Sld5 [Drosophila melanogaster]
DNA replication complex GINS protein SLD5( domain architecture ID 16826204)
DNA replication complex GINS protein SLD5 is a component of the heterotetrameric GINS complex; the GINS complex is essential for both the initiation and elongation stages of eukaryotic DNA replication
List of domain hits
Name | Accession | Description | Interval | E-value | |||
GINS_A_Sld5 | cd11711 | Alpha-helical domain of GINS complex protein Sld5; Sld5 is a component of GINS tetrameric ... |
38-156 | 6.07e-44 | |||
Alpha-helical domain of GINS complex protein Sld5; Sld5 is a component of GINS tetrameric protein complex, and within the complex Sld5 interacts with Psf1 via its N-terminal A-domain, and with Psf2 through a combination of the A and B domains. Sld5 in Drosophila is required for normal cell cycle progression and the maintenance of genomic integrity. 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: 212549 Cd Length: 119 Bit Score: 143.52 E-value: 6.07e-44
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GINS_B_Sld5 | cd21692 | beta-strand (B) domain of GINS complex protein Sld5; Sld5 is a component of the GINS (named ... |
175-228 | 1.41e-16 | |||
beta-strand (B) domain of GINS complex protein Sld5; Sld5 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, within which Sld5 interacts with Psf1 via its N-terminal A-domain, and with Psf2 through a combination of the A and B domains. In Drosophila, Sld5 is required for normal cell cycle progression and the maintenance of genomic integrity. 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 Sld5, Psf1, Psf2 and Psf3 are homologous, and homologs are also found in archaea; the complex is not found in bacteria. Each subunit of the complex consists of two domains 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 Sld5. : Pssm-ID: 412028 Cd Length: 55 Bit Score: 71.04 E-value: 1.41e-16
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Name | Accession | Description | Interval | E-value | ||||
GINS_A_Sld5 | cd11711 | Alpha-helical domain of GINS complex protein Sld5; Sld5 is a component of GINS tetrameric ... |
38-156 | 6.07e-44 | ||||
Alpha-helical domain of GINS complex protein Sld5; Sld5 is a component of GINS tetrameric protein complex, and within the complex Sld5 interacts with Psf1 via its N-terminal A-domain, and with Psf2 through a combination of the A and B domains. Sld5 in Drosophila is required for normal cell cycle progression and the maintenance of genomic integrity. 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: 212549 Cd Length: 119 Bit Score: 143.52 E-value: 6.07e-44
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GINS_B_Sld5 | cd21692 | beta-strand (B) domain of GINS complex protein Sld5; Sld5 is a component of the GINS (named ... |
175-228 | 1.41e-16 | ||||
beta-strand (B) domain of GINS complex protein Sld5; Sld5 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, within which Sld5 interacts with Psf1 via its N-terminal A-domain, and with Psf2 through a combination of the A and B domains. In Drosophila, Sld5 is required for normal cell cycle progression and the maintenance of genomic integrity. 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 Sld5, Psf1, Psf2 and Psf3 are homologous, and homologs are also found in archaea; the complex is not found in bacteria. Each subunit of the complex consists of two domains 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 Sld5. Pssm-ID: 412028 Cd Length: 55 Bit Score: 71.04 E-value: 1.41e-16
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COG5086 | COG5086 | Uncharacterized conserved protein [Function unknown]; |
36-228 | 8.26e-16 | ||||
Uncharacterized conserved protein [Function unknown]; Pssm-ID: 227418 [Multi-domain] Cd Length: 218 Bit Score: 73.46 E-value: 8.26e-16
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SLD5_C | pfam16922 | DNA replication complex GINS protein SLD5 C-terminus; The C-terminal domain of DNA replication ... |
175-228 | 2.57e-13 | ||||
DNA replication complex GINS protein SLD5 C-terminus; The C-terminal domain of DNA replication complex GINS protein SLD5 is important in the assembly of the GINS complex, a complex which is involved in initiation of DNA replication and progression of DNA replication forks. Pssm-ID: 465315 Cd Length: 57 Bit Score: 62.56 E-value: 2.57e-13
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Sld5 | pfam05916 | GINS complex protein; The eukaryotic GINS complex is essential for the initiation and ... |
74-137 | 7.94e-07 | ||||
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: 46.34 E-value: 7.94e-07
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GET3_arsA_TRC40 | TIGR00345 | transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ... |
61-168 | 1.77e-03 | ||||
