|
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 312433960 163 SPCIIEGESGKGKSTLLQRIAMLWGSGKCKALtkFKFVFFLRLSRAQG-----GLFETLCDQLLDIPGTIRKqtFMAMLL 237
Cdd:pfam05729 1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRsgnarSLADLLFSQWPEPAAPVSE--VWAVIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 238 KLRQRVLFLLDGYNEFKPQNCPE---------IEALIKENHRFKNMVIVTTTTECLRHIRQFGALT--AEVGDMTEDSAQ 306
Cdd:pfam05729 77 ELPERLLLILDGLDELVSDLGQLdgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
|
170
....*....|
gi 312433960 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 312433960 465 EEVTKGNGYLQKMVSISDITSTYSSLLRYTCGSSVEATRAVMKHLAAVYQH-GCLLGLSiakrplwrqESLQSVKNTTEQ 543
Cdd:pfam17889 1 EDQDLGLYYLKQINSILKAVSRYNNFLLYTCHSSTKAGPKIVSHLLHLVDHkESLENLS---------ENDDYLKHHPET 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 312433960 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 312433960 148 RVEQLTLNGLLQALQSPCIIEGESGKGKSTLLQRIAMLWGSGKCKALTKFKFVFFLRLSRAQGGLFETLCDQLLDIPGTI 227
Cdd:COG5635 166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLAEEASLEDLLAEALEKRGGEP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 228 RKQTfmAMLLKlRQRVLFLLDGYNEFKPQN-----CPEIEALIKENHRFKnmVIVTTTTECLRHIRQFGALTAEVGDMTE 302
Cdd:COG5635 246 EDAL--ERLLR-NGRLLLLLDGLDEVPDEAdrdevLNQLRRFLERYPKAR--VIITSRPEGYDSSELEGFEVLELAPLSD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 303 DSAQALIRE--VLIKELAEGLLLQIQKSRCLRNLMKTPLFVVITCAIQMGESEFhSHTQTTLFHTFYDLLI-----QKNK 375
Cdd:COG5635 321 EQIEEFLKKwfEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGEL-PDTRAELYEQFVELLLerwdeQRGL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 376 HKHKGVAASDFIRSLdhcGDLALEGVFSHKFDF---ELQ-----------DVSSVNEDVLLTTGLLCkytaQRFKPKYKF 441
Cdd:COG5635 400 TIYRELSREELRELL---SELALAMQENGRTEFareELEeilreylgrrkDAEALLDELLLRTGLLV----ERGEGRYSF 472
|
330 340
....*....|....*....|....*...
gi 312433960 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 312433960 1 MNFIKDNSRALIQRMgmTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPL 80
Cdd:pfam00619 1 RKLLKKNRVALVERL--GTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDL 78
|
....*..
gi 312433960 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 312433960 646 SRAVSLFFNWKQEFRTLEVTLRDFSKLNKQDIRYLGKIFSSATSLRLQIKRCAGVAGSLSLVLSTCKNIYSLMVEASPLT 725
Cdd:COG4886 23 TLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 726 IEDERHITSVTNLKTLSIHDLQNQRLPggltDSLGNLKNLTKLIMDNIKMNEedaikLAEGLKNLKKMCLFHL--THLSD 803
Cdd:COG4886 103 LSGNEELSNLTNLESLDLSGNQLTDLP----EELANLTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLsnNQLTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 804 IGEGMDYIVK---------SLSSEPCDLEEI-QLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKdgnealhelID 873
Cdd:COG4886 174 LPEELGNLTNlkeldlsnnQITDLPEPLGNLtNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD---------LP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 874 RMNVLEQLTALmlpwgcDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQLNLAGNRVSSDG 953
Cdd:COG4886 245 ELGNLTNLEEL------DLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLL 318
|
..
