NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1858697021|pdb|6WUC|W]
View 

Chain W, Inner kinetochore subunit WIP1

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
WIP1_HFD super family cl45566
C-terminal histone fold domain of Saccharomyces cerevisiae W-like protein 1 (Wip1) and similar ...
44-89 6.29e-08

C-terminal histone fold domain of Saccharomyces cerevisiae W-like protein 1 (Wip1) and similar proteins; Wip1, also called CENP-W homolog, or constitutive centromere-associated network protein Wip1, is a component of the inner kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. The model corresponds to the C-terminal histone fold domain of Wip1, which interacts with Cnn1 to form a heterodimer. In budding yeast, the Cnn1-Wip1 heterodimer associated with the Ctf3 complex (Ctf3c) to form a sub-complex of the larger Ctf19 complex (Ctf19c).


The actual alignment was detected with superfamily member cd22575:

Pssm-ID: 439342  Cd Length: 73  Bit Score: 45.47  E-value: 6.29e-08
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
6WUC_W      44 NKKLLLACGFQAILRKILLDARTRATAEGLREVYPYHIEAATQAFL 89
Cdd:cd22575 27 NKKLLLACGFQAILRKILLDARTRATAEGLREVYPYHIEAATQAFL 72
 
Name Accession Description Interval E-value
WIP1_HFD cd22575
C-terminal histone fold domain of Saccharomyces cerevisiae W-like protein 1 (Wip1) and similar ...
44-89 6.29e-08

C-terminal histone fold domain of Saccharomyces cerevisiae W-like protein 1 (Wip1) and similar proteins; Wip1, also called CENP-W homolog, or constitutive centromere-associated network protein Wip1, is a component of the inner kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. The model corresponds to the C-terminal histone fold domain of Wip1, which interacts with Cnn1 to form a heterodimer. In budding yeast, the Cnn1-Wip1 heterodimer associated with the Ctf3 complex (Ctf3c) to form a sub-complex of the larger Ctf19 complex (Ctf19c).


Pssm-ID: 439342  Cd Length: 73  Bit Score: 45.47  E-value: 6.29e-08
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
6WUC_W      44 NKKLLLACGFQAILRKILLDARTRATAEGLREVYPYHIEAATQAFL 89
Cdd:cd22575 27 NKKLLLACGFQAILRKILLDARTRATAEGLREVYPYHIEAATQAFL 72
 
Name Accession Description Interval E-value
WIP1_HFD cd22575
C-terminal histone fold domain of Saccharomyces cerevisiae W-like protein 1 (Wip1) and similar ...
44-89 6.29e-08

C-terminal histone fold domain of Saccharomyces cerevisiae W-like protein 1 (Wip1) and similar proteins; Wip1, also called CENP-W homolog, or constitutive centromere-associated network protein Wip1, is a component of the inner kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. The model corresponds to the C-terminal histone fold domain of Wip1, which interacts with Cnn1 to form a heterodimer. In budding yeast, the Cnn1-Wip1 heterodimer associated with the Ctf3 complex (Ctf3c) to form a sub-complex of the larger Ctf19 complex (Ctf19c).


Pssm-ID: 439342  Cd Length: 73  Bit Score: 45.47  E-value: 6.29e-08
                       10        20        30        40
               ....*....|....*....|....*....|....*....|....*.
6WUC_W      44 NKKLLLACGFQAILRKILLDARTRATAEGLREVYPYHIEAATQAFL 89
Cdd:cd22575 27 NKKLLLACGFQAILRKILLDARTRATAEGLREVYPYHIEAATQAFL 72
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH