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Conserved domains on  [gi|1039779040|ref|XP_017177801|]
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NACHT, LRR and PYD domains-containing protein 9C isoform X1 [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 ...
 693-961 6.48e-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: 130.17  E-value: 6.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  693 PQLKYLNL--YGTDLSNDVVEMLCSALKcSTCRVEELLLGKCDISSEACGIMATFLINSKVKHLSLVENPLKNKGVMFLC 770
Cdd:cd00116     51 PSLKELCLslNETGRIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  771 KMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNKHLSLLDLGSNFLEDIGVNLLCEALKYpNCTLKELWLPGCYLTSE 850
Cdd:cd00116    130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  851 CCEEISAVLTCNKNLKTLKLGNNNIQDTGVKRLCEALCHPKCKVQCLGLDMCELSNDCCEDLALALITCNTLKSLNLDWN 930
Cdd:cd00116    209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1039779040  931 ALHHSGLVMLCEALNHKKCKLNMLGLDKSSF 961
Cdd:cd00116    289 KFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-304 2.36e-27

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: 109.32  E-value: 2.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  144 TAVVLGTRGKGKTVFLRKAMLDWASGVLLQNrFQYVFFFSVFSLN-NTTELSLAELISSKLPE----CSETLDDILSNPK 218
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEpaapVSEVWAVILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  219 RILFVLDGFDYLKFDLELRTNLCndwrkrlPTQNVLSSLLQKIMLPECSLLLELGESSCSKIIPLLQNPREIIMSGLSEQ 298
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153


                   ....*...
gi 1039779040  299 SI--YFYC 304
Cdd:pfam05729  154 DRkqYVRK 161
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-91 6.05e-26

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: 102.32  E-value: 6.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040    9 LLQYFQKLSDEEFQRFKELLQKEQEKFKLKPLSWTKIKNTSKEDLVTQLYTHYP-RQVWDMVLNLFLQVNRKDLSTMAQI 87
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPeQQAWDVALSIFEKMNRTDLCEKARA 80


                   ....
gi 1039779040   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 7.63e-18

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: 80.41  E-value: 7.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  441 HSTLQWYFATLFYFLKQDKDTYHPVI--------GSLPQLLGEIYAHKQNQWTHAQTFFFGIATKHVITLLKPCFGNISF 512
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039779040  513 KTIRQEIIRYLKSLSQPECNEklVHPKKLFFCLIENQEERFVSQ 556
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELSS--ERFLNLFHCLYELQDESFVKE 122
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 388-431 6.40e-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: 44.48  E-value: 6.40e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1039779040  388 LKTLCTLAVEGMWKQVYVFDSEDLRRNKISESDKTVWLKMKFLQ 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 ...
 693-961 6.48e-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: 130.17  E-value: 6.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  693 PQLKYLNL--YGTDLSNDVVEMLCSALKcSTCRVEELLLGKCDISSEACGIMATFLINSKVKHLSLVENPLKNKGVMFLC 770
Cdd:cd00116     51 PSLKELCLslNETGRIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  771 KMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNKHLSLLDLGSNFLEDIGVNLLCEALKYpNCTLKELWLPGCYLTSE 850
Cdd:cd00116    130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  851 CCEEISAVLTCNKNLKTLKLGNNNIQDTGVKRLCEALCHPKCKVQCLGLDMCELSNDCCEDLALALITCNTLKSLNLDWN 930
Cdd:cd00116    209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1039779040  931 ALHHSGLVMLCEALNHKKCKLNMLGLDKSSF 961
Cdd:cd00116    289 KFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-304 2.36e-27

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: 109.32  E-value: 2.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  144 TAVVLGTRGKGKTVFLRKAMLDWASGVLLQNrFQYVFFFSVFSLN-NTTELSLAELISSKLPE----CSETLDDILSNPK 218
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEpaapVSEVWAVILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  219 RILFVLDGFDYLKFDLELRTNLCndwrkrlPTQNVLSSLLQKIMLPECSLLLELGESSCSKIIPLLQNPREIIMSGLSEQ 298
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153


                   ....*...
gi 1039779040  299 SI--YFYC 304
Cdd:pfam05729  154 DRkqYVRK 161
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-91 6.05e-26

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: 102.32  E-value: 6.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040    9 LLQYFQKLSDEEFQRFKELLQKEQEKFKLKPLSWTKIKNTSKEDLVTQLYTHYP-RQVWDMVLNLFLQVNRKDLSTMAQI 87
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPeQQAWDVALSIFEKMNRTDLCEKARA 80


