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Conserved domains on  [gi|79313201|ref|NP_001030680|]
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PSF2 [Arabidopsis thaliana]

Protein Classification

DNA replication complex GINS protein PSF2( domain architecture ID 16902698)

DNA replication complex GINS protein PSF2 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:  1.20.58.1020|3.40.5.50
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_psf2 cd11712
Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of ...
 47-162 1.55e-45

Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of GINS tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis. 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: 212550  Cd Length: 119  Bit Score: 146.22  E-value: 1.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201  47 RGKCTFRPPGWMSVDNLTQILEAERESQsTFQALPFSYVEIARLLFDHARDDIPDMYMVRSLVEDIRDVRLHKLETNLGS 126
Cdd:cd11712   1 RNKCRIVPPDWLTVEYLKEILEEEKKSE-TFSPLPFHYLEIAKLLLEVASDDIPDADEIRSLVEDIRDVRQAKLRSGLEK 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 79313201 127 F--QGTSAVKISNVSAMEVNIVRPFVIRALEAFYKHDK 162
Cdd:cd11712  80 LlgSGEVHAKLDNLTAMEINEIRPFLSGALDKLRKLRA 117
GINS_B_Psf2 cd21694
beta-strand (B) domain of GINS complex protein Psf2; Psf2 (partner of Sld5 2) is a component ...
 1-55 2.09e-27

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.


:

Pssm-ID: 412030  Cd Length: 62  Bit Score: 97.98  E-value: 2.09e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 79313201   1 MAEDELVEIVPNMNMEQLNFISGDFGRFIPQIPTKVPLWLAVALKRRGKCTFRPP 55
Cdd:cd21694   8 LAEDELVTIIPNFSLDKLNLISGDYGPFRPGRPVEVPLWLAINLKKRQKCRIVPP 62
 
Name Accession Description Interval E-value
GINS_A_psf2 cd11712
Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of ...
 47-162 1.55e-45

Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of GINS tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis. 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: 212550  Cd Length: 119  Bit Score: 146.22  E-value: 1.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201  47 RGKCTFRPPGWMSVDNLTQILEAERESQsTFQALPFSYVEIARLLFDHARDDIPDMYMVRSLVEDIRDVRLHKLETNLGS 126
Cdd:cd11712   1 RNKCRIVPPDWLTVEYLKEILEEEKKSE-TFSPLPFHYLEIAKLLLEVASDDIPDADEIRSLVEDIRDVRQAKLRSGLEK 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 79313201 127 F--QGTSAVKISNVSAMEVNIVRPFVIRALEAFYKHDK 162
Cdd:cd11712  80 LlgSGEVHAKLDNLTAMEINEIRPFLSGALDKLRKLRA 117
COG5093 COG5093
Uncharacterized conserved protein [Function unknown];
1-155 2.74e-30

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227424 [Multi-domain]  Cd Length: 185  Bit Score: 109.59  E-value: 2.74e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201   1 MAEDELVEIVPNMNMEQLNFISGD-FGRFIPQIPTKVPLWLAVALKRRGKCTFRPPGWMSVDNLTQILEAERESQSTFQA 79
Cdd:COG5093  19 IAYNELIEIEPMTTIPQLRLLERAtYPPMMPLDIARVPLWAALLLKKQNMCKIVLPSWLQLESLKMSIDVEIEKADEFSE 98

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79313201  80 LPFSYVEIARLLFDHARDDIPDMYMVRSLVEDIRDVRLHKLETNLGSFQGtSAVKISNVSAMEVNIVRPFVIRALE 155
Cdd:COG5093  99 LPPYWLPLATELLNENCDDVEDIEESRMIVEDIREIRQAKTLKGLKCLNE-KALNLDNLTLFEINEIRPLILESMD 173
GINS_B_Psf2 cd21694
beta-strand (B) domain of GINS complex protein Psf2; Psf2 (partner of Sld5 2) is a component ...
 1-55 2.09e-27

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.


