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Conserved domains on  [gi|40788015|ref|NP_067032|]
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NLR family CARD domain-containing protein 4 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
163-316 3.80e-37

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: 137.44  E-value: 3.80e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    163 SPCIIEGESGKGKSTLLQRIAMLWGSGKCKALtkFKFVFFLRLSRAQG-----GLFETLCDQLLDIPGTIRKqtFMAMLL 237
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRsgnarSLADLLFSQWPEPAAPVSE--VWAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    238 KLRQRVLFLLDGYNEFKPQNCPE---------IEALIKENHRFKNMVIVTTTTECLRHIRQFGALT--AEVGDMTEDSAQ 306
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQLdgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
                          170
                   ....*....|
gi 40788015    307 ALIREVLIKE 316
Cdd:pfam05729  157 QYVRKYFSDE 166
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
465-579 1.72e-35

NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins. Structural and functional studies indicate that the helical domain HD2 repressively contacted a conserved and functionally important alpha-helix of the NBD (nucleotide binding domain) in Swiss:Q3UP24. Furthermore, the HD2 domain was shown to cap the N-terminal side of the LRR (leucine-rich repeat) domain via extensive interactions. Other family members carrying this domain include baculoviral IAP repeat-containing protein 1 (Birc1) also known as neuronal apoptosis inhibitory protein (Naip).


:

Pssm-ID: 436120  Cd Length: 106  Bit Score: 130.09  E-value: 1.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    465 EEVTKGNGYLQKMVSISDITSTYSSLLRYTCGSSVEATRAVMKHLAAVYQH-GCLLGLSiakrplwrqESLQSVKNTTEQ 543
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLYTCHSSTKAGPKIVSHLLHLVDHkESLENLS---------ENDDYLKHHPET 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 40788015    544 EILKAiNINSFVECGIHLYQESTSKSALSQEFEAFF 579
Cdd:pfam17889   72 SLLMQ-NIRSLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
148-469 1.19e-24

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


:

Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 111.05  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  148 RVEQLTLNGLLQALQSPCIIEGESGKGKSTLLQRIAMLWGSGKCKALTKFKFVFFLRLSRAQGGLFETLCDQLLDIPGTI 227
Cdd:COG5635  166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLAEEASLEDLLAEALEKRGGEP 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  228 RKQTfmAMLLKlRQRVLFLLDGYNEFKPQN-----CPEIEALIKENHRFKnmVIVTTTTECLRHIRQFGALTAEVGDMTE 302
Cdd:COG5635  246 EDAL--ERLLR-NGRLLLLLDGLDEVPDEAdrdevLNQLRRFLERYPKAR--VIITSRPEGYDSSELEGFEVLELAPLSD 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  303 DSAQALIRE--VLIKELAEGLLLQIQKSRCLRNLMKTPLFVVITCAIQMGESEFhSHTQTTLFHTFYDLLI-----QKNK 375
Cdd:COG5635  321 EQIEEFLKKwfEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGEL-PDTRAELYEQFVELLLerwdeQRGL 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  376 HKHKGVAASDFIRSLdhcGDLALEGVFSHKFDF---ELQ-----------DVSSVNEDVLLTTGLLCkytaQRFKPKYKF 441
Cdd:COG5635  400 TIYRELSREELRELL---SELALAMQENGRTEFareELEeilreylgrrkDAEALLDELLLRTGLLV----ERGEGRYSF 472
                        330       340
                 ....*....|....*....|....*...
gi 40788015  442 FHKSFQEYTAGRRLSSLLTSHEPEEVTK 469
Cdd:COG5635  473 AHRSFQEYLAARALVEELDEELLELLAE 500
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
1-87 3.79e-19

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


:

Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 82.99  E-value: 3.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015      1 MNFIKDNSRALIQRMgmTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPL 80
Cdd:pfam00619    1 RKLLKKNRVALVERL--GTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDL 78

                   ....*..
gi 40788015     81 FQDLNGQ 87
Cdd:pfam00619   79 ASDLEGL 85
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
646-955 1.54e-08

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


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.02  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  646 SRAVSLFFNWKQEFRTLEVTLRDFSKLNKQDIRYLGKIFSSATSLRLQIKRCAGVAGSLSLVLSTCKNIYSLMVEASPLT 725
Cdd:COG4886   23 TLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  726 IEDERHITSVTNLKTLSIHDLQNQRLPggltDSLGNLKNLTKLIMDNIKMNEedaikLAEGLKNLKKMCLFHL--THLSD 803
Cdd:COG4886  103 LSGNEELSNLTNLESLDLSGNQLTDLP----EELANLTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLsnNQLTD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  804 IGEGMDYIVK---------SLSSEPCDLEEI-QLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKdgnealhelID 873
Cdd:COG4886  174 LPEELGNLTNlkeldlsnnQITDLPEPLGNLtNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD---------LP 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  874 RMNVLEQLTALmlpwgcDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQLNLAGNRVSSDG 953
Cdd:COG4886  245 ELGNLTNLEEL------DLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLL 318

                 ..
gi 40788015  954 WL 955
Cdd:COG4886  319 LL 320
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
163-316 3.80e-37

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: 137.44  E-value: 3.80e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    163 SPCIIEGESGKGKSTLLQRIAMLWGSGKCKALtkFKFVFFLRLSRAQG-----GLFETLCDQLLDIPGTIRKqtFMAMLL 237
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRsgnarSLADLLFSQWPEPAAPVSE--VWAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    238 KLRQRVLFLLDGYNEFKPQNCPE---------IEALIKENHRFKNMVIVTTTTECLRHIRQFGALT--AEVGDMTEDSAQ 306
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQLdgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
                          170
                   ....*....|
gi 40788015    307 ALIREVLIKE 316
Cdd:pfam05729  157 QYVRKYFSDE 166
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
465-579 1.72e-35

NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins. Structural and functional studies indicate that the helical domain HD2 repressively contacted a conserved and functionally important alpha-helix of the NBD (nucleotide binding domain) in Swiss:Q3UP24. Furthermore, the HD2 domain was shown to cap the N-terminal side of the LRR (leucine-rich repeat) domain via extensive interactions. Other family members carrying this domain include baculoviral IAP repeat-containing protein 1 (Birc1) also known as neuronal apoptosis inhibitory protein (Naip).


Pssm-ID: 436120  Cd Length: 106  Bit Score: 130.09  E-value: 1.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    465 EEVTKGNGYLQKMVSISDITSTYSSLLRYTCGSSVEATRAVMKHLAAVYQH-GCLLGLSiakrplwrqESLQSVKNTTEQ 543
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLYTCHSSTKAGPKIVSHLLHLVDHkESLENLS---------ENDDYLKHHPET 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 40788015    544 EILKAiNINSFVECGIHLYQESTSKSALSQEFEAFF 579
Cdd:pfam17889   72 SLLMQ-NIRSLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
148-469 1.19e-24

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 111.05  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  148 RVEQLTLNGLLQALQSPCIIEGESGKGKSTLLQRIAMLWGSGKCKALTKFKFVFFLRLSRAQGGLFETLCDQLLDIPGTI 227
Cdd:COG5635  166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLAEEASLEDLLAEALEKRGGEP 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  228 RKQTfmAMLLKlRQRVLFLLDGYNEFKPQN-----CPEIEALIKENHRFKnmVIVTTTTECLRHIRQFGALTAEVGDMTE 302
Cdd:COG5635  246 EDAL--ERLLR-NGRLLLLLDGLDEVPDEAdrdevLNQLRRFLERYPKAR--VIITSRPEGYDSSELEGFEVLELAPLSD 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  303 DSAQALIRE--VLIKELAEGLLLQIQKSRCLRNLMKTPLFVVITCAIQMGESEFhSHTQTTLFHTFYDLLI-----QKNK 375
Cdd:COG5635  321 EQIEEFLKKwfEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGEL-PDTRAELYEQFVELLLerwdeQRGL 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  376 HKHKGVAASDFIRSLdhcGDLALEGVFSHKFDF---ELQ-----------DVSSVNEDVLLTTGLLCkytaQRFKPKYKF 441
Cdd:COG5635  400 TIYRELSREELRELL---SELALAMQENGRTEFareELEeilreylgrrkDAEALLDELLLRTGLLV----ERGEGRYSF 472
                        330       340
                 ....*....|....*....|....*...
gi 40788015  442 FHKSFQEYTAGRRLSSLLTSHEPEEVTK 469
Cdd:COG5635  473 AHRSFQEYLAARALVEELDEELLELLAE 500
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
1-87 3.79e-19

