pirin [Homo sapiens]
Protein Classification
pirin family protein( domain architecture ID 11448280)
pirin family protein such as quercetin 2,3-dioxygenase, a copper-containing enzyme that catalyzes the insertion of molecular oxygen into polyphenolic flavonols
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| YhaK | COG1741 | Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only]; |
14-271 | 3.96e-102 | |||||
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only]; : Pssm-ID: 441347 [Multi-domain] Cd Length: 253 Bit Score: 298.61 E-value: 3.96e-102
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| Name | Accession | Description | Interval | E-value | |||||
| YhaK | COG1741 | Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only]; |
14-271 | 3.96e-102 | |||||
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only]; Pssm-ID: 441347 [Multi-domain] Cd Length: 253 Bit Score: 298.61 E-value: 3.96e-102
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| cupin_pirin_N | cd02909 | pirin, N-terminal cupin domain; This family contains the N-terminal domain of pirin, a nuclear ... |
22-120 | 1.61e-58 | |||||
pirin, N-terminal cupin domain; This family contains the N-terminal domain of pirin, a nuclear protein that is highly conserved among mammals, plants, fungi, and prokaryotes. It is widely expressed in dot-like subnuclear structures in human tissues such as liver and heart. Pirin functions as both a transcriptional cofactor and an apoptosis-related protein in mammals and is involved in seed germination and seedling development in plants. The pirins have been assigned as a subfamily of the cupin superfamily based on structure and sequence similarity. The pirins have two tandem cupin-like folds but the C-terminal cupin fold has diverged considerably and does not have a metal binding site. The exact functions of pirins are unknown but they have quercitinase activity in Escherichia coli and are thought to play important roles in transcription and apoptosis. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold generally capable of homodimerization. Pssm-ID: 380374 Cd Length: 104 Bit Score: 182.35 E-value: 1.61e-58
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| Pirin | pfam02678 | Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The ... |
21-118 | 2.44e-42 | |||||
Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The function of Pirin is unknown but the gene coding for this protein is known to be expressed in all tissues in the human body although it is expressed most strongly in the liver and heart. Pirin is known to be a nuclear protein, exclusively localized within the nucleoplasma and predominantly concentrated within dot-like subnuclear structures. A tomato homolog of human Pirin has been found to be induced during programmed cell death. Human Pirin interacts with Bcl-3 and NFI and hence is probably involved in the regulation of DNA transcription and replication. It appears to be an Fe(II)-containing member of the Cupin superfamily. Pssm-ID: 426921 Cd Length: 104 Bit Score: 140.85 E-value: 2.44e-42
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| anti_sig_ChrR | TIGR02451 | anti-sigma factor, putative, ChrR family; The member of this family from Rhodobacter ... |
19-101 | 2.46e-03 | |||||
anti-sigma factor, putative, ChrR family; The member of this family from Rhodobacter sphaeroides has been shown both to form a complex with sigma(E) and to negatively regulate tetrapyrrole biosynthesis. This protein likely contains (at least) two distinct functional domains; several smaller homologs (excluded by the model) show homology only to the C-terminal, including a motif PxHxHxGxE. [Regulatory functions, Other] Pssm-ID: 131504 [Multi-domain] Cd Length: 215 Bit Score: 38.57 E-value: 2.46e-03
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| Name | Accession | Description | Interval | E-value | |||||
| YhaK | COG1741 | Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only]; |
14-271 | 3.96e-102 | |||||
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only]; Pssm-ID: 441347 [Multi-domain] Cd Length: 253 Bit Score: 298.61 E-value: 3.96e-102
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| cupin_pirin_N | cd02909 | pirin, N-terminal cupin domain; This family contains the N-terminal domain of pirin, a nuclear ... |
22-120 | 1.61e-58 | |||||
pirin, N-terminal cupin domain; This family contains the N-terminal domain of pirin, a nuclear protein that is highly conserved among mammals, plants, fungi, and prokaryotes. It is widely expressed in dot-like subnuclear structures in human tissues such as liver and heart. Pirin functions as both a transcriptional cofactor and an apoptosis-related protein in mammals and is involved in seed germination and seedling development in plants. The pirins have been assigned as a subfamily of the cupin superfamily based on structure and sequence similarity. The pirins have two tandem cupin-like folds but the C-terminal cupin fold has diverged considerably and does not have a metal binding site. The exact functions of pirins are unknown but they have quercitinase activity in Escherichia coli and are thought to play important roles in transcription and apoptosis. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold generally capable of homodimerization. Pssm-ID: 380374 Cd Length: 104 Bit Score: 182.35 E-value: 1.61e-58
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| Pirin | pfam02678 | Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The ... |
21-118 | 2.44e-42 | |||||
Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The function of Pirin is unknown but the gene coding for this protein is known to be expressed in all tissues in the human body although it is expressed most strongly in the liver and heart. Pirin is known to be a nuclear protein, exclusively localized within the nucleoplasma and predominantly concentrated within dot-like subnuclear structures. A tomato homolog of human Pirin has been found to be induced during programmed cell death. Human Pirin interacts with Bcl-3 and NFI and hence is probably involved in the regulation of DNA transcription and replication. It appears to be an Fe(II)-containing member of the Cupin superfamily. Pssm-ID: 426921 Cd Length: 104 Bit Score: 140.85 E-value: 2.44e-42
