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Conserved domains on  [gi|67460137|sp|Q12248|]
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RecName: Full=DASH complex subunit DAD1; AltName: Full=DUO1 and DAM1-interacting protein 1; AltName: Full=Outer kinetochore protein DAD1

Protein Classification

DASH complex subunit DAD1( domain architecture ID 10554552)

DASH complex subunit DAD1 is a component of the DASH complex, a microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DASH_Dad1 pfam08649
DASH complex subunit Dad1; The DASH complex is a ~10 subunit microtubule-binding complex that ...
 19-73 1.03e-22

DASH complex subunit Dad1; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro. Components of the DASH complex, including Dam1, Duo1, Spc34, Dad1 and Ask1, are essential and connect the centromere to the plus end of spindle microtubules. Throughout the cell cycle Dad1 remains bound to kinetochores throughout the cell cycle and its association is dependent on the Mis6 and Mal2.


:

Pssm-ID: 430129  Cd Length: 55  Bit Score: 82.63  E-value: 1.03e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 67460137   19 YFIEQRNIVLQEINETMNSILNGLNGLNISLESSIAVGREFQSVSDLWKTLYDGL 73
Cdd:pfam08649  1 YFERQRDRLIQEIANSMESVLNNLNALNRSLESVIGVGKEFESVAALWSQFYNGM 55
 
Name Accession Description Interval E-value
DASH_Dad1 pfam08649
DASH complex subunit Dad1; The DASH complex is a ~10 subunit microtubule-binding complex that ...
 19-73 1.03e-22

DASH complex subunit Dad1; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro. Components of the DASH complex, including Dam1, Duo1, Spc34, Dad1 and Ask1, are essential and connect the centromere to the plus end of spindle microtubules. Throughout the cell cycle Dad1 remains bound to kinetochores throughout the cell cycle and its association is dependent on the Mis6 and Mal2.


Pssm-ID: 430129  Cd Length: 55  Bit Score: 82.63  E-value: 1.03e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 67460137   19 YFIEQRNIVLQEINETMNSILNGLNGLNISLESSIAVGREFQSVSDLWKTLYDGL 73
Cdd:pfam08649  1 YFERQRDRLIQEIANSMESVLNNLNALNRSLESVIGVGKEFESVAALWSQFYNGM 55
 
Name Accession Description Interval E-value
DASH_Dad1 pfam08649
DASH complex subunit Dad1; The DASH complex is a ~10 subunit microtubule-binding complex that ...
 19-73 1.03e-22

DASH complex subunit Dad1; The DASH complex is a ~10 subunit microtubule-binding complex that is transferred to the kinetochore prior to mitosis. In Saccharomyces cerevisiae DASH forms both rings and spiral structures on microtubules in vitro. Components of the DASH complex, including Dam1, Duo1, Spc34, Dad1 and Ask1, are essential and connect the centromere to the plus end of spindle microtubules. Throughout the cell cycle Dad1 remains bound to kinetochores throughout the cell cycle and its association is dependent on the Mis6 and Mal2.


Pssm-ID: 430129  Cd Length: 55  Bit Score: 82.63  E-value: 1.03e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 67460137   19 YFIEQRNIVLQEINETMNSILNGLNGLNISLESSIAVGREFQSVSDLWKTLYDGL 73
Cdd:pfam08649  1 YFERQRDRLIQEIANSMESVLNNLNALNRSLESVIGVGKEFESVAALWSQFYNGM 55
 
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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