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Conserved domains on  [gi|672041543|ref|XP_008758983|]
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caspase recruitment domain-containing protein 6 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 11-79 8.94e-14

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: 67.54  E-value: 8.94e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672041543   11 IEKQRTKLLSVLqqDPDSILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFLKCL 79
Cdd:cd01671     1 LRKNRVELVEDL--DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEAL 67
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 782-1121 2.65e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 61.71  E-value: 2.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   782 TNCSAKSQQNQNGPFGRsQRQTSHPENRQTSRTRQRSGTAASHVGHIHSSGSQATKATGKPHSEKARAQGMQLTKAAGKS 861
Cdd:pfam03154  158 SDSSAQQQILQTQPPVL-QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPT 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   862 IRTQsHIKHPHP------QPCQPAgaiqeRIIPTSHQEAQRTTQGRPSDLAFKPG---------SQSTSGNKHSSASQYN 926
Cdd:pfam03154  237 LHPQ-RLPSPHPplqpmtQPPPPS-----QVSPQPLPQPSLHGQMPPMPHSLQTGpshmqhpvpPQPFPLTPQSSQSQVP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   927 SHPPNFQSKHFQPKPFQPvPSHSQPSQAKPTH---LNPSPANYTHVQP-------------SHAKPTHSKA---FQANSH 987
Cdd:pfam03154  311 PGPSPAAPGQSQQRIHTP-PSQSQLQSQQPPReqpLPPAPLSMPHIKPppttpipqlpnpqSHKHPPHLSGpspFQMNSN 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   988 HPHPSHAKPTHLNPSHANPT-HVQPSHAKPthsKAFQAKPTPSQTSWSQANSNHPHPSlakPSHPNPSHANPTHVQPSHA 1066
Cdd:pfam03154  390 LPPPPALKPLSSLSTHHPPSaHPPPLQLMP---QSQQLPPPPAQPPVLTQSQSLPPPA---ASHPPTSGLHQVPSQSPFP 463

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 672041543  1067 KPAHLQSSQTKPSPSQSTQFTAHKPQQSQSKPSQQRPSqpkSSQTKPSQARASHP 1121
Cdd:pfam03154  464 QHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVS---SSGPVPAAVSCPLP 515
 
Name Accession Description Interval E-value
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 11-79 8.94e-14

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: 67.54  E-value: 8.94e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672041543   11 IEKQRTKLLSVLqqDPDSILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFLKCL 79
Cdd:cd01671     1 LRKNRVELVEDL--DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEAL 67
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 9-93 5.99e-13

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: 65.27  E-value: 5.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543     9 EIIEKQRTKLLSVLQqDPDSILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFLKCLSNAFPQSAS 88
Cdd:pfam00619    2 KLLKKNRVALVERLG-TLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ....*
gi 672041543    89 TLGLK 93
Cdd:pfam00619   81 DLEGL 85
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 782-1121 2.65e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 61.71  E-value: 2.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   782 TNCSAKSQQNQNGPFGRsQRQTSHPENRQTSRTRQRSGTAASHVGHIHSSGSQATKATGKPHSEKARAQGMQLTKAAGKS 861
Cdd:pfam03154  158 SDSSAQQQILQTQPPVL-QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPT 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   862 IRTQsHIKHPHP------QPCQPAgaiqeRIIPTSHQEAQRTTQGRPSDLAFKPG---------SQSTSGNKHSSASQYN 926
Cdd:pfam03154  237 LHPQ-RLPSPHPplqpmtQPPPPS-----QVSPQPLPQPSLHGQMPPMPHSLQTGpshmqhpvpPQPFPLTPQSSQSQVP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   927 SHPPNFQSKHFQPKPFQPvPSHSQPSQAKPTH---LNPSPANYTHVQP-------------SHAKPTHSKA---FQANSH 987
Cdd:pfam03154  311 PGPSPAAPGQSQQRIHTP-PSQSQLQSQQPPReqpLPPAPLSMPHIKPppttpipqlpnpqSHKHPPHLSGpspFQMNSN 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   988 HPHPSHAKPTHLNPSHANPT-HVQPSHAKPthsKAFQAKPTPSQTSWSQANSNHPHPSlakPSHPNPSHANPTHVQPSHA 1066
Cdd:pfam03154  390 LPPPPALKPLSSLSTHHPPSaHPPPLQLMP---QSQQLPPPPAQPPVLTQSQSLPPPA---ASHPPTSGLHQVPSQSPFP 463

