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Conserved domains on  [gi|115299752|ref|NP_001041685|]
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NACHT, LRR and PYD domains-containing protein 9A isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 638-902 3.44e-34

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: 133.63  E-value: 3.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 638 PHLKYMNLYGTNL--SNDAVERLCSALKfSTCGVEELLLGKCDISSEACGIIAASLINSEVKHLSLVENPLKNKGVMSLC 715
Cdd:cd00116   51 PSLKELCLSLNETgrIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 716 EMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCYLTSE 795
Cdd:cd00116  130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 796 CCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWN 875
Cdd:cd00116  209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                        250       260
                 ....*....|....*....|....*..
gi 115299752 876 AFDHSGLEMLCKALNHKACNLEVLGLD 902
Cdd:cd00116  289 KFGEEGAQLLAESLLEPGNELESLWVK 315
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-303 1.22e-29

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


:

Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 115.48  E-value: 1.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  144 TVVVSGSRGGGKTTFLRKAMLDWASRNLLQNrFQYVFYFSVFSLNNIT-ELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  219 RILFILDGFDYLKFDLELRTNLCndwrkklPIQIVLSSLLQKIMLPECSLLLELGNASLSNIIPLLQYPREIIMSGFSEQ 298
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153


                  ....*
gi 115299752  299 TIEIY 303
Cdd:pfam05729 154 DRKQY 158
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-91 5.01e-29

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: 110.79  E-value: 5.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752   9 LLQYLQKLSDEEFQRFKEHLRKEPEKFKLKPISWTKIKNTSKEDLVMQLYTHYPG-KAWDMVLSLFLQVNREDLSTMAQT 87
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEqQAWDVALSIFEKMNRTDLCEKARA 80


                 ....
gi 115299752  88 ERRD 91
Cdd:cd08320   81 EMNE 84
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 441-556 6.41e-26

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: 103.53  E-value: 6.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  441 HSTLQWYFAVLFYFLQYKDTRHPVIGN---------LAQLLGEIYAHKQNQWFHTRILLFGMATEQVNSLLEPCFGCISS 511
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEffglrkresLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 115299752  512 KEVRQEIIRYIKSLSQQECNeklVVHPQNLFFCILDNQEERFVRQ 556
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELS---SERFLNLFHCLYELQDESFVKE 122
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 388-431 1.77e-06

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: 46.02  E-value: 1.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 115299752  388 IRTLCTLAVEGMWKQVYVFDSDDLRRNGISESDKKVWLRMKFLQ 431
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQ 46
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 638-902 3.44e-34

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: 133.63  E-value: 3.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 638 PHLKYMNLYGTNL--SNDAVERLCSALKfSTCGVEELLLGKCDISSEACGIIAASLINSEVKHLSLVENPLKNKGVMSLC 715
Cdd:cd00116   51 PSLKELCLSLNETgrIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 716 EMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCYLTSE 795
Cdd:cd00116  130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 796 CCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWN 875
Cdd:cd00116  209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                        250       260
                 ....*....|....*....|....*..
gi 115299752 876 AFDHSGLEMLCKALNHKACNLEVLGLD 902
Cdd:cd00116  289 KFGEEGAQLLAESLLEPGNELESLWVK 315
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-303 1.22e-29

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


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 115.48  E-value: 1.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  144 TVVVSGSRGGGKTTFLRKAMLDWASRNLLQNrFQYVFYFSVFSLNNIT-ELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  219 RILFILDGFDYLKFDLELRTNLCndwrkklPIQIVLSSLLQKIMLPECSLLLELGNASLSNIIPLLQYPREIIMSGFSEQ 298
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153


                  ....*
gi 115299752  299 TIEIY 303
Cdd:pfam05729 154 DRKQY 158
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-91 5.01e-29

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: 110.79  E-value: 5.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752   9 LLQYLQKLSDEEFQRFKEHLRKEPEKFKLKPISWTKIKNTSKEDLVMQLYTHYPG-KAWDMVLSLFLQVNREDLSTMAQT 87
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEqQAWDVALSIFEKMNRTDLCEKARA 80


