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Conserved domains on  [gi|115299743|ref|NP_001041684|]
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NACHT, LRR and PYD domains-containing protein 9A isoform 1 [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 ...
 693-957 1.11e-33

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


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 132.48  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  693 PHLKYMNLYGTNL--SNDAVERLCSALKfSTCGVEELLLGKCDISSEACGIIAASLINSEVKHLSLVENPLKNKGVMSLC 770
Cdd:cd00116    51 PSLKELCLSLNETgrIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  771 EMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCYLTSE 850
Cdd:cd00116   130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  851 CCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWN 930
Cdd:cd00116   209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                         250       260
                  ....*....|....*....|....*..
gi 115299743  931 AFDHSGLEMLCKALNHKACNLEVLGLD 957
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 2.51e-29

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


:

Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 114.71  E-value: 2.51e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   144 TVVVSGSRGGGKTTFLRKAMLDWASRNLLQNrFQYVFYFSVFSLNNIT-ELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   219 RILFILDGFDYLKFDLELRTNLCndwrkklPIQIVLSSLLQKIMLPECSLLLELGNASLSNIIPLLQYPREIIMSGFSEQ 298
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153


                   ....*
gi 115299743   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 6.38e-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: 6.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743    9 LLQYLQKLSDEEFQRFKEHLRKEPEKFKLKPISWTKIKNTSKEDLVMQLYTHYPG-KAWDMVLSLFLQVNREDLSTMAQT 87
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEqQAWDVALSIFEKMNRTDLCEKARA 80


                  ....
gi 115299743   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 1.25e-25

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: 102.76  E-value: 1.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   441 HSTLQWYFAVLFYFLQYKDTRHPVIGN---------LAQLLGEIYAHKQNQWFHTRILLFGMATEQVNSLLEPCFGCISS 511
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEffglrkresLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 115299743   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 2.26e-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: 45.63  E-value: 2.26e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 115299743   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 ...
 693-957 1.11e-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: 132.48  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  693 PHLKYMNLYGTNL--SNDAVERLCSALKfSTCGVEELLLGKCDISSEACGIIAASLINSEVKHLSLVENPLKNKGVMSLC 770
Cdd:cd00116    51 PSLKELCLSLNETgrIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  771 EMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCYLTSE 850
Cdd:cd00116   130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  851 CCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWN 930
Cdd:cd00116   209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                         250       260
                  ....*....|....*....|....*..
gi 115299743  931 AFDHSGLEMLCKALNHKACNLEVLGLD 957
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 2.51e-29

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


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 114.71  E-value: 2.51e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   144 TVVVSGSRGGGKTTFLRKAMLDWASRNLLQNrFQYVFYFSVFSLNNIT-ELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   219 RILFILDGFDYLKFDLELRTNLCndwrkklPIQIVLSSLLQKIMLPECSLLLELGNASLSNIIPLLQYPREIIMSGFSEQ 298
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153


                   ....*
gi 115299743   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 6.38e-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: 6.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743    9 LLQYLQKLSDEEFQRFKEHLRKEPEKFKLKPISWTKIKNTSKEDLVMQLYTHYPG-KAWDMVLSLFLQVNREDLSTMAQT 87
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEqQAWDVALSIFEKMNRTDLCEKARA 80


                  ....
gi 115299743   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 1.25e-25

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: 102.76  E-value: 1.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   441 HSTLQWYFAVLFYFLQYKDTRHPVIGN---------LAQLLGEIYAHKQNQWFHTRILLFGMATEQVNSLLEPCFGCISS 511
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEffglrkresLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 115299743   512 KEVRQEIIRYIKSLSQQECNeklVVHPQNLFFCILDNQEERFVRQ 556
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELS---SERFLNLFHCLYELQDESFVKE 122
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 689-944 3.90e-22

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 100.63  E-value: 3.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  689 FLHLPHLKYMNLYGTNLSNDAVERLCSALKFSTcGVEELLLGKCDISSEACGIIAASLI-NSEVKHLSLVENPLKNKGVM 767
Cdd:COG5238   176 ALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKgNKSLTTLDLSNNQIGDEGVI 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  768 SLCEMLKDPSCVlESLMLSyccLTFIACGH---LYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPG 844
Cdd:COG5238   255 ALAEALKNNTTV-ETLYLS---GNQIGAEGaiaLAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAY 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  845 CYLTSECCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALchpNCEMQCLGLDMCD--FTSDCCEDLALVLTTcNTL 922
Cdd:COG5238   330 NGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL---EGNTTLRELNLGKnnIGKQGAEALIDALQT-NRL 405