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 672041543  1067 KPAHLQSSQTKPSPSQSTQFTAHKPQQSQSKPSQQRPSqpkSSQTKPSQARASHP 1121
Cdd:pfam03154  464 QHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVS---SSGPVPAAVSCPLP 515
PHA03378 PHA03378
EBNA-3B; Provisional
 929-1082 1.09e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 59.70  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  929 PPNFQSKHFQPK-------PFQPVP---SHSQPSQAKPTHLNPSPANYTHVQPSHAKPTHSKAFQANSHHPHPSHAKPTH 998
Cdd:PHA03378  654 PPQVEITPYKPTwtqighiPYQPSPtgaNTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGR 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  999 LNPSHANPTHVQPSHAKPTHSKAFQAKPTPSQTswsqansnhPHPSLAKPSHPNPSHANPTHVQPSHAKPAHLQSSQTKP 1078
Cdd:PHA03378  734 ARPPAAAPGRARPPAAAPGRARPPAAAPGRARP---------PAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGP 804


                  ....
gi 672041543 1079 SPSQ 1082
Cdd:PHA03378  805 TSMQ 808
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 8-92 6.29e-07

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 48.49  E-value: 6.29e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543      8 SEIIEKQRTKLLSVLQqdPDSILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFLKCLSNAFPQSA 87
Cdd:smart00114    6 KRLLRRNRVRLGEELG--VDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQETDQKLA 83


                    ....*
gi 672041543     88 STLGL 92
Cdd:smart00114   84 DFLEL 88
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 907-1068 4.08e-05

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 47.96  E-value: 4.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  907 FKPGSQSTSGNKHSSASQYNSHPPNFQSKHFQPKPFQP-VPSHSQPSQAKPT-----HLNPSPANYTHVQPSHAKPT--- 977
Cdd:COG5422   113 FSPASDSLSFNPSSTQSRKDSGPGDGSPVQKRKNPLLPsSSTHGTHPPIVFTdnngsHAGAPNARSRKEIPSLGSQSmql 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  978 HSKAFQ---ANSHHPHPSHAKPTHLNPSHANPTHvqPSHAKPTHSKAFQAKPTPSQTSWSQANSnhphpslakpshpNPS 1054
Cdd:COG5422   193 PSPHFRqkfSSSDTSNGFSYPSIRKNSRHSSNSM--PSFPHSSTAVLLKRHSGSSGASLISSNI-------------TPS 257

                         170
                  ....*....|....
gi 672041543 1055 HANPTHVQPSHAKP 1068
Cdd:COG5422   258 SSNSEAMSTSSKRP 271
 
Name Accession Description Interval E-value
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 11-79 8.94e-14

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: 67.54  E-value: 8.94e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672041543   11 IEKQRTKLLSVLqqDPDSILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFLKCL 79
Cdd:cd01671     1 LRKNRVELVEDL--DVEDILDHLIQKGVLTEEDKEEILSEKTRQDKARKLLDILPRRGPKAFEVFCEAL 67
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 9-93 5.99e-13

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: 65.27  E-value: 5.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543     9 EIIEKQRTKLLSVLQqDPDSILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFLKCLSNAFPQSAS 88
Cdd:pfam00619    2 KLLKKNRVALVERLG-TLDGLLDYLLEKNVLTEEEEEKIKANPTRLDKARELLDLVLKKGPKACQIFLEALKEGDPDLAS 80


                   ....*
gi 672041543    89 TLGLK 93
Cdd:pfam00619   81 DLEGL 85
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 782-1121 2.65e-09

