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Conserved domains on  [gi|32261320|ref|NP_037422|]
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homologous-pairing protein 2 homolog isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
 15-74 6.43e-19

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: 76.64  E-value: 6.43e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32261320    15 ILLRYLQEQNRPYSSQDVFGNLQreHGLGKAVVVKTLEQLAQQGKIKEKMYGKQKIYFAD 74
Cdd:pfam07106   5 LVYEYLQEQNRPTSVQDVVLNLQ--HGLGKTVVQKALDQLVDEGKIKVKEYGKQKIYLCN 62
LZ3wCH pfam18517
Leucine zipper with capping helix domain; This domain is found at the C-terminal region of ...
 142-198 2.55e-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: 2.55e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 32261320   142 VTPEEKEQVYRERQKYCKEWRKrkrMATELSDAILEGYPKSKKQFFEEVGIETDEDY 198
Cdd:pfam18517   1 ETPEEKKKATKVAKEAANRWTD---NIFDIKSWIKEKFPKSKKELNEEFGIETDEDY 54
 
Name Accession Description Interval E-value
TBPIP pfam07106
TBPIP/Hop2 winged helix domain; This family consists of several eukaryotic TBP-1 interacting ...
 15-74 6.43e-19

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: 76.64  E-value: 6.43e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32261320    15 ILLRYLQEQNRPYSSQDVFGNLQreHGLGKAVVVKTLEQLAQQGKIKEKMYGKQKIYFAD 74
Cdd:pfam07106   5 LVYEYLQEQNRPTSVQDVVLNLQ--HGLGKTVVQKALDQLVDEGKIKVKEYGKQKIYLCN 62
LZ3wCH pfam18517
Leucine zipper with capping helix domain; This domain is found at the C-terminal region of ...
 142-198 2.55e-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: 2.55e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 32261320   142 VTPEEKEQVYRERQKYCKEWRKrkrMATELSDAILEGYPKSKKQFFEEVGIETDEDY 198
Cdd:pfam18517   1 ETPEEKKKATKVAKEAANRWTD---NIFDIKSWIKEKFPKSKKELNEEFGIETDEDY 54
Fur_like cd07153
Ferric uptake regulator(Fur) and related metalloregulatory proteins; typically iron-dependent, ...
 15-72 1.60e-03

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: 36.79  E-value: 1.60e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32261320  15 ILLRYLQEQNRPYSSQDVFGNLQREH-GLGKAVVVKTLEQLAQQGKIKEKMYGKQKIYF 72
Cdd:cd07153   5 AILEVLLESDGHLTAEEIYERLRKKGpSISLATVYRTLELLEEAGLVREIELGDGKARY 63
 
Name Accession Description Interval E-value
TBPIP pfam07106
TBPIP/Hop2 winged helix domain; This family consists of several eukaryotic TBP-1 interacting ...
 15-74 6.43e-19

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: 76.64  E-value: 6.43e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 32261320    15 ILLRYLQEQNRPYSSQDVFGNLQreHGLGKAVVVKTLEQLAQQGKIKEKMYGKQKIYFAD 74
Cdd:pfam07106   5 LVYEYLQEQNRPTSVQDVVLNLQ--HGLGKTVVQKALDQLVDEGKIKVKEYGKQKIYLCN 62
LZ3wCH pfam18517
Leucine zipper with capping helix domain; This domain is found at the C-terminal region of ...
 142-198 2.55e-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: 2.55e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 32261320   142 VTPEEKEQVYRERQKYCKEWRKrkrMATELSDAILEGYPKSKKQFFEEVGIETDEDY 198
Cdd:pfam18517   1 ETPEEKKKATKVAKEAANRWTD---NIFDIKSWIKEKFPKSKKELNEEFGIETDEDY 54
Fur_like cd07153
Ferric uptake regulator(Fur) and related metalloregulatory proteins; typically iron-dependent, ...
 15-72 1.60e-03

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: 36.79  E-value: 1.60e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 32261320  15 ILLRYLQEQNRPYSSQDVFGNLQREH-GLGKAVVVKTLEQLAQQGKIKEKMYGKQKIYF 72
Cdd:cd07153   5 AILEVLLESDGHLTAEEIYERLRKKGpSISLATVYRTLELLEEAGLVREIELGDGKARY 63
 
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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