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Conserved domains on  [gi|323334262|gb|EGA75644|]
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Psf1p [Saccharomyces cerevisiae AWRI796]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5230 COG5230
Uncharacterized conserved protein [Function unknown];
1-208 8.71e-100

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 227555 [Multi-domain]  Cd Length: 194  Bit Score: 287.23  E-value: 8.71e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262   1 MYGDLGNKLVLEAKRTKQLyarsnqDVnLPMYHEDIIRNILKEVSNL-RKNTEYLKEQQQLGMLDDKVAKCQYFVTLLCM 79
Cdd:COG5230    1 MFGELGNKLLLEDKRTDVL------DP-LPPYRRDEIKAIEGENEHLdRRMEEILQEASQAGSGIDEELSVNYVMMKYFK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262  80 ERNKRCLLAYQRLRTDILDSMAWNNnGLDLMSSItfsqqDTNnLSHQEQEYLKEYCDLITDLKsGDLVDIDLSGSLVPPS 159
Cdd:COG5230   74 ERNKRCLRAYKFLRSAALFDSFWSK-GKRMKSVG-----DTM-LSHEEEEYLEKYSNLLREYK-GPFKHIDLTGSLVPPV 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 323334262 160 DVFIDVRVLKDAGEIQTEYGVFNLIKDSQFFVRQSDVERLIQQGYLQKI 208
Cdd:COG5230  146 QFFIDVRVLKDCGVIMTEYGLINLKKDSQYFVRKNDVERLIDQGFLRKI 194
 
Name Accession Description Interval E-value
COG5230 COG5230
Uncharacterized conserved protein [Function unknown];
1-208 8.71e-100

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227555 [Multi-domain]  Cd Length: 194  Bit Score: 287.23  E-value: 8.71e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262   1 MYGDLGNKLVLEAKRTKQLyarsnqDVnLPMYHEDIIRNILKEVSNL-RKNTEYLKEQQQLGMLDDKVAKCQYFVTLLCM 79
Cdd:COG5230    1 MFGELGNKLLLEDKRTDVL------DP-LPPYRRDEIKAIEGENEHLdRRMEEILQEASQAGSGIDEELSVNYVMMKYFK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262  80 ERNKRCLLAYQRLRTDILDSMAWNNnGLDLMSSItfsqqDTNnLSHQEQEYLKEYCDLITDLKsGDLVDIDLSGSLVPPS 159
Cdd:COG5230   74 ERNKRCLRAYKFLRSAALFDSFWSK-GKRMKSVG-----DTM-LSHEEEEYLEKYSNLLREYK-GPFKHIDLTGSLVPPV 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 323334262 160 DVFIDVRVLKDAGEIQTEYGVFNLIKDSQFFVRQSDVERLIQQGYLQKI 208
Cdd:COG5230  146 QFFIDVRVLKDCGVIMTEYGLINLKKDSQYFVRKNDVERLIDQGFLRKI 194
GINS_A_psf1 cd11710
Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric ...
 3-143 3.43e-36

Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric protein complex. Psf1 is mainly expressed in highly proliferative tissues, such as blastocysts, adult bone marrow, and testis, in which the stem cell system is active. Loss of Psf1 causes embryonic lethality. 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: 212548  Cd Length: 129  Bit Score: 123.52  E-value: 3.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262   3 GDLGNKLVLEAKRTkqlyarsnQDVNLPMYHEDIIRNILKEVSNLRKNTEYLKEQQQLGMLDDKVaKCQYFVTLLCMERN 82
Cdd:cd11710    1 GDKANKLVKELKRS--------ENDTLPPYNEDLVRQVLEEIRDLYEENQALLEEAQEEEEDPGL-IPGLLVRHLSILRN 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323334262  83 KRCLLAYQRLRTDILDSMAWNNNGldlmssiTFSQQDTNNLSHQEQEYLKEYCDLITDLKS 143
Cdd:cd11710   72 KRCLLAYLYERLDRIRELRWENGS-------VLPEDIKENLSPAEKEYFKQYSKLLAEYMS 125
Sld5 pfam05916
GINS complex protein; The eukaryotic GINS complex is essential for the initiation and ...
 27-128 1.22e-06

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: 45.57  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262   27 VNLPMYHEDII-RNILKEVSNL-RKNTEYLKEQQQLGMLDDKVAKCQYF----VTLLCMERN---KRCLLAYQRLRTDIL 97
Cdd:pfam05916   1 PELPLWLAELLkRRGLVEIEPPeWLSIEELEAILADETKNDLSLLPPYFyelaVLLLELERDdelKRLLRDYLRIRLAKI 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 323334262   98 DSMAWNNNGLDlmssitFSQQDTNNLSHQEQ 128
Cdd:pfam05916  81 RKLAWHLNGSL------SPSDLLDNLSEEEL 105
 
Name Accession Description Interval E-value
COG5230 COG5230
Uncharacterized conserved protein [Function unknown];
1-208 8.71e-100