                 ....
gi 115299752  88 ERRD 91
Cdd:cd08320   81 EMNE 84
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 441-556 6.41e-26

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: 103.53  E-value: 6.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  441 HSTLQWYFAVLFYFLQYKDTRHPVIGN---------LAQLLGEIYAHKQNQWFHTRILLFGMATEQVNSLLEPCFGCISS 511
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEffglrkresLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 115299752  512 KEVRQEIIRYIKSLSQQECNeklVVHPQNLFFCILDNQEERFVRQ 556
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELS---SERFLNLFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 634-889 2.10e-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: 101.41  E-value: 2.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 634 FLHLPHLKYMNLYGTNLSNDAVERLCSALKFSTcGVEELLLGKCDISSEACGIIAASLI-NSEVKHLSLVENPLKNKGVM 712
Cdd:COG5238  176 ALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKgNKSLTTLDLSNNQIGDEGVI 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 713 SLCEMLKDPSCVlESLMLSyccLTFIACGH---LYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPG 789
Cdd:COG5238  255 ALAEALKNNTTV-ETLYLS---GNQIGAEGaiaLAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAY 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 790 CYLTSECCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALchpNCEMQCLGLDMCD--FTSDCCEDLALVLTTcNTL 867
Cdd:COG5238  330 NGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL---EGNTTLRELNLGKnnIGKQGAEALIDALQT-NRL 405

                        250       260
                 ....*....|....*....|....*
gi 115299752 868 KSLNLDWN---AFDHSGLEMLCKAL 889
Cdd:COG5238  406 HTLILDGNligAEAQQRLEQLLERI 430
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-82 3.16e-18

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: 79.94  E-value: 3.16e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115299752    8 GLLQYLQKLSDEEFQRFKEHLRKEPEkFKLKPISWTKIKNTSKEDLVMQLYTHYPGK-AWDMVLSLFLQVNREDLS 82
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEPE-EGLRSIPRGKLEKADRLDLADLLVEHYGEDaAVDVTIEILKKINLKDLA 75
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 388-431 1.77e-06

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: 46.02  E-value: 1.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 115299752  388 IRTLCTLAVEGMWKQVYVFDSDDLRRNGISESDKKVWLRMKFLQ 431
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQ 46
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
807-832 5.23e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.08  E-value: 5.23e-03
                           10        20
                   ....*....|....*....|....*.
gi 115299752   807 NTNLKTLKLGNNNIQDTGVKRLCEAL 832
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEAL 26
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 638-902 3.44e-34

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: 133.63  E-value: 3.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 638 PHLKYMNLYGTNL--SNDAVERLCSALKfSTCGVEELLLGKCDISSEACGIIAASLINSEVKHLSLVENPLKNKGVMSLC 715
Cdd:cd00116   51 PSLKELCLSLNETgrIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 716 EMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCYLTSE 795
Cdd:cd00116  130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 796 CCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWN 875
Cdd:cd00116  209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                        250       260
                 ....*....|....*....|....*..
gi 115299752 876 AFDHSGLEMLCKALNHKACNLEVLGLD 902
Cdd:cd00116  289 KFGEEGAQLLAESLLEPGNELESLWVK 315
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-303 1.22e-29

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


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 115.48  E-value: 1.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  144 TVVVSGSRGGGKTTFLRKAMLDWASRNLLQNrFQYVFYFSVFSLNNIT-ELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  219 RILFILDGFDYLKFDLELRTNLCndwrkklPIQIVLSSLLQKIMLPECSLLLELGNASLSNIIPLLQYPREIIMSGFSEQ 298
Cdd:pfam05729  81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153


                  ....*
gi 115299752  299 TIEIY 303
Cdd:pfam05729 154 DRKQY 158
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-91 5.01e-29