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 82.99  E-value: 3.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015      1 MNFIKDNSRALIQRMgmTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPL 80
Cdd:pfam00619    1 RKLLKKNRVALVERL--GTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDL 78

                   ....*..
gi 40788015     81 FQDLNGQ 87
Cdd:pfam00619   79 ASDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
4-79 1.25e-11

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 61.38  E-value: 1.25e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40788015    4 IKDNSRALIQRMgmtVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYP 79
Cdd:cd01671    1 LRKNRVELVEDL---DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQP 73
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
646-955 1.54e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.02  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  646 SRAVSLFFNWKQEFRTLEVTLRDFSKLNKQDIRYLGKIFSSATSLRLQIKRCAGVAGSLSLVLSTCKNIYSLMVEASPLT 725
Cdd:COG4886   23 TLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  726 IEDERHITSVTNLKTLSIHDLQNQRLPggltDSLGNLKNLTKLIMDNIKMNEedaikLAEGLKNLKKMCLFHL--THLSD 803
Cdd:COG4886  103 LSGNEELSNLTNLESLDLSGNQLTDLP----EELANLTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLsnNQLTD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  804 IGEGMDYIVK---------SLSSEPCDLEEI-QLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKdgnealhelID 873
Cdd:COG4886  174 LPEELGNLTNlkeldlsnnQITDLPEPLGNLtNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD---------LP 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  874 RMNVLEQLTALmlpwgcDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQLNLAGNRVSSDG 953
Cdd:COG4886  245 ELGNLTNLEEL------DLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLL 318

                 ..
gi 40788015  954 WL 955
Cdd:COG4886  319 LL 320
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
738-978 1.54e-08

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 57.37  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  738 LKTLSIHDLQNQRLPGGLTDSLGNLKNLTKL----IMDNikmneEDAIKLAEGLKNLKKMCLFHLTHLSDIGEG---MDY 810
Cdd:cd00116   53 LKELCLSLNETGRIPRGLQSLLQGLTKGCGLqeldLSDN-----ALGPDGCGVLESLLRSSSLQELKLNNNGLGdrgLRL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  811 IVKSLSSEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEAL-HELIDRMNvLEQL----TALM 885
Cdd:cd00116  128 LAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALaEGLKANCN-LEVLdlnnNGLT 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  886 lPWGCdvqGSLSSLLKHLeevPQLVKLGLKNWRLTDTEIRILGAFFgKNPLKNFQQLNLAGNRVSSDGWLAFMGVFENLK 965
Cdd:cd00116  207 -DEGA---SALAETLASL---KSLEVLNLGDNNLTDAGAAALASAL-LSPNISLLTLSLSCNDITDDGAKDLAEVLAEKE 278
                        250
                 ....*....|...
gi 40788015  966 QLVFFDFSTKEFL 978
Cdd:cd00116  279 SLLELDLRGNKFG 291
 
Name Accession Description Interval E-value
NACHT pfam05729
NACHT domain; This NTPase domain is found in apoptosis proteins as well as those involved in ...
163-316 3.80e-37

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: 137.44  E-value: 3.80e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    163 SPCIIEGESGKGKSTLLQRIAMLWGSGKCKALtkFKFVFFLRLSRAQG-----GLFETLCDQLLDIPGTIRKqtFMAMLL 237
Cdd:pfam05729    1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRsgnarSLADLLFSQWPEPAAPVSE--VWAVIL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    238 KLRQRVLFLLDGYNEFKPQNCPE---------IEALIKENHRFKNMVIVTTTTECLRHIRQFGALT--AEVGDMTEDSAQ 306
Cdd:pfam05729   77 ELPERLLLILDGLDELVSDLGQLdgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
                          170
                   ....*....|
gi 40788015    307 ALIREVLIKE 316
Cdd:pfam05729  157 QYVRKYFSDE 166
NLRC4_HD pfam17889
NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and ...
465-579 1.72e-35

