RecName: Full=Homologous-pairing protein 2 homolog; AltName: Full=PSMC3-interacting protein; AltName: Full=Proteasome 26S ATPase subunit 3-interacting protein; AltName: Full=Tat-binding protein 1-interacting protein; Short=TBP-1-interacting protein
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| TBPIP | pfam07106 | TBPIP/Hop2 winged helix domain; This family consists of several eukaryotic TBP-1 interacting ... |
11-74 | 1.37e-22 | ||
TBPIP/Hop2 winged helix domain; This family consists of several eukaryotic TBP-1 interacting protein (TBPIP) sequences. TBP-1 has been demonstrated to interact with the human immunodeficiency virus type 1 (HIV-1) viral protein Tat, then modulate the essential replication process of HIV. In addition, TBP-1 has been shown to be a component of the 26S proteasome, a basic multiprotein complex that degrades ubiquitinated proteins in an ATP-dependent fashion. Human TBPIP interacts with human TBP-1 then modulates the inhibitory action of human TBP-1 on HIV-Tat-mediated transactivation. TBPIP was found to be an activator that specifically stimulates the homologous pairing catalyzed by DMC1. Family members also include yeast homologous-pairing protein 2 (Hop2) and its homologs from animals and plants. They are required for proper homologous pairing and efficient cross-over and intragenic recombination during meiosis. : Pssm-ID: 429296 Cd Length: 62 Bit Score: 86.65 E-value: 1.37e-22
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| LZ3wCH | pfam18517 | Leucine zipper with capping helix domain; This domain is found at the C-terminal region of ... |
154-210 | 3.52e-15 | ||
Leucine zipper with capping helix domain; This domain is found at the C-terminal region of Hop2 and Mnd1 proteins. In meiotic DNA recombination, the Hop2-Mnd1 complex promotes Dmc1-mediated single-stranded DNA (ssDNA) invasion into homologous chromosomes to form a synaptic complex. Hop2 (for homologous pairing; also known as TBPIP) is expressed specifically during meiosis, same as Mnd1 (for meiotic nuclear divisions 1). The C-terminal region of both Hop2 and Mnd1, folds into three alpha-helices that are interrupted by two short non-helical regions. These alpha-helices of the two proteins together form a parallel coiled coil that provides the major interface for heterodimer formation. The non-helical regions form substantially kinked junctions between adjacent leucine zippers: the LZ1-LZ2 and LZ2-LZ3 junctions.This domain is the C-terminal segment of Hop2 and Mnd1 which folds back onto the C-terminal leucine zipper (LZ3) to form a helical bundle-like structure, hence designated LZ3wCH (for LZ3 with capping helices). The LZ3wCH region plays a role in interacting with the Dmc1 nucleofilament. : Pssm-ID: 465789 Cd Length: 55 Bit Score: 67.18 E-value: 3.52e-15
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| Name | Accession | Description | Interval | E-value | ||
| TBPIP | pfam07106 | TBPIP/Hop2 winged helix domain; This family consists of several eukaryotic TBP-1 interacting ... |
11-74 | 1.37e-22 | ||
TBPIP/Hop2 winged helix domain; This family consists of several eukaryotic TBP-1 interacting protein (TBPIP) sequences. TBP-1 has been demonstrated to interact with the human immunodeficiency virus type 1 (HIV-1) viral protein Tat, then modulate the essential replication process of HIV. In addition, TBP-1 has been shown to be a component of the 26S proteasome, a basic multiprotein complex that degrades ubiquitinated proteins in an ATP-dependent fashion. Human TBPIP interacts with human TBP-1 then modulates the inhibitory action of human TBP-1 on HIV-Tat-mediated transactivation. TBPIP was found to be an activator that specifically stimulates the homologous pairing catalyzed by DMC1. Family members also include yeast homologous-pairing protein 2 (Hop2) and its homologs from animals and plants. They are required for proper homologous pairing and efficient cross-over and intragenic recombination during meiosis. Pssm-ID: 429296 Cd Length: 62 Bit Score: 86.65 E-value: 1.37e-22