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| Pirin_C | pfam05726 | Pirin C-terminal cupin domain; This region is found the C-terminal half of the Pirin protein. |
171-277 | 2.51e-42 | |||||
Pirin C-terminal cupin domain; This region is found the C-terminal half of the Pirin protein. Pssm-ID: 399031 Cd Length: 103 Bit Score: 140.81 E-value: 2.51e-42
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| cupin_pirin-like_N | cd20287 | pirin-like, N-terminal cupin domain; This family contains the N-terminal cupin domain of pirin ... |
39-119 | 3.78e-41 | |||||
pirin-like, N-terminal cupin domain; This family contains the N-terminal cupin domain of pirin and pirin-like proteins, including Escherichia coli YhhW and YhaK. Pirin functions as both a transcriptional cofactor and an apoptosis-related protein in mammals and is involved in seed germination and seedling development in plants. Proteins in this family have two tandem cupin-like folds but the C-terminal cupin fold has diverged considerably and does not have a metal binding site. The exact functions of pirins are unknown but they have quercitinase activity in Escherichia coli and are thought to play important roles in transcription and apoptosis. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380421 [Multi-domain] Cd Length: 81 Bit Score: 137.34 E-value: 3.78e-41
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| cupin_pirin-like_C | cd20288 | pirin-like, C-terminal cupin domain; This family contains the C-terminal cupin domain of pirin ... |
170-243 | 5.28e-30 | |||||
pirin-like, C-terminal cupin domain; This family contains the C-terminal cupin domain of pirin and pirin-like proteins, including Escherichia coli YhhW and YhaK. Pirin functions as both a transcriptional cofactor and an apoptosis-related protein in mammals and is involved in seed germination and seedling development in plants. Proteins in this family have two tandem cupin-like folds but the C-terminal cupin fold has diverged considerably and does not have a metal binding site. The exact functions of pirins are unknown but they have quercitinase activity in Escherichia coli and are thought to play important roles in transcription and apoptosis. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380422 Cd Length: 70 Bit Score: 108.03 E-value: 5.28e-30
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| cupin_pirin_C | cd02247 | pirin, C-terminal cupin domain; This family contains the C-terminal domain of pirin, a nuclear ... |
168-245 | 3.87e-29 | |||||
pirin, C-terminal cupin domain; This family contains the C-terminal domain of pirin, a nuclear protein that is highly conserved among mammals, plants, fungi, and prokaryotes. It is widely expressed in dot-like subnuclear structures in human tissues such as liver and heart. Pirin functions as both a transcriptional cofactor and an apoptosis-related protein in mammals and is involved in seed germination and seedling development in plants. The pirins have been assigned as a subfamily of the cupin superfamily based on structure and sequence similarity. The pirins have two tandem cupin-like folds but the C-terminal cupin fold has diverged considerably and does not have a metal binding site. The exact functions of pirins are unknown but they have quercitinase activity in Escherichia coli and are thought to play important roles in transcription and apoptosis. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380373 Cd Length: 76 Bit Score: 105.78 E-value: 3.87e-29
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| cupin_Yhhw_N | cd02910 | Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, N-terminal cupin ... |
50-135 | 9.39e-22 | |||||
Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, N-terminal cupin domain; This family includes the N-terminal cupin domains of YhhW and YhaK, Escherichia coli pirin-like proteins with unknown function. YhhW is structurally similar not only to human pirin but also to quercitin 2,3-dioxygenase (quercitinase). Although the function of YhhW is not completely understood, YhhW and its human ortholog have quercitinase activity and are likely to play an important role in transcription and apoptosis. This N-terminal cupin domain of YhhW has a metal coordination site and is thought to have catalytic activity while the C-terminal cupin-like domain has diverged considerably and has closer alignment with C-terminal pirin. YhaK is found in low abundance in the cytosol of E. coli and is strongly up-regulated by nitroso-glutathione (GSNO). There are major structural differences at the N-terminus of YhaK compared with YhhW; YhaK lacks the canonical cupin metal-binding residues of pirins and may be involved in chloride binding and/or sensing of oxidative stress in enterobacteria. YhaK showed no quercetinase and peroxidase activity; however, reduced YhaK was very sensitive to reactive oxygen species (ROS). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold. Pssm-ID: 380375 Cd Length: 119 Bit Score: 88.00 E-value: 9.39e-22
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| anti_sig_ChrR | TIGR02451 | anti-sigma factor, putative, ChrR family; The member of this family from Rhodobacter ... |
19-101 | 2.46e-03 | |||||
anti-sigma factor, putative, ChrR family; The member of this family from Rhodobacter sphaeroides has been shown both to form a complex with sigma(E) and to negatively regulate tetrapyrrole biosynthesis. This protein likely contains (at least) two distinct functional domains; several smaller homologs (excluded by the model) show homology only to the C-terminal, including a motif PxHxHxGxE. [Regulatory functions, Other] Pssm-ID: 131504 [Multi-domain] Cd Length: 215 Bit Score: 38.57 E-value: 2.46e-03
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| Blast search parameters | ||||
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