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Conserved domains on  [gi|767917541|ref|XP_011509252|]
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TRAF3-interacting protein 1 isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MIP-T3_C pfam17749
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ...
 188-341 2.22e-78

Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


:

Pssm-ID: 465481 [Multi-domain]  Cd Length: 154  Bit Score: 236.96  E-value: 2.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917541  188 EEEEKHGGLVKKILETKKDYEKLQQSPKPGEKERSLFESAWKKEKDIVSKEIEKLRTSIQTLCKSALPLGKIMDYIQEDV 267
Cdd:pfam17749   1 EDEDAQGGLVKKILETKKEYEKGGAEAEPGESDRSLQESSAKKGRTVSASDINQLRESIQTLTKSANPLGKLLDFIQDDI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917541  268 DAMQNELQMWHSENRQHAEALQQEQRITDCAVEPLKAELAELEQLIKDQQDKICAVKANILKNEEKIQKMVYSI 341
Cdd:pfam17749  81 DSMQRELQMWRSEYRQNAQALQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQILKNEARIQKMVKSI 154
 
Name Accession Description Interval E-value
MIP-T3_C pfam17749
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ...
 188-341 2.22e-78

Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


Pssm-ID: 465481 [Multi-domain]  Cd Length: 154  Bit Score: 236.96  E-value: 2.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917541  188 EEEEKHGGLVKKILETKKDYEKLQQSPKPGEKERSLFESAWKKEKDIVSKEIEKLRTSIQTLCKSALPLGKIMDYIQEDV 267
Cdd:pfam17749   1 EDEDAQGGLVKKILETKKEYEKGGAEAEPGESDRSLQESSAKKGRTVSASDINQLRESIQTLTKSANPLGKLLDFIQDDI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917541  268 DAMQNELQMWHSENRQHAEALQQEQRITDCAVEPLKAELAELEQLIKDQQDKICAVKANILKNEEKIQKMVYSI 341
Cdd:pfam17749  81 DSMQRELQMWRSEYRQNAQALQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQILKNEARIQKMVKSI 154
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 236-336 1.13e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917541 236 SKEIEKLRTSIQTLCKSalPLGKIMDYiQEDVDAMQNELQMWHSENRQHAEALQQ------------EQRITDCAVEPLK 303
Cdd:cd22656  109 DEELEEAKKTIKALLDD--LLKEAKKY-QDKAAKVVDKLTDFENQTEKDQTALETlekalkdlltdeGGAIARKEIKDLQ 185

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767917541 304 AELAEL-EQLIKDQQDKICAVKANILKNEEKIQK 336
Cdd:cd22656  186 KELEKLnEEYAAKLKAKIDELKALIADDEAKLAA 219
 
Name Accession Description Interval E-value
MIP-T3_C pfam17749
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ...
 188-341 2.22e-78

Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both microtubules and TRAF3 (tumour necrosis factor receptor-associated factor 3), is conserved from worms to humans. The N-terminal region is the microtubule binding domain and is well-conserved; the C-terminal 100 residues, also well-conserved, constitute the coiled-coil region which binds to TRAF3. The central region of the protein is rich in lysine and glutamic acid and carries KKE motifs which may also be necessary for tubulin-binding, but this region is the least well-conserved.


Pssm-ID: 465481 [Multi-domain]  Cd Length: 154  Bit Score: 236.96  E-value: 2.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917541  188 EEEEKHGGLVKKILETKKDYEKLQQSPKPGEKERSLFESAWKKEKDIVSKEIEKLRTSIQTLCKSALPLGKIMDYIQEDV 267
Cdd:pfam17749   1 EDEDAQGGLVKKILETKKEYEKGGAEAEPGESDRSLQESSAKKGRTVSASDINQLRESIQTLTKSANPLGKLLDFIQDDI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767917541  268 DAMQNELQMWHSENRQHAEALQQEQRITDCAVEPLKAELAELEQLIKDQQDKICAVKANILKNEEKIQKMVYSI 341
Cdd:pfam17749  81 DSMQRELQMWRSEYRQNAQALQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQILKNEARIQKMVKSI 154
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 236-336 1.13e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917541 236 SKEIEKLRTSIQTLCKSalPLGKIMDYiQEDVDAMQNELQMWHSENRQHAEALQQ------------EQRITDCAVEPLK 303
Cdd:cd22656  109 DEELEEAKKTIKALLDD--LLKEAKKY-QDKAAKVVDKLTDFENQTEKDQTALETlekalkdlltdeGGAIARKEIKDLQ 185

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767917541 304 AELAEL-EQLIKDQQDKICAVKANILKNEEKIQK 336
Cdd:cd22656  186 KELEKLnEEYAAKLKAKIDELKALIADDEAKLAA 219
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 152-341 4.54e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.93  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917541  152 TESHNSDNEEDDQFVV-----EAAPQLSEMSEIEMVTAVELEEEEKHGGLVKKILETKKDYEKLQQSPKPGEKERSLFES 226
Cdd:pfam05483 367 TEQQRLEKNEDQLKIItmelqKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767917541  227 AWKKEKDIVSKEIEKLRTSIQtlcksalplgkimdYIQEDVDAMQNELQ---MWHSENRQHAEALQQEQRitdcavePLK 303
Cdd:pfam05483 447 AREKEIHDLEIQLTAIKTSEE--------------HYLKEVEDLKTELEkekLKNIELTAHCDKLLLENK-------ELT 505

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767917541  304 AELAELEQLIKDQQDKIcavkANILKNEEKIQKMVYSI 341
Cdd:pfam05483 506 QEASDMTLELKKHQEDI----INCKKQEERMLKQIENL 539
 
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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