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Conserved domains on  [gi|1879298391|ref|NP_001372608|]
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TIR domain-containing adapter molecule 1 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TRIF-NTD super family cl39298
TRIF N-terminal domain; The N-terminal domain of TRIF/TICAM-1 has a structure that consists of ...
 1-103 2.87e-35

TRIF N-terminal domain; The N-terminal domain of TRIF/TICAM-1 has a structure that consists of eight antiparallel helices. This domain believed to be involved in self-regulation of TRIF by interacting with its TIR domain.


The actual alignment was detected with superfamily member pfam17798:

Pssm-ID: 436052  Cd Length: 157  Bit Score: 130.71  E-value: 2.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391   1 MVLLKLGQETEARISLEALKADAVARLVARQWAGVDSTED-------PEEPPDVSWAVARLYHLLAEEKLCPASLRDVAY 73
Cdd:pfam17798  46 MCLLTLKREAAARRKLDALRDDPVANHLAEKWHGGGKLDLngahcslEEKTAESLLAVARIYKLLVEERLCDASLRDKAY 125

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1879298391  74 QEAVRTLSSRDD--HRLGELQDEARNRCGWDI 103
Cdd:pfam17798 126 KAAVSAFRSGLDtsLELLDLREEARAVCGPDF 157
RHIM pfam12721
RIP homotypic interaction motif; RIP proteins are receptor-interacting serine ...
 632-651 4.56e-06

RIP homotypic interaction motif; RIP proteins are receptor-interacting serine/threonine-protein kinases or cell death proteins. This interacting domain is involved in virus recognition. The RHIM domain is necessary for the recruitment of RIP and RIP3 by the IFN-inducible protein DNA-dependent activator of IRFs (DAI), also known as DLM-1 or Z-DNA binding protein (ZBP1). Both the RIP kinases contribute to DAI-induced NF-kappaB activation. RIP3 undergoes auto phosphorylation on binding to DAI.


:

Pssm-ID: 463679  Cd Length: 21  Bit Score: 43.49  E-value: 4.56e-06
                          10        20
                  ....*....|....*....|
gi 1879298391 632 QPLIIHHAQMVQLGLNNHMW 651
Cdd:pfam12721   1 PPVIINNCSGVQIGNNNHMS 20
TIR_2 super family cl48220
TIR domain; This is a family of Toll-like receptors.
 352-445 9.48e-04

TIR domain; This is a family of Toll-like receptors.


The actual alignment was detected with superfamily member pfam13676:

Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 39.61  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391 352 FVILHARADEHIALRVREKLEALGVPdgaTFCEDFQVPGRGEL-SCLQDAIDHSAFIILLLTSNFdcrLSLHQVNQAMMS 430
Cdd:pfam13676   1 VFISYAGEDRAWAEWLADALEAAGYR---VWLDRWDIRPGDDWvEEIEEAIENSDRVLVVLSPNY---LESPWCRAEWEA 74

                          90
                  ....*....|....*
gi 1879298391 431 NLTRQGSPDCVIPFL 445
Cdd:pfam13676  75 ALADPEGRKRLIPVR 89
PABP-1234 super family cl31127
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 530-664 2.07e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


The actual alignment was detected with superfamily member TIGR01628:

Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 41.33  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391 530 QSYLSYQAQMEQLQV------AFGSHMSFGTGApygaRMPFGGQV---PLGAPPPFPTWPGCPQPPplhawQAGTPPPPS 600
Cdd:TIGR01628 373 DQFMQLQPRMRQLPMgspmggAMGQPPYYGQGP----QQQFNGQPlgwPRMSMMPTPMGPGGPLRP-----NGLAPMNAV 443

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879298391 601 PQPAAFPQSLPFPQSPAFPTASPAPPQSPGLQPLIIHHAQMVQLGLNNHMWNQRGSQAPEDKTQ 664
Cdd:TIGR01628 444 RAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQMQKQ 507
 
Name Accession Description Interval E-value
TRIF-NTD pfam17798
TRIF N-terminal domain; The N-terminal domain of TRIF/TICAM-1 has a structure that consists of ...
 1-103 2.87e-35

TRIF N-terminal domain; The N-terminal domain of TRIF/TICAM-1 has a structure that consists of eight antiparallel helices. This domain believed to be involved in self-regulation of TRIF by interacting with its TIR domain.