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 61.71  E-value: 2.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   782 TNCSAKSQQNQNGPFGRsQRQTSHPENRQTSRTRQRSGTAASHVGHIHSSGSQATKATGKPHSEKARAQGMQLTKAAGKS 861
Cdd:pfam03154  158 SDSSAQQQILQTQPPVL-QAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPT 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   862 IRTQsHIKHPHP------QPCQPAgaiqeRIIPTSHQEAQRTTQGRPSDLAFKPG---------SQSTSGNKHSSASQYN 926
Cdd:pfam03154  237 LHPQ-RLPSPHPplqpmtQPPPPS-----QVSPQPLPQPSLHGQMPPMPHSLQTGpshmqhpvpPQPFPLTPQSSQSQVP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   927 SHPPNFQSKHFQPKPFQPvPSHSQPSQAKPTH---LNPSPANYTHVQP-------------SHAKPTHSKA---FQANSH 987
Cdd:pfam03154  311 PGPSPAAPGQSQQRIHTP-PSQSQLQSQQPPReqpLPPAPLSMPHIKPppttpipqlpnpqSHKHPPHLSGpspFQMNSN 389

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   988 HPHPSHAKPTHLNPSHANPT-HVQPSHAKPthsKAFQAKPTPSQTSWSQANSNHPHPSlakPSHPNPSHANPTHVQPSHA 1066
Cdd:pfam03154  390 LPPPPALKPLSSLSTHHPPSaHPPPLQLMP---QSQQLPPPPAQPPVLTQSQSLPPPA---ASHPPTSGLHQVPSQSPFP 463

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 672041543  1067 KPAHLQSSQTKPSPSQSTQFTAHKPQQSQSKPSQQRPSqpkSSQTKPSQARASHP 1121
Cdd:pfam03154  464 QHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVS---SSGPVPAAVSCPLP 515
PHA03378 PHA03378
EBNA-3B; Provisional
 929-1082 1.09e-08

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 59.70  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  929 PPNFQSKHFQPK-------PFQPVP---SHSQPSQAKPTHLNPSPANYTHVQPSHAKPTHSKAFQANSHHPHPSHAKPTH 998
Cdd:PHA03378  654 PPQVEITPYKPTwtqighiPYQPSPtgaNTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGR 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  999 LNPSHANPTHVQPSHAKPTHSKAFQAKPTPSQTswsqansnhPHPSLAKPSHPNPSHANPTHVQPSHAKPAHLQSSQTKP 1078
Cdd:PHA03378  734 ARPPAAAPGRARPPAAAPGRARPPAAAPGRARP---------PAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQAGP 804


                  ....
gi 672041543 1079 SPSQ 1082
Cdd:PHA03378  805 TSMQ 808
CARD_NOD2_1_CARD15 cd08787
Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and ...
 11-88 2.97e-07

Caspase activation and recruitment domain of NOD2, repeat 1; Caspase activation and recruitment domain (CARD) similar to that found in human NOD2 (CARD15), repeat 1. NOD2 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD2, as well as NOD1, the N-terminal effector domain is a CARD. NOD2 contains two N-terminal CARD repeats. Mutations in NOD2 have been associated with Crohns disease and Blau syndrome. Nod2-CARDs have been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. 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: 176765  Cd Length: 87  Bit Score: 49.15  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   11 IEKQRTKLLSVL----QQDP-DSILDTLTSRRLISEEEYETLEAITDPL-KKSRKLLILIQKKGEDSCCCFLKCLSNAFP 84
Cdd:cd08787     1 FLAQRSELLEVLcsggSLEPfESVLDWLLSQEVLSWEDYEGFHVLGQPLsHNARQLLDTVYNKGEWACQKFLAAAQQALA 80


                  ....
gi 672041543   85 QSAS 88
Cdd:cd08787    81 EEQS 84
CARD smart00114
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. ...
 8-92 6.29e-07

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signalling. Mediates homodimerisation. Structure consists of six antiparallel helices arranged in a topology homologue to the DEATH and the DED domain.


Pssm-ID: 128424  Cd Length: 88  Bit Score: 48.49  E-value: 6.29e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543      8 SEIIEKQRTKLLSVLQqdPDSILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFLKCLSNAFPQSA 87
Cdd:smart00114    6 KRLLRRNRVRLGEELG--VDGLLDYLVEKNVLTEKEIEAIKAATTKLRDKRELVDSLQKRGSQAFDTFLDSLQETDQKLA 83


                    ....*
gi 672041543     88 STLGL 92
Cdd:smart00114   84 DFLEL 88
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 803-1074 3.19e-06

