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Conserved domains on  [gi|17550058|ref|NP_508149|]
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TRAF3-interacting protein 1 [Caenorhabditis elegans]

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 ...
 389-535 1.74e-54

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: 180.72  E-value: 1.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550058   389 VDEEDRGALVQKIMETKAEIEDGGGQDQVEESD-------ADKIMTVEREKMKQLQEKLQDLTRSAYPLARLFDFANDDI 461
Cdd:pfam17749   1 EDEDAQGGLVKKILETKKEYEKGGAEAEPGESDrslqessAKKGRTVSASDINQLRESIQTLTKSANPLGKLLDFIQDDI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17550058   462 ESMIKELERWRSEQRRNEQEDQNKKAAGFGDSSRLYNIIANLQKEINDTKEELSKARGRVLNNEKRIQLFISNV 535
Cdd:pfam17749  81 DSMQRELQMWRSEYRQNAQALQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQILKNEARIQKMVKSI 154
MIP-T3 pfam10243
Microtubule-binding protein MIP-T3 CH-like domain; This protein, which interacts with both ...
 2-111 1.28e-51

Microtubule-binding protein MIP-T3 CH-like domain; 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: 463020  Cd Length: 113  Bit Score: 171.86  E-value: 1.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550058     2 SVEETREILEKVIQKPQLTDQLLSRPPFKFIVDIVSNVIKSTGYLKTDFTDDEIKSAG-NDKNTKTAFLDKLIKILDDGS 80
Cdd:pfam10243   1 FVEPTQELLGAVIQKPKLTEKLLSKPPFKYIHDIIMETIKATGFPKGLYTDDELDSNNvNDKDAKIAFLQKLIDLVEMGS 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17550058    81 LKNVKA--AKIISGKDAEETNKMLQMLGTNATS 111
Cdd:pfam10243  81 GKPVAAkpAKIVAGLEPEKTNELLQMLGRCATS 113
dermokine super family cl42387
dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a ...
 301-328 6.93e-04

dermokine; Dermokine, also known as epidermis-specific secreted protein SK30/SK89, is a skin-specific glycoprotein that may play a regulatory role in the crosstalk between barrier dysfunction and inflammation, and therefore play a role in inflammatory diseases such as psoriasis. Dermokine is one of the most highly expressed proteins in differentiating keratinocytes, found mainly in the spinous and granular layers of the epidermis, but also in the epithelia of the small intestine, macrophages of the lung, and endothelial cells of the lung. Mouse dermokine has been reported to be encoded by 22 exons, and its expression leads to alpha, beta, and gamma transcripts.


The actual alignment was detected with superfamily member cd21341:

Pssm-ID: 455732 [Multi-domain]  Cd Length: 139  Bit Score: 39.98  E-value: 6.93e-04
                        10        20
                ....*....|....*....|....*...
gi 17550058 301 PLIRPMTGagGGRPMTSMGRPGTAASRP 328
Cdd:cd21341  67 QAMRPTTS--SGRPITGFVRPGTQSGRP 92
 
Name Accession Description Interval E-value
MIP-T3_C pfam17749
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ...
 389-535 1.74e-54

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: 180.72  E-value: 1.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550058   389 VDEEDRGALVQKIMETKAEIEDGGGQDQVEESD-------ADKIMTVEREKMKQLQEKLQDLTRSAYPLARLFDFANDDI 461
Cdd:pfam17749   1 EDEDAQGGLVKKILETKKEYEKGGAEAEPGESDrslqessAKKGRTVSASDINQLRESIQTLTKSANPLGKLLDFIQDDI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17550058   462 ESMIKELERWRSEQRRNEQEDQNKKAAGFGDSSRLYNIIANLQKEINDTKEELSKARGRVLNNEKRIQLFISNV 535
Cdd:pfam17749  81 DSMQRELQMWRSEYRQNAQALQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQILKNEARIQKMVKSI 154
MIP-T3 pfam10243
Microtubule-binding protein MIP-T3 CH-like domain; This protein, which interacts with both ...
 2-111 1.28e-51

