2E9X,2Q9Q,2EHO


Conserved Protein Domain Family
GINS_B_Psf2

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cd21694: GINS_B_Psf2 
beta-strand (B) domain of GINS complex protein Psf2
Psf2 (partner of Sld5 2) is a component of GINS (named from the Japanese go-ichi-ni-san, meaning 5-1-2-3 for the Sld5, Psf1, Psf2, and Psf3 subunits) tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis and in ICL (interstrand crosslinks) repair. ICLs are toxic lesions that covalently attach opposite strands of DNA. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) and is involved in both the initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits Sld5, Psf1, Psf2, and Psf3 are homologous, and homologs are also found in archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, called the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3. This model represents the B-domain of GINS subunit Psf2.
Statistics
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PSSM-Id: 412030
Aligned: 80 rows
Threshold Bit Score: 50.9823
Created: 23-Apr-2020
Updated: 25-Oct-2021
Structure
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Program:
Drawing:
Aligned Rows:
 
tetramer
Conserved site includes 19 residues -Click on image for an interactive view with Cn3D
Feature 1:tetramer interface [polypeptide binding site]
Evidence:
  • Structure:2Q9Q, human GINS subunit Psf2 interface with other subunits in the heterotetramer; contacts at 4A
    View structure with Cn3D
  • Comment:the GINS complex contains four subunits: Sld5, Psf1, Psf2, and Psf3; it functions as a tight heterotetrameric complex in which major interactions are mediated through helix-helix interactions that amplify the helix-bundle-like structure of each individual subunit

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1        #### ###                  ##  #####                ##  #  #  #      
2E9X_B         2 DAAEVEFLAe-----kELVTIIPNFSLDk-IYLIGGDLGPFNPGLPVEVPLWLAINLKQrQKCRLLPP 63  human
2Q9Q_A         8 DAAEVEFLAe-----kELVTIIPNFSLDk-IYLIGGDLGPFNPGLPVEVPLWLAINLKQrQKCRLLPP 69  human
XP_001706618   7 APASDSFTTayfegqdTLVTVSMRGTIRetINLLNLQIHGLHCYRSAEVPLYLALQLFDtQQATICMP 74  Giardia lamblia ATCC 50803
EGX43749       9 TPQEVSFICe-----sELITIVPRQRLGa-LNLISIDTRPLVPPQRADVPLWLAVFLRKqKRCNIVPP 70  Arthrobotrys oligospora ATC...
Q8SV74         4 SPEEILHIAy-----eELVEIEPMTSIPe-LRLLERTYPPLMPLDIARIPLYAALLLKKsNMCKIRLP 65  Encephalitozoon cuniculi GB-M1
EHY52989      10 SPAEVAFLCe-----mEQVTIVPRQRLEr-LDLLGGTTRPLMPPQKTTLPLWLAILLKRqRRANIVPP 71  Exophiala dermatitidis NIH/...
Q6BZ44        12 MPSEVSFLAe-----nEYITILPRYSMKk-LELIGTKVPTLRGMRREKIPIWIAVILKSqDKCNIVPP 73  Debaryomyces hansenii CBS767
Q6C5R2        12 LPSELHFMAe-----nETIEILPRRVGNp-IKLAGTDLPLMHPLRKNRVPIWMAIALKKqQRCQFVPP 73  Yarrowia lipolytica CLIB122
Q7SAA9        10 TQNEVAFLAe-----mEMVTVVPRQRLDs-IDLLGGKTPQLRPPHRAQLPLWLALLLKKqRRANIVPP 71  Neurospora crassa OR74A
Q59MA3        12 MPSEITFLAe-----nELITILPRYSIKk-IDLIGTSIPNLRAMRRELVPLWVALILKSqDKCSIVPP 73  Candida albicans SC5314

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