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 51.61  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  803 TSHPENRQTSRT------RQRSGTAASHVGHIHSSGSQATKATgkphsekaraQGMQLTKAAGKSIRTQSHIKHPHPQPC 876
Cdd:PTZ00395  247 TSPPANENNAVTlscsndQQRGASSAAESGYAHHRGSNIASHT----------PNDNIMHAANNPLNNTNDAQRNAIQGD 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  877 QPAGAIQERiiPTSHQEAQRTTQgrpsdlaFKPGSQSTSGNKHSSASQYNSHPPNFQSKHFqpkpfqpvpSHSQPSQAKP 956
Cdd:PTZ00395  317 LVRGAPNDK--NSFDRGNEKTYQ-------IYGGFHDGSPNAASAGAPFNGLGNQADGGHI---------NQVHPDARGA 378

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  957 THLNPSpANYTHVQPSHAKPTHSKAFQANSHHPHPSHAKPTHLNPSHANPTHVQPSHAKPTHSKAFQAKPTPSQTSWSQ- 1035
Cdd:PTZ00395  379 WAGGPH-SNASYNCAAYSNAAQSNAAQSNAGFSNAGYSNPGNSNPGYNNAPNSNTPYNNPPNSNTPYSNPPNSNPPYSNl 457

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 672041543 1036 --ANSNHPHPSL--AKPS----HPNPSHANPTHV---QPSHAKPAHLQSS 1074
Cdd:PTZ00395  458 pySNTPYSNAPLsnAPPSsakdHHSAYHAAYQHRaanQPAANLPTANQPA 507
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 869-1062 7.02e-06

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 50.42  E-value: 7.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   869 KHPHPQPCQPAGAIQERIIPTSHQ-------EAQRTTQgrpsdlAFKPGSQSTSGNKHSSASQYNSHPPNFQSKHFQPKP 941
Cdd:pfam09770  169 KAAAPAPAPQPAAQPASLPAPSRKmmsleevEAAMRAQ------AKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQ 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   942 FQPVPSHSQPSQAKPTHLNPsPANYTHVQPSHAKPthskafqanshhPHPSHAKPTHLNPSHANPTHVQPSHAKPT---H 1018
Cdd:pfam09770  243 QQQPQQQPQQPQQHPGQGHP-VTILQRPQSPQPDP------------AQPSIQPQAQQFHQQPPPVPVQPTQILQNpnrL 309

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 672041543  1019 SKAFQAKPTPSQTSWSQANSNHPHPSLAKPSHPNPSHANPTHVQ 1062
Cdd:pfam09770  310 SAARVGYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQLA 353
AF-4 pfam05110
AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and ...
 871-1064 1.78e-05

AF-4 proto-oncoprotein N-terminal region; This family consists of AF4 (Proto-oncogene AF4) and FMR2 (Fragile X E mental retardation syndrome) nuclear proteins. These proteins have been linked to human diseases such as acute lymphoblastic leukaemia and mental retardation. The family also contains a Drosophila AF4 protein homolog Lilliputian which contains an AT-hook domain. Lilliputian represents a novel pair-rule gene that acts in cytoskeleton regulation, segmentation and morphogenesis in Drosophila.


Pssm-ID: 461550 [Multi-domain]  Cd Length: 514  Bit Score: 48.58  E-value: 1.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   871 PHPQPCQPA-GAIQERIIPTSHQEAQRTTQGRPSdlafkPGSQSTSGNKHSSASQYNSHPPNFQ--SKHFQPKPFQPVPS 947
Cdd:pfam05110   84 PQEKPDQPFfPDKTSGLPPSFHTSSHSQPMGPPS-----SSSPSVSSSQSQKKSQARTEPAHGGhsSSGSQSSQRSQGQS 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   948 HSQPSQAKPTHLNPSPANYTHVQPSHAKPTHSKAFQANSHHPHPSHAKPthLNPSHAN-PTHVQPSHAKPTHSKAFQAKP 1026
Cdd:pfam05110  159 RSKGGQESHSSSHHKRQERREDLFSCASLSHSLEELSPLLSSLSSPVKP--LSPSHSRqHTGSKAQNSSDHHGKEYSHSK 236

