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Conserved domains on  [gi|768012005|ref|XP_011525784|]
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NACHT, LRR and PYD domains-containing protein 12 isoform X6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 212-381 2.04e-61

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: 206.00  E-value: 2.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  212 TVVMQGAAGIGKSMLAHKVMLDWADGKLFQGrFDYLFYINCREMNQSATECSMQDLIFSCWPEPSAPLQE----LIRVPE 287
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  288 RLLFIIDGFDELKPSFHDPQGPWclcweekrPTELLLNSLIRKKLLPELSLLITTRPTALEKLHRLLEHPRHVEILGFSE 367
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                         170
                  ....*....|....
gi 768012005  368 AERKEYFYKYFHNA 381
Cdd:pfam05729 153 SDRKQYVRKYFSDE 166
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 705-922 4.40e-38

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


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 145.19  E-value: 4.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 705 HLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHPNCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVG 784
Cdd:cd00116   99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 785 FPGMMLLCEGLRHpQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCRLRTLWL 864
Cdd:cd00116  179 DAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768012005 865 DSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHPGCKLRVLWLF 922
Cdd:cd00116  258 SCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 514-628 6.17e-35

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: 129.33  E-value: 6.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  514 HLSFQEFFAAMYYILDEGEG---------GAGPDQDVTRLLTEYAFSERSFLALTSRFLFGLLNEETRSHLEKSLCWKVS 584
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEksnplkeffGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 768012005  585 PHIKMDLLQWIQSKAQSDGStlQQGSLEFFSCLYEIQEEEFIQQ 628
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELS--SERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 13-92 4.04e-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: 108.10  E-value: 4.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  13 LSTYLEELEAVELKKFKLYLGTAT-ELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWERGQR 91
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESlEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 .
gi 768012005  92 E 92
Cdd:cd08320   81 E 81
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 459-512 1.28e-17

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: 77.61  E-value: 1.28e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768012005  459 RGLCSLAADGLWNQKILFEEQDLRKHGLDGEDVSAFLNMNIFQKDINCERYYSF 512
Cdd:pfam17779   4 LKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 129-200 1.42e-13

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: 66.48  E-value: 1.42e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768012005  129 YRDYVRRKFRLMEDRNARLGECVNLSHRYTRLLLVKEHSNPMQVQQQLLDTGRGHaRTVGHQASPIKIETLF 200
Cdd:pfam14484   1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAS-KKPESEETPIRCEDIF 71
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 212-381 2.04e-61

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: 206.00  E-value: 2.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  212 TVVMQGAAGIGKSMLAHKVMLDWADGKLFQGrFDYLFYINCREMNQSATECSMQDLIFSCWPEPSAPLQE----LIRVPE 287
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  288 RLLFIIDGFDELKPSFHDPQGPWclcweekrPTELLLNSLIRKKLLPELSLLITTRPTALEKLHRLLEHPRHVEILGFSE 367
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                         170
                  ....*....|....
gi 768012005  368 AERKEYFYKYFHNA 381
Cdd:pfam05729 153 SDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 705-922 4.40e-38

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 145.19  E-value: 4.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 705 HLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHPNCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVG 784
Cdd:cd00116   99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 785 FPGMMLLCEGLRHpQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCRLRTLWL 864
Cdd:cd00116  179 DAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768012005 865 DSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHPGCKLRVLWLF 922
Cdd:cd00116  258 SCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 514-628 6.17e-35

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: 129.33  E-value: 6.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  514 HLSFQEFFAAMYYILDEGEG---------GAGPDQDVTRLLTEYAFSERSFLALTSRFLFGLLNEETRSHLEKSLCWKVS 584
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEksnplkeffGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 768012005  585 PHIKMDLLQWIQSKAQSDGStlQQGSLEFFSCLYEIQEEEFIQQ 628
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELS--SERFLNLFHCLYELQDESFVKE 122
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 13-92 4.04e-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: 108.10  E-value: 4.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  13 LSTYLEELEAVELKKFKLYLGTAT-ELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWERGQR 91
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESlEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 .
gi 768012005  92 E 92
Cdd:cd08320   81 E 81
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 12-87 4.12e-27

