-08

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: 56.34  E-value: 5.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  910 NQNLTHLYLRSNALGDMGLKLLCEGLLHPDcKLQMLELDNCSLTSHSCWDLSTILTHNQSLRKLNLSNNDLGDLCVVTLC 989
Cdd:COG5238    179 NNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALA 257

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958656977  990 EVLkQQGCLLQSLQLGEMYLNCETKRTL-EALQEEK 1024
Cdd:COG5238    258 EAL-KNNTTVETLYLSGNQIGAEGAIALaKALQGNT 292
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
739-766 6.86e-07

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 46.25  E-value: 6.86e-07
                            10        20
                    ....*....|....*....|....*...
gi 1958656977   739 NQSLTELDLSDNTLGDPGMRVLCEALQH 766
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
967-994 1.90e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.31  E-value: 1.90e-04
                            10        20
                    ....*....|....*....|....*...
gi 1958656977   967 NQSLRKLNLSNNDLGDLCVVTLCEVLKQ 994
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 ...
 575-952 6.98e-62

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: 213.37  E-value: 6.98e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  575 FVVRFLFGLVNQERTSYLEKKLSCKISQQVRLELLKWIEVKAKAKKLQRQPSQLELFYCLYEMQE-EDFVQSAMGHFPKi 653
Cdd:cd00116      1 LQLSLKGELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTK- 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  654 eINLSTRMDHVVSSFCIKNCHRvktlslgflhnspkeeeeekrgsqpldqvqcvfpdphvacssrlvnccltssfcrglF 733
Cdd:cd00116     80 -GCGLQELDLSDNALGPDGCGV---------------------------------------------------------L 101

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  734 SSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFG 813
Cdd:cd00116    102 ESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAG 181

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  814 VRLLCVGLKHlLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQCNLQKLGLVNS 893
Cdd:cd00116    182 IRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCN 260

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656977  894 GLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPDCKLQMLELDNCSL 952
Cdd:cd00116    261 DITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 218-387 3.72e-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: 191.36  E-value: 3.72e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  218 HTVVFQGAAGIGKTILARKIMLDWALGKLFKDkFDYLFFIHCREVSLRAPK-SLADLIISCWPDPNPPVCK----ILCKP 292
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEvwavILELP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  293 SRILFLMDGFDELQGAFDEHIEEVctdwqkavRGDILLSSLIRKKLLPKASLLITTRPVALEKLQHLLDHPRHVEILGFS 372
Cdd:pfam05729   80 ERLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFS 151

                          170
                   ....*....|....*
gi 1958656977  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 3.61e-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: 115.85  E-value: 3.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  520 HMTFQEFFAAMYYLLEEEEEGVTVRKGPEGCSdlLNRDVKVLLENYGKFEKGYLIFVVRFLFGLVNQERTSYLEKKLSCK 599
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEFFGLR--KRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958656977  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 1.54e-27

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: 106.56  E-value: 1.54e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977   10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAKK 89
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                   .
gi 1958656977   90 D 90
Cdd:cd08320     81 E 81
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 739-1023 4.04e-26

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: 112.58  E-value: 4.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  739 NQSLTELDLSDNTLGDPGMRVLCEALQHpGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALGDFGVRLLc 818
Cdd:COG5238    179 NNSVETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIAL- 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  819 vgLKHLLCN--LQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQcNLQKLGLVNSGLT 896
Cdd:COG5238    257 --AEALKNNttVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIG 333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  897 SLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEgllhpdcklqmleldncsltshscwdlstILTHNQSLRKLNLS 976
Cdd:COG5238    334 AQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAK-----------------------------YLEGNTTLRELNLG 384

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958656977  977 NNDLGDLCVVTLCEVLkqQGCLLQSLQLGEMYLNCETKRTLEALQEE 1023
Cdd:COG5238    385 KNNIGKQGAEALIDAL--QTNRLHTLILDGNLIGAEAQQRLEQLLER 429
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 10-85 4.53e-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: 99.59  E-value: 4.53e-25
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958656977   10 LAQYLEDLEDVDLKKFKMHLEDYPPEKGCvPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWE 85
Cdd:pfam02758    2 LLWYLEELSEEEFKKFKSLLEDEPEEGLR-SIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
199-529 2.05e-23