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 672041543  1027 TP--SQTSWSQANSNHPHPSLAKPSHPNPSHANPTHVQPS 1064
Cdd:pfam05110  237 SPrdSEAGSHGPESPSTSLLASSSQLSSQTFPPSLPSKTS 276
PHA03378 PHA03378
EBNA-3B; Provisional
 939-1122 2.15e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 48.91  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  939 PKPFQPV--PSHSQPSQAKPTHL---NPSPANYTHVQPShAKPTHSKAFQANSHHPHPSHAKPTHlnPSHANPTHVQPSh 1013
Cdd:PHA03378  571 PLQIQPLtsPTTSQLASSAPSYAqtpWPVPHPSQTPEPP-TTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPITFNVL- 646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543 1014 AKPTHSKAFQAKPTPSQTSWSQANSNHPHPSLAKPSHPNPSHANPTHVQPSHAKPAHLQSSQTKPSPSQSTQFTAHKPQQ 1093
Cdd:PHA03378  647 VFPTPHQPPQVEITPYKPTWTQIGHIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARP 726

                         170       180
                  ....*....|....*....|....*....
gi 672041543 1094 SQSKPSQQRPSQPKSSQTKPSQARASHPR 1122
Cdd:PHA03378  727 PAAAPGRARPPAAAPGRARPPAAAPGRAR 755
ROM1 COG5422
RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction ...
 907-1068 4.08e-05

RhoGEF, Guanine nucleotide exchange factor for Rho/Rac/Cdc42-like GTPases [Signal transduction mechanisms];


Pssm-ID: 227709 [Multi-domain]  Cd Length: 1175  Bit Score: 47.96  E-value: 4.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  907 FKPGSQSTSGNKHSSASQYNSHPPNFQSKHFQPKPFQP-VPSHSQPSQAKPT-----HLNPSPANYTHVQPSHAKPT--- 977
Cdd:COG5422   113 FSPASDSLSFNPSSTQSRKDSGPGDGSPVQKRKNPLLPsSSTHGTHPPIVFTdnngsHAGAPNARSRKEIPSLGSQSmql 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  978 HSKAFQ---ANSHHPHPSHAKPTHLNPSHANPTHvqPSHAKPTHSKAFQAKPTPSQTSWSQANSnhphpslakpshpNPS 1054
Cdd:COG5422   193 PSPHFRqkfSSSDTSNGFSYPSIRKNSRHSSNSM--PSFPHSSTAVLLKRHSGSSGASLISSNI-------------TPS 257

                         170
                  ....*....|....
gi 672041543 1055 HANPTHVQPSHAKP 1068
Cdd:COG5422   258 SSNSEAMSTSSKRP 271
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 806-1123 5.32e-05

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 47.60  E-value: 5.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   806 PENRQTSRTRQRSGTAASHVGHIHSSGSQATKATGKPHSEKARAQGMQLTKA--AGKSIRTQSHIKHPHPQPCQPAGAIQ 883
Cdd:pfam05109  425 PESTTTSPTLNTTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADVTSPtpAGTTSGASPVTPSPSPRDNGTESKAP 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   884 ERIIPTSHQEAQRTTQGRPSDLAFKPGSQSTSGN--KHSSASQYNSHPPNFQSkhfqPKPFQPVPShsqPSQAKPTHLNP 961
Cdd:pfam05109  505 DMTSPTSAVTTPTPNATSPTPAVTTPTPNATSPTlgKTSPTSAVTTPTPNATS----PTPAVTTPT---PNATIPTLGKT 577

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   962 SPAN-YTHVQPSHAKPTHSKAF-QANS--HHPHPSHAKPTHLNPSHANPTHVQPSHAKPTHSKAFQAKPTPSQTSW---- 1033
Cdd:pfam05109  578 SPTSaVTTPTPNATSPTVGETSpQANTtnHTLGGTSSTPVVTSPPKNATSAVTTGQHNITSSSTSSMSLRPSSISEtlsp 657

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  1034 SQANSNHPHPSLAKPSHPNPSHaNPTHVQPSHAKPAHLQSSQTKPSPSQSTQFTAhkpqqSQSKPSQQRPSQPKSSQTKP 1113
Cdd:pfam05109  658 STSDNSTSHMPLLTSAHPTGGE-NITQVTPASTSTHHVSTSSPAPRPGTTSQASG-----PGNSSTSTKPGEVNVTKGTP 731

