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Conserved domains on  [gi|1958665360|ref|XP_038944218|]
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TBCC domain-containing protein 1 isoform X3 [Rattus norvegicus]

Protein Classification

TBCC domain-containing protein( domain architecture ID 1006203)

TBCC (Tubulin binding cofactor C) domain-containing protein similar to Saccharomyces cerevisiae tubulin-specific chaperone C, which is a tubulin-folding protein involved in the early step of the tubulin folding pathway

Gene Ontology:  GO:0007023

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TBCC super family cl29757
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 362-407 6.92e-12

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


The actual alignment was detected with superfamily member pfam07986:

Pssm-ID: 475252  Cd Length: 119  Bit Score: 62.62  E-value: 6.92e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958665360 362 GAHVRAHRCNESFIYLLSPLRSMTIEKCRNSTFVLGPVETALHLHG 407
Cdd:pfam07986   1 GVDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRD 46
 
Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 362-407 6.92e-12

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: 62.62  E-value: 6.92e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958665360 362 GAHVRAHRCNESFIYLLSPLRSMTIEKCRNSTFVLGPVETALHLHG 407
Cdd:pfam07986   1 GVDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRD 46
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
370-406 4.38e-04

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


Pssm-ID: 197827  Cd Length: 38  Bit Score: 37.88  E-value: 4.38e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958665360  370 CNESFIYLLSPLRSMTIEKCRNSTFVLGPVETALHLH 406
Cdd:smart00673   1 CESCTIQVSGKVNTISIDKCKKCSIYLGPVSGSPEIV 37
 
Name Accession Description Interval E-value
TBCC pfam07986
Tubulin binding cofactor C; Members of this family are involved in the folding pathway of ...
 362-407 6.92e-12

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: 62.62  E-value: 6.92e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1958665360 362 GAHVRAHRCNESFIYLLSPLRSMTIEKCRNSTFVLGPVETALHLHG 407
Cdd:pfam07986   1 GVDVKLSNLSNCTIYLLDPLSSVTIDDCKNCTIFLGPVSGSVFIRD 46
CARP smart00673
Domain in CAPs (cyclase-associated proteins) and X-linked retinitis pigmentosa 2 gene product;
370-406 4.38e-04

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


Pssm-ID: 197827  Cd Length: 38  Bit Score: 37.88  E-value: 4.38e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1958665360  370 CNESFIYLLSPLRSMTIEKCRNSTFVLGPVETALHLH 406
Cdd:smart00673   1 CESCTIQVSGKVNTISIDKCKKCSIYLGPVSGSPEIV 37
 
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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