                         250       260
                  ....*....|....*....|....*
gi 115299743  923 KSLNLDWN---AFDHSGLEMLCKAL 944
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 4.14e-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: 79.56  E-value: 4.14e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115299743     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 2.26e-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: 45.63  E-value: 2.26e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 115299743   388 IRTLCTLAVEGMWKQVYVFDSDDLRRNGISESDKKVWLRMKFLQ 431
Cdd:pfam17779    3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQ 46
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
862-887 7.35e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.08  E-value: 7.35e-03
                            10        20
                    ....*....|....*....|....*.
gi 115299743    862 NTNLKTLKLGNNNIQDTGVKRLCEAL 887
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 ...
 693-957 1.11e-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: 132.48  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  693 PHLKYMNLYGTNL--SNDAVERLCSALKfSTCGVEELLLGKCDISSEACGIIAASLINSEVKHLSLVENPLKNKGVMSLC 770
Cdd:cd00116    51 PSLKELCLSLNETgrIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  771 EMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCYLTSE 850
Cdd:cd00116   130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  851 CCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWN 930
Cdd:cd00116   209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                         250       260
                  ....*....|....*....|....*..
gi 115299743  931 AFDHSGLEMLCKALNHKACNLEVLGLD 957
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 2.51e-29

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


Pssm-ID: 428606 [Multi-domain]  Cd Length: 166  Bit Score: 114.71  E-value: 2.51e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   144 TVVVSGSRGGGKTTFLRKAMLDWASRNLLQNrFQYVFYFSVFSLNNIT-ELSLAELISSTLPESSETVDD----ILSDPK 218
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGnARSLADLLFSQWPEPAAPVSEvwavILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   219 RILFILDGFDYLKFDLELRTNLCndwrkklPIQIVLSSLLQKIMLPECSLLLELGNASLSNIIPLLQYPREIIMSGFSEQ 298
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153


                   ....*
gi 115299743   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 6.38e-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: 6.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743    9 LLQYLQKLSDEEFQRFKEHLRKEPEKFKLKPISWTKIKNTSKEDLVMQLYTHYPG-KAWDMVLSLFLQVNREDLSTMAQT 87
Cdd:cd08320     1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEqQAWDVALSIFEKMNRTDLCEKARA 80


                  ....
gi 115299743   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 1.25e-25

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: 102.76  E-value: 1.25e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   441 HSTLQWYFAVLFYFLQYKDTRHPVIGN---------LAQLLGEIYAHKQNQWFHTRILLFGMATEQVNSLLEPCFGCISS 511
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKEffglrkresLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 115299743   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 ...
 617-904 2.56e-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: 104.74  E-value: 2.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  617 QKLLAKHWTTLCTFLCNLHVLDLDSCHFNEKAIEVLCNCL---PLTSLVPLTGFK-------LHRLLCSFTTN------- 679
Cdd:cd00116     8 ELLKTERATELLPKLLCLQVLRLEGNTLGEEAAKALASALrpqPSLKELCLSLNEtgriprgLQSLLQGLTKGcglqeld 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  680 -----FGDGL--LFCTFLHLPHLKYMNLYGTNLSNDAVERLCSALKFSTCGVEELLLGKCDISSEACGIIAASLI-NSEV 751
Cdd:cd00116    88 lsdnaLGPDGcgVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRaNRDL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  752 KHLSLVENPLKNKGVMSLCEMLKDpSCVLESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALK 831
Cdd:cd00116   168 KELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALL 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 115299743  832 DPNCTLKELWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDF 904
Cdd:cd00116   247 SPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 780-984 2.20e-23

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: 102.05  E-value: 2.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  780 LESLMLSYCCLTFIACGHLYEALLSNEHLSLLDLGSNFLE--DTGVNLLCEALKDpNCTLKELWLPGCYLTSECCEEISA 857
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGLTK-GCGLQELDLSDNALGPDGCGVLES 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  858 VLTcNTNLKTLKLGNNNIQDTGVKRLCEALCHPNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWNAFDHSGL 937
Cdd:cd00116   104 LLR-SSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGI 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 115299743  938 EMLCKALNHKaCNLEVLGLDKSLFSEESQTLLQAVEKKNKNLKVLHF 984
Cdd:cd00116   183 RALAEGLKAN-CNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNL 228
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 689-944 3.90e-22

