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Conserved domains on  [gi|1907149697|ref|XP_036018886|]
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TRAF-interacting protein with FHA domain-containing protein A isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FHA_TIFA cd22714
forkhead associated (FHA) domain found in TRAF-interacting protein with FHA domain-containing ...
 141-274 3.58e-87

forkhead associated (FHA) domain found in TRAF-interacting protein with FHA domain-containing protein A (TIFA) and similar proteins; TIFA, also called putative MAPK-activating protein PM14, putative NF-kappa-B-activating protein 20, or TRAF2-binding protein (T2BP), is an adapter molecule that plays a key role in the activation of proinflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs). It promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism. TIFA-dependent innate immune response is triggered by ADP-D-glycero-beta-D-manno-heptose (ADP-heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria: ADP-heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of proinflammatory NF-kappa-B signaling. TIFA contains an FHA domain, which is a small phosphopeptide recognition module.


:

Pssm-ID: 438766  Cd Length: 135  Bit Score: 257.35  E-value: 3.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149697 141 VTCLQMTIYHPGQQ-SGIFKSIRFCSKEKFPSIEVVKFGRNSNMCQYTFQDKQVSRIQFVLQPFKQFNSSVLSFEIKNMS 219
Cdd:cd22714     1 VTCLQMTVYHPGQEqKGVFQSINFSKKEKFPSDEVVKFGRDSNICHYTLQDKRVSRIQFSLQAFKKFNSSVLCFEIKNLS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907149697 220 KKTSLMVDNQELGYLNKMDLPYKCMLRFGEYQFLLQKEDGESVESFETQFIMSSR 274
Cdd:cd22714    81 KKTKLYVDNTELGYLNKVELPYKCMLRFGEYQFLLEKEDGESLEKFETQFILSPV 135
 
Name Accession Description Interval E-value
FHA_TIFA cd22714
forkhead associated (FHA) domain found in TRAF-interacting protein with FHA domain-containing ...
 141-274 3.58e-87

forkhead associated (FHA) domain found in TRAF-interacting protein with FHA domain-containing protein A (TIFA) and similar proteins; TIFA, also called putative MAPK-activating protein PM14, putative NF-kappa-B-activating protein 20, or TRAF2-binding protein (T2BP), is an adapter molecule that plays a key role in the activation of proinflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs). It promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism. TIFA-dependent innate immune response is triggered by ADP-D-glycero-beta-D-manno-heptose (ADP-heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria: ADP-heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of proinflammatory NF-kappa-B signaling. TIFA contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438766  Cd Length: 135  Bit Score: 257.35  E-value: 3.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149697 141 VTCLQMTIYHPGQQ-SGIFKSIRFCSKEKFPSIEVVKFGRNSNMCQYTFQDKQVSRIQFVLQPFKQFNSSVLSFEIKNMS 219
Cdd:cd22714     1 VTCLQMTVYHPGQEqKGVFQSINFSKKEKFPSDEVVKFGRDSNICHYTLQDKRVSRIQFSLQAFKKFNSSVLCFEIKNLS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907149697 220 KKTSLMVDNQELGYLNKMDLPYKCMLRFGEYQFLLQKEDGESVESFETQFIMSSR 274
Cdd:cd22714    81 KKTKLYVDNTELGYLNKVELPYKCMLRFGEYQFLLEKEDGESLEKFETQFILSPV 135
 
Name Accession Description Interval E-value
FHA_TIFA cd22714
forkhead associated (FHA) domain found in TRAF-interacting protein with FHA domain-containing ...
 141-274 3.58e-87