                   ....
gi 1039779040   88 ERRD 91
Cdd:cd08320     81 EMNE 84
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 689-948 2.97e-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: 101.02  E-value: 2.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  689 FLQIPQLKYLNLYGTDLSNDVVEMLCSALKCSTcRVEELLLGKCDISSEACGIMATFLI-NSKVKHLSLVENPLKNKGVM 767
Cdd:COG5238    176 ALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKgNKSLTTLDLSNNQIGDEGVI 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  768 FLCKMLKDPSCVlESLMLSyccLTFIACGH---LYEALLSNKHLSLLDLGSNFLEDIGVNLLCEALKYpNCTLKELWLPG 844
Cdd:COG5238    255 ALAEALKNNTTV-ETLYLS---GNQIGAEGaiaLAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAY 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  845 CYLTSECCEEISAVLTCNKNLKTLKLGNNNIQDTGVKRLCEALchpKCKVQCLGLDMC--ELSNDCCEDLALALITcNTL 922
Cdd:COG5238    330 NGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL---EGNTTLRELNLGknNIGKQGAEALIDALQT-NRL 405

                          250       260
                   ....*....|....*....|....*.
gi 1039779040  923 KSLNLDWNALHHSGLVMLCEALNHKK 948
Cdd:COG5238    406 HTLILDGNLIGAEAQQRLEQLLERIK 431
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 441-556 7.63e-18

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: 80.41  E-value: 7.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  441 HSTLQWYFATLFYFLKQDKDTYHPVI--------GSLPQLLGEIYAHKQNQWTHAQTFFFGIATKHVITLLKPCFGNISF 512
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039779040  513 KTIRQEIIRYLKSLSQPECNEklVHPKKLFFCLIENQEERFVSQ 556
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELSS--ERFLNLFHCLYELQDESFVKE 122
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-82 1.73e-17

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: 77.63  E-value: 1.73e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779040    8 GLLQYFQKLSDEEFQRFKELLQKEQEkFKLKPLSWTKIKNTSKEDLVTQLYTHYP-RQVWDMVLNLFLQVNRKDLS 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 6.40e-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: 44.48  E-value: 6.40e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1039779040  388 LKTLCTLAVEGMWKQVYVFDSEDLRRNKISESDKTVWLKMKFLQ 431
Cdd:pfam17779    3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQ 46
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
862-887 5.70e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.08  E-value: 5.70e-03
                            10        20
                    ....*....|....*....|....*.
gi 1039779040   862 NKNLKTLKLGNNNIQDTGVKRLCEAL 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 ...
 693-961 6.48e-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: 130.17  E-value: 6.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  693 PQLKYLNL--YGTDLSNDVVEMLCSALKcSTCRVEELLLGKCDISSEACGIMATFLINSKVKHLSLVENPLKNKGVMFLC 770
Cdd:cd00116     51 PSLKELCLslNETGRIPRGLQSLLQGLT-KGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLA 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  771 KMLKDPSCVLESLMLSYCCLTFIACGHLYEALLSNKHLSLLDLGSNFLEDIGVNLLCEALKYpNCTLKELWLPGCYLTSE 850
Cdd:cd00116    130 KGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVLDLNNNGLTDE 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  851 CCEEISAVLTCNKNLKTLKLGNNNIQDTGVKRLCEALCHPKCKVQCLGLDMCELSNDCCEDLALALITCNTLKSLNLDWN 930
Cdd:cd00116    209 GASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLELDLRGN 288

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1039779040  931 ALHHSGLVMLCEALNHKKCKLNMLGLDKSSF 961
Cdd:cd00116    289 KFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 144-304 2.36e-27

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: 109.32  E-value: 2.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  144 TAVVLGTRGKGKTVFLRKAMLDWASGVLLQNrFQYVFFFSVFSLN-NTTELSLAELISSKLPE----CSETLDDILSNPK 218
Cdd:pfam05729    2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSrSGNARSLADLLFSQWPEpaapVSEVWAVILELPE 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  219 RILFVLDGFDYLKFDLELRTNLCndwrkrlPTQNVLSSLLQKIMLPECSLLLELGESSCSKIIPLLQNPREIIMSGLSEQ 298
Cdd:pfam05729   81 RLLLILDGLDELVSDLGQLDGPC-------PVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153


                   ....*...
gi 1039779040  299 SI--YFYC 304
Cdd:pfam05729  154 DRkqYVRK 161
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 778-986 8.36e-27