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| LZ3wCH | pfam18517 | Leucine zipper with capping helix domain; This domain is found at the C-terminal region of ... |
154-210 | 3.52e-15 | ||
Leucine zipper with capping helix domain; This domain is found at the C-terminal region of Hop2 and Mnd1 proteins. In meiotic DNA recombination, the Hop2-Mnd1 complex promotes Dmc1-mediated single-stranded DNA (ssDNA) invasion into homologous chromosomes to form a synaptic complex. Hop2 (for homologous pairing; also known as TBPIP) is expressed specifically during meiosis, same as Mnd1 (for meiotic nuclear divisions 1). The C-terminal region of both Hop2 and Mnd1, folds into three alpha-helices that are interrupted by two short non-helical regions. These alpha-helices of the two proteins together form a parallel coiled coil that provides the major interface for heterodimer formation. The non-helical regions form substantially kinked junctions between adjacent leucine zippers: the LZ1-LZ2 and LZ2-LZ3 junctions.This domain is the C-terminal segment of Hop2 and Mnd1 which folds back onto the C-terminal leucine zipper (LZ3) to form a helical bundle-like structure, hence designated LZ3wCH (for LZ3 with capping helices). The LZ3wCH region plays a role in interacting with the Dmc1 nucleofilament. Pssm-ID: 465789 Cd Length: 55 Bit Score: 67.18 E-value: 3.52e-15
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| Fur_like | cd07153 | Ferric uptake regulator(Fur) and related metalloregulatory proteins; typically iron-dependent, ... |
15-72 | 9.72e-06 | ||
Ferric uptake regulator(Fur) and related metalloregulatory proteins; typically iron-dependent, DNA-binding repressors and activators; Ferric uptake regulator (Fur) and related metalloregulatory proteins are iron-dependent, DNA-binding repressors and activators mainly involved in iron metabolism. A general model for Fur repression under iron-rich conditions is that activated Fur (a dimer having one Fe2+ coordinated per monomer) binds to specific DNA sequences (Fur boxes) in the promoter region of iron-responsive genes, hindering access of RNA polymerase, and repressing transcription. Positive regulation by Fur can be direct or indirect, as in the Fur repression of an anti-sense regulatory small RNA. Some members sense metal ions other than Fe2+. For example, the zinc uptake regulator (Zur) responds to Zn2+, the manganese uptake regulator (Mur) responds to Mn2+, and the nickel uptake regulator (Nur) responds to Ni2+. Other members sense signals other than metal ions. For example, PerR, a metal-dependent sensor of hydrogen peroxide. PerR regulates DNA-binding activity through metal-based protein oxidation, and co-ordinates Mn2+ or Fe2+ at its regulatory site. Fur family proteins contain an N-terminal winged-helix DNA-binding domain followed by a dimerization domain; this CD spans both those domains. Pssm-ID: 133478 [Multi-domain] Cd Length: 116 Bit Score: 43.34 E-value: 9.72e-06
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| Fur | COG0735 | Fe2+ or Zn2+ uptake regulation protein Fur/Zur [Inorganic ion transport and metabolism]; |
16-72 | 1.44e-04 | ||
Fe2+ or Zn2+ uptake regulation protein Fur/Zur [Inorganic ion transport and metabolism]; Pssm-ID: 440498 Cd Length: 140 Bit Score: 40.32 E-value: 1.44e-04
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| Name | Accession | Description | Interval | E-value | ||
| TBPIP | pfam07106 | TBPIP/Hop2 winged helix domain; This family consists of several eukaryotic TBP-1 interacting ... |
11-74 | 1.37e-22 | ||