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 100.63  E-value: 3.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  689 FLHLPHLKYMNLYGTNLSNDAVERLCSALKFSTcGVEELLLGKCDISSEACGIIAASLI-NSEVKHLSLVENPLKNKGVM 767
Cdd:COG5238   176 ALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKgNKSLTTLDLSNNQIGDEGVI 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  768 SLCEMLKDPSCVlESLMLSyccLTFIACGH---LYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPG 844
Cdd:COG5238   255 ALAEALKNNTTV-ETLYLS---GNQIGAEGaiaLAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAY 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  845 CYLTSECCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALchpNCEMQCLGLDMCD--FTSDCCEDLALVLTTcNTL 922
Cdd:COG5238   330 NGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL---EGNTTLRELNLGKnnIGKQGAEALIDALQT-NRL 405

                         250       260
                  ....*....|....*....|....*
gi 115299743  923 KSLNLDWN---AFDHSGLEMLCKAL 944
Cdd:COG5238   406 HTLILDGNligAEAQQRLEQLLERI 430
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 717-945 8.29e-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: 90.23  E-value: 8.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  717 LKFSTCGVEELLLG-KCDISSEACGIIAASLINSEVKHLSLVENPLKNKGVMSLCEMLKDPSCVlESLMLSYCCLTFIAC 795
Cdd:COG5238   147 LKDPLGGNAVHLLGlAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTV-TTLWLKRNPIGDEGA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  796 GHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDpNCTLKELWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNI 875
Cdd:COG5238   226 EILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRI 304

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  876 QDTGVKRLCEALCHpNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWNAFDHSGLEMLCKALN 945
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 4.14e-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: 79.56  E-value: 4.14e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115299743     8 GLLQYLQKLSDEEFQRFKEHLRKEPEkFKLKPISWTKIKNTSKEDLVMQLYTHYPGK-AWDMVLSLFLQVNREDLS 82
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLEDEPE-EGLRSIPRGKLEKADRLDLADLLVEHYGEDaAVDVTIEILKKINLKDLA 75
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 796-983 8.71e-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: 84.07  E-value: 8.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  796 GHLYEALLSNEHLSLLDLGSNFLEDTGVNLLCEALKDPNcTLKELWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNI 875
Cdd:COG5238   170 AISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  876 QDTGVKRLCEALCHpNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWNAFDHSGLEMLCKALNHKAcNLEVLG 955
Cdd:COG5238   249 GDEGVIALAEALKN-NTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLN 326

                         170       180
                  ....*....|....*....|....*...
gi 115299743  956 LDKSLFSEESQTLLQAVEKKNKNLKVLH 983
Cdd:COG5238   327 LAYNGIGAQGAIALAKALQENTTLHSLD 354
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
76-496 1.98e-15

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 81.39  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743   76 VNREDLSTMAQTERRDKQTKYKEFMKNTFQHIWTMETNTYIPDRsyhefIEVQYRALQDIFDCESEPVTVVVSGSRGGGK 155
Cdd:COG5635   119 LSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLN-----LLERIESLKRLELLEAKKKRLLILGEPGSGK 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  156 TTFLRKAMLDWASRNLLQNRfQYVFYFSvfsLNNI-TELSLAELISSTL----PESSETVDDILSDpKRILFILDGFDYL 230
Cdd:COG5635   194 TTLLRYLALELAERYLDAED-PIPILIE---LRDLaEEASLEDLLAEALekrgGEPEDALERLLRN-GRLLLLLDGLDEV 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  231 kFDLELRTNLCN---DWRKKLP-IQIVLSSLLQkimlpecslllELGNASLSNIipllqypREIIMSGFSEQTIEIYCVS 306
Cdd:COG5635   269 -PDEADRDEVLNqlrRFLERYPkARVIITSRPE-----------GYDSSELEGF-------EVLELAPLSDEQIEEFLKK 329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  307 FF--NTQTGVEIFKNLKSIKPLFNLCRCPHLCWMICSTIKWQyerrevaSRFGRTLGLLYTIFMVSAF-------KSTYA 377
Cdd:COG5635   330 WFeaTERKAERLLEALEENPELRELARNPLLLTLLALLLRER-------GELPDTRAELYEQFVELLLerwdeqrGLTIY 402