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 112.06  E-value: 8.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  778 CVLESLMLSYCCLTFIACgHLYEALLSNKHLSLLDLGSNFLEDIGVNLLCEALKYPNCTLKELWLPGCYLTSECCEEISA 857
Cdd:cd00116     81 CGLQELDLSDNALGPDGC-GVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAK 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  858 VLTCNKNLKTLKLGNNNIQDTGVKRLCEALCHPK---------------------------CKVQCLGLDMCELSNDCCE 910
Cdd:cd00116    160 ALRANRDLKELNLANNGIGDAGIRALAEGLKANCnlevldlnnngltdegasalaetlaslKSLEVLNLGDNNLTDAGAA 239

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  911 DLALALITCN-TLKSLNLDWNALHHSGLVMLCEALNHKKCKLNmLGLDKSSFSEESQTFLQAVEKKNNN----LNVLHFP 985
Cdd:cd00116    240 ALASALLSPNiSLLTLSLSCNDITDDGAKDLAEVLAEKESLLE-LDLRGNKFGEEGAQLLAESLLEPGNelesLWVKDDS 318


                   .
gi 1039779040  986 W 986
Cdd:cd00116    319 F 319
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 9-91 6.05e-26

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: 102.32  E-value: 6.05e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040    9 LLQYFQKLSDEEFQRFKELLQKEQEKFKLKPLSWTKIKNTSKEDLVTQLYTHYP-RQVWDMVLNLFLQVNRKDLSTMAQI 87
Cdd:cd08320      1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPeQQAWDVALSIFEKMNRTDLCEKARA 80


                   ....
gi 1039779040   88 ERRD 91
Cdd:cd08320     81 EMNE 84
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 780-984 9.88e-26

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: 108.98  E-value: 9.88e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  780 LESLMLSYCCLTFIACGHLYEALLSNKHLSLLDLGSNFLEDIGVNLLCEALKYPNCT-LKELWLPGCYLTSECCEEISAV 858
Cdd:cd00116     25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGRIPRGLQSLLQGLTKGCgLQELDLSDNALGPDGCGVLESL 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  859 LTcNKNLKTLKLGNNNIQDTGVKRLCEALCHPKCKVQCLGLDMCELSNDCCEDLALALITCNTLKSLNLDWNALHHSGLV 938
Cdd:cd00116    105 LR-SSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIR 183

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1039779040  939 MLCEALNHkKCKLNMLGLDKSSFSEESQTFLQAVEKKNNNLNVLHF 984
Cdd:cd00116    184 ALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNL 228
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 689-904 1.07e-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: 105.90  E-value: 1.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  689 FLQIPQLKYLNLYGTDLSNDVVEMLCSALKCSTCRVEELLLGKCDISSEACGIMATFLI-NSKVKHLSLVENPLKNKGVM 767
Cdd:cd00116    104 LLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRaNRDLKELNLANNGIGDAGIR 183

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  768 FLCKMLKDpSCVLESLMLSYCCLTFIACGHLYEALLSNKHLSLLDLGSNFLEDIGVNLLCEALKYPNCTLKELWLPGCYL 847
Cdd:cd00116    184 ALAEGLKA-NCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDI 262

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039779040  848 TSECCEEISAVLTCNKNLKTLKLGNNNIQDTGVKRLCEALCHPKCKVQCLGLDMCEL 904
Cdd:cd00116    263 TDDGAKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 689-948 2.97e-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: 101.02  E-value: 2.97e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  689 FLQIPQLKYLNLYGTDLSNDVVEMLCSALKCSTcRVEELLLGKCDISSEACGIMATFLI-NSKVKHLSLVENPLKNKGVM 767
Cdd:COG5238    176 ALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKgNKSLTTLDLSNNQIGDEGVI 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  768 FLCKMLKDPSCVlESLMLSyccLTFIACGH---LYEALLSNKHLSLLDLGSNFLEDIGVNLLCEALKYpNCTLKELWLPG 844
Cdd:COG5238    255 ALAEALKNNTTV-ETLYLS---GNQIGAEGaiaLAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAY 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  845 CYLTSECCEEISAVLTCNKNLKTLKLGNNNIQDTGVKRLCEALchpKCKVQCLGLDMC--ELSNDCCEDLALALITcNTL 922
Cdd:COG5238    330 NGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL---EGNTTLRELNLGknNIGKQGAEALIDALQT-NRL 405