Pssm-ID: 436052  Cd Length: 157  Bit Score: 130.71  E-value: 2.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391   1 MVLLKLGQETEARISLEALKADAVARLVARQWAGVDSTED-------PEEPPDVSWAVARLYHLLAEEKLCPASLRDVAY 73
Cdd:pfam17798  46 MCLLTLKREAAARRKLDALRDDPVANHLAEKWHGGGKLDLngahcslEEKTAESLLAVARIYKLLVEERLCDASLRDKAY 125

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1879298391  74 QEAVRTLSSRDD--HRLGELQDEARNRCGWDI 103
Cdd:pfam17798 126 KAAVSAFRSGLDtsLELLDLREEARAVCGPDF 157
RHIM pfam12721
RIP homotypic interaction motif; RIP proteins are receptor-interacting serine ...
 632-651 4.56e-06

RIP homotypic interaction motif; RIP proteins are receptor-interacting serine/threonine-protein kinases or cell death proteins. This interacting domain is involved in virus recognition. The RHIM domain is necessary for the recruitment of RIP and RIP3 by the IFN-inducible protein DNA-dependent activator of IRFs (DAI), also known as DLM-1 or Z-DNA binding protein (ZBP1). Both the RIP kinases contribute to DAI-induced NF-kappaB activation. RIP3 undergoes auto phosphorylation on binding to DAI.


Pssm-ID: 463679  Cd Length: 21  Bit Score: 43.49  E-value: 4.56e-06
                          10        20
                  ....*....|....*....|
gi 1879298391 632 QPLIIHHAQMVQLGLNNHMW 651
Cdd:pfam12721   1 PPVIINNCSGVQIGNNNHMS 20
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 352-445 9.48e-04

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 39.61  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391 352 FVILHARADEHIALRVREKLEALGVPdgaTFCEDFQVPGRGEL-SCLQDAIDHSAFIILLLTSNFdcrLSLHQVNQAMMS 430
Cdd:pfam13676   1 VFISYAGEDRAWAEWLADALEAAGYR---VWLDRWDIRPGDDWvEEIEEAIENSDRVLVVLSPNY---LESPWCRAEWEA 74

                          90
                  ....*....|....*
gi 1879298391 431 NLTRQGSPDCVIPFL 445
Cdd:pfam13676  75 ALADPEGRKRLIPVR 89
TIR smart00255
Toll - interleukin 1 - resistance;
354-482 1.12e-03

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 39.61  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391  354 ILHARAD---EHIALRVREKLEALGVpdgaTFCEDFQVPGRGELSCLQDAIDHSAFIILLLTSNF-DCRLSLHQVnQAMM 429
Cdd:smart00255   6 ISYSGKEdvrNEFLSHLLEKLRGYGL----CVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYaESEWCLDEL-VAAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1879298391  430 SNLTRQGSpDCVIP-FL-PLESSPAQLSSDTASLL--SGLVRLDEHSQIFARKVANT 482
Cdd:smart00255  81 ENALEEGG-LRVIPiFYeVIPSDVRKQPGKFRKVFkkNYLKWPEDEKEQFWKKALYA 136
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 530-664 2.07e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 41.33  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391 530 QSYLSYQAQMEQLQV------AFGSHMSFGTGApygaRMPFGGQV---PLGAPPPFPTWPGCPQPPplhawQAGTPPPPS 600
Cdd:TIGR01628 373 DQFMQLQPRMRQLPMgspmggAMGQPPYYGQGP----QQQFNGQPlgwPRMSMMPTPMGPGGPLRP-----NGLAPMNAV 443

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879298391 601 PQPAAFPQSLPFPQSPAFPTASPAPPQSPGLQPLIIHHAQMVQLGLNNHMWNQRGSQAPEDKTQ 664
Cdd:TIGR01628 444 RAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQMQKQ 507
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 536-645 3.17e-03

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: 40.91  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391 536 QAQMEQLQVAFGSHMSFGTGAPYGARMPFGGQVPLGAPPPFPTWPGCPQPPPLHAWQAGTPPPPSPQPAAFPQSLPFPQS 615
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHP 247

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1879298391 616 PAFPTASPAPPQSPGLQPL--IIHHAQMVQLG 645
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPLpqPSLHGQMPPMP 279
 
Name Accession Description Interval E-value
TRIF-NTD pfam17798
TRIF N-terminal domain; The N-terminal domain of TRIF/TICAM-1 has a structure that consists of ...
 1-103 2.87e-35

TRIF N-terminal domain; The N-terminal domain of TRIF/TICAM-1 has a structure that consists of eight antiparallel helices. This domain believed to be involved in self-regulation of TRIF by interacting with its TIR domain.