NLRC4 helical domain; This is a helical domain found in NLRC4, Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins. Structural and functional studies indicate that the helical domain HD2 repressively contacted a conserved and functionally important alpha-helix of the NBD (nucleotide binding domain) in Swiss:Q3UP24. Furthermore, the HD2 domain was shown to cap the N-terminal side of the LRR (leucine-rich repeat) domain via extensive interactions. Other family members carrying this domain include baculoviral IAP repeat-containing protein 1 (Birc1) also known as neuronal apoptosis inhibitory protein (Naip).


Pssm-ID: 436120  Cd Length: 106  Bit Score: 130.09  E-value: 1.72e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    465 EEVTKGNGYLQKMVSISDITSTYSSLLRYTCGSSVEATRAVMKHLAAVYQH-GCLLGLSiakrplwrqESLQSVKNTTEQ 543
Cdd:pfam17889    1 EDQDLGLYYLKQINSILKAVSRYNNFLLYTCHSSTKAGPKIVSHLLHLVDHkESLENLS---------ENDDYLKHHPET 71
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 40788015    544 EILKAiNINSFVECGIHLYQESTSKSALSQEFEAFF 579
Cdd:pfam17889   72 SLLMQ-NIRSLWQLSPELYLSSVSEHLLSLALEIAY 106
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
148-469 1.19e-24

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 111.05  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  148 RVEQLTLNGLLQALQSPCIIEGESGKGKSTLLQRIAMLWGSGKCKALTKFKFVFFLRLSRAQGGLFETLCDQLLDIPGTI 227
Cdd:COG5635  166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLAEEASLEDLLAEALEKRGGEP 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  228 RKQTfmAMLLKlRQRVLFLLDGYNEFKPQN-----CPEIEALIKENHRFKnmVIVTTTTECLRHIRQFGALTAEVGDMTE 302
Cdd:COG5635  246 EDAL--ERLLR-NGRLLLLLDGLDEVPDEAdrdevLNQLRRFLERYPKAR--VIITSRPEGYDSSELEGFEVLELAPLSD 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  303 DSAQALIRE--VLIKELAEGLLLQIQKSRCLRNLMKTPLFVVITCAIQMGESEFhSHTQTTLFHTFYDLLI-----QKNK 375
Cdd:COG5635  321 EQIEEFLKKwfEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGEL-PDTRAELYEQFVELLLerwdeQRGL 399
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  376 HKHKGVAASDFIRSLdhcGDLALEGVFSHKFDF---ELQ-----------DVSSVNEDVLLTTGLLCkytaQRFKPKYKF 441
Cdd:COG5635  400 TIYRELSREELRELL---SELALAMQENGRTEFareELEeilreylgrrkDAEALLDELLLRTGLLV----ERGEGRYSF 472
                        330       340
                 ....*....|....*....|....*...
gi 40788015  442 FHKSFQEYTAGRRLSSLLTSHEPEEVTK 469
Cdd:COG5635  473 AHRSFQEYLAARALVEELDEELLELLAE 500
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
1-87 3.79e-19

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 82.99  E-value: 3.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015      1 MNFIKDNSRALIQRMgmTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPL 80
Cdd:pfam00619    1 RKLLKKNRVALVERL--GTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDL 78

                   ....*..
gi 40788015     81 FQDLNGQ 87
Cdd:pfam00619   79 ASDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
4-79 1.25e-11