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 227555 [Multi-domain]  Cd Length: 194  Bit Score: 287.23  E-value: 8.71e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262   1 MYGDLGNKLVLEAKRTKQLyarsnqDVnLPMYHEDIIRNILKEVSNL-RKNTEYLKEQQQLGMLDDKVAKCQYFVTLLCM 79
Cdd:COG5230    1 MFGELGNKLLLEDKRTDVL------DP-LPPYRRDEIKAIEGENEHLdRRMEEILQEASQAGSGIDEELSVNYVMMKYFK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262  80 ERNKRCLLAYQRLRTDILDSMAWNNnGLDLMSSItfsqqDTNnLSHQEQEYLKEYCDLITDLKsGDLVDIDLSGSLVPPS 159
Cdd:COG5230   74 ERNKRCLRAYKFLRSAALFDSFWSK-GKRMKSVG-----DTM-LSHEEEEYLEKYSNLLREYK-GPFKHIDLTGSLVPPV 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 323334262 160 DVFIDVRVLKDAGEIQTEYGVFNLIKDSQFFVRQSDVERLIQQGYLQKI 208
Cdd:COG5230  146 QFFIDVRVLKDCGVIMTEYGLINLKKDSQYFVRKNDVERLIDQGFLRKI 194
GINS_A_psf1 cd11710
Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric ...
 3-143 3.43e-36

Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric protein complex. Psf1 is mainly expressed in highly proliferative tissues, such as blastocysts, adult bone marrow, and testis, in which the stem cell system is active. Loss of Psf1 causes embryonic lethality. 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: 212548  Cd Length: 129  Bit Score: 123.52  E-value: 3.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262   3 GDLGNKLVLEAKRTkqlyarsnQDVNLPMYHEDIIRNILKEVSNLRKNTEYLKEQQQLGMLDDKVaKCQYFVTLLCMERN 82
Cdd:cd11710    1 GDKANKLVKELKRS--------ENDTLPPYNEDLVRQVLEEIRDLYEENQALLEEAQEEEEDPGL-IPGLLVRHLSILRN 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 323334262  83 KRCLLAYQRLRTDILDSMAWNNNGldlmssiTFSQQDTNNLSHQEQEYLKEYCDLITDLKS 143
Cdd:cd11710   72 KRCLLAYLYERLDRIRELRWENGS-------VLPEDIKENLSPAEKEYFKQYSKLLAEYMS 125
GINS_B_Psf1 cd21696
beta-strand (B) domain of GINS complex protein Psf1; Psf1 (partner of Sld5 1) is a component ...
 161-208 4.38e-17

beta-strand (B) domain of GINS complex protein Psf1; Psf1 (partner of Sld5 1) is a component of the 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 is mainly expressed in highly proliferative tissues, such as blastocysts, adult bone marrow, and testis, in which the stem cell system is active. Psf1 has been reported to be a prognostic biomarker in breast cancer, prostate cancer, hepatocellular carcinoma, and non-small cell lung cancer (NSCLC) patients treated with surgery following preoperative chemotherapy or chemoradiotherapy. Loss of Psf1 causes embryonic lethality. 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 Psf1.


Pssm-ID: 412032  Cd Length: 49  Bit Score: 71.79  E-value: 4.38e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 323334262 161 VFIDVRVLKDAGEIQTEYG-VFNLIKDSQFFVRQSDVERLIQQGYLQKI 208
Cdd:cd21696    1 LYIEVRVLKDYGEVETEDGtVINLKKGSQHFLPRSDVEPLIRQGVLEHV 49
GINS_B cd21396
beta-strand (B) domain of GINS complex proteins: Sld5, Psf1, Psf2, Psf3, Gins51 and Gins23; ...
 162-208 3.30e-10

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.


Pssm-ID: 412027  Cd Length: 49  Bit Score: 53.62  E-value: 3.30e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 323334262 162 FIDVRVLKDAGEIQTE--YGVFNLIKDSQFFVRQSDVERLIQQGYLQKI 208
Cdd:cd21396    1 KVAVRVEKDLPRILAEfaETVGPFPKGSQVEVPLWLARGLVQRGALRLI 49
Sld5 pfam05916
GINS complex protein; The eukaryotic GINS complex is essential for the initiation and ...
 27-128 1.22e-06

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: 45.57  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 323334262   27 VNLPMYHEDII-RNILKEVSNL-RKNTEYLKEQQQLGMLDDKVAKCQYF----VTLLCMERN---KRCLLAYQRLRTDIL 97
Cdd:pfam05916   1 PELPLWLAELLkRRGLVEIEPPeWLSIEELEAILADETKNDLSLLPPYFyelaVLLLELERDdelKRLLRDYLRIRLAKI 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 323334262   98 DSMAWNNNGLDlmssitFSQQDTNNLSHQEQ 128
Cdd:pfam05916  81 RKLAWHLNGSL------SPSDLLDNLSEEEL 105
 
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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