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Conserved domains on  [gi|15236084|ref|NP_195702|]
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C-CAP/cofactor C-like domain-containing protein [Arabidopsis thaliana]

Protein Classification

TBCC_N and TBCC domain-containing protein( domain architecture ID 11245415)

TBCC_N and TBCC domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 201-316 8.69e-49

Tubulin binding cofactor C; Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.


:

Pssm-ID: 462331  Cd Length: 119  Bit Score: 159.69  E-value: 8.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236084   201 FTLSDLDSCQVKLTGTVNALFLHRLKKCSVYTGPVIGSILIDDVEDCVLVLASHQIRIHCARKSDFYLRVRSRPIIEDSN 280
Cdd:pfam07986   4 VKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIEDST 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15236084   281 GVRFAPYCLDYKGIDEDLKTAGLEEETNNWANVDDF 316
Cdd:pfam07986  84 GIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
TBCC_N pfam16752
Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific ...
 26-139 1.05e-27

Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific chaperone C has a spectrin-like fold and binds to tubulin.


:

Pssm-ID: 465258 [Multi-domain]  Cd Length: 115  Bit Score: 104.66  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236084    26 ERLSARHQARKSDSPDSSSSSSSTLEST---SSFLAKFSDSKRSIESRIAESRlassSTDSSKLKSDLAEISVAIDNLEK 102
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEesvDYFLSAFNEEKASIEELLSQCR----SADKSKLKSHLDEITEEIQDLQK 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15236084   103 LLAENSYFLPSYEVRSSLKIVSDLKQSLDILSGELVP 139
Cdd:pfam16752  77 FLADSSYFLPSYDIRSAQEALQKLQKSLEEARAELLP 113
 
Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 201-316 8.69e-49

Tubulin binding cofactor C; Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.


Pssm-ID: 462331  Cd Length: 119  Bit Score: 159.69  E-value: 8.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236084   201 FTLSDLDSCQVKLTGTVNALFLHRLKKCSVYTGPVIGSILIDDVEDCVLVLASHQIRIHCARKSDFYLRVRSRPIIEDSN 280
Cdd:pfam07986   4 VKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIEDST 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15236084   281 GVRFAPYCLDYKGIDEDLKTAGLEEETNNWANVDDF 316
Cdd:pfam07986  84 GIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
TBCC_N pfam16752
Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific ...
 26-139 1.05e-27

Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific chaperone C has a spectrin-like fold and binds to tubulin.


Pssm-ID: 465258 [Multi-domain]  Cd Length: 115  Bit Score: 104.66  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236084    26 ERLSARHQARKSDSPDSSSSSSSTLEST---SSFLAKFSDSKRSIESRIAESRlassSTDSSKLKSDLAEISVAIDNLEK 102
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEesvDYFLSAFNEEKASIEELLSQCR----SADKSKLKSHLDEITEEIQDLQK 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15236084   103 LLAENSYFLPSYEVRSSLKIVSDLKQSLDILSGELVP 139
Cdd:pfam16752  77 FLADSSYFLPSYDIRSAQEALQKLQKSLEEARAELLP 113
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
206-243 8.45e-07

Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;


Pssm-ID: 197827  Cd Length: 38  Bit Score: 44.82  E-value: 8.45e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 15236084    206 LDSCQVKLTGTVNALFLHRLKKCSVYTGPVIGSILIDD 243
Cdd:smart00673   1 CESCTIQVSGKVNTISIDKCKKCSIYLGPVSGSPEIVN 38
 
Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 201-316 8.69e-49

Tubulin binding cofactor C; Members of this family are involved in the folding pathway of tubulins and form a beta helix structure.


Pssm-ID: 462331  Cd Length: 119  Bit Score: 159.69  E-value: 8.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236084   201 FTLSDLDSCQVKLTGTVNALFLHRLKKCSVYTGPVIGSILIDDVEDCVLVLASHQIRIHCARKSDFYLRVRSRPIIEDSN 280
Cdd:pfam07986   4 VKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIEDST 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15236084   281 GVRFAPYCLDYKGIDEDLKTAGLEEETNNWANVDDF 316
Cdd:pfam07986  84 GIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
TBCC_N pfam16752
Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific ...
 26-139 1.05e-27

Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific chaperone C has a spectrin-like fold and binds to tubulin.


Pssm-ID: 465258 [Multi-domain]  Cd Length: 115  Bit Score: 104.66  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15236084    26 ERLSARHQARKSDSPDSSSSSSSTLEST---SSFLAKFSDSKRSIESRIAESRlassSTDSSKLKSDLAEISVAIDNLEK 102
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEesvDYFLSAFNEEKASIEELLSQCR----SADKSKLKSHLDEITEEIQDLQK 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 15236084   103 LLAENSYFLPSYEVRSSLKIVSDLKQSLDILSGELVP 139
Cdd:pfam16752  77 FLADSSYFLPSYDIRSAQEALQKLQKSLEEARAELLP 113
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
206-243 8.45e-07

Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;


Pssm-ID: 197827  Cd Length: 38  Bit Score: 44.82  E-value: 8.45e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 15236084    206 LDSCQVKLTGTVNALFLHRLKKCSVYTGPVIGSILIDD 243
Cdd:smart00673   1 CESCTIQVSGKVNTISIDKCKKCSIYLGPVSGSPEIVN 38
 
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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