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 61.38  E-value: 1.25e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40788015    4 IKDNSRALIQRMgmtVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYP 79
Cdd:cd01671    1 LRKNRVELVEDL---DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEALRETGQP 73
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
646-955 1.54e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.02  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  646 SRAVSLFFNWKQEFRTLEVTLRDFSKLNKQDIRYLGKIFSSATSLRLQIKRCAGVAGSLSLVLSTCKNIYSLMVEASPLT 725
Cdd:COG4886   23 TLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  726 IEDERHITSVTNLKTLSIHDLQNQRLPggltDSLGNLKNLTKLIMDNIKMNEedaikLAEGLKNLKKMCLFHL--THLSD 803
Cdd:COG4886  103 LSGNEELSNLTNLESLDLSGNQLTDLP----EELANLTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLsnNQLTD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  804 IGEGMDYIVK---------SLSSEPCDLEEI-QLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKdgnealhelID 873
Cdd:COG4886  174 LPEELGNLTNlkeldlsnnQITDLPEPLGNLtNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD---------LP 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  874 RMNVLEQLTALmlpwgcDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQLNLAGNRVSSDG 953
Cdd:COG4886  245 ELGNLTNLEEL------DLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLL 318

                 ..
gi 40788015  954 WL 955
Cdd:COG4886  319 LL 320
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
738-978 1.54e-08

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


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 57.37  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  738 LKTLSIHDLQNQRLPGGLTDSLGNLKNLTKL----IMDNikmneEDAIKLAEGLKNLKKMCLFHLTHLSDIGEG---MDY 810
Cdd:cd00116   53 LKELCLSLNETGRIPRGLQSLLQGLTKGCGLqeldLSDN-----ALGPDGCGVLESLLRSSSLQELKLNNNGLGdrgLRL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  811 IVKSLSSEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEAL-HELIDRMNvLEQL----TALM 885
Cdd:cd00116  128 LAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALaEGLKANCN-LEVLdlnnNGLT 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  886 lPWGCdvqGSLSSLLKHLeevPQLVKLGLKNWRLTDTEIRILGAFFgKNPLKNFQQLNLAGNRVSSDGWLAFMGVFENLK 965
Cdd:cd00116  207 -DEGA---SALAETLASL---KSLEVLNLGDNNLTDAGAAALASAL-LSPNISLLTLSLSCNDITDDGAKDLAEVLAEKE 278
                        250
                 ....*....|...
gi 40788015  966 QLVFFDFSTKEFL 978
Cdd:cd00116  279 SLLELDLRGNKFG 291
CARD_CASP1-like cd08325
Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase ...
5-75 1.69e-06

Caspase activation and recruitment domain found in Caspase-1 and related proteins; Caspase activation and recruitment domain (CARD) similar to those found in Caspase-1 (CASP1, ICE) and related proteins, including CARD-only proteins such as ICEBERG or CARD18, INCA (CARD17), CARD16 (COP1, PSEUDO-ICE), CARD8 (DACAR, NDPP1, TUCAN), and CARD12 (NLRC4), as well as ICE-like caspases such as CASP12, CASP5 (ICH-3) and CASP4 (TX, ICH-2). Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. CASP1 plays a central role in the cellular response to a wide variety of microbial and non-microbial stimuli, being activated by the inflammasome or the pyroptosome. CARD8 binds itself and the initiator caspase-9, interfering with the binding of APAF-1 and suppressing caspase-9 activation. CARD12 is a Nod-like receptor (NLR) that plays an important role in the innate immune response to Gram-negative bacteria. Caspase-4 (CASP4), -5 (CASP5), and -12 (CASP12) are inflammatory caspases implicated in inflammation and endoplasmic reticulum stress-induced apoptosis. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260036  Cd Length: 83  Bit Score: 46.82  E-value: 1.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 40788015    5 KDNSRALIQRMGMTVIKQITDDLFVWNVLNREEVNIICCEKVE-QDAARGIIHMILKKGSESCNLFLKSLKE 75
Cdd:cd08325    3 KEKRVKFVESVGKGVINGLLDDLLEKNVLNEEEMEKIKEENNTiVDKARVLIDSVTEKGQMAGQIFIQHLCN 74
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
754-906 6.72e-06

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 49.79  E-value: 6.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  754 GLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKMCLFHLTHlSDIG-EGMDYIVKSLSSEPcDLEEIQLVSCCL 832
Cdd:COG5238  283 ALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY-NGIGaQGAIALAKALQENT-TLHSLDLSDNQI 360
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 40788015  833 SANAVKILAQNLHNLVKLSILDLSENYLEKDGNEAlheLIDRMNVlEQLTALMLPW---GCDVQGSLSSLLKHLEEV 906
Cdd:COG5238  361 GDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEA---LIDALQT-NRLHTLILDGnliGAEAQQRLEQLLERIKSV 433
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
722-973 1.56e-05