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: 104.98  E-value: 4.12e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768012005   12 RLSTYLEELEAVELKKFKLYLGTATELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWE 87
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
213-569 1.36e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.50  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 213 VVMQGAAGIGKSMLAHKVMLDWADGKLFQGRFdYLFYINCREMnqsATECSMQDLI----FSCWPEPSAPLQELIRvPER 288
Cdd:COG5635  183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDL---AEEASLEDLLaealEKRGGEPEDALERLLR-NGR 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 289 LLFIIDGFDELKPSFHDPQgpwCLCWeekrptellLNSLIRKklLPELSLLITTRPTALEKlhRLLEHPRHVEILGFSEA 368
Cdd:COG5635  258 LLLLLDGLDEVPDEADRDE---VLNQ---------LRRFLER--YPKARVIITSRPEGYDS--SELEGFEVLELAPLSDE 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 369 ERKEYFYKYF-HNAEQAGQVFNYVRDNEPLFTMCFVPLVCWVVCTCLQQQlegggllRQTSRTTTAVYMLYLLSLMQ--- 444
Cdd:COG5635  322 QIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLALLLRER-------GELPDTRAELYEQFVELLLErwd 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 445 ---PKPGAPRLQPPPNQRGLCSLAADGLWNQKILFEEQDLRKHGLD----GEDVSAFLNMNIFQKDINCER---YYSFIH 514
Cdd:COG5635  395 eqrGLTIYRELSREELRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDELLLRTGLLVERgegRYSFAH 474

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768012005 515 LSFQEFFAAmYYILDEGEggAGPDQDVTRLLTEYAFSErsflalTSRFLFGLLNE 569
Cdd:COG5635  475 RSFQEYLAA-RALVEELD--EELLELLAEHLEDPRWRE------VLLLLAGLLDD 520
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 705-909 3.77e-21

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 97.55  E-value: 3.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 705 HLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHPNcKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVG 784
Cdd:COG5238  171 ISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIG 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 785 FPGMMLLCEGLRHPQcRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCrLRTLWL 864
Cdd:COG5238  250 DEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKT-LHTLNL 327

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 768012005 865 DSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRL 909
Cdd:COG5238  328 AYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL 372
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 459-512 1.28e-17

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: 77.61  E-value: 1.28e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768012005  459 RGLCSLAADGLWNQKILFEEQDLRKHGLDGEDVSAFLNMNIFQKDINCERYYSF 512
Cdd:pfam17779   4 LKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 129-200 1.42e-13

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: 66.48  E-value: 1.42e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768012005  129 YRDYVRRKFRLMEDRNARLGECVNLSHRYTRLLLVKEHSNPMQVQQQLLDTGRGHaRTVGHQASPIKIETLF 200
Cdd:pfam14484   1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAS-KKPESEETPIRCEDIF 71
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
827-854 5.51e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.16  E-value: 5.51e-04
                           10        20
                   ....*....|....*....|....*...
gi 768012005   827 NPHLVELDLTGNALEDLGLRLLCQGLRH 854
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 212-381 2.04e-61

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: 206.00  E-value: 2.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  212 TVVMQGAAGIGKSMLAHKVMLDWADGKLFQGrFDYLFYINCREMNQSATECSMQDLIFSCWPEPSAPLQE----LIRVPE 287
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  288 RLLFIIDGFDELKPSFHDPQGPWclcweekrPTELLLNSLIRKKLLPELSLLITTRPTALEKLHRLLEHPRHVEILGFSE 367
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC--------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSE 152

                         170
                  ....*....|....
gi 768012005  368 AERKEYFYKYFHNA 381
Cdd:pfam05729 153 SDRKQYVRKYFSDE 166
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 705-922 4.40e-38

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 145.19  E-value: 4.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 705 HLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHPNCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVG 784
Cdd:cd00116   99 GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 785 FPGMMLLCEGLRHpQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCRLRTLWL 864
Cdd:cd00116  179 DAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSL 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768012005 865 DSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHPGCKLRVLWLF 922
Cdd:cd00116  258 SCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVK 315
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 514-628 6.17e-35

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: 129.33  E-value: 6.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  514 HLSFQEFFAAMYYILDEGEG---------GAGPDQDVTRLLTEYAFSERSFLALTSRFLFGLLNEETRSHLEKSLCWKVS 584
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEksnplkeffGLRKRESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 768012005  585 PHIKMDLLQWIQSKAQSDGStlQQGSLEFFSCLYEIQEEEFIQQ 628
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELS--SERFLNLFHCLYELQDESFVKE 122
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 688-926 9.12e-33

