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Conserved domains on  [gi|1622890924|ref|XP_014978020|]
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TIR domain-containing adapter molecule 1 isoform X1 [Macaca mulatta]

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 ...
 1-148 2.69e-49

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: 170.00  E-value: 2.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890924   1 MACTGPSLPSAFDILGAAGQDKLLYLKHKLKTPRPGCQGQDLLHAMVLLKLGQETEARISLEALKADAAARLVARQWAGV 80
Cdd:pfam17798   1 SEGLGPSLRGVFDILSQAPQEKLLSLTHKLKCERGGSPEDDLLHAMCLLTLKREAAARRKLDALRDDPVANHLAEKWHGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622890924  81 DSTED-------PEEPPDVSWTVARLYHLLAEEKLCPASLRDVAYQEALHTLSSRDD--HRLGELQDEARNRCGWDV 148
Cdd:pfam17798  81 GKLDLngahcslEEKTAESLLAVARIYKLLVEERLCDASLRDKAYKAAVSAFRSGLDtsLELLDLREEARAVCGPDF 157
RHIM pfam12721
RIP homotypic interaction motif; RIP proteins are receptor-interacting serine ...
 676-695 4.85e-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: 4.85e-06
                          10        20
                  ....*....|....*....|
gi 1622890924 676 QPLIIHHAQMVQLGLNNHMW 695
Cdd:pfam12721   1 PPVIINNCSGVQIGNNNHMS 20
TIR_2 super family cl48220
TIR domain; This is a family of Toll-like receptors.
 396-489 1.26e-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: 41.92  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890924 396 FVILHARADEHIALRVREKLEALGVPdgaTFCEDFQVPGRGEL-SCLQDAIDHSAFIILLLTPNFdchLSLHQVNQAMMS 474
Cdd:pfam13676   1 VFISYAGEDRAWAEWLADALEAAGYR---VWLDRWDIRPGDDWvEEIEEAIENSDRVLVVLSPNY---LESPWCRAEWEA 74

                          90
                  ....*....|....*
gi 1622890924 475 NLKRQGSPDCVIPFL 489
Cdd:pfam13676  75 ALADPEGRKRLIPVR 89
 
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 ...
 1-148 2.69e-49

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: 170.00  E-value: 2.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890924   1 MACTGPSLPSAFDILGAAGQDKLLYLKHKLKTPRPGCQGQDLLHAMVLLKLGQETEARISLEALKADAAARLVARQWAGV 80
Cdd:pfam17798   1 SEGLGPSLRGVFDILSQAPQEKLLSLTHKLKCERGGSPEDDLLHAMCLLTLKREAAARRKLDALRDDPVANHLAEKWHGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622890924  81 DSTED-------PEEPPDVSWTVARLYHLLAEEKLCPASLRDVAYQEALHTLSSRDD--HRLGELQDEARNRCGWDV 148
Cdd:pfam17798  81 GKLDLngahcslEEKTAESLLAVARIYKLLVEERLCDASLRDKAYKAAVSAFRSGLDtsLELLDLREEARAVCGPDF 157
RHIM pfam12721
RIP homotypic interaction motif; RIP proteins are receptor-interacting serine ...
 676-695 4.85e-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: 4.85e-06
                          10        20
                  ....*....|....*....|
gi 1622890924 676 QPLIIHHAQMVQLGLNNHMW 695
Cdd:pfam12721   1 PPVIINNCSGVQIGNNNHMS 20
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 396-489 1.26e-04

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


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 41.92  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890924 396 FVILHARADEHIALRVREKLEALGVPdgaTFCEDFQVPGRGEL-SCLQDAIDHSAFIILLLTPNFdchLSLHQVNQAMMS 474
Cdd:pfam13676   1 VFISYAGEDRAWAEWLADALEAAGYR---VWLDRWDIRPGDDWvEEIEEAIENSDRVLVVLSPNY---LESPWCRAEWEA 74