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  378 RNPSKQNRARIrtLCTLAVEgMWKQ-VYVFDSDDLRRN----GISESDKKVWL-----RMKFLQNQGSNIV-FYHSTLQW 446
Cdd:COG5635   403 RELSREELREL--LSELALA-MQENgRTEFAREELEEIlreyLGRRKDAEALLdelllRTGLLVERGEGRYsFAHRSFQE 479

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 115299743  447 YFAVLFYFlqykdtRHPVIGNLAQLLGEIyahKQNQWFHTRILLFGMATE 496
Cdd:COG5635   480 YLAARALV------EELDEELLELLAEHL---EDPRWREVLLLLAGLLDD 520
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 810-983 2.51e-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: 70.20  E-value: 2.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  810 LLDLGSNFLEDTGVNLLCEALKDPNCTLkeLWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNIQDTGVKRLCEALCH 889
Cdd:COG5238   157 HLLGLAARLGLLAAISMAKALQNNSVET--VYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKG 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  890 pNCEMQCLGLDMCDFTSDCCEDLALVLTTCNTLKSLNLDWNAFDHSGLEMLCKALNhKACNLEVLGLDKSLFSEESQTLL 969
Cdd:COG5238   235 -NKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQ-GNTTLTSLDLSVNRIGDEGAIAL 312

                         170
                  ....*....|....
gi 115299743  970 QAVEKKNKNLKVLH 983
Cdd:COG5238   313 AEGLQGNKTLHTLN 326
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 837-985 1.95e-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: 56.98  E-value: 1.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  837 LKELWLPGCYLTSECCEEISAVLTCNTNLKTLKLGNNNIQ--DTGVKRLCEALcHPNCEMQCLGLDMCDFTSDCCEDLAL 914
Cdd:cd00116    25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGL-TKGCGLQELDLSDNALGPDGCGVLES 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115299743  915 VLTTcNTLKSLNLDWNAFDHSGLEMLCKALNHKACNLEVLGLDKSLFSEESQTLLQAVEKKNKNLKVLHFP 985
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 2.26e-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: 45.63  E-value: 2.26e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 115299743   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 3.35e-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: 3.35e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 115299743    9 LLQYLQKLSDEEFQRFKEHLRKEPEKFKlKPISWTKIKNTSKEDLVMQLYTHY-PGKAWDMVLSLFLQVNREDLS 82
Cdd:cd08321     4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYgEDYAVEVTVEVLRAINQNDLA 77
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
780-932 7.35e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 7.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  780 LESLMLSYCCLTfiacgHLYEALLSNEHLSLLDLGSNFLEDtgvnlLCEALKdpNCT-LKELWLPGCYLTSecceeISAV 858
Cdd:COG4886   115 LESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQLTD-----LPEPLG--NLTnLKSLDLSNNQLTD-----LPEE 177

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115299743  859 LTCNTNLKTLKLGNNNIQDtgvkrLCEALCHPNcEMQCLGLDMCDFTsdcceDLALVLTTCNTLKSLNLDWNAF 932
Cdd:COG4886   178 LGNLTNLKELDLSNNQITD-----LPEPLGNLT-NLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQL 240
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
691-883 6.48e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.30  E-value: 6.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  691 HLPHLKYMNLYGTNLSNdaverLCSALKFSTcGVEELLLGKCDISSeacgiIAASLIN-SEVKHLSLVENPLKNKGvMSL 769
Cdd:COG4886   134 NLTNLKELDLSNNQLTD-----LPEPLGNLT-NLKSLDLSNNQLTD-----LPEELGNlTNLKELDLSNNQITDLP-EPL 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115299743  770 CEMLKdpscvLESLMLSYCCLTfiacgHLYEALLSNEHLSLLDLGSNFLEDtgvnlLCEALKDPNctLKELWLPGCYLTS 849
Cdd:COG4886   202 GNLTN-----LEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQLTD-----LPELGNLTN--LEELDLSNNQLTD 264

                         170       180       190
                  ....*....|....*....|....*....|....
gi 115299743  850 ecceeISAvLTCNTNLKTLKLGNNNIQDTGVKRL 883
Cdd:COG4886   265 -----LPP-LANLTNLKTLDLSNNQLTDLKLKEL 292
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
862-887 7.35e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.08  E-value: 7.35e-03
                            10        20
                    ....*....|....*....|....*.
gi 115299743    862 NTNLKTLKLGNNNIQDTGVKRLCEAL 887
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEAL 26
 
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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