TBPIP/Hop2 winged helix domain; This family consists of several eukaryotic TBP-1 interacting protein (TBPIP) sequences. TBP-1 has been demonstrated to interact with the human immunodeficiency virus type 1 (HIV-1) viral protein Tat, then modulate the essential replication process of HIV. In addition, TBP-1 has been shown to be a component of the 26S proteasome, a basic multiprotein complex that degrades ubiquitinated proteins in an ATP-dependent fashion. Human TBPIP interacts with human TBP-1 then modulates the inhibitory action of human TBP-1 on HIV-Tat-mediated transactivation. TBPIP was found to be an activator that specifically stimulates the homologous pairing catalyzed by DMC1. Family members also include yeast homologous-pairing protein 2 (Hop2) and its homologs from animals and plants. They are required for proper homologous pairing and efficient cross-over and intragenic recombination during meiosis. Pssm-ID: 429296 Cd Length: 62 Bit Score: 86.65 E-value: 1.37e-22
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| LZ3wCH | pfam18517 | Leucine zipper with capping helix domain; This domain is found at the C-terminal region of ... |
154-210 | 3.52e-15 | ||
Leucine zipper with capping helix domain; This domain is found at the C-terminal region of Hop2 and Mnd1 proteins. In meiotic DNA recombination, the Hop2-Mnd1 complex promotes Dmc1-mediated single-stranded DNA (ssDNA) invasion into homologous chromosomes to form a synaptic complex. Hop2 (for homologous pairing; also known as TBPIP) is expressed specifically during meiosis, same as Mnd1 (for meiotic nuclear divisions 1). The C-terminal region of both Hop2 and Mnd1, folds into three alpha-helices that are interrupted by two short non-helical regions. These alpha-helices of the two proteins together form a parallel coiled coil that provides the major interface for heterodimer formation. The non-helical regions form substantially kinked junctions between adjacent leucine zippers: the LZ1-LZ2 and LZ2-LZ3 junctions.This domain is the C-terminal segment of Hop2 and Mnd1 which folds back onto the C-terminal leucine zipper (LZ3) to form a helical bundle-like structure, hence designated LZ3wCH (for LZ3 with capping helices). The LZ3wCH region plays a role in interacting with the Dmc1 nucleofilament. Pssm-ID: 465789 Cd Length: 55 Bit Score: 67.18 E-value: 3.52e-15
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| Fur_like | cd07153 | Ferric uptake regulator(Fur) and related metalloregulatory proteins; typically iron-dependent, ... |
15-72 | 9.72e-06 | ||
Ferric uptake regulator(Fur) and related metalloregulatory proteins; typically iron-dependent, DNA-binding repressors and activators; Ferric uptake regulator (Fur) and related metalloregulatory proteins are iron-dependent, DNA-binding repressors and activators mainly involved in iron metabolism. A general model for Fur repression under iron-rich conditions is that activated Fur (a dimer having one Fe2+ coordinated per monomer) binds to specific DNA sequences (Fur boxes) in the promoter region of iron-responsive genes, hindering access of RNA polymerase, and repressing transcription. Positive regulation by Fur can be direct or indirect, as in the Fur repression of an anti-sense regulatory small RNA. Some members sense metal ions other than Fe2+. For example, the zinc uptake regulator (Zur) responds to Zn2+, the manganese uptake regulator (Mur) responds to Mn2+, and the nickel uptake regulator (Nur) responds to Ni2+. Other members sense signals other than metal ions. For example, PerR, a metal-dependent sensor of hydrogen peroxide. PerR regulates DNA-binding activity through metal-based protein oxidation, and co-ordinates Mn2+ or Fe2+ at its regulatory site. Fur family proteins contain an N-terminal winged-helix DNA-binding domain followed by a dimerization domain; this CD spans both those domains. Pssm-ID: 133478 [Multi-domain] Cd Length: 116 Bit Score: 43.34 E-value: 9.72e-06
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| Fur | COG0735 | Fe2+ or Zn2+ uptake regulation protein Fur/Zur [Inorganic ion transport and metabolism]; |
16-72 | 1.44e-04 | ||
Fe2+ or Zn2+ uptake regulation protein Fur/Zur [Inorganic ion transport and metabolism]; Pssm-ID: 440498 Cd Length: 140 Bit Score: 40.32 E-value: 1.44e-04
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| Blast search parameters | ||||
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