                          330
                   ....*....|
gi 672041543  1114 SQaRASHPRA 1123
Cdd:pfam05109  732 PK-NATSPQA 740
PHA03247 PHA03247
large tegument protein UL36; Provisional
 795-1123 6.24e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 47.63  E-value: 6.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  795 PFGRSQRQTSHPENRQTSRTRQRSGTAASHVGHIhsSGSQATKATGKPHSEKARAQGMQlTKAAGKSIRTQSHIKHPHPQ 874
Cdd:PHA03247 2628 PPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRV--SRPRRARRLGRAAQASSPPQRPR-RRAARPTVGSLTSLADPPPP 2704

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  875 PCQPAGAiqeriiPTSHQEAQRTTQGRPSDLAFKPGSQSTSGNKHSSASQYNSHPPNFQSKHFQPK-PFQPVPSHSQPSQ 953
Cdd:PHA03247 2705 PPTPEPA------PHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAgPPAPAPPAAPAAG 2778

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  954 AKPThlNPSPANYTHVQPSHAKPTHSKAFQANSHHPHPSHAKPTHLNPSHANPTHVQPSHAKPTHSKAFQAKPTPSQTSW 1033
Cdd:PHA03247 2779 PPRR--LTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSV 2856

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543 1034 S-------QANSNHPHPSLAKPSHPNPShanpthvqpSHAKPAHLQSSQTKPSPSQSTQFTAHKPQQSQSKPSQQRPSQP 1106
Cdd:PHA03247 2857 ApggdvrrRPPSRSPAAKPAAPARPPVR---------RLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP 2927

                         330
                  ....*....|....*..
gi 672041543 1107 KSSQTKPSQARASHPRA 1123
Cdd:PHA03247 2928 QPQPPPPPPPRPQPPLA 2944
PHA03378 PHA03378
EBNA-3B; Provisional
 914-1121 7.05e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.98  E-value: 7.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  914 TSGNKHSSASQYNSHPPNFQSKHFQPKPFQPVPSHsqPSQAKPTHLNPsPANYTHVQPSHAKPTHSKafqanshhphPSH 993
Cdd:PHA03378  600 PHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMR--PLRMQPITFNV-LVFPTPHQPPQVEITPYK----------PTW 666

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  994 AKPTHLNpshanpthVQPSHAKPTHSKAFQAKPTPSQtswsqansnhphPSLAKPSHPNPSHANPTHVQPSHAKPAHLQS 1073
Cdd:PHA03378  667 TQIGHIP--------YQPSPTGANTMLPIQWAPGTMQ------------PPPRAPTPMRPPAAPPGRAQRPAAATGRARP 726

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 672041543 1074 SQTKPSPSQSTQFTAHKPQQSQSKPSQQRPSQPKSSQTKPSQARASHP 1121
Cdd:PHA03378  727 PAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAP 774
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 798-1113 1.05e-04

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.68  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   798 RSQRQTShPENRQTSRTRQRSGTAASHVGHIHSSGSQATKATgKPHSEKARAQGMQLTKAAGKSIRTQSHIKHPHPQPCQ 877
Cdd:pfam03154   40 RSSGRNS-PSAASTSSNDSKAESMKKSSKKIKEEAPSPLKSA-KRQREKGASDTEEPERATAKKSKTQEISRPNSPSEGE 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   878 PAGAIQERIIPTSHQEAQRTTQGRPSDLAFKPGSQSTSGNKHSSASQ--YNSHPPNFQSKHFQPKPFQ-PVPSHSQPSQA 954
Cdd:pfam03154  118 GESSDGRSVNDEGSSDPKDIDQDNRSTSPSIPSPQDNESDSDSSAQQqiLQTQPPVLQAQSGAASPPSpPPPGTTQAATA 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543   955 KPTHLNPS-------PANYTHVQPSHAKPTHSKAFQANSHHPH--PSHAKPTHLNPSHANPTHVQPshakpthskafQAK 1025
Cdd:pfam03154  198 GPTPSAPSvppqgspATSQPPNQTQSTAAPHTLIQQTPTLHPQrlPSPHPPLQPMTQPPPPSQVSP-----------QPL 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  1026 PTPSQtswsqansNHPHPSLAKPSHPNPSHANptHVQPSHAKPAHLQSSQTKPSPSQSTQFTAHKPQQSQSKPSQQRPSQ 1105
Cdd:pfam03154  267 PQPSL--------HGQMPPMPHSLQTGPSHMQ--HPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQS 336