gi 312433960 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 312433960 163 SPCIIEGESGKGKSTLLQRIAMLWGSGKCKALtkFKFVFFLRLSRAQG-----GLFETLCDQLLDIPGTIRKqtFMAMLL 237
Cdd:pfam05729 1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRsgnarSLADLLFSQWPEPAAPVSE--VWAVIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 238 KLRQRVLFLLDGYNEFKPQNCPE---------IEALIKENHRFKNMVIVTTTTECLRHIRQFGALT--AEVGDMTEDSAQ 306
Cdd:pfam05729 77 ELPERLLLILDGLDELVSDLGQLdgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
|
170
....*....|
gi 312433960 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 312433960 465 EEVTKGNGYLQKMVSISDITSTYSSLLRYTCGSSVEATRAVMKHLAAVYQH-GCLLGLSiakrplwrqESLQSVKNTTEQ 543
Cdd:pfam17889 1 EDQDLGLYYLKQINSILKAVSRYNNFLLYTCHSSTKAGPKIVSHLLHLVDHkESLENLS---------ENDDYLKHHPET 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 312433960 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 312433960 148 RVEQLTLNGLLQALQSPCIIEGESGKGKSTLLQRIAMLWGSGKCKALTKFKFVFFLRLSRAQGGLFETLCDQLLDIPGTI 227
Cdd:COG5635 166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLAEEASLEDLLAEALEKRGGEP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 228 RKQTfmAMLLKlRQRVLFLLDGYNEFKPQN-----CPEIEALIKENHRFKnmVIVTTTTECLRHIRQFGALTAEVGDMTE 302
Cdd:COG5635 246 EDAL--ERLLR-NGRLLLLLDGLDEVPDEAdrdevLNQLRRFLERYPKAR--VIITSRPEGYDSSELEGFEVLELAPLSD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 303 DSAQALIRE--VLIKELAEGLLLQIQKSRCLRNLMKTPLFVVITCAIQMGESEFhSHTQTTLFHTFYDLLI-----QKNK 375
Cdd:COG5635 321 EQIEEFLKKwfEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGEL-PDTRAELYEQFVELLLerwdeQRGL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 376 HKHKGVAASDFIRSLdhcGDLALEGVFSHKFDF---ELQ-----------DVSSVNEDVLLTTGLLCkytaQRFKPKYKF 441
Cdd:COG5635 400 TIYRELSREELRELL---SELALAMQENGRTEFareELEeilreylgrrkDAEALLDELLLRTGLLV----ERGEGRYSF 472
|
330 340
....*....|....*....|....*...
gi 312433960 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 312433960 1 MNFIKDNSRALIQRMgmTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPL 80
Cdd:pfam00619 1 RKLLKKNRVALVERL--GTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDL 78
|
....*..
gi 312433960 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 312433960 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 312433960 646 SRAVSLFFNWKQEFRTLEVTLRDFSKLNKQDIRYLGKIFSSATSLRLQIKRCAGVAGSLSLVLSTCKNIYSLMVEASPLT 725
Cdd:COG4886 23 TLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 726 IEDERHITSVTNLKTLSIHDLQNQRLPggltDSLGNLKNLTKLIMDNIKMNEedaikLAEGLKNLKKMCLFHL--THLSD 803
Cdd:COG4886 103 LSGNEELSNLTNLESLDLSGNQLTDLP----EELANLTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLsnNQLTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 804 IGEGMDYIVK---------SLSSEPCDLEEI-QLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKdgnealhelID 873
Cdd:COG4886 174 LPEELGNLTNlkeldlsnnQITDLPEPLGNLtNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD---------LP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 874 RMNVLEQLTALmlpwgcDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQLNLAGNRVSSDG 953
Cdd:COG4886 245 ELGNLTNLEEL------DLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLL 318
|
..
gi 312433960 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 312433960 738 LKTLSIHDLQNQRLPGGLTDSLGNLKNLTKL----IMDNikmneEDAIKLAEGLKNLKKMCLFHLTHLSDIGEG---MDY 810
Cdd:cd00116 53 LKELCLSLNETGRIPRGLQSLLQGLTKGCGLqeldLSDN-----ALGPDGCGVLESLLRSSSLQELKLNNNGLGdrgLRL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 811 IVKSLSSEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEAL-HELIDRMNvLEQL----TALM 885
Cdd:cd00116 128 LAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALaEGLKANCN-LEVLdlnnNGLT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 886 lPWGCdvqGSLSSLLKHLeevPQLVKLGLKNWRLTDTEIRILGAFFgKNPLKNFQQLNLAGNRVSSDGWLAFMGVFENLK 965
Cdd:cd00116 207 -DEGA---SALAETLASL---KSLEVLNLGDNNLTDAGAAALASAL-LSPNISLLTLSLSCNDITDDGAKDLAEVLAEKE 278
|
250
....*....|...