Pssm-ID: 412030  Cd Length: 62  Bit Score: 97.98  E-value: 2.09e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 79313201   1 MAEDELVEIVPNMNMEQLNFISGDFGRFIPQIPTKVPLWLAVALKRRGKCTFRPP 55
Cdd:cd21694   8 LAEDELVTIIPNFSLDKLNLISGDYGPFRPGRPVEVPLWLAINLKKRQKCRIVPP 62
Sld5 pfam05916
GINS complex protein; The eukaryotic GINS complex is essential for the initiation and ...
 36-143 9.65e-18

GINS complex protein; The eukaryotic GINS complex is essential for the initiation and elongation phases of DNA replication. It consists of four paralogous protein subunits (Sld5, Psf1, Psf2 and Psf3), all of which are included in this family. The GINS complex is conserved from yeast to humans, and has been shown in human to bind directly to DNA primase.


Pssm-ID: 399129  Cd Length: 105  Bit Score: 74.46  E-value: 9.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201    36 VPLWLAVALKRRGKCTFRPPGWMSVDNLTQILEAEResQSTFQALPFSYVEIARLLFDHARDDIpdmymVRSLVEDIRDV 115
Cdd:pfam05916   3 LPLWLAELLKRRGLVEIEPPEWLSIEELEAILADET--KNDLSLLPPYFYELAVLLLELERDDE-----LKRLLRDYLRI 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 79313201   116 RLHKLETNLGSFQGT--SAVKISNVSAMEV 143
Cdd:pfam05916  76 RLAKIRKLAWHLNGSlsPSDLLDNLSEEEL 105
PTZ00362 PTZ00362
hypothetical protein; Provisional
 2-162 2.55e-08

hypothetical protein; Provisional


Pssm-ID: 240380 [Multi-domain]  Cd Length: 479  Bit Score: 52.84  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201    2 AEDELVEI-----VPNMNmeqLNFISG-DFGRFIPQIPTKVPLWLAVALKRRGKCTFRPPGWMSVDNLTQILEAERESQS 75
Cdd:PTZ00362 282 ALDELVVVkalvdIPYID---LSEIEGfDFKEMKSGERQWLPIYIAKELSHFGLVTVEFPFWFYIKNLKNIYEREFEDQN 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201   76 TFQALPFSY-VEIARLLFDH---ARDDIPDM--------YM--VRSLVEDIRDVRLHKLETNLGSF-QGTSAVKISNVSA 140
Cdd:PTZ00362 359 ELTDLPSPYfFEISSMFLENnifKKVTPIETigqrtvykYIskVAGLVEDIRYKRLKKIMNHLENQdVHSSIIYIDNLQI 438

                        170       180
                 ....*....|....*....|..
gi 79313201  141 MEVNIVRPFviraLEAFYKHDK 162
Cdd:PTZ00362 439 SETYCVNQL----LSVFFQYDK 456
 
Name Accession Description Interval E-value
GINS_A_psf2 cd11712
Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of ...
 47-162 1.55e-45

Alpha-helical domain of GINS complex protein Psf2 (partner of Sld5 2); Psf2 is a component of GINS tetrameric protein complex and has been found to play important roles in normal eye development in Xenopus laevis. 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: 212550  Cd Length: 119  Bit Score: 146.22  E-value: 1.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201  47 RGKCTFRPPGWMSVDNLTQILEAERESQsTFQALPFSYVEIARLLFDHARDDIPDMYMVRSLVEDIRDVRLHKLETNLGS 126
Cdd:cd11712   1 RNKCRIVPPDWLTVEYLKEILEEEKKSE-TFSPLPFHYLEIAKLLLEVASDDIPDADEIRSLVEDIRDVRQAKLRSGLEK 79

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 79313201 127 F--QGTSAVKISNVSAMEVNIVRPFVIRALEAFYKHDK 162
Cdd:cd11712  80 LlgSGEVHAKLDNLTAMEINEIRPFLSGALDKLRKLRA 117
COG5093 COG5093
Uncharacterized conserved protein [Function unknown];
1-155 2.74e-30