                   ....*...
gi 672041543  1106 PKSSQTKP 1113
Cdd:pfam03154  337 QQPPREQP 344
CARD_BIRC2_BIRC3 cd08329
Caspase activation and recruitment domain found in Baculoviral IAP repeat-containing proteins, ...
 1-79 5.13e-04

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: 40.12  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543    1 MASEGASseIIEKQRTKLL----SVLqqdpdSILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFL 76
Cdd:cd08329     3 MASDDLS--LIRKNRMALFqhltCVL-----PILDHLLSANVITEQEYDVIKQKTQTPLQARELIDTILVKGNAAAEVFR 75


                  ...
gi 672041543   77 KCL 79
Cdd:cd08329    76 NCL 78
PHA03247 PHA03247
large tegument protein UL36; Provisional
 831-1074 5.58e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  831 SGSQATKATGKPHSEKARAQGMQLTKAagksirTQSHIKHPHPQPCQPAGAIQERIIPTSHQEAQRTTQGRPSDLAfKPG 910
Cdd:PHA03247 2868 SRSPAAKPAAPARPPVRRLARPAVSRS------TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPP-RPQ 2940

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  911 SQSTSGNKHSSASQYNSHPPNFQSKHFQPKPFqPVPSHSQPSQAKPThlnPSPANYTHVQPSHAKPTHSKAFQANSHHPH 990
Cdd:PHA03247 2941 PPLAPTTDPAGAGEPSGAVPQPWLGALVPGRV-AVPRFRVPQPAPSR---EAPASSTPPLTGHSLSRVSSWASSLALHEE 3016

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  991 PSHaKPTHLNPSHANPTHVQPSHAkpthSKAFQAKPTPSQTSWSQANSNHPHPSLAKPSHPNPSHANPTHVQPSHAKPAH 1070
Cdd:PHA03247 3017 TDP-PPVSLKQTLWPPDDTEDSDA----DSLFDSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSSQFGPPP 3091


                  ....
gi 672041543 1071 LQSS 1074
Cdd:PHA03247 3092 LSAN 3095
CARD_NOD1_CARD4 cd08324
Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation ...
 29-79 1.04e-03

Caspase activation and recruitment domain similar to that found in NOD1; Caspase activation and recruitment domain (CARD) found in human NOD1 (CARD4) and similar proteins. NOD1 is a member of the Nod-like receptor (NLR) family, which plays a central role in the innate immune response. NLRs typically contain an N-terminal effector domain, a central nucleotide-binding domain and a C-terminal ligand-binding region of several leucine-rich repeats (LRRs). In NOD1, as well as NOD2, the N-terminal effector domain is a CARD. Nod1-CARD has been shown to interact with the CARD domain of the downstream effector RICK (RIP2, CARDIAK), a serine/threonine kinase. 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: 260035  Cd Length: 85  Bit Score: 39.00  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 672041543   29 ILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFLKCL 79
Cdd:cd08324    20 LLDNLLKNGYFSTEDAEIVQRCPTQTDKVRKILDLVQSKGEEVSEFFIYIL 70
CARD_ASC_NALP1 cd08330
Caspase activation and recruitment domain found in Human ASC, NALP1, and similar proteins; ...
 27-79 1.52e-03

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: 38.35  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 672041543   27 DSILDTLTSRRLiSEEEYETLEAITDPLKKSRKLLILIQKKGEDSCCCFLKCL 79
Cdd:cd08330    18 DPILDELRGKVL-TQEQYSSIRAERTNQEKMRKLYELVPSWGRTCKDLFYQAL 69
PHA03378 PHA03378
EBNA-3B; Provisional
 902-1126 1.64e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 42.75  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  902 PSDLAFKPGSQSTSGNKHSSASQY--NSHPPNFQSKHFQPKPFQPVPSHSQPSQAKPTHLNPSPANYTHVQPShakpths 979
Cdd:PHA03378  569 LGPLQIQPLTSPTTSQLASSAPSYaqTPWPVPHPSQTPEPPTTQSHIPETSAPRQWPMPLRPIPMRPLRMQPI------- 641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  980 kafqANSHHPHPSHAKPTHLNPSHANPTHVQPSH-------AKPTHSKAFQAKPTPSQTSwSQANSNHPHPSlAKPSHPN 1052
Cdd:PHA03378  642 ----TFNVLVFPTPHQPPQVEITPYKPTWTQIGHipyqpspTGANTMLPIQWAPGTMQPP-PRAPTPMRPPA-APPGRAQ 715