Pssm-ID: 436052  Cd Length: 157  Bit Score: 130.71  E-value: 2.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391   1 MVLLKLGQETEARISLEALKADAVARLVARQWAGVDSTED-------PEEPPDVSWAVARLYHLLAEEKLCPASLRDVAY 73
Cdd:pfam17798  46 MCLLTLKREAAARRKLDALRDDPVANHLAEKWHGGGKLDLngahcslEEKTAESLLAVARIYKLLVEERLCDASLRDKAY 125

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1879298391  74 QEAVRTLSSRDD--HRLGELQDEARNRCGWDI 103
Cdd:pfam17798 126 KAAVSAFRSGLDtsLELLDLREEARAVCGPDF 157
RHIM pfam12721
RIP homotypic interaction motif; RIP proteins are receptor-interacting serine ...
 632-651 4.56e-06

RIP homotypic interaction motif; RIP proteins are receptor-interacting serine/threonine-protein kinases or cell death proteins. This interacting domain is involved in virus recognition. The RHIM domain is necessary for the recruitment of RIP and RIP3 by the IFN-inducible protein DNA-dependent activator of IRFs (DAI), also known as DLM-1 or Z-DNA binding protein (ZBP1). Both the RIP kinases contribute to DAI-induced NF-kappaB activation. RIP3 undergoes auto phosphorylation on binding to DAI.


Pssm-ID: 463679  Cd Length: 21  Bit Score: 43.49  E-value: 4.56e-06
                          10        20
                  ....*....|....*....|
gi 1879298391 632 QPLIIHHAQMVQLGLNNHMW 651
Cdd:pfam12721   1 PPVIINNCSGVQIGNNNHMS 20
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 352-445 9.48e-04

TIR domain; This is a family of Toll-like receptors.


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 39.61  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391 352 FVILHARADEHIALRVREKLEALGVPdgaTFCEDFQVPGRGEL-SCLQDAIDHSAFIILLLTSNFdcrLSLHQVNQAMMS 430
Cdd:pfam13676   1 VFISYAGEDRAWAEWLADALEAAGYR---VWLDRWDIRPGDDWvEEIEEAIENSDRVLVVLSPNY---LESPWCRAEWEA 74

                          90
                  ....*....|....*
gi 1879298391 431 NLTRQGSPDCVIPFL 445
Cdd:pfam13676  75 ALADPEGRKRLIPVR 89
TIR smart00255
Toll - interleukin 1 - resistance;
354-482 1.12e-03

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 39.61  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391  354 ILHARAD---EHIALRVREKLEALGVpdgaTFCEDFQVPGRGELSCLQDAIDHSAFIILLLTSNF-DCRLSLHQVnQAMM 429
Cdd:smart00255   6 ISYSGKEdvrNEFLSHLLEKLRGYGL----CVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYaESEWCLDEL-VAAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1879298391  430 SNLTRQGSpDCVIP-FL-PLESSPAQLSSDTASLL--SGLVRLDEHSQIFARKVANT 482
Cdd:smart00255  81 ENALEEGG-LRVIPiFYeVIPSDVRKQPGKFRKVFkkNYLKWPEDEKEQFWKKALYA 136
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
 530-664 2.07e-03

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 41.33  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391 530 QSYLSYQAQMEQLQV------AFGSHMSFGTGApygaRMPFGGQV---PLGAPPPFPTWPGCPQPPplhawQAGTPPPPS 600
Cdd:TIGR01628 373 DQFMQLQPRMRQLPMgspmggAMGQPPYYGQGP----QQQFNGQPlgwPRMSMMPTPMGPGGPLRP-----NGLAPMNAV 443

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1879298391 601 PQPAAFPQSLPFPQSPAFPTASPAPPQSPGLQPLIIHHAQMVQLGLNNHMWNQRGSQAPEDKTQ 664
Cdd:TIGR01628 444 RAPSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTASQGGQNKKLAQVLASATPQMQKQ 507
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 536-645 3.17e-03

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: 40.91  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1879298391 536 QAQMEQLQVAFGSHMSFGTGAPYGARMPFGGQVPLGAPPPFPTWPGCPQPPPLHAWQAGTPPPPSPQPAAFPQSLPFPQS 615
Cdd:pfam03154 168 QTQPPVLQAQSGAASPPSPPPPGTTQAATAGPTPSAPSVPPQGSPATSQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPHP 247

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1879298391 616 PAFPTASPAPPQSPGLQPL--IIHHAQMVQLG 645
Cdd:pfam03154 248 PLQPMTQPPPPSQVSPQPLpqPSLHGQMPPMP 279
 
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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