                          250       260
                   ....*....|....*....|....*.
gi 1039779040  923 KSLNLDWNALHHSGLVMLCEALNHKK 948
Cdd:COG5238    406 HTLILDGNLIGAEAQQRLEQLLERIK 431
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 796-983 9.16e-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: 9.16e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  796 GHLYEALLSNKHLSLLDLGSNFLEDIGVNLLCEALKYPNcTLKELWLPGCYLTSECCEEISAVLTCNKNLKTLKLGNNNI 875
Cdd:COG5238    170 AISMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  876 QDTGVKRLCEALCHPKcKVQCLGLDMCELSNDCCEDLALALITCNTLKSLNLDWNALHHSGLVMLCEALNHKKcKLNMLG 955
Cdd:COG5238    249 GDEGVIALAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLN 326

                          170       180
                   ....*....|....*....|....*...
gi 1039779040  956 LDKSSFSEESQTFLQAVEKKNNNLNVLH 983
Cdd:COG5238    327 LAYNGIGAQGAIALAKALQENTTLHSLD 354
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 441-556 7.63e-18

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: 80.41  E-value: 7.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  441 HSTLQWYFATLFYFLKQDKDTYHPVI--------GSLPQLLGEIYAHKQNQWTHAQTFFFGIATKHVITLLKPCFGNISF 512
Cdd:pfam17776    1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039779040  513 KTIRQEIIRYLKSLSQPECNEklVHPKKLFFCLIENQEERFVSQ 556
Cdd:pfam17776   81 SEIKQELLQWIKSLIQKELSS--ERFLNLFHCLYELQDESFVKE 122
PYRIN pfam02758
PAAD/DAPIN/Pyrin domain; This domain is predicted to contain 6 alpha helices and to have the ...
 8-82 1.73e-17

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: 77.63  E-value: 1.73e-17
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779040    8 GLLQYFQKLSDEEFQRFKELLQKEQEkFKLKPLSWTKIKNTSKEDLVTQLYTHYP-RQVWDMVLNLFLQVNRKDLS 82
Cdd:pfam02758    1 ILLWYLEELSEEEFKKFKSLLEDEPE-EGLRSIPRGKLEKADRLDLADLLVEHYGeDAAVDVTIEILKKINLKDLA 75
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
14-449 2.29e-13

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 74.46  E-value: 2.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040   14 QKLSDEEFQRFKELLQKEQEKFKLKPLSWTKIKNTSKEDLVTQLYTHYPRQVWDmvLNLFLQVNRKDLSTMAQIERRDKQ 93
Cdd:COG5635     59 LALVSRSALSAAALLARALSALLLVLLLLESLLLLLLLLLLLAEALLALLELAA--LLKAVLLSLSGGSDLVLLLSESDL 136

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040   94 NKYKEFMKNLFQYIWTSETNTYMPDrsyNTIIDRQYKALLDIFDSESDPAtaVVLGTRGKGKTVFLRKAMLDWASGVLLQ 173
Cdd:COG5635    137 LLALLILLLDADGLLVSLDDLYVPL---NLLERIESLKRLELLEAKKKRL--LILGEPGSGKTTLLRYLALELAERYLDA 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  174 NRfQYVFFfsvFSLNN-TTELSLAELISSKL----PECSETLDDILSNpKRILFVLDGFDYLkFDLELRTNLCNDwrkrl 248
Cdd:COG5635    212 ED-PIPIL---IELRDlAEEASLEDLLAEALekrgGEPEDALERLLRN-GRLLLLLDGLDEV-PDEADRDEVLNQ----- 280

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  249 ptqnvLSSLLQKimLPECSLLLelgesSC---SKIIPLLQNPREIIMSGLSEQSIYFYCVSFFKI--QLGVEVFKDLKKN 323
Cdd:COG5635    281 -----LRRFLER--YPKARVII-----TSrpeGYDSSELEGFEVLELAPLSDEQIEEFLKKWFEAteRKAERLLEALEEN 348

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  324 EPLFTLCSNPSMLWMICSSLMWGHY---SREEVISssestSAIHTIF-IMSAFKSIFGLGSSKYKRfKLKTLCTLAVEgM 399
Cdd:COG5635    349 PELRELARNPLLLTLLALLLRERGElpdTRAELYE-----QFVELLLeRWDEQRGLTIYRELSREE-LRELLSELALA-M 421

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779040  400 WKQ-VYVFDSEDLRRN----KISESDKTVWLKMK-----FLQIQGNNIM-FYHSTLQWYFA 449
Cdd:COG5635    422 QENgRTEFAREELEEIlreyLGRRKDAEALLDELllrtgLLVERGEGRYsFAHRSFQEYLA 482
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 810-983 2.16e-11