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672041543 1053 PSHANPTHVQPSHAKPAHLQSSQTKPSPSQSTQFTAHKPQQSQSKPSQQRPSQPKSSQTKPSQARASHPRAGRR 1126
Cdd:PHA03378  716 RPAAATGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQR 789
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 941-1115 1.95e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.38  E-value: 1.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  941 PFQPVPSHSQPSQAKPTHLNPSPANYThvqpshakPTHSKAFQANSHHPHPSHAKPTHLNPSH-ANPTHVQPSHAKPTHS 1019
Cdd:PRK10263  342 QTPPVASVDVPPAQPTVAWQPVPGPQT--------GEPVIAPAPEGYPQQSQYAQPAVQYNEPlQQPVQPQQPYYAPAAE 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543 1020 KAFQAkPTPSQTSWSQANSNHPHPSLAKPSHPNPSHANPThvQPSHAKPAHLQSSQTKPSPSqsTQFTAHKPQQSQSKPS 1099
Cdd:PRK10263  414 QPAQQ-PYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQ--QSTFAPQSTYQTEQTYQQPA--AQEPLYQQPQPVEQQP 488

                         170
                  ....*....|....*.
gi 672041543 1100 QQRPsQPKSSQTKPSQ 1115
Cdd:PRK10263  489 VVEP-EPVVEETKPAR 503
CARD_RIP2_CARD3 cd08786
Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase ...
 9-72 2.29e-03

Caspase activation and recruitment domain of Receptor Interacting Protein 2; Caspase activation and recruitment domain (CARD) of Receptor Interacting Protein 2 (RIP2/RIPK2/RICK/CARDIAK/CARD3). RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP2 harbors a C-terminal CARD domain and functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR)-family, NOD1 and NOD2, which recognizes bacterial peptidoglycans released upon infection. This cascade is implicated in inflammatory immune responses and the clearance of intracellular pathogens. RIP2 associates with NOD1 and NOD2 via CARD-CARD interactions. 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: 176764  Cd Length: 87  Bit Score: 38.37  E-value: 2.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672041543    9 EIIEKQRTKLLSVLQQDP-DSILDTLTSRRLISEEEYETLEAITDPLKKSRKLLILIQKKGEDSC 72
Cdd:cd08786     1 QWIASKREEIVSQMTEAClNQSLDALLSRQLLMREDYELISTKPTRTSKVRQLLDTCDCQGEEFA 65
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 832-1081 7.69e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.54  E-value: 7.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  832 GSQATKATGKPHSEKARA-----QGMQLTKAAGKSIRTQSHIKHPHPQPCQPAGAiqeriiptshqeaQRTTQGRPSDLA 906
Cdd:PHA03307  148 PAASPPAAGASPAAVASDaassrQAALPLSSPEETARAPSSPPAEPPPSTPPAAA-------------SPRPPRRSSPIS 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  907 FKPGSQSTSGNKHS----SASQYNSHPPNFQSKHFQPKPFQPVPSHSqPSQAKPTHLNPSPANYTHVQPSHAKPthSKAF 982
Cdd:PHA03307  215 ASASSPAPAPGRSAaddaGASSSDSSSSESSGCGWGPENECPLPRPA-PITLPTRIWEASGWNGPSSRPGPASS--SSSP 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672041543  983 QANSHHPHPSHAKPTHLNPSHANPTHVQPSHAKPThSKAFQAKPTPSQTSWSQANSNHPHPSLAKPSHPNPSHANPTHVQ 1062
Cdd:PHA03307  292 RERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSS-SSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPR 370

                         250
                  ....*....|....*....
gi 672041543 1063 PSHAKPAhlqSSQTKPSPS 1081
Cdd:PHA03307  371 PSRAPSS---PAASAGRPT 386
 
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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