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 107.20  E-value: 2.05e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  199 SSLKLELLFEPEDEHLepvhtvVFQGAAGIGKTILARKIMLDWALGKLFKDkfDYL-FFIHCREvsLRAPKSLADLI--- 274
Cdd:COG5635    168 ESLKRLELLEAKKKRL------LILGEPGSGKTTLLRYLALELAERYLDAE--DPIpILIELRD--LAEEASLEDLLaea 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  275 ISCWPDPNPPVCKILCKPSRILFLMDGFDELqgAFDEHIEEVCTDwqkavrgdilLSSLIRKklLPKASLLITTRPVALE 354
Cdd:COG5635    238 LEKRGGEPEDALERLLRNGRLLLLLDGLDEV--PDEADRDEVLNQ----------LRRFLER--YPKARVIITSRPEGYD 303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  355 klQHLLDHPRHVEILGFSEAKRKEYFFKYF-SNELQAREAFRLIQENEILFTMCFIPLVCWIVCTGLKQQMETGKSLAQt 433
Cdd:COG5635    304 --SSELEGFEVLELAPLSDEQIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGELPDTRAE- 380

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  434 sktttaVYVFFLSSLLQSRGGIEEHLFSAYLPG------LCSLAADGIWNQKILFEECDLRKHGLQ----KTDVSAFL-- 501
Cdd:COG5635    381 ------LYEQFVELLLERWDEQRGLTIYRELSReelrelLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLde 454

                          330       340       350
                   ....*....|....*....|....*....|.
gi 1958656977  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 1.13e-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: 102.18  E-value: 1.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  731 GLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHpGCNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNALG 810
Cdd:COG5238    227 ILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIG 305

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  811 DFGVRLLCVGLKHlLCNLQKLWLVSCCLTSACCQDLALVLSSNHSLTRLYIGENALGDSGVQVLCEKMKDPQcNLQKLGL 890
Cdd:COG5238    306 DEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNL 383

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958656977  891 VNSGLTSLCCSALTSVLKTNQnLTHLYLRSNALGDMGLKLLCEGLLH 937
Cdd:COG5238    384 GKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGAEAQQRLEQLLER 429
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 7-86 8.72e-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: 90.28  E-value: 8.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977    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 2.53e-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: 74.19  E-value: 2.53e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958656977  138 YRRHVRSRFYSIKDRNARLGESVDLNRRYTQLQLVKEHPSKQEREHELLTIGRT-KMWDRPMSSLKLELLFE 208
Cdd:pfam14484    1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAsKKPESEETPIRCEDIFK 72
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
731-1034 8.47e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 74.58  E-value: 8.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  731 GLFSSLSTNQSLTELDLSDNtlgdpgmrvlcEALQHPGcNIQRLWLGRCGLThqccfNISSVLSSSQKLVELDLSDNALG 810
Cdd:COG4886     87 LGLTDLGDLTNLTELDLSGN-----------EELSNLT-NLESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQLT 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  811 DFGVRLlcVGLKhllcNLQKLWLVSCCLTsaccqDLALVLSSNHSLTRLYIGENALGDSGVQVlcEKMKdpqcNLQKLGL 890
Cdd:COG4886    150 DLPEPL--GNLT----NLKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQITDLPEPL--GNLT----NLEELDL 212

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  891 VNSGLTSLccsalTSVLKTNQNLTHLYLRSNALGDM----GLKllcegllhpdcKLQMLELDNCSLTshscwDLSTiLTH 966
Cdd:COG4886    213 SGNQLTDL-----PEPLANLTNLETLDLSNNQLTDLpelgNLT-----------NLEELDLSNNQLT-----DLPP-LAN 270

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958656977  967 NQSLRKLNLSNNDLGDLCVVTLCEVLKQQGCLLQSLQLGEMYLNCETKRTLEALQEEKPELTVVFEIS 1034
Cdd:COG4886    271 LTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLT 338
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 466-518 6.52e-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: 64.12  E-value: 6.52e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958656977  466 GLCSLAADGIWNQKILFEECDLRKHGLQKTDVSAFLRMNVFQKEVDCERFYSF 518
Cdd:pfam17779    5 KLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 730-890 1.20e-12

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 71.36  E-value: 1.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  730 RGLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGcNIQRLWLGRCGLTHQCCFNISSVLSSSQKLVELDLSDNAL 809
Cdd:COG5238    282 IALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQI 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  810 GDFGVRLLCVGLKhllcnlqklwlvsccltsaccqdlalvlsSNHSLTRLYIGENALGDSGVQVLCEKMKDPQcnLQKLG 889
Cdd:COG5238    361 GDEGAIALAKYLE-----------------------------GNTTLRELNLGKNNIGKQGAEALIDALQTNR--LHTLI 409