forkhead associated (FHA) domain found in TRAF-interacting protein with FHA domain-containing protein A (TIFA) and similar proteins; TIFA, also called putative MAPK-activating protein PM14, putative NF-kappa-B-activating protein 20, or TRAF2-binding protein (T2BP), is an adapter molecule that plays a key role in the activation of proinflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs). It promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism. TIFA-dependent innate immune response is triggered by ADP-D-glycero-beta-D-manno-heptose (ADP-heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria: ADP-heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of proinflammatory NF-kappa-B signaling. TIFA contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438766  Cd Length: 135  Bit Score: 257.35  E-value: 3.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149697 141 VTCLQMTIYHPGQQ-SGIFKSIRFCSKEKFPSIEVVKFGRNSNMCQYTFQDKQVSRIQFVLQPFKQFNSSVLSFEIKNMS 219
Cdd:cd22714     1 VTCLQMTVYHPGQEqKGVFQSINFSKKEKFPSDEVVKFGRDSNICHYTLQDKRVSRIQFSLQAFKKFNSSVLCFEIKNLS 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907149697 220 KKTSLMVDNQELGYLNKMDLPYKCMLRFGEYQFLLQKEDGESVESFETQFIMSSR 274
Cdd:cd22714    81 KKTKLYVDNTELGYLNKVELPYKCMLRFGEYQFLLEKEDGESLEKFETQFILSPV 135
FHA_TIFA-like cd22664
forkhead associated (FHA) domain found in the family of TRAF-interacting protein with FHA ...
 141-273 2.18e-79

forkhead associated (FHA) domain found in the family of TRAF-interacting protein with FHA domain-containing protein A (TIFA); The TIFA family includes TIFA and TIFA-like protein, TIFAB. TIFA, also called putative MAPK-activating protein PM14, putative NF-kappa-B-activating protein 20, or TRAF2-binding protein (T2BP), is an adapter molecule that plays a key role in the activation of proinflammatory NF-kappa-B signaling following detection of bacterial pathogen-associated molecular pattern metabolites (PAMPs). It promotes activation of an innate immune response by inducing the oligomerization and polyubiquitination of TRAF6, which leads to the activation of TAK1 and IKK through a proteasome-independent mechanism. TIFA-dependent innate immune response is triggered by ADP-D-glycero-beta-D-manno-heptose (ADP-heptose), a potent PAMP present in all Gram-negative and some Gram-positive bacteria: ADP-heptose is recognized by ALPK1, which phosphorylates TIFA at Thr-9, leading to TIFA homooligomerization and subsequent activation of proinflammatory NF-kappa-B signaling. TIFAB, also called TIFA-like protein, inhibits TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA. It regulates USP15-mediated p53 signaling during stressed and malignant hematopoiesis. Both TIFA and TIFAB harbor a conserved FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438716  Cd Length: 133  Bit Score: 237.22  E-value: 2.18e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149697 141 VTCLQMTIYHPGQQSGIFKSIRFCSKEKFPSIEVVKFGRNSNMCQYTFQDKQVSRIQFVLQPFKQFNSSVLSFEIKNMSK 220
Cdd:cd22664     1 LTCLQITLYHPGQQDKGFQSIFFDKKEKLQSDEVLKFGRDSNCCHYTLQDKRVSRIQFSLQPFKEFNSSVLCFEIKNLSK 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907149697 221 KTSLMVDNQELGYLNKMDLPYKCMLRFGEYQFLLQKEDGESVESFETQFIMSS 273
Cdd:cd22664    81 KTKLWVNGLELGYLNKVELPAKCTVRFGEFQFLLEKEDGESLEKFETQFHLSP 133
FHA_TIFAB cd22715
forkhead associated (FHA) domain found in TRAF-interacting protein with FHA domain-containing ...
 141-272 4.02e-13

forkhead associated (FHA) domain found in TRAF-interacting protein with FHA domain-containing protein B (TIFAB); TIFAB, also called TIFA-like protein, inhibits TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA. It regulates USP15-mediated p53 signaling during stressed and malignant hematopoiesis. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438767  Cd Length: 129  Bit Score: 65.26  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907149697 141 VTCLQMTIYHPGQQSGIFKSIrfcSKEKFPSIEVVKFGRNSNmCQYTFQDKQVSRIQFVLQPFKQFNSSVLSFEIKNMSK 220
Cdd:cd22715     1 LTKLDISLYHPEGQNGIFQDV---PKKLQCDTQNLSIGRGPK-AHLQLNLPFISRRHLSLEPYLEKGNPYLCFCLKNLSR 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907149697 221 KTSLMVDNQELGYLNKMDLPYKCMLRFGEYQFLLQKEDGESVESFETQFIMS 272
Cdd:cd22715    77 KGIVWVNGLTLEYLEQVPLHAVNTVLFSGFQMLVTVDQGVSWDGFVCEIHVS 128
 
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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