5C9N,2WVR,5C9N,4BRY,4BRY


Conserved Protein Domain Family
geminin-like_CC

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cd21103: geminin-like_CC 
Click on image for an interactive view with Cn3D
coiled-coil domain found in the geminin family
The geminin family includes geminin, geminin coiled-coil domain-containing protein 1 (GemC1), and McIdas. Together, geminin, GemC1, and McIdas (also called Idas or multicilin), controls both the cell cycle and differentiation decisions in cells. They were initially identified as cell cycle regulators associated with the chromosome cycle. Geminin is required to ensure once-per-cell-cycle genome replication, while McIdas and GemC1 bind to geminin and are implicated in DNA replication control. Geminin binds to Cdt1, a key component and crucial regulator of pre-replicative complexes (pre-RC), in a timely manner to inhibit DNA replication. Geminin family members also function as early regulators of multiciliogenesis. GemC1 and McIdas specify the multiciliate cell fate by forming complexes with the E2F4/5 transcription factors, resulting in centriole amplification and cilia formation. Geminin family proteins contain a homologous central coiled-coil domain that mediates homo- and heterodimerization; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of the geminin family.
Statistics
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PSSM-Id: 439141
Aligned: 5 rows
Threshold Bit Score: 53.031
Created: 23-Dec-2019
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
 
dimer interface
Conserved site includes 21 residues -Click on image for an interactive view with Cn3D
Feature 1:dimer interface [polypeptide binding site]
Evidence:
  • Comment:geminin family proteins form homo- and heterodimers between them through their coiled-coil domains; this ability is likely to be important for modulating their function in cycling and differentiating cells
  • Structure:5C9N: Human Geminin coiled-coil domain-containing protein 1 forms a homodimer; contacts at 4.0A
    View structure with Cn3D
  • Structure:4BRY: Human multicilin forms a heterodimer with geminin; contacts at 4A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1     #  ## ##  ## ##  ## ##  ## ##  #   #  #  #                
5C9N_B     10 CSWEEAQLSSQLYRNKQLQDTLVQKEEELARLHEENNHLRQYLNSALVKCEEEKAKKE 67  Homo sapiens
2WVR_A    103 AEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNG 160 human
5C9N_A     10 CSWEEAQLSSQLYRNKQLQDTLVQKEEELARLHEENNHLRQYLNSALVKCEEEKAKKE 67  human
4BRY_B     14 ADQNQRALGDALVENNQLHVTLTQKQEEIASLKERNVQLKELASRTRHLASVLDKLMI 71  human
4BRY_A     21 AEKRRKALYEALKENEKLHKEIEQKDNEIARLKKENKELAEVAEHVQYMAELIERLNG 78  human

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