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227424 [Multi-domain]  Cd Length: 185  Bit Score: 109.59  E-value: 2.74e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201   1 MAEDELVEIVPNMNMEQLNFISGD-FGRFIPQIPTKVPLWLAVALKRRGKCTFRPPGWMSVDNLTQILEAERESQSTFQA 79
Cdd:COG5093  19 IAYNELIEIEPMTTIPQLRLLERAtYPPMMPLDIARVPLWAALLLKKQNMCKIVLPSWLQLESLKMSIDVEIEKADEFSE 98

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79313201  80 LPFSYVEIARLLFDHARDDIPDMYMVRSLVEDIRDVRLHKLETNLGSFQGtSAVKISNVSAMEVNIVRPFVIRALE 155
Cdd:COG5093  99 LPPYWLPLATELLNENCDDVEDIEESRMIVEDIREIRQAKTLKGLKCLNE-KALNLDNLTLFEINEIRPLILESMD 173
GINS_B_Psf2 cd21694
beta-strand (B) domain of GINS complex protein Psf2; Psf2 (partner of Sld5 2) is a component ...
 1-55 2.09e-27

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.


Pssm-ID: 412030  Cd Length: 62  Bit Score: 97.98  E-value: 2.09e-27
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 79313201   1 MAEDELVEIVPNMNMEQLNFISGDFGRFIPQIPTKVPLWLAVALKRRGKCTFRPP 55
Cdd:cd21694   8 LAEDELVTIIPNFSLDKLNLISGDYGPFRPGRPVEVPLWLAINLKKRQKCRIVPP 62
Sld5 pfam05916
GINS complex protein; The eukaryotic GINS complex is essential for the initiation and ...
 36-143 9.65e-18

GINS complex protein; The eukaryotic GINS complex is essential for the initiation and elongation phases of DNA replication. It consists of four paralogous protein subunits (Sld5, Psf1, Psf2 and Psf3), all of which are included in this family. The GINS complex is conserved from yeast to humans, and has been shown in human to bind directly to DNA primase.


Pssm-ID: 399129  Cd Length: 105  Bit Score: 74.46  E-value: 9.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201    36 VPLWLAVALKRRGKCTFRPPGWMSVDNLTQILEAEResQSTFQALPFSYVEIARLLFDHARDDIpdmymVRSLVEDIRDV 115
Cdd:pfam05916   3 LPLWLAELLKRRGLVEIEPPEWLSIEELEAILADET--KNDLSLLPPYFYELAVLLLELERDDE-----LKRLLRDYLRI 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 79313201   116 RLHKLETNLGSFQGT--SAVKISNVSAMEV 143
Cdd:pfam05916  76 RLAKIRKLAWHLNGSlsPSDLLDNLSEEEL 105
PTZ00362 PTZ00362
hypothetical protein; Provisional
 2-162 2.55e-08

hypothetical protein; Provisional


Pssm-ID: 240380 [Multi-domain]  Cd Length: 479  Bit Score: 52.84  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201    2 AEDELVEI-----VPNMNmeqLNFISG-DFGRFIPQIPTKVPLWLAVALKRRGKCTFRPPGWMSVDNLTQILEAERESQS 75
Cdd:PTZ00362 282 ALDELVVVkalvdIPYID---LSEIEGfDFKEMKSGERQWLPIYIAKELSHFGLVTVEFPFWFYIKNLKNIYEREFEDQN 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79313201   76 TFQALPFSY-VEIARLLFDH---ARDDIPDM--------YM--VRSLVEDIRDVRLHKLETNLGSF-QGTSAVKISNVSA 140
Cdd:PTZ00362 359 ELTDLPSPYfFEISSMFLENnifKKVTPIETigqrtvykYIskVAGLVEDIRYKRLKKIMNHLENQdVHSSIIYIDNLQI 438

                        170       180
                 ....*....|....*....|..
gi 79313201  141 MEVNIVRPFviraLEAFYKHDK 162
Cdd:PTZ00362 439 SETYCVNQL----LSVFFQYDK 456
 
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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