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: 110.79  E-value: 5.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752   9 LLQYLQKLSDEEFQRFKEHLRKEPEKFKLKPISWTKIKNTSKEDLVMQLYTHYPG-KAWDMVLSLFLQVNREDLSTMAQT 87
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEqQAWDVALSIFEKMNRTDLCEKARA 80


                 ....
gi 115299752  88 ERRD 91
Cdd:cd08320   81 EMNE 84
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 441-556 6.41e-26

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: 103.53  E-value: 6.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  441 HSTLQWYFAVLFYFLQYKDTRHPVIGN---------LAQLLGEIYAHKQNQWFHTRILLFGMATEQVNSLLEPCFGCISS 511
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKEffglrkresLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 115299752  512 KEVRQEIIRYIKSLSQQECNeklVVHPQNLFFCILDNQEERFVRQ 556
Cdd:pfam17776  81 SEIKQELLQWIKSLIQKELS---SERFLNLFHCLYELQDESFVKE 122
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 612-849 6.51e-24

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: 103.59  E-value: 6.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 612 LFKLDqkcSFTTNFGDGL--LFCTFLHLPHLKYMNLYGTNLSNDAVERLCSALKFSTCGVEELLLGKCDISSEACGIIAA 689
Cdd:cd00116   83 LQELD---LSDNALGPDGcgVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAK 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 690 SLI-NSEVKHLSLVENPLKNKGVMSLCEMLKDpSCVLESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLEDTGV 768
Cdd:cd00116  160 ALRaNRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGA 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 769 NLLCEALKDPNCTLKELWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCD 848
Cdd:cd00116  239 AALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDS 318


                 .
gi 115299752 849 F 849
Cdd:cd00116  319 F 319
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 725-929 8.55e-24

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: 103.20  E-value: 8.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 725 LESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLE--DTGVNLLCEALKDpNCTLKELWLPGCYLTSECCEEISA 802
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVLES 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 803 VLTcNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWNAFDHSGL 882
Cdd:cd00116  104 LLR-SSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 115299752 883 EMLCKALNHKaCNLEVLGLDKSLFSEESQTLLQAVEKKNKNLKVLHF 929
Cdd:cd00116  183 RALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNL 228
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 634-889 2.10e-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: 101.41  E-value: 2.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 634 FLHLPHLKYMNLYGTNLSNDAVERLCSALKFSTcGVEELLLGKCDISSEACGIIAASLI-NSEVKHLSLVENPLKNKGVM 712
Cdd:COG5238  176 ALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKgNKSLTTLDLSNNQIGDEGVI 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 713 SLCEMLKDPSCVlESLMLSyccLTFIACGH---LYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPG 789
Cdd:COG5238  255 ALAEALKNNTTV-ETLYLS---GNQIGAEGaiaLAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAY 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 790 CYLTSECCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALchpNCEMQCLGLDMCD--FTSDCCEDLALVLTTcNTL 867
Cdd:COG5238  330 NGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL---EGNTTLRELNLGKnnIGKQGAEALIDALQT-NRL 405

                        250       260
                 ....*....|....*....|....*
gi 115299752 868 KSLNLDWN---AFDHSGLEMLCKAL 889
Cdd:COG5238  406 HTLILDGNligAEAQQRLEQLLERI 430
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 662-890 5.19e-19

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: 91.00  E-value: 5.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 662 LKFSTCGVEELLLG-KCDISSEACGIIAASLINSEVKHLSLVENPLKNKGVMSLCEMLKDPSCVlESLMLSYCCLTFIAC 740
Cdd:COG5238  147 LKDPLGGNAVHLLGlAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTV-TTLWLKRNPIGDEGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 741 GHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNI 820
Cdd:COG5238  226 EILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRI 304

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 821 QDTGVKRLCEALCHpNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWNAFDHSGLEMLCKALN 890
Cdd:COG5238  305 GDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLE 373
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-82 3.16e-18

