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Conserved domains on  [gi|312922345|ref|NP_001186186|]
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shugoshin 1 isoform 1J [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Shugoshin_N pfam07558
Shugoshin N-terminal coiled-coil region; The Shugoshin protein is found to have this conserved ...
 22-66 3.15e-06

Shugoshin N-terminal coiled-coil region; The Shugoshin protein is found to have this conserved N-terminal coiled-coil region and a highly conserved C-terminal basic region, family Shugoshin_C pfam07557. Shugoshin is a crucial target of Bub1 kinase function at kinetochores, necessary for both meiotic and mitotic localization of shugoshin to the kinetochore. Human shugoshin is diffusible and mediates kinetochore-driven formation of kinetochore-microtubules during bipolar spindle assembly. Further, the primary role of shugoshin is to ensure bipolar attachment of kinetochores, and its role in protecting cohesion has co-developed to facilitate this process.


:

Pssm-ID: 462208  Cd Length: 45  Bit Score: 42.60  E-value: 3.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 312922345   22 MKEKRNKNLAEIGKRRSFIAAPCQIITNTSTLLKNYQDNNKMLVL 66
Cdd:pfam07558   1 LKRKYLRQNRELAKSNSALSLKIRELEKEISELLSENLNLRSQVL 45
 
Name Accession Description Interval E-value
Shugoshin_N pfam07558
Shugoshin N-terminal coiled-coil region; The Shugoshin protein is found to have this conserved ...
 22-66 3.15e-06

Shugoshin N-terminal coiled-coil region; The Shugoshin protein is found to have this conserved N-terminal coiled-coil region and a highly conserved C-terminal basic region, family Shugoshin_C pfam07557. Shugoshin is a crucial target of Bub1 kinase function at kinetochores, necessary for both meiotic and mitotic localization of shugoshin to the kinetochore. Human shugoshin is diffusible and mediates kinetochore-driven formation of kinetochore-microtubules during bipolar spindle assembly. Further, the primary role of shugoshin is to ensure bipolar attachment of kinetochores, and its role in protecting cohesion has co-developed to facilitate this process.


Pssm-ID: 462208  Cd Length: 45  Bit Score: 42.60  E-value: 3.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 312922345   22 MKEKRNKNLAEIGKRRSFIAAPCQIITNTSTLLKNYQDNNKMLVL 66
Cdd:pfam07558   1 LKRKYLRQNRELAKSNSALSLKIRELEKEISELLSENLNLRSQVL 45
 
Name Accession Description Interval E-value
Shugoshin_N pfam07558
Shugoshin N-terminal coiled-coil region; The Shugoshin protein is found to have this conserved ...
 22-66 3.15e-06

Shugoshin N-terminal coiled-coil region; The Shugoshin protein is found to have this conserved N-terminal coiled-coil region and a highly conserved C-terminal basic region, family Shugoshin_C pfam07557. Shugoshin is a crucial target of Bub1 kinase function at kinetochores, necessary for both meiotic and mitotic localization of shugoshin to the kinetochore. Human shugoshin is diffusible and mediates kinetochore-driven formation of kinetochore-microtubules during bipolar spindle assembly. Further, the primary role of shugoshin is to ensure bipolar attachment of kinetochores, and its role in protecting cohesion has co-developed to facilitate this process.


Pssm-ID: 462208  Cd Length: 45  Bit Score: 42.60  E-value: 3.15e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 312922345   22 MKEKRNKNLAEIGKRRSFIAAPCQIITNTSTLLKNYQDNNKMLVL 66
Cdd:pfam07558   1 LKRKYLRQNRELAKSNSALSLKIRELEKEISELLSENLNLRSQVL 45
 
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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