                          90
                  ....*....|....*
gi 1622890924 475 NLKRQGSPDCVIPFL 489
Cdd:pfam13676  75 ALADPEGRKRLIPVR 89
TIR smart00255
Toll - interleukin 1 - resistance;
398-526 3.95e-04

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 41.15  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890924  398 ILHARAD---EHIALRVREKLEALGVpdgaTFCEDFQVPGRGELSCLQDAIDHSAFIILLLTPNF-DCHLSLHQVnQAMM 473
Cdd:smart00255   6 ISYSGKEdvrNEFLSHLLEKLRGYGL----CVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYaESEWCLDEL-VAAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622890924  474 SNLKRQGSpDCVIP-FL-PLESSPAQLSSDTASLL--SGLVRLDEHSQIFARKVANT 526
Cdd:smart00255  81 ENALEEGG-LRVIPiFYeVIPSDVRKQPGKFRKVFkkNYLKWPEDEKEQFWKKALYA 136
 
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 ...
 1-148 2.69e-49

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: 170.00  E-value: 2.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890924   1 MACTGPSLPSAFDILGAAGQDKLLYLKHKLKTPRPGCQGQDLLHAMVLLKLGQETEARISLEALKADAAARLVARQWAGV 80
Cdd:pfam17798   1 SEGLGPSLRGVFDILSQAPQEKLLSLTHKLKCERGGSPEDDLLHAMCLLTLKREAAARRKLDALRDDPVANHLAEKWHGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622890924  81 DSTED-------PEEPPDVSWTVARLYHLLAEEKLCPASLRDVAYQEALHTLSSRDD--HRLGELQDEARNRCGWDV 148
Cdd:pfam17798  81 GKLDLngahcslEEKTAESLLAVARIYKLLVEERLCDASLRDKAYKAAVSAFRSGLDtsLELLDLREEARAVCGPDF 157
RHIM pfam12721
RIP homotypic interaction motif; RIP proteins are receptor-interacting serine ...
 676-695 4.85e-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: 4.85e-06
                          10        20
                  ....*....|....*....|
gi 1622890924 676 QPLIIHHAQMVQLGLNNHMW 695
Cdd:pfam12721   1 PPVIINNCSGVQIGNNNHMS 20
TIR_2 pfam13676
TIR domain; This is a family of Toll-like receptors.
 396-489 1.26e-04

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


Pssm-ID: 463954 [Multi-domain]  Cd Length: 118  Bit Score: 41.92  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890924 396 FVILHARADEHIALRVREKLEALGVPdgaTFCEDFQVPGRGEL-SCLQDAIDHSAFIILLLTPNFdchLSLHQVNQAMMS 474
Cdd:pfam13676   1 VFISYAGEDRAWAEWLADALEAAGYR---VWLDRWDIRPGDDWvEEIEEAIENSDRVLVVLSPNY---LESPWCRAEWEA 74

                          90
                  ....*....|....*
gi 1622890924 475 NLKRQGSPDCVIPFL 489
Cdd:pfam13676  75 ALADPEGRKRLIPVR 89
TIR smart00255
Toll - interleukin 1 - resistance;
398-526 3.95e-04

Toll - interleukin 1 - resistance;


Pssm-ID: 214587 [Multi-domain]  Cd Length: 140  Bit Score: 41.15  E-value: 3.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622890924  398 ILHARAD---EHIALRVREKLEALGVpdgaTFCEDFQVPGRGELSCLQDAIDHSAFIILLLTPNF-DCHLSLHQVnQAMM 473
Cdd:smart00255   6 ISYSGKEdvrNEFLSHLLEKLRGYGL----CVFIDDFEPGGGDLEEIDEAIEKSRIAIVVLSPNYaESEWCLDEL-VAAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622890924  474 SNLKRQGSpDCVIP-FL-PLESSPAQLSSDTASLL--SGLVRLDEHSQIFARKVANT 526
Cdd:smart00255  81 ENALEEGG-LRVIPiFYeVIPSDVRKQPGKFRKVFkkNYLKWPEDEKEQFWKKALYA 136
 
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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