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 129.78  E-value: 9.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 688 LVQLRPERTVLLDAYSEHLAAALCTNPNLIELSLYRNALGS--RGVKLLCQGLRHpNCKLQNLRLKRCRISSSACEDLSA 765
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRipRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVLES 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 766 ALiANKNLTRMDLSGNGVGFPGMMLLCEGLRHPQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGL 845
Cdd:cd00116  104 LL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 846 RLLCQGLRHpVCRLRTLWLDSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHPGCKLRVLWLFGMD 925
Cdd:cd00116  183 RALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCND 261


                 .
gi 768012005 926 L 926
Cdd:cd00116  262 I 262
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 13-92 4.04e-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: 108.10  E-value: 4.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005  13 LSTYLEELEAVELKKFKLYLGTAT-ELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWERGQR 91
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESlEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 .
gi 768012005  92 E 92
Cdd:cd08320   81 E 81
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 561-867 1.40e-27

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: 114.37  E-value: 1.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 561 RFLFGLLN-EETRSHLEKSLCWKVsPHIKMDLLQWIQSKAQSDGSTLQQGSLEFFSCLYEIQE-EEFIQQALSHFQVIVV 638
Cdd:cd00116    4 SLKGELLKtERATELLPKLLCLQV-LRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRiPRGLQSLLQGLTKGCG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 639 SniaSKMEHMVSSFC---------LKRCRSAQVLHLYGATYSADGEDRARCSAGAHTL-LVQLRPERTVLLDAYSEHLAA 708
Cdd:cd00116   83 L---QELDLSDNALGpdgcgvlesLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 709 ALCTNPNLIELSLYRNALGSRGVKLLCQGLRHpNCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVGFPGM 788
Cdd:cd00116  160 ALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGA 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768012005 789 MLLCEGLRHPQCRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCRLRTLWLDSC 867
Cdd:cd00116  239 AALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDD 317
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 12-87 4.12e-27

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: 104.98  E-value: 4.12e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768012005   12 RLSTYLEELEAVELKKFKLYLGTATELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWE 87
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEPEEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLAE 76
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
213-569 1.36e-22

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 104.50  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 213 VVMQGAAGIGKSMLAHKVMLDWADGKLFQGRFdYLFYINCREMnqsATECSMQDLI----FSCWPEPSAPLQELIRvPER 288
Cdd:COG5635  183 LLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILIELRDL---AEEASLEDLLaealEKRGGEPEDALERLLR-NGR 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 289 LLFIIDGFDELKPSFHDPQgpwCLCWeekrptellLNSLIRKklLPELSLLITTRPTALEKlhRLLEHPRHVEILGFSEA 368
Cdd:COG5635  258 LLLLLDGLDEVPDEADRDE---VLNQ---------LRRFLER--YPKARVIITSRPEGYDS--SELEGFEVLELAPLSDE 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 369 ERKEYFYKYF-HNAEQAGQVFNYVRDNEPLFTMCFVPLVCWVVCTCLQQQlegggllRQTSRTTTAVYMLYLLSLMQ--- 444
Cdd:COG5635  322 QIEEFLKKWFeATERKAERLLEALEENPELRELARNPLLLTLLALLLRER-------GELPDTRAELYEQFVELLLErwd 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 445 ---PKPGAPRLQPPPNQRGLCSLAADGLWNQKILFEEQDLRKHGLD----GEDVSAFLNMNIFQKDINCER---YYSFIH 514
Cdd:COG5635  395 eqrGLTIYRELSREELRELLSELALAMQENGRTEFAREELEEILREylgrRKDAEALLDELLLRTGLLVERgegRYSFAH 474

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768012005 515 LSFQEFFAAmYYILDEGEggAGPDQDVTRLLTEYAFSErsflalTSRFLFGLLNE 569
Cdd:COG5635  475 RSFQEYLAA-RALVEELD--EELLELLAEHLEDPRWRE------VLLLLAGLLDD 520
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 718-937 1.30e-21