gi 312433960 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 312433960 163 SPCIIEGESGKGKSTLLQRIAMLWGSGKCKALtkFKFVFFLRLSRAQG-----GLFETLCDQLLDIPGTIRKqtFMAMLL 237
Cdd:pfam05729 1 RTVILQGEAGSGKTTLLQKLALLWAQGKLPQG--FDFVFFLPCRELSRsgnarSLADLLFSQWPEPAAPVSE--VWAVIL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 238 KLRQRVLFLLDGYNEFKPQNCPE---------IEALIKENHRFKNMVIVTTTTECLRHIRQFGALT--AEVGDMTEDSAQ 306
Cdd:pfam05729 77 ELPERLLLILDGLDELVSDLGQLdgpcpvltlLSSLLRKKLLPGASLLLTVRPDALRDLRRGLEEPryLEVRGFSESDRK 156
|
170
....*....|
gi 312433960 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 312433960 465 EEVTKGNGYLQKMVSISDITSTYSSLLRYTCGSSVEATRAVMKHLAAVYQH-GCLLGLSiakrplwrqESLQSVKNTTEQ 543
Cdd:pfam17889 1 EDQDLGLYYLKQINSILKAVSRYNNFLLYTCHSSTKAGPKIVSHLLHLVDHkESLENLS---------ENDDYLKHHPET 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 312433960 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 312433960 148 RVEQLTLNGLLQALQSPCIIEGESGKGKSTLLQRIAMLWGSGKCKALTKFKFVFFLRLSRAQGGLFETLCDQLLDIPGTI 227
Cdd:COG5635 166 RIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPIPILIELRDLAEEASLEDLLAEALEKRGGEP 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 228 RKQTfmAMLLKlRQRVLFLLDGYNEFKPQN-----CPEIEALIKENHRFKnmVIVTTTTECLRHIRQFGALTAEVGDMTE 302
Cdd:COG5635 246 EDAL--ERLLR-NGRLLLLLDGLDEVPDEAdrdevLNQLRRFLERYPKAR--VIITSRPEGYDSSELEGFEVLELAPLSD 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 303 DSAQALIRE--VLIKELAEGLLLQIQKSRCLRNLMKTPLFVVITCAIQMGESEFhSHTQTTLFHTFYDLLI-----QKNK 375
Cdd:COG5635 321 EQIEEFLKKwfEATERKAERLLEALEENPELRELARNPLLLTLLALLLRERGEL-PDTRAELYEQFVELLLerwdeQRGL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 376 HKHKGVAASDFIRSLdhcGDLALEGVFSHKFDF---ELQ-----------DVSSVNEDVLLTTGLLCkytaQRFKPKYKF 441
Cdd:COG5635 400 TIYRELSREELRELL---SELALAMQENGRTEFareELEeilreylgrrkDAEALLDELLLRTGLLV----ERGEGRYSF 472
|
330 340
....*....|....*....|....*...
gi 312433960 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 312433960 1 MNFIKDNSRALIQRMgmTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPL 80
Cdd:pfam00619 1 RKLLKKNRVALVERL--GTLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDL 78
|
....*..
gi 312433960 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 312433960 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 312433960 646 SRAVSLFFNWKQEFRTLEVTLRDFSKLNKQDIRYLGKIFSSATSLRLQIKRCAGVAGSLSLVLSTCKNIYSLMVEASPLT 725
Cdd:COG4886 23 TLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 726 IEDERHITSVTNLKTLSIHDLQNQRLPggltDSLGNLKNLTKLIMDNIKMNEedaikLAEGLKNLKKMCLFHL--THLSD 803
Cdd:COG4886 103 LSGNEELSNLTNLESLDLSGNQLTDLP----EELANLTNLKELDLSNNQLTD-----LPEPLGNLTNLKSLDLsnNQLTD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 804 IGEGMDYIVK---------SLSSEPCDLEEI-QLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKdgnealhelID 873
Cdd:COG4886 174 LPEELGNLTNlkeldlsnnQITDLPEPLGNLtNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTD---------LP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 874 RMNVLEQLTALmlpwgcDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQLNLAGNRVSSDG 953
Cdd:COG4886 245 ELGNLTNLEEL------DLSNNQLTDLPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLL 318
|
..
gi 312433960 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 312433960 738 LKTLSIHDLQNQRLPGGLTDSLGNLKNLTKL----IMDNikmneEDAIKLAEGLKNLKKMCLFHLTHLSDIGEG---MDY 810
Cdd:cd00116 53 LKELCLSLNETGRIPRGLQSLLQGLTKGCGLqeldLSDN-----ALGPDGCGVLESLLRSSSLQELKLNNNGLGdrgLRL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 811 IVKSLSSEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEAL-HELIDRMNvLEQL----TALM 885
Cdd:cd00116 128 LAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALaEGLKANCN-LEVLdlnnNGLT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 886 lPWGCdvqGSLSSLLKHLeevPQLVKLGLKNWRLTDTEIRILGAFFgKNPLKNFQQLNLAGNRVSSDGWLAFMGVFENLK 965
Cdd:cd00116 207 -DEGA---SALAETLASL---KSLEVLNLGDNNLTDAGAAALASAL-LSPNISLLTLSLSCNDITDDGAKDLAEVLAEKE 278
|
250
....*....|...
