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Conserved domains on  [gi|2052815776|ref|XP_041937646|]
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E3 ubiquitin ligase TRAF3IP2 isoform X1 [Alosa sapidissima]

Protein Classification

TIR domain-containing protein( domain architecture ID 581104)

TIR (Toll/interleukin-1 receptor) domain-containing protein

CATH:  3.40.50.10140
PubMed:  32002590|29395922|34868065

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SEFIR super family cl23749
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 273-418 6.94e-24

SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are feedback inhibitors of FGF signalling and are also thought to be receptors. Due to its similarity to the TIR domain (pfam01582), the SEFIR region is thought to be involved in homotypic interactions with other SEFIR/TIR-domain-containing proteins. Thus, SEFs and IL17Rs may be involved in TOLL/IL1R-like signalling pathways.


The actual alignment was detected with superfamily member pfam08357:

Pssm-ID: 474043  Cd Length: 150  Bit Score: 97.08  E-value: 6.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052815776 273 RKVFVTYESDSEDHVKEIIKFVALLRHN-GFDTHIDVFEqqLNSISKIDC---TERYIQEKDYLIIIAI-SPKYFEVVSG 347
Cdd:pfam08357   1 RKVFIVYSSDSALHTEVVLKFAEFLQDYcGCEVALDLWE--LNEIAEIGPvawLERQIQEADKVIIVCSkGAKAFCDKKA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2052815776 348 DSMFVERDERTLNTVYIH--KQLQNEFIQNGCKNfRFIPVLFPGAKKSHVPTWLQNTHVYNWPKDRDDILRRL 418
Cdd:pfam08357  79 DKRKGGVGTESQHDLFIPalSLILRDFKQSAALR-KYLVVYFGYADKKDVPTILRVLPKYSLMDQLPQLLAEL 150
Atrophin-1 super family cl38111
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 91-241 2.10e-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.


The actual alignment was detected with superfamily member pfam03154:

Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.52  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052815776  91 TPFPSQAVAGTSAADHYQWAWAYPSyaSGREEGGYQHPHSMPSSLPSDEYSSYPDDGSHLQARSHSLPGRNSPSLAsleQ 170
Cdd:pfam03154 204 PSVPPQGSPATSQPPNQTQSTAAPH--TLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP---M 278

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2052815776 171 PSSLLSNPPLAaahphPHPLPYGCVPMAPACCTQYTPPGHHHRGPGPLHQLSPQPAYHMAYKPSGPEQHHP 241
Cdd:pfam03154 279 PHSLQTGPSHM-----QHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP 344
 
Name Accession Description Interval E-value
SEFIR pfam08357
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 273-418 6.94e-24

SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are feedback inhibitors of FGF signalling and are also thought to be receptors. Due to its similarity to the TIR domain (pfam01582), the SEFIR region is thought to be involved in homotypic interactions with other SEFIR/TIR-domain-containing proteins. Thus, SEFs and IL17Rs may be involved in TOLL/IL1R-like signalling pathways.


Pssm-ID: 254756  Cd Length: 150  Bit Score: 97.08  E-value: 6.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052815776 273 RKVFVTYESDSEDHVKEIIKFVALLRHN-GFDTHIDVFEqqLNSISKIDC---TERYIQEKDYLIIIAI-SPKYFEVVSG 347
Cdd:pfam08357   1 RKVFIVYSSDSALHTEVVLKFAEFLQDYcGCEVALDLWE--LNEIAEIGPvawLERQIQEADKVIIVCSkGAKAFCDKKA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2052815776 348 DSMFVERDERTLNTVYIH--KQLQNEFIQNGCKNfRFIPVLFPGAKKSHVPTWLQNTHVYNWPKDRDDILRRL 418
Cdd:pfam08357  79 DKRKGGVGTESQHDLFIPalSLILRDFKQSAALR-KYLVVYFGYADKKDVPTILRVLPKYSLMDQLPQLLAEL 150
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 91-241 2.10e-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: 40.52  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052815776  91 TPFPSQAVAGTSAADHYQWAWAYPSyaSGREEGGYQHPHSMPSSLPSDEYSSYPDDGSHLQARSHSLPGRNSPSLAsleQ 170
Cdd:pfam03154 204 PSVPPQGSPATSQPPNQTQSTAAPH--TLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP---M 278

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2052815776 171 PSSLLSNPPLAaahphPHPLPYGCVPMAPACCTQYTPPGHHHRGPGPLHQLSPQPAYHMAYKPSGPEQHHP 241
Cdd:pfam03154 279 PHSLQTGPSHM-----QHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP 344
 
Name Accession Description Interval E-value
SEFIR pfam08357
SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are ...
 273-418 6.94e-24

SEFIR domain; This family comprises IL17 receptors (IL17Rs) and SEF proteins. The latter are feedback inhibitors of FGF signalling and are also thought to be receptors. Due to its similarity to the TIR domain (pfam01582), the SEFIR region is thought to be involved in homotypic interactions with other SEFIR/TIR-domain-containing proteins. Thus, SEFs and IL17Rs may be involved in TOLL/IL1R-like signalling pathways.


Pssm-ID: 254756  Cd Length: 150  Bit Score: 97.08  E-value: 6.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052815776 273 RKVFVTYESDSEDHVKEIIKFVALLRHN-GFDTHIDVFEqqLNSISKIDC---TERYIQEKDYLIIIAI-SPKYFEVVSG 347
Cdd:pfam08357   1 RKVFIVYSSDSALHTEVVLKFAEFLQDYcGCEVALDLWE--LNEIAEIGPvawLERQIQEADKVIIVCSkGAKAFCDKKA 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2052815776 348 DSMFVERDERTLNTVYIH--KQLQNEFIQNGCKNfRFIPVLFPGAKKSHVPTWLQNTHVYNWPKDRDDILRRL 418
Cdd:pfam08357  79 DKRKGGVGTESQHDLFIPalSLILRDFKQSAALR-KYLVVYFGYADKKDVPTILRVLPKYSLMDQLPQLLAEL 150
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 91-241 2.10e-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: 40.52  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052815776  91 TPFPSQAVAGTSAADHYQWAWAYPSyaSGREEGGYQHPHSMPSSLPSDEYSSYPDDGSHLQARSHSLPGRNSPSLAsleQ 170
Cdd:pfam03154 204 PSVPPQGSPATSQPPNQTQSTAAPH--TLIQQTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPP---M 278

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2052815776 171 PSSLLSNPPLAaahphPHPLPYGCVPMAPACCTQYTPPGHHHRGPGPLHQLSPQPAYHMAYKPSGPEQHHP 241
Cdd:pfam03154 279 PHSLQTGPSHM-----QHPVPPQPFPLTPQSSQSQVPPGPSPAAPGQSQQRIHTPPSQSQLQSQQPPREQP 344
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 83-228 9.73e-03

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: 38.48  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2052815776  83 AAQARFPQTPFPSQAVAGTSAADHYQWAWAYPSYASGREEGGYQHPHSMPSSLPSDEYSSYPDDG-SHLQARSHSLPGRN 161
Cdd:pfam09770 213 QPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILQRPQSPQPDPAqPSIQPQAQQFHQQP 292

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2052815776 162 SPSLAsleQPSSLLSNPPLAAAHPHPhplpygcVPMAPACCTQYTPPGHHHRGPGPLHQLSPQPAYH 228
Cdd:pfam09770 293 PPVPV---QPTQILQNPNRLSAARVG-------YPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHP 349
 
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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