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: 96.66  E-value: 1.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 718 ELSLYRNALGSRGVKLLCQGLRHpnckLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGN-------GVGFPGMML 790
Cdd:cd00116    2 QLSLKGELLKTERATELLPKLLC----LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNetgriprGLQSLLQGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 791 LceglrhPQCRLQMIQLRKCQLESGACQEMASVLgTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCRLRTLWLDSCGLT 870
Cdd:cd00116   78 T------KGCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLE 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768012005 871 AKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRLSHpGCKLRVLWLfgmDLNKMTHSRLAAL 937
Cdd:cd00116  151 GASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDL---NNNGLTDEGASAL 213
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 705-909 3.77e-21

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 97.55  E-value: 3.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 705 HLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHPNcKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVG 784
Cdd:COG5238  171 ISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIG 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 785 FPGMMLLCEGLRHPQcRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVCrLRTLWL 864
Cdd:COG5238  250 DEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKT-LHTLNL 327

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 768012005 865 DSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTGVRLLCKRL 909
Cdd:COG5238  328 AYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL 372
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 11-88 2.90e-19

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: 82.96  E-value: 2.90e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768012005  11 CRLSTYLEELEAVELKKFKLYLGTATELGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWER 88
Cdd:cd08321    2 DLLLDALEDLGEEELKKFKWKLRDIPLEGYPRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDLAEK 79
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 459-512 1.28e-17

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: 77.61  E-value: 1.28e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 768012005  459 RGLCSLAADGLWNQKILFEEQDLRKHGLDGEDVSAFLNMNIFQKDINCERYYSF 512
Cdd:pfam17779   4 LKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGCEKVYSF 57
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 703-909 5.83e-16

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: 81.37  E-value: 5.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 703 SEHLAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHpNCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNG 782
Cdd:COG5238  225 AEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNR 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 783 VGFPGMMLLCEGLRHPQcRLQMIQLRKCQLESGACQEMASVLGTNPHLVELDLTGNALEDLGLRLLCQGL-RHPvcRLRT 861
Cdd:COG5238  304 IGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLeGNT--TLRE 380

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768012005 862 LWLDSCGLTAKACENLYFTLGINQtLTDLYLTNNALGDTGVRLL---CKRL 909
Cdd:COG5238  381 LNLGKNNIGKQGAEALIDALQTNR-LHTLILDGNLIGAEAQQRLeqlLERI 430
FISNA pfam14484
Fish-specific NACHT associated domain; This domain is frequently found associated with the ...
 129-200 1.42e-13

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: 66.48  E-value: 1.42e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768012005  129 YRDYVRRKFRLMEDRNARLGECVNLSHRYTRLLLVKEHSNPMQVQQQLLDTGRGHaRTVGHQASPIKIETLF 200
Cdd:pfam14484   1 LKSNLKKKFQCIFEGNAKGGESTLLNEIYTELYITEGESGEVNEEHEVRQIEAAS-KKPESEETPIRCEDIF 71
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 742-911 1.26e-10

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: 64.81  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 742 NCKLQNLRLKRCRISSSACEDLSAALIANKNLTRMDLSGNGVGFPGMmllceglrhpqcrlqmiqlrkcqlesgacQEMA 821
Cdd:COG5238  179 NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGA-----------------------------EILA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 822 SVLGTNPHLVELDLTGNALEDLGLRLLCQGLRHPVcRLRTLWLDSCGLTAKACENLYFTLGINQTLTDLYLTNNALGDTG 901
Cdd:COG5238  230 EALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEG 308

                        170
                 ....*....|
gi 768012005 902 VRLLCKRLSH 911
Cdd:COG5238  309 AIALAEGLQG 318
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
704-905 5.71e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.01  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 704 EHLAAALCTNPNLIELSLYRNALGSRGVKLlcqglrhPNCK-LQNLRLKRCRISssaceDLSAALIANKNLTRMDLSGNG 782
Cdd:COG4886  126 TDLPEELANLTNLKELDLSNNQLTDLPEPL-------GNLTnLKSLDLSNNQLT-----DLPEELGNLTNLKELDLSNNQ 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 783 VGFPGMMLlcEGLRhpqcRLQMIQLRKCQLESgacqeMASVLGTNPHLVELDLTGNALEDL----GLRllcqglrhpvcR 858
Cdd:COG4886  194 ITDLPEPL--GNLT----NLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLTDLpelgNLT-----------N 251

