2Q9Q,2E9X,2EHO,6RAW,6XTX


Conserved Protein Domain Family
GINS_B_Psf3

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cd21693: GINS_B_Psf3 
beta-strand (B) domain of GINS complex protein Psf3
Psf3 (partner of Sld5 3) is one of the proteins known to comprise the GINS (named from the Japanese go-ichi-ni-san, meaning 5-1-2-3 for the Sld5, Psf1, Psf2, and Psf3 subunits) complex, which is a macromolecular protein complex associated with DNA replication. Psf3 is dysregulated in cancer cells, and its overexpression may be related to tumor progression in some cancers including colon, breast, and lung cancers; its expression can be used as a prognostic indicator in some cancers. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that 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 Psf3.
Statistics
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PSSM-Id: 412029
Aligned: 80 rows
Threshold Bit Score: 54.8513
Created: 22-Apr-2020
Updated: 25-Oct-2021
Structure
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Program:
Drawing:
Aligned Rows:
 
tetramer
Conserved site includes 17 residues -Click on image for an interactive view with Cn3D
Feature 1:tetramer interface [polypeptide binding site]
Evidence:
  • Structure:2Q9Q, human GINS subunit Psf3 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        ## # ### ##          ####                           ##  ##      #      
2Q9Q_D        23 FLSLDDILMSHEKLPVRTETAMPRLGafflersagaetdnaVPQGSKLELPLWLAKGLFDnkrRILSVELP 93  human
ACO10293       5 YLDLHDILATSYRIPVKTSSSLKSLGfldps-----sgledLPENFKVEMPLWMVFPLLR---HGLGPDFP 67  Caligus rogercresseyi
XP_002506457   4 YFDIDSFLAEQTRVPVVFNSGCTGLGkemdkm----cqtrdLPMGEEVELPFWLVPKLFEq--NMVGPKMP 68  Micromonas sp. RCC299
ADF43165       4 YWNLDAALAEETTVPLKFKYGILGVArvlepg----stnndIDSGTKVDAPLWLAAALSRr--GMTSFGAP 68  Chlamydomonas reinhardtii
XP_003063351   6 YLSVSAFLTEQEKVPLVFNSGCSGLGrevdeq----cetddLPPGSAASMPLWLVPKLYEq--NMVGPRMP 70  Micromonas pusilla CCMP1545
EFN54484       5 YYRVDAMMAEETYVPVRLVHGCTGVGtvidps----sdqadLPPGTRLDLPLWMVPPMAGr--NMLQVDLP 69  Chlorella variabilis
XP_003377900  11 YLELVDILATEEKVKVKVNKDIRKLGyldpn-----gnrenLPKGFVVELPLWIARELSSgtqPPLNLILP 76  Trichinella spiralis
EIE20749      15 YYSLDAVLAEETLIPCVFKCGSRGVGraidps----cgaedVKSRAAVELPLWMLQPLTSr--DMLTVKAP 79  Coccomyxa sp. C-169
XP_011270110   3 YHDIDEILMEQELVPVAFKTEAKWLGhldpg-----saspdLPEGARLDIPFWMVVNLHHq--DAIEVFAP 66  Capsaspora owczarzaki AT...
XP_011401933   5 YYSPLAISAEETLVRVRLEHGCTGVGsvidps----adgadLAPGSTLDVPLWLASSLAQr--GMARVELP 69  Auxenochlorella protothe...

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