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that energize transport, although with different partner proteins for different functions. Recent findings show that TRC40 (GET3 in yeast) in involved in the insertion of tail-anchored membrane proteins in eukaryotes. A similar function is expected for members of this family in archaea. However, the earliest discovery of a function for this protein family is ArsA, an arsenic resistance protein that partners with ArsB (see pfam02040) for As(III) efflux. [Hypothetical proteins, Conserved] Pssm-ID: 273027 [Multi-domain] Cd Length: 284 Bit Score: 38.61 E-value: 1.77e-03
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Name | Accession | Description | Interval | E-value | ||||
GINS_A_Sld5 | cd11711 | Alpha-helical domain of GINS complex protein Sld5; Sld5 is a component of GINS tetrameric ... |
38-156 | 6.07e-44 | ||||
Alpha-helical domain of GINS complex protein Sld5; Sld5 is a component of GINS tetrameric protein complex, and within the complex Sld5 interacts with Psf1 via its N-terminal A-domain, and with Psf2 through a combination of the A and B domains. Sld5 in Drosophila is required for normal cell cycle progression and the maintenance of genomic integrity. 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: 212549 Cd Length: 119 Bit Score: 143.52 E-value: 6.07e-44
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GINS_B_Sld5 | cd21692 | beta-strand (B) domain of GINS complex protein Sld5; Sld5 is a component of the GINS (named ... |
175-228 | 1.41e-16 | ||||
beta-strand (B) domain of GINS complex protein Sld5; Sld5 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, within which Sld5 interacts with Psf1 via its N-terminal A-domain, and with Psf2 through a combination of the A and B domains. In Drosophila, Sld5 is required for normal cell cycle progression and the maintenance of genomic integrity. 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 Sld5, Psf1, Psf2 and Psf3 are homologous, and homologs are also found in archaea; the complex is not found in bacteria. Each subunit of the complex consists of two domains 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 Sld5. Pssm-ID: 412028 Cd Length: 55 Bit Score: 71.04 E-value: 1.41e-16
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COG5086 | COG5086 | Uncharacterized conserved protein [Function unknown]; |
36-228 | 8.26e-16 | ||||
Uncharacterized conserved protein [Function unknown]; Pssm-ID: 227418 [Multi-domain] Cd Length: 218 Bit Score: 73.46 E-value: 8.26e-16
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SLD5_C | pfam16922 | DNA replication complex GINS protein SLD5 C-terminus; The C-terminal domain of DNA replication ... |
175-228 | 2.57e-13 | ||||
DNA replication complex GINS protein SLD5 C-terminus; The C-terminal domain of DNA replication complex GINS protein SLD5 is important in the assembly of the GINS complex, a complex which is involved in initiation of DNA replication and progression of DNA replication forks. Pssm-ID: 465315 Cd Length: 57 Bit Score: 62.56 E-value: 2.57e-13
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GINS_A | cd11581 | Alpha-helical domain of GINS complex proteins; Sld5, Psf1, Psf2 and Psf3; The GINS complex is ... |
40-150 | 1.36e-09 | ||||
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: 53.65 E-value: 1.36e-09
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Sld5 | pfam05916 | GINS complex protein; The eukaryotic GINS complex is essential for the initiation and ... |
74-137 | 7.94e-07 | ||||
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: 46.34 E-value: 7.94e-07
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GET3_arsA_TRC40 | TIGR00345 | transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that ... |
61-168 | 1.77e-03 | ||||
transport-energizing ATPase, TRC40/GET3/ArsA family; Members of this family are ATPases that energize transport, although with different partner proteins for different functions. Recent findings show that TRC40 (GET3 in yeast) in involved in the insertion of tail-anchored membrane proteins in eukaryotes. A similar function is expected for members of this family in archaea. However, the earliest discovery of a function for this protein family is ArsA, an arsenic resistance protein that partners with ArsB (see pfam02040) for As(III) efflux. [Hypothetical proteins, Conserved] Pssm-ID: 273027 [Multi-domain] Cd Length: 284 Bit Score: 38.61 E-value: 1.77e-03
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GINS_B | cd21396 | beta-strand (B) domain of GINS complex proteins: Sld5, Psf1, Psf2, Psf3, Gins51 and Gins23; ... |
181-228 | 7.12e-03 | ||||
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: 33.59 E-value: 7.12e-03
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Blast search parameters | ||||
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