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 48.63  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  722 SPLTIEDERHITSVT-----NLKTLSIHDLQNQRLPGGLTDSLGNLkNLTKLIMDNIKM--NEEDAIKLAEGLKNLKKMC 794
Cdd:COG5238   76 VALEKAAEAFPTQLLvvdweGAEEVSPVALAETATAVATPPPDLRR-IMAKTLEDSLILylALPRRINLIQVLKDPLGGN 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  795 LFHLT-----HLSDIGEGMDYIVKSLSSEPCDL--EEIQLVSCCLSANAV---------------------KILAQNLHN 846
Cdd:COG5238  155 AVHLLglaarLGLLAAISMAKALQNNSVETVYLgcNQIGDEGIEELAEALtqnttvttlwlkrnpigdegaEILAEALKG 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  847 LVKLSILDLSENYLekdGNEALHELIDRMNVLEQLTALMLpwGC---DVQGsLSSLLKHLEEVPQLVKLGLKNWRLTDTE 923
Cdd:COG5238  235 NKSLTTLDLSNNQI---GDEGVIALAEALKNNTTVETLYL--SGnqiGAEG-AIALAKALQGNTTLTSLDLSVNRIGDEG 308
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 40788015  924 IRILGAFFGKNplKNFQQLNLAGNRVSSDGWLAFMGVFENLKQLVFFDFS 973
Cdd:COG5238  309 AIALAEGLQGN--KTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLS 356
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
754-953 2.59e-05

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 47.86  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  754 GLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKmclfhLTHLS----DIG-EGMDYIVKSLSsEPCDLEEIQLV 828
Cdd:COG5238  199 ELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKS-----LTTLDlsnnQIGdEGVIALAEALK-NNTTVETLYLS 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  829 SCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEALHELIDRMNVLEQLTaLMLPwGCDVQGSLsSLLKHLEEVPQ 908
Cdd:COG5238  273 GNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLN-LAYN-GIGAQGAI-ALAKALQENTT 349
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 40788015  909 LVKLGLKNWRLTDTEIRILGAFFGKNPlkNFQQLNLAGNRVSSDG 953
Cdd:COG5238  350 LHSLDLSDNQIGDEGAIALAKYLEGNT--TLRELNLGKNNIGKQG 392
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
3-88 3.43e-05

Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, BIRC2 (c-IAP1) and BIRC3 (c-IAP2); Caspase activation and recruitment domain (CARD) similar to those found in Baculoviral IAP repeat (BIR)-containing protein 2 (BIRC2) or cellular Inhibitor of Apoptosis Protein 1 (c-IAP1), and BIRC3 (or c-IAP2). IAPs are anti-apoptotic proteins that contain at least one BIR domain. Most IAPs also contain a C-terminal RING domain. In addition, both BIRC2 and BIRC3 contain a CARD. BIRC2 and BIRC3, through their binding with TRAF (TNF receptor-associated factor) 2, are recruited to TNFR-1/2 signaling complexes, where they regulate caspase-8 activity. They also play important roles in pro-survival NF-kB signaling pathways. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260038  Cd Length: 94  Bit Score: 43.59  E-value: 3.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    3 FIKDNSRALIQRMgmTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPLFQ 82
Cdd:cd08329   10 LIRKNRMALFQHL--TCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKEIDVVLYR 87

                 ....*.
gi 40788015   83 DLNGQS 88
Cdd:cd08329   88 DLFVQK 93
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
731-872 6.94e-05