gi 312433960 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 312433960 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 312433960 754 GLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKMCLFHLTHlSDIG-EGMDYIVKSLSSEPcDLEEIQLVSCCL 832
Cdd:COG5238 283 ALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY-NGIGaQGAIALAKALQENT-TLHSLDLSDNQI 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312433960 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 312433960 722 SPLTIEDERHITSVT-----NLKTLSIHDLQNQRLPGGLTDSLGNLkNLTKLIMDNIKM--NEEDAIKLAEGLKNLKKMC 794
Cdd:COG5238 76 VALEKAAEAFPTQLLvvdweGAEEVSPVALAETATAVATPPPDLRR-IMAKTLEDSLILylALPRRINLIQVLKDPLGGN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 795 LFHLT-----HLSDIGEGMDYIVKSLSSEPCDL--EEIQLVSCCLSANAV---------------------KILAQNLHN 846
Cdd:COG5238 155 AVHLLglaarLGLLAAISMAKALQNNSVETVYLgcNQIGDEGIEELAEALtqnttvttlwlkrnpigdegaEILAEALKG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 847 LVKLSILDLSENYLekdGNEALHELIDRMNVLEQLTALMLpwGC---DVQGsLSSLLKHLEEVPQLVKLGLKNWRLTDTE 923
Cdd:COG5238 235 NKSLTTLDLSNNQI---GDEGVIALAEALKNNTTVETLYL--SGnqiGAEG-AIALAKALQGNTTLTSLDLSVNRIGDEG 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 312433960 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 312433960 754 GLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKmclfhLTHLS----DIG-EGMDYIVKSLSsEPCDLEEIQLV 828
Cdd:COG5238 199 ELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKS-----LTTLDlsnnQIGdEGVIALAEALK-NNTTVETLYLS 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 829 SCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEALHELIDRMNVLEQLTaLMLPwGCDVQGSLsSLLKHLEEVPQ 908
Cdd:COG5238 273 GNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLN-LAYN-GIGAQGAI-ALAKALQENTT 349
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312433960 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 312433960 3 FIKDNSRALIQRMgmTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPLFQ 82
Cdd:cd08329 10 LIRKNRMALFQHL--TCVLPILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFRNCLKEIDVVLYR 87
|
....*.
gi 312433960 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 312433960 731 HITSVTNLKTLSIHDlqNQRLPGG---LTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKMCLFHLTHlSDIG-E 806
Cdd:COG5238 231 ALKGNKSLTTLDLSN--NQIGDEGviaLAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSV-NRIGdE 307
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 312433960 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 312433960 713 NIYSLMVEASPLTIEDERHITSVTNLKTLSIHDLQNQRLPGGLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKK 792
Cdd:COG4886 1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 793 MCLFHLTHLSDIGEGMDYIVKSLSSEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLekdgnEALHELI 872
Cdd:COG4886 81 LLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-----TDLPEPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 873 DRMNVLEQLtalmlpwgcDVQG-SLSSLLKHLEEVPQLVKLGlknwrLTDTEIRILGAFFGKnpLKNFQQLNLAGNRVSS 951
Cdd:COG4886 156 GNLTNLKSL---------DLSNnQLTDLPEELGNLTNLKELD-----LSNNQITDLPEPLGN--LTNLEELDLSGNQLTD 219
|
250 260
....*....|....*....|..
gi 312433960 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 312433960 2 NFIKDNSRALIQRMgmTVIKQITDDLfVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPLF 81
Cdd:cd08330 1 HFVDRHREALIQRV--TNVDPILDEL-RGKVLTQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQALKETNPYLV 77
|
...
gi 312433960 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 312433960 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 312433960 804 -IGEGMdyivkSLSSEPcdlEEIQLVSCCL-----SANAVKILAQnLHNLVKLSILDLSENYLEKDgnEALHELIDRMNV 877
Cdd:cd21340 101 rLPPGE-----KLTFDP---RSLAALSNSLrvlniSGNNIDSLEP-LAPLRNLEQLDASNNQISDL--EELLDLLSSWPS 169
|
....
gi 312433960 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 312433960 703 SLSLVLSTCKNIYSLMVEASPLTiEDERHITSVTNLKTLSIHDLQNQRLPggltDSLGNLKNLTKLIMDNIKMNE-EDAI 781
Cdd:COG4886 150 DLPEPLGNLTNLKSLDLSNNQLT-DLPEELGNLTNLKELDLSNNQITDLP----EPLGNLTNLEELDLSGNQLTDlPEPL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 782 KlaeGLKNLKKMCLFHlTHLSDIGEgmdyiVKSLSSepcdLEEIQLvscclSANAVKILAqNLHNLVKLSILDLSENYLE 861
Cdd:COG4886 225 A---NLTNLETLDLSN-NQLTDLPE-----LGNLTN----LEELDL-----SNNQLTDLP-PLANLTNLKTLDLSNNQLT 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312433960 862 KDGNEALHELIDRMNVLEQLTALMLPWGCDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQ 941
Cdd:COG4886 286 DLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTL 365
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 312433960 942 LNLAGNRVSSDGWLAFMGVFENLKQLVFFDFSTKEFLPDPAL 983
Cdd:COG4886 366 LLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLAL 407
|
|
| |
