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Conserved domains on  [gi|122135250|sp|Q288C4|]
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RecName: Full=NACHT, LRR and PYD domains-containing protein 9

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 ...
 682-954 2.28e-38

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


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 145.96  E-value: 2.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 682 LFKVILHNPHLKHLNfygssLSHMDARQLCEALKHPM------CNIEELMLGKCDITGEACEDIASVLvHNKKLNLLSLC 755
Cdd:cd00116   43 LASALRPQPSLKELC-----LSLNETGRIPRGLQSLLqgltkgCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLN 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 756 ENALKDDGVLVLCEALKNPDCALEALLLSHCCFSSAACDHLSQVLLYNRSLTFLDLGSNVLKDEGVTTLCESLKHpSCNL 835
Cdd:cd00116  117 NNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNL 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 836 QELWLMNCYFTSVCCVDIATVLIHSEKLKTLKLGNNKIYDAGAKQLCKALKHPKCKLENLGLEACELSPASCEDLASALT 915
Cdd:cd00116  196 EVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLA 275

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 122135250 916 TCKSLTCVNLEWITLDYDGAAVLCEALVSLECSLQLLGL 954
Cdd:cd00116  276 EKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWV 314
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 151-315 1.36e-35

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: 132.81  E-value: 1.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  151 TVVLHGPEGIGKTTFLRKVMLEWAKGNLWRDrFSFVFFLTGREMNGVTDM-SLVELLSRDWPESSEPIEDIF----SQPE 225
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEVWavilELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  226 RILFILDGMEELKfdldcnADLCEDwEQPQSMQVVLQSLLQKQMLPECSLLLALSKMGMRKNYSLLKHMKCIFLLGFSEH 305
Cdd:pfam05729  81 RLLLILDGLDELV------SDLGQL-DGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                         170
                  ....*....|
gi 122135250  306 QRKLYFSHYF 315
Cdd:pfam05729 154 DRKQYVRKYF 163
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-93 1.81e-33

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: 123.51  E-value: 1.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  11 LLWYLEELKKEEFWKFKELLKQEPLKLKLKPIPWTELKKASRENVSKLLSKHYPGKLAWDVTLNLFLQISRDDLWRKARN 90
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ...
gi 122135250  91 EIR 93
Cdd:cd08320   81 EMN 83
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 449-564 3.25e-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: 101.60  E-value: 3.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  449 HTCIQEFCAAMFYMFTRPKDPPHSVI--------GNVTQLITRAVSGHYSRLSWTAVFLFVFSTERMTHRLETSFGFPLS 520
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 122135250  521 KEIKQEITQSLDTLSQCDPNNvmMSFQALFNCLFETQDPEFVAQ 564
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 ...
 396-444 2.52e-09

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: 54.11  E-value: 2.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 122135250  396 LKSLCTLAAEGMWTCTFLFCPEDLRRNGVSESDTSMWLDMKLLHRSGDC 444
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGC 51
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 682-954 2.28e-38

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 145.96  E-value: 2.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 682 LFKVILHNPHLKHLNfygssLSHMDARQLCEALKHPM------CNIEELMLGKCDITGEACEDIASVLvHNKKLNLLSLC 755
Cdd:cd00116   43 LASALRPQPSLKELC-----LSLNETGRIPRGLQSLLqgltkgCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLN 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 756 ENALKDDGVLVLCEALKNPDCALEALLLSHCCFSSAACDHLSQVLLYNRSLTFLDLGSNVLKDEGVTTLCESLKHpSCNL 835
Cdd:cd00116  117 NNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNL 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 836 QELWLMNCYFTSVCCVDIATVLIHSEKLKTLKLGNNKIYDAGAKQLCKALKHPKCKLENLGLEACELSPASCEDLASALT 915
Cdd:cd00116  196 EVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLA 275

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 122135250 916 TCKSLTCVNLEWITLDYDGAAVLCEALVSLECSLQLLGL 954
Cdd:cd00116  276 EKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWV 314
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 151-315 1.36e-35

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: 132.81  E-value: 1.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  151 TVVLHGPEGIGKTTFLRKVMLEWAKGNLWRDrFSFVFFLTGREMNGVTDM-SLVELLSRDWPESSEPIEDIF----SQPE 225
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEVWavilELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  226 RILFILDGMEELKfdldcnADLCEDwEQPQSMQVVLQSLLQKQMLPECSLLLALSKMGMRKNYSLLKHMKCIFLLGFSEH 305
Cdd:pfam05729  81 RLLLILDGLDELV------SDLGQL-DGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                         170
                  ....*....|
gi 122135250  306 QRKLYFSHYF 315
Cdd:pfam05729 154 DRKQYVRKYF 163
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-93 1.81e-33

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: 123.51  E-value: 1.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  11 LLWYLEELKKEEFWKFKELLKQEPLKLKLKPIPWTELKKASRENVSKLLSKHYPGKLAWDVTLNLFLQISRDDLWRKARN 90
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ...
gi 122135250  91 EIR 93
Cdd:cd08320   81 EMN 83
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 687-942 5.48e-27

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: 115.27  E-value: 5.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 687 LHNPHLKHLNFYGSSLSHMDARQLCEALKHPMcNIEELMLGKCDITGEACEDIASVLVHNKKLNLLSLCENALKDDGVLV 766
Cdd:COG5238  177 LQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 767 LCEALKNPDcALEALLLSHCCFSSAACDHLSQVLLYNRSLTFLDLGSNVLKDEGVTTLCESLKHPScNLQELWLMNCYFT 846
Cdd:COG5238  256 LAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIG 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 847 SVCCVDIATVLIHSEKLKTLKLGNNKIYDAGAKQLCKALKHPKcKLENLGLEACELSPASCEDLASALTTCKsLTCVNLE 926
Cdd:COG5238  334 AQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILD 411

                        250
                 ....*....|....*.
gi 122135250 927 WITLDYDGAAVLCEAL 942
Cdd:COG5238  412 GNLIGAEAQQRLEQLL 427
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 449-564 3.25e-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: 101.60  E-value: 3.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  449 HTCIQEFCAAMFYMFTRPKDPPHSVI--------GNVTQLITRAVSGHYSRLSWTAVFLFVFSTERMTHRLETSFGFPLS 520
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 122135250  521 KEIKQEITQSLDTLSQCDPNNvmMSFQALFNCLFETQDPEFVAQ 564
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 ...
 10-85 3.05e-24

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: 96.89  E-value: 3.05e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122135250   10 GLLWYLEELKKEEFWKFKELLKQEPlKLKLKPIPWTELKKASRENVSKLLSKHYPGKLAWDVTLNLFLQISRDDLW 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 396-444 2.52e-09

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: 54.11  E-value: 2.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 122135250  396 LKSLCTLAAEGMWTCTFLFCPEDLRRNGVSESDTSMWLDMKLLHRSGDC 444
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGC 51
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
860-887 5.65e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.85  E-value: 5.65e-05
                           10        20
                   ....*....|....*....|....*...
gi 122135250   860 SEKLKTLKLGNNKIYDAGAKQLCKALKH 887
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 148-277 8.18e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.12  E-value: 8.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250   148 SSPTVVLHGPEGIGKTTFLRKVMlewakgNLWRDRFSFVFFLTGREMNGVTDMSLVELLSRDWPESSEPIEDIfsqpeRI 227
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALA------RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRL-----RL 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 122135250   228 LFILdgMEELKFD---LDcNADLCEDWEQPQSMQVVLQSLLQKQMLPECSLLL 277
Cdd:smart00382  70 ALAL--ARKLKPDvliLD-EITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV 119
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 682-954 2.28e-38

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 145.96  E-value: 2.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 682 LFKVILHNPHLKHLNfygssLSHMDARQLCEALKHPM------CNIEELMLGKCDITGEACEDIASVLvHNKKLNLLSLC 755
Cdd:cd00116   43 LASALRPQPSLKELC-----LSLNETGRIPRGLQSLLqgltkgCGLQELDLSDNALGPDGCGVLESLL-RSSSLQELKLN 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 756 ENALKDDGVLVLCEALKNPDCALEALLLSHCCFSSAACDHLSQVLLYNRSLTFLDLGSNVLKDEGVTTLCESLKHpSCNL 835
Cdd:cd00116  117 NNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNL 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 836 QELWLMNCYFTSVCCVDIATVLIHSEKLKTLKLGNNKIYDAGAKQLCKALKHPKCKLENLGLEACELSPASCEDLASALT 915
Cdd:cd00116  196 EVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLA 275

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 122135250 916 TCKSLTCVNLEWITLDYDGAAVLCEALVSLECSLQLLGL 954
Cdd:cd00116  276 EKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWV 314
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 624-902 5.54e-38

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 144.81  E-value: 5.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 624 RDVCSAFAASEDFEILNL--DNCRFDEPSLAVLCRTLsQPVCKLRKFVCNFASNLANSLELFKVILHNPHLKHLNFYGSS 701
Cdd:cd00116   41 KALASALRPQPSLKELCLslNETGRIPRGLQSLLQGL-TKGCGLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNG 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 702 LSHMDARQLCEALKHPMCNIEELMLGKCDITGEACEDIASVLVHNKKLNLLSLCENALKDDGVLVLCEALKNpDCALEAL 781
Cdd:cd00116  120 LGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKA-NCNLEVL 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 782 LLSHCCFSSAACDHLSQVLLYNRSLTFLDLGSNVLKDEGVTTLCESLKHPSCNLQELWLMNCYFTSVCCVDIATVLIHSE 861
Cdd:cd00116  199 DLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKE 278

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 122135250 862 KLKTLKLGNNKIYDAGAKQLCKALKHPKCKLENLGLEACEL 902
Cdd:cd00116  279 SLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDDSF 319
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
 151-315 1.36e-35

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: 132.81  E-value: 1.36e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  151 TVVLHGPEGIGKTTFLRKVMLEWAKGNLWRDrFSFVFFLTGREMNGVTDM-SLVELLSRDWPESSEPIEDIF----SQPE 225
Cdd:pfam05729   2 TVILQGEAGSGKTTLLQKLALLWAQGKLPQG-FDFVFFLPCRELSRSGNArSLADLLFSQWPEPAAPVSEVWavilELPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  226 RILFILDGMEELKfdldcnADLCEDwEQPQSMQVVLQSLLQKQMLPECSLLLALSKMGMRKNYSLLKHMKCIFLLGFSEH 305
Cdd:pfam05729  81 RLLLILDGLDELV------SDLGQL-DGPCPVLTLLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPRYLEVRGFSES 153

                         170
                  ....*....|
gi 122135250  306 QRKLYFSHYF 315
Cdd:pfam05729 154 DRKQYVRKYF 163
Pyrin_NALPs cd08320
Pyrin death domain found in NALP proteins; Pyrin Death Domain found in NALP (NACHT, LRR and ...
 11-93 1.81e-33

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: 123.51  E-value: 1.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  11 LLWYLEELKKEEFWKFKELLKQEPLKLKLKPIPWTELKKASRENVSKLLSKHYPGKLAWDVTLNLFLQISRDDLWRKARN 90
Cdd:cd08320    1 LLWYLEELSKEELKKFKLLLKEESLEGGLKPIPWTEVKKADGEELAELLTEHYPEQQAWDVALSIFEKMNRTDLCEKARA 80


                 ...
gi 122135250  91 EIR 93
Cdd:cd08320   81 EMN 83
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 687-942 5.48e-27

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: 115.27  E-value: 5.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 687 LHNPHLKHLNFYGSSLSHMDARQLCEALKHPMcNIEELMLGKCDITGEACEDIASVLVHNKKLNLLSLCENALKDDGVLV 766
Cdd:COG5238  177 LQNNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 767 LCEALKNPDcALEALLLSHCCFSSAACDHLSQVLLYNRSLTFLDLGSNVLKDEGVTTLCESLKHPScNLQELWLMNCYFT 846
Cdd:COG5238  256 LAEALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIG 333

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 847 SVCCVDIATVLIHSEKLKTLKLGNNKIYDAGAKQLCKALKHPKcKLENLGLEACELSPASCEDLASALTTCKsLTCVNLE 926
Cdd:COG5238  334 AQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLGKNNIGKQGAEALIDALQTNR-LHTLILD 411

                        250
                 ....*....|....*.
gi 122135250 927 WITLDYDGAAVLCEAL 942
Cdd:COG5238  412 GNLIGAEAQQRLEQLL 427
NLRC4_HD2 pfam17776
NLRC4 helical domain HD2; This entry represents a helical domain found in the NLRC4 protein ...
 449-564 3.25e-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: 101.60  E-value: 3.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250  449 HTCIQEFCAAMFYMFTRPKDPPHSVI--------GNVTQLITRAVSGHYSRLSWTAVFLFVFSTERMTHRLETSFGFPLS 520
Cdd:pfam17776   1 HLSFQEFFAALFYVLSFKEEKSNPLKeffglrkrESLKSLLDKALKSKNGHLDLFLRFLFGLLNEENQRLLEGLLGCKLS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 122135250  521 KEIKQEITQSLDTLSQCDPNNvmMSFQALFNCLFETQDPEFVAQ 564
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 ...
 10-85 3.05e-24

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: 96.89  E-value: 3.05e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 122135250   10 GLLWYLEELKKEEFWKFKELLKQEPlKLKLKPIPWTELKKASRENVSKLLSKHYPGKLAWDVTLNLFLQISRDDLW 85
Cdd:pfam02758   1 ILLWYLEELSEEEFKKFKSLLEDEP-EEGLRSIPRGKLEKADRLDLADLLVEHYGEDAAVDVTIEILKKINLKDLA 75
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 746-944 1.37e-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: 92.93  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 746 NKKLNLLSLCENALKDDGVLVLCEALKNPDcALEALLLSHCCFSSAACDHLSQVLLYNRSLTFLDLGSNVLKDEGVTTLC 825
Cdd:COG5238  179 NNSVETVYLGCNQIGDEGIEELAEALTQNT-TVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALA 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 826 ESLKHPScNLQELWLMNCYFTSVCCVDIATVLIHSEKLKTLKLGNNKIYDAGAKQLCKALKHPKcKLENLGLEACELSPA 905
Cdd:COG5238  258 EALKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK-TLHTLNLAYNGIGAQ 335

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 122135250 906 SCEDLASALTTCKSLTCVNLEWITLDYDGAAVLCEALVS 944
Cdd:COG5238  336 GAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEG 374
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
110-503 1.11e-18

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 91.79  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 110 LWEKEPCLLVPEDFYEETTKIEYELLSTVyLDAFKpgESSPTVVLHGPEGIGKTTFLRKVMLEWAKGNLWRDRFsFVFFL 189
Cdd:COG5635  144 LLDADGLLVSLDDLYVPLNLLERIESLKR-LELLE--AKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDP-IPILI 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 190 TGREMNgvTDMSLVELLS----RDWPESSEPIEDIFSQPeRILFILDGMEELKFDLDcNADLCEDweqpqsmqvvLQSLL 265
Cdd:COG5635  220 ELRDLA--EEASLEDLLAealeKRGGEPEDALERLLRNG-RLLLLLDGLDEVPDEAD-RDEVLNQ----------LRRFL 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 266 QKqmLPECSLLLALSKMGMRknYSLLKHMKCIFLLGFSEHQRKLYFSHYFQEKDASSRAF-SFVREKSSLFVLCQSPFLC 344
Cdd:COG5635  286 ER--YPKARVIITSRPEGYD--SSELEGFEVLELAPLSDEQIEEFLKKWFEATERKAERLlEALEENPELRELARNPLLL 361

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 345 WLVCTSlkcqLEKGEDLEldsETITGLYVSFFTKVFRSGSETCPLKQRRA-----RLKSLCTLAAEgMWTC-TFLFCPED 418
Cdd:COG5635  362 TLLALL----LRERGELP---DTRAELYEQFVELLLERWDEQRGLTIYRElsreeLRELLSELALA-MQENgRTEFAREE 433

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 419 LRRN----GVSESDTSMWLDmKLLHRSG-------DCLAFIHTCIQEFCAAMfYMFTRPKDPPHSVIGNvtqlitravsg 487
Cdd:COG5635  434 LEEIlreyLGRRKDAEALLD-ELLLRTGllvergeGRYSFAHRSFQEYLAAR-ALVEELDEELLELLAE----------- 500

                        410
                 ....*....|....*.
gi 122135250 488 HYSRLSWTAVFLFVFS 503
Cdd:COG5635  501 HLEDPRWREVLLLLAG 516
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 637-889 9.68e-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: 9.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 637 EILNLDNCRFDEPSLAVLCRTLSQPVcKLRKFVcnFASN---LANSLELFKVILHNPHLKHLNFYGSSLSHMDARQLCEA 713
Cdd:COG5238  183 ETVYLGCNQIGDEGIEELAEALTQNT-TVTTLW--LKRNpigDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEA 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 714 LKHPMcNIEELMLGKCDITGEACEDIASVLVHNKKLNLLSLCENALKDDGVLVLCEALKNpDCALEALLLSHCCFSSAAC 793
Cdd:COG5238  260 LKNNT-TVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGA 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 794 DHLSQVLLYNRSLTFLDLGSNVLKDEGVTTLCESLKHPScNLQELWLMNCYFTSVCCVDIATVLIHSeKLKTLKLGNNKI 873
Cdd:COG5238  338 IALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT-TLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLI 415

                        250
                 ....*....|....*.
gi 122135250 874 YDAGAKQLCKALKHPK 889
Cdd:COG5238  416 GAEAQQRLEQLLERIK 431
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 681-920 6.32e-14

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: 75.21  E-value: 6.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 681 ELFKVILHNPHLKHLNFYGSSLSHMDARQLCEALKHPMcNIEELMLGKCDITGEACEDIASVLVHNKKLNLLSLCENALK 760
Cdd:COG5238  255 ALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNT-TLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIG 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 761 DDGVLVLCEALKNpdcalealllshccfssaacdhlsqvllyNRSLTFLDLGSNVLKDEGVTTLCESLK-HPScnlqelw 839
Cdd:COG5238  334 AQGAIALAKALQE-----------------------------NTTLHSLDLSDNQIGDEGAIALAKYLEgNTT------- 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 840 lmncyftsvccvdiatvlihsekLKTLKLGNNKIYDAGAKQLCKALKHPkcKLENLGLEACELSPASCEDLASALTTCKS 919
Cdd:COG5238  378 -----------------------LRELNLGKNNIGKQGAEALIDALQTN--RLHTLILDGNLIGAEAQQRLEQLLERIKS 432


                 .
gi 122135250 920 L 920
Cdd:COG5238  433 V 433
Pyrin_ASC-like cd08321
Pyrin Death Domain found in ASC; Pyrin Death Domain found in ASC (Apoptosis-associated ...
 11-84 3.75e-10

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: 57.15  E-value: 3.75e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122135250  11 LLWYLEELKKEEFWKFKELLKQEPLKLKlKPIPWTELKKASRENVSKLLSKHYPGKLAWDVTLNLFLQISRDDL 84
Cdd:cd08321    4 LLDALEDLGEEELKKFKWKLRDIPLEGY-PRIPRGKLENADRVDLVDLLVSYYGEDYAVEVTVEVLRAINQNDL 76
NOD2_WH pfam17779
NOD2 winged helix domain; This winged helix domain is found in the NOD2 protein. Its molecular ...
 396-444 2.52e-09

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: 54.11  E-value: 2.52e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 122135250  396 LKSLCTLAAEGMWTCTFLFCPEDLRRNGVSESDTSMWLDMKLLHRSGDC 444
Cdd:pfam17779   3 LLKLGKLAFEGLWKKKLVFSEEDLKEYGLDESDLSSGLLTEILQKDLGC 51
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
720-873 4.52e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 50.32  E-value: 4.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 720 NIEELMLGKCDITgeaceDIASVLVHNKKLNLLSLCENALKDdgvlvLCEALKNPDcALEALLLSHCCFSSaacdhLSQV 799
Cdd:COG4886  114 NLESLDLSGNQLT-----DLPEELANLTNLKELDLSNNQLTD-----LPEPLGNLT-NLKSLDLSNNQLTD-----LPEE 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122135250 800 LLYNRSLTFLDLGSNvlkdeGVTTLCESLKHPScNLQELWLMNCYFTsvccvDIATVLIHSEKLKTLKLGNNKI 873
Cdd:COG4886  178 LGNLTNLKELDLSNN-----QITDLPEPLGNLT-NLEELDLSGNQLT-----DLPEPLANLTNLETLDLSNNQL 240
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
860-887 5.65e-05

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 40.85  E-value: 5.65e-05
                           10        20
                   ....*....|....*....|....*...
gi 122135250   860 SEKLKTLKLGNNKIYDAGAKQLCKALKH 887
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
800-925 8.66e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 8.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 800 LLYNRSLTFLDLGSNvlkdeGVTTLCESLKHPScNLQELWLMNCYFTsvccvDIATVLIHSEKLKTLKLGNNKIydagaK 879
Cdd:COG4886  109 LSNLTNLESLDLSGN-----QLTDLPEELANLT-NLKELDLSNNQLT-----DLPEPLGNLTNLKSLDLSNNQL-----T 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 122135250 880 QLCKALKHPKcKLENLGLEACELSpasceDLASALTTCKSLTCVNL 925
Cdd:COG4886  173 DLPEELGNLT-NLKELDLSNNQIT-----DLPEPLGNLTNLEELDL 212
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
681-886 4.10e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 4.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 681 ELFKVILHNPHLKHLNFYGSSLShmdarQLCEALKhPMCNIEELMLGKCDITgeaceDIASVLVHNKKLNLLSLCENALK 760
Cdd:COG4886  150 DLPEPLGNLTNLKSLDLSNNQLT-----DLPEELG-NLTNLKELDLSNNQIT-----DLPEPLGNLTNLEELDLSGNQLT 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250 761 DdgvlvLCEALKNPDcALEALLLSHCCFSSAAcdhlsqVLLYNRSLTFLDLGSNvlkdeGVTTLCESLKHPscNLQELWL 840
Cdd:COG4886  219 D-----LPEPLANLT-NLETLDLSNNQLTDLP------ELGNLTNLEELDLSNN-----QLTDLPPLANLT--NLKTLDL 279

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 122135250 841 MNCYFTSVCCVDIATVLIHSEKLKTLKLGNNKIYDAGAKQLCKALK 886
Cdd:COG4886  280 SNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLL 325
Pyrin cd08305
Pyrin: a protein-protein interaction domain; The Pyrin domain (or PYD), also called DAPIN or ...
 11-84 6.20e-03

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


Pssm-ID: 260019  Cd Length: 73  Bit Score: 36.51  E-value: 6.20e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 122135250  11 LLWYLEELKKEEFWKFKELLKQEpLKLKLKpipwtELKKASRENVSKLLSKHYPGKLAWDVTLNLFLQISRDDL 84
Cdd:cd08305    1 LLTGLENITDEEFKMFKSLLASE-LKLTRK-----MQEEYDRIEIADLMEEKFGEDAGLDKLIEVFEDMPLRSL 68
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 148-277 8.18e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 38.12  E-value: 8.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 122135250   148 SSPTVVLHGPEGIGKTTFLRKVMlewakgNLWRDRFSFVFFLTGREMNGVTDMSLVELLSRDWPESSEPIEDIfsqpeRI 227
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALA------RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRL-----RL 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 122135250   228 LFILdgMEELKFD---LDcNADLCEDWEQPQSMQVVLQSLLQKQMLPECSLLL 277
Cdd:smart00382  70 ALAL--ARKLKPDvliLD-EITSLLDAEQEALLLLLEELRLLLLLKSEKNLTV 119
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
803-830 8.97e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 34.69  E-value: 8.97e-03
                           10        20
                   ....*....|....*....|....*...
gi 122135250   803 NRSLTFLDLGSNVLKDEGVTTLCESLKH 830
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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