                   .
gi 1958656977  890 L 890
Cdd:COG5238    410 L 410
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
787-983 4.80e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 66.11  E-value: 4.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  787 FNISSVLSSSQKLVELDLSDNAlgdfgvrllcvGLKHLLcNLQKLWLVSCCLTsaccqDLALVLSSNHSLTRLYIGENAL 866
Cdd:COG4886     86 LLGLTDLGDLTNLTELDLSGNE-----------ELSNLT-NLESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQL 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  867 GDSGVQVlcEKMKdpqcNLQKLGLVNSGLTSLccsalTSVLKTNQNLTHLYLRSNALGDMGLKLlcEGLlhpdCKLQMLE 946
Cdd:COG4886    149 TDLPEPL--GNLT----NLKSLDLSNNQLTDL-----PEELGNLTNLKELDLSNNQITDLPEPL--GNL----TNLEELD 211

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1958656977  947 LDNCSLTshscwDLSTILTHNQSLRKLNLSNNDLGDL 983
Cdd:COG4886    212 LSGNQLT-----DLPEPLANLTNLETLDLSNNQLTDL 243
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
732-1004 1.20e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.95  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  732 LFSSLSTNQSLTELDLSDNTLGDpgmrvLCEALqhPGC-NIQRLWLGRCGLThqccfNISSVLSSSQKLVELDLSDNALG 810
Cdd:COG4886    128 LPEELANLTNLKELDLSNNQLTD-----LPEPL--GNLtNLKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQIT 195

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  811 DFGVRLLCvglkhlLCNLQKLWLVSCCLTsaccqDLALVLSSNHSLTRLYIGENALGD-------SGVQVL--------- 874
Cdd:COG4886    196 DLPEPLGN------LTNLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTDlpelgnlTNLEELdlsnnqltd 264

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  875 ---CEKMKdpqcNLQKLGLVNSGLTSLCCSALTSVLKTNQNLTHLYLRSNALGDMGLKLLCEGLLHPDCKLQMLELDNCS 951
Cdd:COG4886    265 lppLANLT----NLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTL 340

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958656977  952 LTSHSCWDLSTILTHNQSLRKLNLSNNDLGDLCVVTLCEVLKQQGCLLQSLQL 1004
Cdd:COG4886    341 ALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLL 393
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 910-1024 5.93e-08

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: 56.34  E-value: 5.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  910 NQNLTHLYLRSNALGDMGLKLLCEGLLHPDcKLQMLELDNCSLTSHSCWDLSTILTHNQSLRKLNLSNNDLGDLCVVTLC 989
Cdd:COG5238    179 NNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALA 257

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1958656977  990 EVLkQQGCLLQSLQLGEMYLNCETKRTL-EALQEEK 1024
Cdd:COG5238    258 EAL-KNNTTVETLYLSGNQIGAEGAIALaKALQGNT 292
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
739-766 6.86e-07

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 46.25  E-value: 6.86e-07
                            10        20
                    ....*....|....*....|....*...
gi 1958656977   739 NQSLTELDLSDNTLGDPGMRVLCEALQH 766
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 729-824 3.68e-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: 3.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958656977  729 CRGLFSSLSTNQSLTELDLSDNTLGDPGMRVLCEALQHPGcNIQRLWLGRCGLTHQccfNISSVLSSSQ--KLVELDLSD 806
Cdd:COG5238    337 AIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLGKNNIGKQ---GAEALIDALQtnRLHTLILDG 412

                           90
                   ....*....|....*...
gi 1958656977  807 NALGDFGVRLLCVGLKHL 824
Cdd:COG5238    413 NLIGAEAQQRLEQLLERI 430
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 10-88 1.17e-05

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


Pssm-ID: 260019  Cd Length: 73  Bit Score: 44.22  E-value: 1.17e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958656977   10 LAQYLEDLEDVDLKKFKMHLEDYppekgcVPIPRGQMEKADHLDLATLMIDFNGEEKAWGMAVWIFAAINRRDLWEKAK 88
Cdd:cd08305      1 LLTGLENITDEEFKMFKSLLASE------LKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
796-823 1.24e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.08  E-value: 1.24e-04
                            10        20
                    ....*....|....*....|....*...
gi 1958656977   796 SQKLVELDLSDNALGDFGVRLLCVGLKH 823
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
967-994 1.90e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 39.31  E-value: 1.90e-04
                            10        20
                    ....*....|....*....|....*...
gi 1958656977   967 NQSLRKLNLSNNDLGDLCVVTLCEVLKQ 994
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_6 pfam13516
Leucine Rich repeat;
738-761 5.82e-04

Leucine Rich repeat;


Pssm-ID: 463907 [Multi-domain]  Cd Length: 24  Bit Score: 37.99  E-value: 5.82e-04
                           10        20
                   ....*....|....*....|....
gi 1958656977  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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH