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Conserved domains on  [gi|558178208|ref|XP_006100650|]
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MAD2L1-binding protein [Myotis lucifugus]

Protein Classification

p31comet domain-containing protein( domain architecture ID 10534978)

p31comet domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
p31comet pfam06581
Mad1 and Cdc20-bound-Mad2 binding; This family is involved in the cell-cycle surveillance ...
10-274 0e+00

Mad1 and Cdc20-bound-Mad2 binding; This family is involved in the cell-cycle surveillance mechanism called the spindle checkpoint. This mechanism monitors the proper bipolar attachment of sister chromatids to spindle microtubules and ensures the fidelity of chromosome segregation during mitosis. A key player in mitosis is Mad2, and Mad2 exhibits an unusual two-state behaviour. A Mad1-Mad2 core complex recruits cytosolic Mad2 to kinetochores through Mad2 dimerization and converts Mad2 to a conformer amenable to Cdc20 binding. p31comet inactivates the checkpoint by binding to Mad1- or Cdc20-bound Mad2 in such a way as to stop Mad2 activation and to promote the dissociation of the Mad2-Cdc20 complex.


:

Pssm-ID: 461953  Cd Length: 265  Bit Score: 546.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558178208   10 SLTAAPGLEWYEEAEDTHAPHIELLDTTAAQELPSRSESFRPRHGLVPVVFPGPVSQDGCCQFTCEFLKHVMYQRLQLPL 89
Cdd:pfam06581   1 SPAAAPELEWYEESEETHAPQIELLETTSTQEPSSNSEHFCPRDSLVPVVFPGPVSQEGCCQFTCELLKHIMYQRQQLPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558178208   90 PYEQLKHFYRQSSPQAEDMVKKKPWAITEASSRKCQQTLEELESVLSHLESLFARTLVPRVLILLGGSVLNPKEFYELDL 169
Cdd:pfam06581  81 PYEQLKHFYRKPSPQAEDMMRKKAWAATEASSRKCQQALAELESVLSHLESLFARTLVPRVLILLGGSALSPKEFYELDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558178208  170 SRLAPSNVDQRVSTAACLRLIFRAIFMADAFSELQAPPLMGTIVMAQGHRDCGEDWFRPKLNYRVPIRGHKLTVTLSCGR 249
Cdd:pfam06581 161 SRLAPGRVDQSLSTAACLRRLFRAIFMADAFSELQAPPLMGTIVMAQGHRDCGEDWFRPKLNYRVPSRGHKLTVTLSCGR 240
                         250       260
                  ....*....|....*....|....*
gi 558178208  250 PSIPVTAWEDYIWFQAPVTLKGFHE 274
Cdd:pfam06581 241 PSIPDTAWEDYIWFQAPVTLKGFRE 265
 
Name Accession Description Interval E-value
p31comet pfam06581
Mad1 and Cdc20-bound-Mad2 binding; This family is involved in the cell-cycle surveillance ...
10-274 0e+00

Mad1 and Cdc20-bound-Mad2 binding; This family is involved in the cell-cycle surveillance mechanism called the spindle checkpoint. This mechanism monitors the proper bipolar attachment of sister chromatids to spindle microtubules and ensures the fidelity of chromosome segregation during mitosis. A key player in mitosis is Mad2, and Mad2 exhibits an unusual two-state behaviour. A Mad1-Mad2 core complex recruits cytosolic Mad2 to kinetochores through Mad2 dimerization and converts Mad2 to a conformer amenable to Cdc20 binding. p31comet inactivates the checkpoint by binding to Mad1- or Cdc20-bound Mad2 in such a way as to stop Mad2 activation and to promote the dissociation of the Mad2-Cdc20 complex.


Pssm-ID: 461953  Cd Length: 265  Bit Score: 546.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558178208   10 SLTAAPGLEWYEEAEDTHAPHIELLDTTAAQELPSRSESFRPRHGLVPVVFPGPVSQDGCCQFTCEFLKHVMYQRLQLPL 89
Cdd:pfam06581   1 SPAAAPELEWYEESEETHAPQIELLETTSTQEPSSNSEHFCPRDSLVPVVFPGPVSQEGCCQFTCELLKHIMYQRQQLPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558178208   90 PYEQLKHFYRQSSPQAEDMVKKKPWAITEASSRKCQQTLEELESVLSHLESLFARTLVPRVLILLGGSVLNPKEFYELDL 169
Cdd:pfam06581  81 PYEQLKHFYRKPSPQAEDMMRKKAWAATEASSRKCQQALAELESVLSHLESLFARTLVPRVLILLGGSALSPKEFYELDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558178208  170 SRLAPSNVDQRVSTAACLRLIFRAIFMADAFSELQAPPLMGTIVMAQGHRDCGEDWFRPKLNYRVPIRGHKLTVTLSCGR 249
Cdd:pfam06581 161 SRLAPGRVDQSLSTAACLRRLFRAIFMADAFSELQAPPLMGTIVMAQGHRDCGEDWFRPKLNYRVPSRGHKLTVTLSCGR 240
                         250       260
                  ....*....|....*....|....*
gi 558178208  250 PSIPVTAWEDYIWFQAPVTLKGFHE 274
Cdd:pfam06581 241 PSIPDTAWEDYIWFQAPVTLKGFRE 265
 
Name Accession Description Interval E-value
p31comet pfam06581
Mad1 and Cdc20-bound-Mad2 binding; This family is involved in the cell-cycle surveillance ...
10-274 0e+00

Mad1 and Cdc20-bound-Mad2 binding; This family is involved in the cell-cycle surveillance mechanism called the spindle checkpoint. This mechanism monitors the proper bipolar attachment of sister chromatids to spindle microtubules and ensures the fidelity of chromosome segregation during mitosis. A key player in mitosis is Mad2, and Mad2 exhibits an unusual two-state behaviour. A Mad1-Mad2 core complex recruits cytosolic Mad2 to kinetochores through Mad2 dimerization and converts Mad2 to a conformer amenable to Cdc20 binding. p31comet inactivates the checkpoint by binding to Mad1- or Cdc20-bound Mad2 in such a way as to stop Mad2 activation and to promote the dissociation of the Mad2-Cdc20 complex.


Pssm-ID: 461953  Cd Length: 265  Bit Score: 546.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558178208   10 SLTAAPGLEWYEEAEDTHAPHIELLDTTAAQELPSRSESFRPRHGLVPVVFPGPVSQDGCCQFTCEFLKHVMYQRLQLPL 89
Cdd:pfam06581   1 SPAAAPELEWYEESEETHAPQIELLETTSTQEPSSNSEHFCPRDSLVPVVFPGPVSQEGCCQFTCELLKHIMYQRQQLPL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558178208   90 PYEQLKHFYRQSSPQAEDMVKKKPWAITEASSRKCQQTLEELESVLSHLESLFARTLVPRVLILLGGSVLNPKEFYELDL 169
Cdd:pfam06581  81 PYEQLKHFYRKPSPQAEDMMRKKAWAATEASSRKCQQALAELESVLSHLESLFARTLVPRVLILLGGSALSPKEFYELDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 558178208  170 SRLAPSNVDQRVSTAACLRLIFRAIFMADAFSELQAPPLMGTIVMAQGHRDCGEDWFRPKLNYRVPIRGHKLTVTLSCGR 249
Cdd:pfam06581 161 SRLAPGRVDQSLSTAACLRRLFRAIFMADAFSELQAPPLMGTIVMAQGHRDCGEDWFRPKLNYRVPSRGHKLTVTLSCGR 240
                         250       260
                  ....*....|....*....|....*
gi 558178208  250 PSIPVTAWEDYIWFQAPVTLKGFHE 274
Cdd:pfam06581 241 PSIPDTAWEDYIWFQAPVTLKGFRE 265
 
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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