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Conserved domains on  [gi|187169266|ref|NP_001119602|]
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DNA replication complex GINS protein PSF3 isoform c [Homo sapiens]

Protein Classification

DNA replication complex GINS protein PSF3( domain architecture ID 15823745)

DNA replication complex GINS protein PSF3 is a component of the heterotetrameric GINS complex; the GINS complex is essential for both the initiation and elongation stages of eukaryotic DNA replication

CATH:  1.20.58.2050
Gene Ontology:  GO:0006260
PubMed:  22918584|20070258

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GINS_A_psf3 cd11713
Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of ...
42-114 4.89e-21

Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of GINS, a tetrameric protein complex. Psf3 expression is up regulated in malignant colon cancer and it might be involved in cancer cell proliferation. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both 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 are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


:

Pssm-ID: 212551  Cd Length: 109  Bit Score: 81.54  E-value: 4.89e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187169266  42 RLGAFFLErsaGAETDNAVPQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLFQTGQKGLNDFQCWEKG 114
Cdd:cd11713   40 KLLSLFPE---DEELAEVLLETFKERFREIMDHAQNASNEDNSEFLRKLDELERKLFRAGQESLKDFKKWLKG 109
GINS_B super family cl41778
beta-strand (B) domain of GINS complex proteins: Sld5, Psf1, Psf2, Psf3, Gins51 and Gins23; ...
19-62 1.99e-07

beta-strand (B) domain of GINS complex proteins: Sld5, Psf1, Psf2, Psf3, Gins51 and Gins23; The GINS (named from the Japanese go-ichi-ni-san, meaning 5-1-2-3 for the Sld5, Psf1, Psf2, and Psf3 subunits) complex is involved in both the initiation and elongation stages of eukaryotic chromosome replication, with GINS being the component that most likely serves as the replicative helicase that unwinds duplex DNA ahead of the moving replication fork. This complex is found in eukaryotes and archaea, but not in bacteria. In eukaryotes, GINS is a tetrameric arrangement of four subunits Sld5, Psf1, Psf2 and Psf3, while in archaea, it consists of two different proteins named Gins51 and Gins23. The archaeal GINS complex can be either an alpha2beta2-type heterotetramer composed of Gins51 and Gins23, or a Gins51-only alpha4-type homotetramer. All GINS subunits are homologous and consist of two domains, called the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1/Gins51 are permuted with respect to Psf1/Psf3/Gins23. The overall tetrameric assemblies of GINS are similar, but the relative locations of the C-terminal small domains are different with respect to the alpha-helical domain, resulting in different subunit contacts. However, the basic function of GINS in DNA replication is conserved across eukaryotes and archaea. This model represents the beta-strand domain (B-domain) of GINS complex proteins.


The actual alignment was detected with superfamily member cd21693:

Pssm-ID: 425409  Cd Length: 64  Bit Score: 45.22  E-value: 1.99e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 187169266  19 FLSLDDILMSHEKLPVRTETAMPRLGafFLErsaGAETDNAVPQ 62
Cdd:cd21693    1 YYDIDDILAEEEKVPCRFEVDLPGLG--FLD---PSSDDDDLPP 39
 
Name Accession Description Interval E-value
GINS_A_psf3 cd11713
Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of ...
42-114 4.89e-21

Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of GINS, a tetrameric protein complex. Psf3 expression is up regulated in malignant colon cancer and it might be involved in cancer cell proliferation. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both 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 are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212551  Cd Length: 109  Bit Score: 81.54  E-value: 4.89e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187169266  42 RLGAFFLErsaGAETDNAVPQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLFQTGQKGLNDFQCWEKG 114
Cdd:cd11713   40 KLLSLFPE---DEELAEVLLETFKERFREIMDHAQNASNEDNSEFLRKLDELERKLFRAGQESLKDFKKWLKG 109
GINS_B_Psf3 cd21693
beta-strand (B) domain of GINS complex protein Psf3; Psf3 (partner of Sld5 3) is one of the ...
19-62 1.99e-07

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.


Pssm-ID: 412029  Cd Length: 64  Bit Score: 45.22  E-value: 1.99e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 187169266  19 FLSLDDILMSHEKLPVRTETAMPRLGafFLErsaGAETDNAVPQ 62
Cdd:cd21693    1 YYDIDDILAEEEKVPCRFEVDLPGLG--FLD---PSSDDDDLPP 39
 
Name Accession Description Interval E-value
GINS_A_psf3 cd11713
Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of ...
42-114 4.89e-21

Alpha-helical domain of GINS complex protein Psf3 (partner of Sld5 3); Psf3 is a component of GINS, a tetrameric protein complex. Psf3 expression is up regulated in malignant colon cancer and it might be involved in cancer cell proliferation. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both 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 are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212551  Cd Length: 109  Bit Score: 81.54  E-value: 4.89e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 187169266  42 RLGAFFLErsaGAETDNAVPQTFIGRFRRIMDSSQNAYNEDTSALVARLDEMERGLFQTGQKGLNDFQCWEKG 114
Cdd:cd11713   40 KLLSLFPE---DEELAEVLLETFKERFREIMDHAQNASNEDNSEFLRKLDELERKLFRAGQESLKDFKKWLKG 109
GINS_B_Psf3 cd21693
beta-strand (B) domain of GINS complex protein Psf3; Psf3 (partner of Sld5 3) is one of the ...
19-62 1.99e-07

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.


Pssm-ID: 412029  Cd Length: 64  Bit Score: 45.22  E-value: 1.99e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 187169266  19 FLSLDDILMSHEKLPVRTETAMPRLGafFLErsaGAETDNAVPQ 62
Cdd:cd21693    1 YYDIDDILAEEEKVPCRFEVDLPGLG--FLD---PSSDDDDLPP 39
GINS_A cd11581
Alpha-helical domain of GINS complex proteins; Sld5, Psf1, Psf2 and Psf3; The GINS complex is ...
62-107 5.58e-05

Alpha-helical domain of GINS complex proteins; Sld5, Psf1, Psf2 and Psf3; The GINS complex is involved in both initiation and elongation stages of eukaryotic chromosome replication, with GINS being the component that most likely serves as the replicative helicase that unwinds duplex DNA ahead of the moving replication fork. In eukaryotes, GINS is a tetrameric arrangement of four subunits Sld5, Psf1, Psf2 and Psf3. The GINS complex has been found in eukaryotes and archaea, but not in bacteria. The four subunits of the complex are homologous and consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212547  Cd Length: 103  Bit Score: 39.79  E-value: 5.58e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 187169266  62 QTFIGRFRRIMDSSQNAynedtsaLVARLDEMERGLFQTGQKGLND 107
Cdd:cd11581   65 TYLNSRLDKIRDLSPEF-------LPSNLTEEEIGYFQTYWKEVAE 103
 
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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