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768012005 859 LRTLWLDSCGLTA-KACENLyftlginQTLTDLYLTNNALGDTGVRLL 905
Cdd:COG4886  252 LEELDLSNNQLTDlPPLANL-------TNLKTLDLSNNQLTDLKLKEL 292
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 809-937 2.11e-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: 51.33  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 809 KCQLESGACQEMASVLgTNPHLVELDLTGNALEDLGLRLLCQGLRHPVcRLRTLWLDSCGLTAKACENLYFTLGINQTLT 888
Cdd:COG5238  162 AARLGLLAAISMAKAL-QNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLT 239

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 768012005 889 DLYLTNNALGDTGVRLLCKRLSHpGCKLRVLWLFGmdlNKMTHSRLAAL 937
Cdd:COG5238  240 TLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSG---NQIGAEGAIAL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
704-898 3.45e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.70  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 704 EHLAAALCTNPNLIELSLYRNALGSRGVKLlcQGLRhpncKLQNLRLKRCRISssaceDLSAALIANKNLTRMDLSGNGV 783
Cdd:COG4886  149 TDLPEPLGNLTNLKSLDLSNNQLTDLPEEL--GNLT----NLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQL 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 784 G-FPGMMLLCEGLRHpqcrlqmIQLRKCQLESgacqemASVLGTNPHLVELDLTGNALEDLGLRLLCQglrhpvcRLRTL 862
Cdd:COG4886  218 TdLPEPLANLTNLET-------LDLSNNQLTD------LPELGNLTNLEELDLSNNQLTDLPPLANLT-------NLKTL 277

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 768012005 863 WLDSCGLTAKACENLYFTLGINQTLTDLYLTNNALG 898
Cdd:COG4886  278 DLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLEL 313
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 13-90 7.82e-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: 7.82e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768012005  13 LSTYLEELEAVELKKFKLYLgtateLGEGKIPWGSMEKAGPLEMAQLLITHFGPEEAWRLALSTFERINRKDLWERGQ 90
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLL-----ASELKLTRKMQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSLANQLQ 73
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 682-801 1.00e-05

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: 49.02  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 682 AGAHTLLVQLRPERTV-LLDAYSEH--------LAAALCTNPNLIELSLYRNALGSRGVKLLCQGLRHpNCKLQNLRLKR 752
Cdd:COG5238  251 EGVIALAEALKNNTTVeTLYLSGNQigaegaiaLAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAY 329

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768012005 753 CRISSSACEDLSAALIANKNLTRMD----------------------------LSGNGVGFPGMMLLCEGLRHPQCR 801
Cdd:COG5238  330 NGIGAQGAIALAKALQENTTLHSLDlsdnqigdegaialakylegnttlrelnLGKNNIGKQGAEALIDALQTNRLH 406
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
715-947 7.31e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.47  E-value: 7.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 715 NLIELSLYRNALGSRGVKLLCQGLRHPNCKLQNLRLKRC-RISSSACEDLSAAlianKNLTRMDLSGNGVGFPGMMLlcE 793
Cdd:COG4886   60 LLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLtELDLSGNEELSNL----TNLESLDLSGNQLTDLPEEL--A 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768012005 794 GLRHpqcrLQMIQLRKCQLESgacqeMASVLGTNPHLVELDLTGNALEDLGLRLlcQGLRHpvcrLRTLWLDSCGLTaka 873
Cdd:COG4886  134 NLTN----LKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTDLPEEL--GNLTN----LKELDLSNNQIT--- 195

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768012005 874 ceNLYFTLGINQTLTDLYLTNNALGDTGVRLlcKRLShpgcKLRVLWLFGmdlNKMTH----SRLAALRvtkpYLDIG 947
Cdd:COG4886  196 --DLPEPLGNLTNLEELDLSGNQLTDLPEPL--ANLT----NLETLDLSN---NQLTDlpelGNLTNLE----ELDLS 258
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
827-854 5.51e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 38.16  E-value: 5.51e-04
                           10        20
                   ....*....|....*....|....*...
gi 768012005   827 NPHLVELDLTGNALEDLGLRLLCQGLRH 854
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
770-797 2.01e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 36.23  E-value: 2.01e-03
                           10        20
                   ....*....|....*....|....*...
gi 768012005   770 NKNLTRMDLSGNGVGFPGMMLLCEGLRH 797
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
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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