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


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 46.71  E-value: 6.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  731 HITSVTNLKTLSIHDlqNQRLPGG---LTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKMCLFHLTHlSDIG-E 806
Cdd:COG5238  231 ALKGNKSLTTLDLSN--NQIGDEGviaLAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSV-NRIGdE 307
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 40788015  807 GMDYIVKSLSsEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEALHELI 872
Cdd:COG5238  308 GAIALAEGLQ-GNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYL 372
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
713-973 7.29e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.47  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  713 NIYSLMVEASPLTIEDERHITSVTNLKTLSIHDLQNQRLPGGLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKK 792
Cdd:COG4886    1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  793 MCLFHLTHLSDIGEGMDYIVKSLSSEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLekdgnEALHELI 872
Cdd:COG4886   81 LLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-----TDLPEPL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  873 DRMNVLEQLtalmlpwgcDVQG-SLSSLLKHLEEVPQLVKLGlknwrLTDTEIRILGAFFGKnpLKNFQQLNLAGNRVSS 951
Cdd:COG4886  156 GNLTNLKSL---------DLSNnQLTDLPEELGNLTNLKELD-----LSNNQITDLPEPLGN--LTNLEELDLSGNQLTD 219
                        250       260
                 ....*....|....*....|..
gi 40788015  952 dgwlaFMGVFENLKQLVFFDFS 973
Cdd:COG4886  220 -----LPEPLANLTNLETLDLS 236
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
2-84 3.51e-04

Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; Caspase activation and recruitment domain (CARD) similar to those found in human ASC (Apoptosis-associated speck-like protein containing a CARD) and NALP1 (CARD7, NLRP1). ASC, an adaptor molecule, and NALP1, a member of the Nod-like receptor (NLR) family, are involved in the assembly of the 'inflammasome', a multiprotein platform, which is responsible for caspase-1 activation and regulation of IL-1beta maturation. In general, CARDs are death domains (DDs) associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation and host-defense mechanisms. 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 PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260039  Cd Length: 81  Bit Score: 40.28  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015    2 NFIKDNSRALIQRMgmTVIKQITDDLfVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPLF 81
Cdd:cd08330    1 HFVDRHREALIQRV--TNVDPILDEL-RGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLV 77

                 ...
gi 40788015   82 QDL 84
Cdd:cd08330   78 EDL 80
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
731-881 6.30e-04

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.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 42.47  E-value: 6.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  731 HITSVTNLKTLS--IH-DLQN---QRLPGgltdsLGNLKNLTKLIMDNikmNEedaIKLAEGLKNLKkmCLFHLtHLSD- 803
Cdd:cd21340   35 KITKIENLEFLTnlTHlYLQNnqiEKIEN-----LENLVNLKKLYLGG---NR---ISVVEGLENLT--NLEEL-HIENq 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  804 -IGEGMdyivkSLSSEPcdlEEIQLVSCCL-----SANAVKILAQnLHNLVKLSILDLSENYLEKDgnEALHELIDRMNV 877
Cdd:cd21340  101 rLPPGE-----KLTFDP---RSLAALSNSLrvlniSGNNIDSLEP-LAPLRNLEQLDASNNQISDL--EELLDLLSSWPS 169

                 ....
gi 40788015  878 LEQL 881
Cdd:cd21340  170 LREL 173
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
703-983 5.82e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.30  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  703 SLSLVLSTCKNIYSLMVEASPLTiEDERHITSVTNLKTLSIHDLQNQRLPggltDSLGNLKNLTKLIMDNIKMNE-EDAI 781
Cdd:COG4886  150 DLPEPLGNLTNLKSLDLSNNQLT-DLPEELGNLTNLKELDLSNNQITDLP----EPLGNLTNLEELDLSGNQLTDlPEPL 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  782 KlaeGLKNLKKMCLFHlTHLSDIGEgmdyiVKSLSSepcdLEEIQLvscclSANAVKILAqNLHNLVKLSILDLSENYLE 861
Cdd:COG4886  225 A---NLTNLETLDLSN-NQLTDLPE-----LGNLTN----LEELDL-----SNNQLTDLP-PLANLTNLKTLDLSNNQLT 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40788015  862 KDGNEALHELIDRMNVLEQLTALMLPWGCDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQ 941
Cdd:COG4886  286 DLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 40788015  942 LNLAGNRVSSDGWLAFMGVFENLKQLVFFDFSTKEFLPDPAL 983
Cdd:COG4886  366 LLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLAL 407
 
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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