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: 67.12  E-value: 2.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  810 LLDLGSNFLEDIGVNLLCEALKypNCTLKELWLPGCYLTSECCEEISAVLTCNKNLKTLKLGNNNIQDTGVKRLCEALCH 889
Cdd:COG5238    157 HLLGLAARLGLLAAISMAKALQ--NNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKG 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  890 PKcKVQCLGLDMCELSNDCCEDLALALITCNTLKSLNLDWNALHHSGLVMLCEALNHKKcKLNMLGLDKSSFSEESQTFL 969
Cdd:COG5238    235 NK-SLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNT-TLTSLDLSVNRIGDEGAIAL 312

                          170
                   ....*....|....
gi 1039779040  970 QAVEKKNNNLNVLH 983
Cdd:COG5238    313 AEGLQGNKTLHTLN 326
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 837-985 4.13e-07

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: 53.13  E-value: 4.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  837 LKELWLPGCYLTSECCEEISAVLTCNKNLKTLKLGNNNIQ--DTGVKRLCEALcHPKCKVQCLGLDMCELSNDCCEDLAl 914
Cdd:cd00116     25 LQVLRLEGNTLGEEAAKALASALRPQPSLKELCLSLNETGriPRGLQSLLQGL-TKGCGLQELDLSDNALGPDGCGVLE- 102

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039779040  915 ALITCNTLKSLNLDWNALHHSGLVMLCEALNHKKCKLNMLGLDKSSFSEESQTFLQAVEKKNNNLNVLHFP 985
Cdd:cd00116    103 SLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLA 173
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 388-431 6.40e-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: 44.48  E-value: 6.40e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1039779040  388 LKTLCTLAVEGMWKQVYVFDSEDLRRNKISESDKTVWLKMKFLQ 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 7.45e-04

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: 39.43  E-value: 7.45e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039779040    9 LLQYFQKLSDEEFQRFK-ELLQKEQEKFklKPLSWTKIKNTSKEDLVTQLYTHY-PRQVWDMVLNLFLQVNRKDLS 82
Cdd:cd08321      4 LLDALEDLGEEELKKFKwKLRDIPLEGY--PRIPRGKLENADRVDLVDLLVSYYgEDYAVEVTVEVLRAINQNDLA 77
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
800-932 7.88e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 7.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  800 EALLSNKHLSLLDLGSNFLEDIGVNLlcEALKypncTLKELWLPGCYLTSecceeISAVLTCNKNLKTLKLGNNNIQDtg 879
Cdd:COG4886    107 EELSNLTNLESLDLSGNQLTDLPEEL--ANLT----NLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLSNNQLTD-- 173

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039779040  880 vkrLCEALCHPKcKVQCLGLDMCELSndcceDLALALITCNTLKSLNLDWNAL 932
Cdd:COG4886    174 ---LPEELGNLT-NLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQL 217
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
780-877 8.02e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 8.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  780 LESLMLSYCCLTfiacgHLYEALLSNKHLSLLDLGSNFLEDIGVNLLcealkypNCT-LKELWLPGCYLTsecceEISAV 858
Cdd:COG4886    138 LKELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQLTDLPEELG-------NLTnLKELDLSNNQIT-----DLPEP 200

                           90
                   ....*....|....*....
gi 1039779040  859 LTCNKNLKTLKLGNNNIQD 877
Cdd:COG4886    201 LGNLTNLEELDLSGNQLTD 219
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 631-783 2.63e-03

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: 41.19  E-value: 2.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039779040  631 FCNLHVLDLGSCHFNKKvievlcnslsptpnmpltvfklqrllcsfmtnfGDGSLFCTFLQIPQLKYLNLYGTDLSNDVV 710
Cdd:cd00116    192 NCNLEVLDLNNNGLTDE---------------------------------GASALAETLASLKSLEVLNLGDNNLTDAGA 238

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039779040  711 EMLCSALKCSTCRVEELLLGKCDISSEACGIMATFLINSK-VKHLSLVENPLKNKGVMFLCKMLKDPSCVLESL 783
Cdd:cd00116    239 AALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKEsLLELDLRGNKFGEEGAQLLAESLLEPGNELESL 312
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
862-887 5.70e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 35.08  E-value: 5.70e-03
                            10        20
                    ....*....|....*....|....*.
gi 1039779040   862 NKNLKTLKLGNNNIQDTGVKRLCEAL 887
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEAL 26
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
805-831 9.40e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 34.69  E-value: 9.40e-03
                            10        20
                    ....*....|....*....|....*..
gi 1039779040   805 NKHLSLLDLGSNFLEDIGVNLLCEALK 831
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEALK 27
 
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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