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: 79.94  E-value: 3.16e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115299752    8 GLLQYLQKLSDEEFQRFKEHLRKEPEkFKLKPISWTKIKNTSKEDLVMQLYTHYPGK-AWDMVLSLFLQVNREDLS 82
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEPE-EGLRSIPRGKLEKADRLDLADLLVEHYGEDaAVDVTIEILKKINLKDLA 75
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 741-928 5.93e-17

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 84.46  E-value: 5.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 741 GHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDPNcTLKELWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNI 820
Cdd:COG5238  170 AISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 821 QDTGVKRLCEALCHpNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWNAFDHSGLEMLCKALNHKAcNLEVLG 900
Cdd:COG5238  249 GDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLN 326

                        170       180
                 ....*....|....*....|....*...
gi 115299752 901 LDKSLFSEESQTLLQAVEKKNKNLKVLH 928
Cdd:COG5238  327 LAYNGIGAQGAIALAKALQENTTLHSLD 354
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
76-496 9.18e-16

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 82.16  E-value: 9.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752  76 VNREDLSTMAQTERRDKQTKYKEFMKNTFQHIWTMETNTYIPDRsyhefIEVQYRALQDIFDCESEPVTVVVSGSRGGGK 155
Cdd:COG5635  119 LSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLN-----LLERIESLKRLELLEAKKKRLLILGEPGSGK 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 156 TTFLRKAMLDWASRNLLQNRfQYVFYFSvfsLNNI-TELSLAELISSTL----PESSETVDDILSDpKRILFILDGFDYL 230
Cdd:COG5635  194 TTLLRYLALELAERYLDAED-PIPILIE---LRDLaEEASLEDLLAEALekrgGEPEDALERLLRN-GRLLLLLDGLDEV 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 231 kFDLELRTNLCN---DWRKKLP-IQIVLSSLLQkimlpecslllELGNASLSNIipllqypREIIMSGFSEQTIEIYCVS 306
Cdd:COG5635  269 -PDEADRDEVLNqlrRFLERYPkARVIITSRPE-----------GYDSSELEGF-------EVLELAPLSDEQIEEFLKK 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 307 FF--NTQTGVEIFKNLKSIKPLFNLCRCPHLCWMICSTIKWQyerrevaSRFGRTLGLLYTIFMVSAF-------KSTYA 377
Cdd:COG5635  330 WFeaTERKAERLLEALEENPELRELARNPLLLTLLALLLRER-------GELPDTRAELYEQFVELLLerwdeqrGLTIY 402

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 378 RNPSKQNRARIrtLCTLAVEgMWKQ-VYVFDSDDLRRN----GISESDKKVWL-----RMKFLQNQGSNIV-FYHSTLQW 446
Cdd:COG5635  403 RELSREELREL--LSELALA-MQENgRTEFAREELEEIlreyLGRRKDAEALLdelllRTGLLVERGEGRYsFAHRSFQE 479

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 115299752 447 YFAVLFYFlqykdtRHPVIGNLAQLLGEIyahKQNQWFHTRILLFGMATE 496
Cdd:COG5635  480 YLAARALV------EELDEELLELLAEHL---EDPRWREVLLLLAGLLDD 520
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 755-928 1.79e-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: 70.59  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 755 LLDLGSNFLEDTGVNLLCEALKDPNCTLkeLWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCH 834
Cdd:COG5238  157 HLLGLAARLGLLAAISMAKALQNNSVET--VYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKG 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 835 pNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWNAFDHSGLEMLCKALNhKACNLEVLGLDKSLFSEESQTLL 914
Cdd:COG5238  235 -NKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ-GNTTLTSLDLSVNRIGDEGAIAL 312

                        170
                 ....*....|....
gi 115299752 915 QAVEKKNKNLKVLH 928
Cdd:COG5238  313 AEGLQGNKTLHTLN 326
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 782-930 1.07e-08

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: 57.75  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 782 LKELWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNIQ--DTGVKRLCEALcHPNCEMQCLGLDMCDFTSDCCEDLAL 859
Cdd:cd00116   25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGL-TKGCGLQELDLSDNALGPDGCGVLES 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115299752 860 VLTTcNTLKSLNLDWNAFDHSGLEMLCKALNHKACNLEVLGLDKSLFSEESQTLLQAVEKKNKNLKVLHFP 930
Cdd:cd00116  104 LLRS-SSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLA 173
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 388-431 1.77e-06