Microtubule-binding protein MIP-T3 CH-like domain; 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: 463020  Cd Length: 113  Bit Score: 171.86  E-value: 1.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550058     2 SVEETREILEKVIQKPQLTDQLLSRPPFKFIVDIVSNVIKSTGYLKTDFTDDEIKSAG-NDKNTKTAFLDKLIKILDDGS 80
Cdd:pfam10243   1 FVEPTQELLGAVIQKPKLTEKLLSKPPFKYIHDIIMETIKATGFPKGLYTDDELDSNNvNDKDAKIAFLQKLIDLVEMGS 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17550058    81 LKNVKA--AKIISGKDAEETNKMLQMLGTNATS 111
Cdd:pfam10243  81 GKPVAAkpAKIVAGLEPEKTNELLQMLGRCATS 113
TTC8_N cd21341
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 ...
 301-328 6.93e-04

N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 (TTC80), also known a BBS8, has been directly linked to Bardet-Biedl syndrome, an autosomal recessive ciliopathy characterized by retinal degeneration, renal failure, obesity, diabetes, male infertility, polydactyly and cognitive impairment. Mutations in BBS8 cause early vision loss. In addition to C-terminal tetratricopeptide repeats, TTC8 also contains an N-terminal domain of unknown function.


Pssm-ID: 411061 [Multi-domain]  Cd Length: 139  Bit Score: 39.98  E-value: 6.93e-04
                        10        20
                ....*....|....*....|....*...
gi 17550058 301 PLIRPMTGagGGRPMTSMGRPGTAASRP 328
Cdd:cd21341  67 QAMRPTTS--SGRPITGFVRPGTQSGRP 92
 
Name Accession Description Interval E-value
MIP-T3_C pfam17749
Microtubule-binding protein MIP-T3 C-terminal region; This protein, which interacts with both ...
 389-535 1.74e-54

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: 180.72  E-value: 1.74e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550058   389 VDEEDRGALVQKIMETKAEIEDGGGQDQVEESD-------ADKIMTVEREKMKQLQEKLQDLTRSAYPLARLFDFANDDI 461
Cdd:pfam17749   1 EDEDAQGGLVKKILETKKEYEKGGAEAEPGESDrslqessAKKGRTVSASDINQLRESIQTLTKSANPLGKLLDFIQDDI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17550058   462 ESMIKELERWRSEQRRNEQEDQNKKAAGFGDSSRLYNIIANLQKEINDTKEELSKARGRVLNNEKRIQLFISNV 535
Cdd:pfam17749  81 DSMQRELQMWRSEYRQNAQALQNEQRATDEALQPLYAQLAELEEAIKDQKEKISNVKAQILKNEARIQKMVKSI 154
MIP-T3 pfam10243
Microtubule-binding protein MIP-T3 CH-like domain; This protein, which interacts with both ...
 2-111 1.28e-51

Microtubule-binding protein MIP-T3 CH-like domain; 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: 463020  Cd Length: 113  Bit Score: 171.86  E-value: 1.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17550058     2 SVEETREILEKVIQKPQLTDQLLSRPPFKFIVDIVSNVIKSTGYLKTDFTDDEIKSAG-NDKNTKTAFLDKLIKILDDGS 80
Cdd:pfam10243   1 FVEPTQELLGAVIQKPKLTEKLLSKPPFKYIHDIIMETIKATGFPKGLYTDDELDSNNvNDKDAKIAFLQKLIDLVEMGS 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 17550058    81 LKNVKA--AKIISGKDAEETNKMLQMLGTNATS 111
Cdd:pfam10243  81 GKPVAAkpAKIVAGLEPEKTNELLQMLGRCATS 113
TTC8_N cd21341
N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 ...
 301-328 6.93e-04

N-terminal domain of tetratricopeptide repeat domain 8; Tetratricopeptide repeat domain 8 (TTC80), also known a BBS8, has been directly linked to Bardet-Biedl syndrome, an autosomal recessive ciliopathy characterized by retinal degeneration, renal failure, obesity, diabetes, male infertility, polydactyly and cognitive impairment. Mutations in BBS8 cause early vision loss. In addition to C-terminal tetratricopeptide repeats, TTC8 also contains an N-terminal domain of unknown function.


Pssm-ID: 411061 [Multi-domain]  Cd Length: 139  Bit Score: 39.98  E-value: 6.93e-04
                        10        20
                ....*....|....*....|....*...
gi 17550058 301 PLIRPMTGagGGRPMTSMGRPGTAASRP 328
Cdd:cd21341  67 QAMRPTTS--SGRPITGFVRPGTQSGRP 92
 
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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