peroxynitrite isomerase THAP4 isoform X2 [Homo sapiens]
lipocalin/fatty acid-binding family protein; lipocalin family protein( domain architecture ID 10527263)
lipocalin/fatty acid-binding family protein contains a large beta-barrel cavity that binds hydrophobic ligands| lipocalin/fatty-acid binding family protein similar to Arabidopsis thaliana temperature-induced lipocalin-1, which is involved in basal (BT) and acquired thermotolerance (AT), probably by preventing plasma membrane lipids peroxidation induced by severe heat-shock (HS)
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
lipocalin_heme-bd-THAP4-like | cd07828 | heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar ... |
446-626 | 7.17e-56 | ||||
heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar proteins; Proteins in this subfamily use a beta-barrel domain to bind ferric heme. This group also includes the beta-barrel domain of human THAP domain containing 4 (THAP4). The THAP domain is found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. Arabidopsis thaliana nitrobindin may reversibly bind nitric oxide (NO) and be involved in NO transport. It also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development. : Pssm-ID: 381185 Cd Length: 150 Bit Score: 185.91 E-value: 7.17e-56
|
||||||||
THAP | pfam05485 | THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a ... |
50-109 | 1.38e-16 | ||||
THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion. It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes. : Pssm-ID: 461662 Cd Length: 76 Bit Score: 74.49 E-value: 1.38e-16
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
lipocalin_heme-bd-THAP4-like | cd07828 | heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar ... |
446-626 | 7.17e-56 | ||||
heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar proteins; Proteins in this subfamily use a beta-barrel domain to bind ferric heme. This group also includes the beta-barrel domain of human THAP domain containing 4 (THAP4). The THAP domain is found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. Arabidopsis thaliana nitrobindin may reversibly bind nitric oxide (NO) and be involved in NO transport. It also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development. Pssm-ID: 381185 Cd Length: 150 Bit Score: 185.91 E-value: 7.17e-56
|
||||||||
THAP4_heme-bd | pfam08768 | THAP4-like, heme-binding beta-barrel domain; This domain can be found in THAP4 from mammals ... |
446-625 | 2.79e-48 | ||||
THAP4-like, heme-binding beta-barrel domain; This domain can be found in THAP4 from mammals and At1g79260 from Arabidopsis. THAP4 catalyzes the heme-based conversion of peroxynitrite into nitrate-NO3- in vitro. At1g79260 is a nitrophorin-like heme-binding protein that may reversibly bind nitric oxide (NO) and be involved in NO transport. This entry also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-beta-barrel structural organization. Proteins containing this domain are putatively related to fatty acid-binding proteins (FABPs). Pssm-ID: 462593 Cd Length: 151 Bit Score: 165.83 E-value: 2.79e-48
|
||||||||
THAP | pfam05485 | THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a ... |
50-109 | 1.38e-16 | ||||
THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion. It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes. Pssm-ID: 461662 Cd Length: 76 Bit Score: 74.49 E-value: 1.38e-16
|
||||||||
THAP | smart00980 | The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It ... |
50-109 | 2.27e-16 | ||||
The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes. Pssm-ID: 214951 Cd Length: 80 Bit Score: 74.01 E-value: 2.27e-16
|
||||||||
Name | Accession | Description | Interval | E-value | ||||
lipocalin_heme-bd-THAP4-like | cd07828 | heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar ... |
446-626 | 7.17e-56 | ||||
heme-binding beta-barrel domain of human THAP4, Arabidopsis thaliana nitrobindin, and similar proteins; Proteins in this subfamily use a beta-barrel domain to bind ferric heme. This group also includes the beta-barrel domain of human THAP domain containing 4 (THAP4). The THAP domain is found in proteins involved in transcriptional regulation, cell-cycle control, apoptosis and chromatin modification. Arabidopsis thaliana nitrobindin may reversibly bind nitric oxide (NO) and be involved in NO transport. It also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development. Pssm-ID: 381185 Cd Length: 150 Bit Score: 185.91 E-value: 7.17e-56
|
||||||||
THAP4_heme-bd | pfam08768 | THAP4-like, heme-binding beta-barrel domain; This domain can be found in THAP4 from mammals ... |
446-625 | 2.79e-48 | ||||
THAP4-like, heme-binding beta-barrel domain; This domain can be found in THAP4 from mammals and At1g79260 from Arabidopsis. THAP4 catalyzes the heme-based conversion of peroxynitrite into nitrate-NO3- in vitro. At1g79260 is a nitrophorin-like heme-binding protein that may reversibly bind nitric oxide (NO) and be involved in NO transport. This entry also includes the beta-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology. Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-beta-barrel structural organization. Proteins containing this domain are putatively related to fatty acid-binding proteins (FABPs). Pssm-ID: 462593 Cd Length: 151 Bit Score: 165.83 E-value: 2.79e-48
|
||||||||
THAP | pfam05485 | THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a ... |
50-109 | 1.38e-16 | ||||
THAP domain; The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion. It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes. Pssm-ID: 461662 Cd Length: 76 Bit Score: 74.49 E-value: 1.38e-16
|
||||||||
THAP | smart00980 | The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It ... |
50-109 | 2.27e-16 | ||||
The THAP domain is a putative DNA-binding domain (DBD) and probably also binds a zinc ion; It features the conserved C2CH architecture (consensus sequence: Cys - 2-4 residues - Cys - 35-50 residues - Cys - 2 residues - His). Other universal features include the location of the domain at the N-termini of proteins, its size of about 90 residues, a C-terminal AVPTIF box and several other conserved residues. Orthologues of the human THAP domain have been identified in other vertebrates and probably worms and flies, but not in other eukaryotes or any prokaryotes. Pssm-ID: 214951 Cd Length: 80 Bit Score: 74.01 E-value: 2.27e-16
|
||||||||
DM3 | smart00692 | Zinc finger domain in CG10631, C. elegans LIN-15B and human P52rIPK; |
50-109 | 4.73e-08 | ||||
Zinc finger domain in CG10631, C. elegans LIN-15B and human P52rIPK; Pssm-ID: 128933 Cd Length: 59 Bit Score: 50.00 E-value: 4.73e-08
|
||||||||
Blast search parameters | ||||
|