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: 46.02  E-value: 1.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 115299752  388 IRTLCTLAVEGMWKQVYVFDSDDLRRNGISESDKKVWLRMKFLQ 431
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQ 46
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 9-82 3.22e-06

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: 45.98  E-value: 3.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115299752   9 LLQYLQKLSDEEFQRFKEHLRKEPEKFKlKPISWTKIKNTSKEDLVMQLYTHY-PGKAWDMVLSLFLQVNREDLS 82
Cdd:cd08321    4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYgEDYAVEVTVEVLRAINQNDLA 77
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
725-877 3.57e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 3.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 725 LESLMLSYCCLTfiacgHLYEALLSNEHLSLLDLGSNFLEDtgvnlLCEALKdpNCT-LKELWLPGCYLTSecceeISAV 803
Cdd:COG4886  115 LESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQLTD-----LPEPLG--NLTnLKSLDLSNNQLTD-----LPEE 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115299752 804 LTCNTNLKTLKLGNNNIQDtgvkrLCEALCHPNcEMQCLGLDMCDFTsdcceDLALVLTTCNTLKSLNLDWNAF 877
Cdd:COG4886  178 LGNLTNLKELDLSNNQITD-----LPEPLGNLT-NLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQL 240
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 611-728 7.59e-04

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: 42.73  E-value: 7.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 611 ELFKLDQKCSFTTNFGDGLLFCTFLHLPHLKYMNLYGTNLSNDAVERLCSALKFSTCGVEELLLGKCDISSEACGIIAAS 690
Cdd:cd00116  194 NLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEV 273

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 115299752 691 LINSE-VKHLSLVENPLKNKGVMSLCEMLKDPSCVLESL 728
Cdd:cd00116  274 LAEKEsLLELDLRGNKFGEEGAQLLAESLLEPGNELESL 312
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
636-828 2.94e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.07  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 636 HLPHLKYMNLYGTNLSNdaverLCSALKFSTcGVEELLLGKCDISSeacgiIAASLIN-SEVKHLSLVENPLKNKGvMSL 714
Cdd:COG4886  134 NLTNLKELDLSNNQLTD-----LPEPLGNLT-NLKSLDLSNNQLTD-----LPEELGNlTNLKELDLSNNQITDLP-EPL 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 715 CEMLKdpscvLESLMLSYCCLTfiacgHLYEALLSNEHLSLLDLGSNFLEDtgvnlLCEALKDPNctLKELWLPGCYLTS 794
Cdd:COG4886  202 GNLTN-----LEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTD-----LPELGNLTN--LEELDLSNNQLTD 264

                        170       180       190
                 ....*....|....*....|....*....|....
gi 115299752 795 ecceeISAvLTCNTNLKTLKLGNNNIQDTGVKRL 828
Cdd:COG4886  265 -----LPP-LANLTNLKTLDLSNNQLTDLKLKEL 292
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
807-832 5.23e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.08  E-value: 5.23e-03
                           10        20
                   ....*....|....*....|....*.
gi 115299752   807 NTNLKTLKLGNNNIQDTGVKRLCEAL 832
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEAL 26
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
745-875 7.59e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.92  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299752 745 EALLSNEHLSLLDLGSNFLEDTGVNLlcEALKDpnctLKELWLPGCYLTSecceeISAVLTCNTNLKTLKLGNNNIQDtg 824
Cdd:COG4886  107 EELSNLTNLESLDLSGNQLTDLPEEL--ANLTN----LKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD-- 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 115299752 825 vkrLCEALCH-PNceMQCLGLDMCDFTsdcceDLALVLTTCNTLKSLNLDWN 875
Cdd:COG4886  174 ---LPEELGNlTN--LKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGN 215
 
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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