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Conserved domains on  [gi|24581584|ref|NP_722960|]
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Tubulin-binding cofactor C, isoform B [Drosophila melanogaster]

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 ...
 188-306 2.18e-43

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: 146.20  E-value: 2.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581584   188 GQDITISKLNHCLVELQGHPGSVQVSRASKCTLLCGPIARSFFAENLEDCTLSIACQQLRLHSSRSIRIYMHVTCRAIIE 267
Cdd:pfam07986   1 GVDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 24581584   268 DCKSIEIGEYNYDYSKLEADYLASGLNKAQNNYTDVADF 306
Cdd:pfam07986  81 DSTGIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
TBCC_N pfam16752
Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific ...
 14-128 2.82e-41

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: 140.48  E-value: 2.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581584    14 ERLNKRNKDRQNYLDVKSELRSKETVQNEGVDYFYQTFSQKTMDIEQRLKdvQCGDGQPTDLARNFADITVEIQDLQRYL 93
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEESVDYFLSAFNEEKASIEELLS--QCRSADKSKLKSHLDEITEEIQDLQKFL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 24581584    94 TASTMFLPDFKIKSCQNILNTLTAVSDETRQRLLP 128
Cdd:pfam16752  79 ADSSYFLPSYDIRSAQEALQKLQKSLEEARAELLP 113
 
Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 188-306 2.18e-43

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: 146.20  E-value: 2.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581584   188 GQDITISKLNHCLVELQGHPGSVQVSRASKCTLLCGPIARSFFAENLEDCTLSIACQQLRLHSSRSIRIYMHVTCRAIIE 267
Cdd:pfam07986   1 GVDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 24581584   268 DCKSIEIGEYNYDYSKLEADYLASGLNKAQNNYTDVADF 306
Cdd:pfam07986  81 DSTGIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
TBCC_N pfam16752
Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific ...
 14-128 2.82e-41

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: 140.48  E-value: 2.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581584    14 ERLNKRNKDRQNYLDVKSELRSKETVQNEGVDYFYQTFSQKTMDIEQRLKdvQCGDGQPTDLARNFADITVEIQDLQRYL 93
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEESVDYFLSAFNEEKASIEELLS--QCRSADKSKLKSHLDEITEEIQDLQKFL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 24581584    94 TASTMFLPDFKIKSCQNILNTLTAVSDETRQRLLP 128
Cdd:pfam16752  79 ADSSYFLPSYDIRSAQEALQKLQKSLEEARAELLP 113
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
196-233 4.48e-04

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


Pssm-ID: 197827  Cd Length: 38  Bit Score: 37.11  E-value: 4.48e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 24581584    196 LNHCLVELQGHPGSVQVSRASKCTLLCGPIARSFFAEN 233
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 ...
 188-306 2.18e-43

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: 146.20  E-value: 2.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581584   188 GQDITISKLNHCLVELQGHPGSVQVSRASKCTLLCGPIARSFFAENLEDCTLSIACQQLRLHSSRSIRIYMHVTCRAIIE 267
Cdd:pfam07986   1 GVDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRDCENCTIVVACRQLRIHDCTNCDFYLHTTSRPIIE 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 24581584   268 DCKSIEIGEYNYDYSKLEADYLASGLNKAQNNYTDVADF 306
Cdd:pfam07986  81 DSTGIRFAPYNTSYPGLEEHLKSAGLDPENNNWSQVDDF 119
TBCC_N pfam16752
Tubulin-specific chaperone C N-terminal domain; This N-terminal domain of tubulin-specific ...
 14-128 2.82e-41

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: 140.48  E-value: 2.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581584    14 ERLNKRNKDRQNYLDVKSELRSKETVQNEGVDYFYQTFSQKTMDIEQRLKdvQCGDGQPTDLARNFADITVEIQDLQRYL 93
Cdd:pfam16752   1 ERLEKRHQERQEQLEKRKEERESEAVPEESVDYFLSAFNEEKASIEELLS--QCRSADKSKLKSHLDEITEEIQDLQKFL 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 24581584    94 TASTMFLPDFKIKSCQNILNTLTAVSDETRQRLLP 128
Cdd:pfam16752  79 ADSSYFLPSYDIRSAQEALQKLQKSLEEARAELLP 113
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
196-233 4.48e-04

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


Pssm-ID: 197827  Cd Length: 38  Bit Score: 37.11  E-value: 4.48e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 24581584    196 LNHCLVELQGHPGSVQVSRASKCTLLCGPIARSFFAEN 233
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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