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Conserved domains on  [gi|546445029|ref|WP_021862028|]
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pirin family protein [Parabacteroides johnsonii]

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

CATH:  2.60.120.10

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YhaK COG1741
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];
11-235 1.81e-69

Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];


:

Pssm-ID: 441347 [Multi-domain]  Cd Length: 253  Bit Score: 213.48  E-value: 1.81e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  11 RGYANHGWLKTHHTFSfanyyNPKRVHFGMLRVLNDDSIAP---GEGFDTHPHKNMEVISIPLKGYMCHGDSIRNSEVIT 87
Cdd:COG1741    1 RPTDLGGGLKVRRYLP-----SRDRRGFGPFRVLDHDGPAPpgyGAGFPPHPHRGMETVTYVLEGELEHRDSLGNGGVIR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  88 PGDIQVMSAGSGIFHSEFNDSGEEQLDLLQIWVF--PREENTEPHYKNY-DIRSVLKKNELGVMIA--PDG-SAPASINQ 161
Cdd:COG1741   76 PGDVQWMTAGSGIVHSERNPSEGGPLHGLQLWVNlpPADKGLAPRYQHIpDIPEVELGGGRLRVIAgpLDGvDGPVKIHQ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546445029 162 DAWFSMGTLDAGLVKEYKLHgKKNGVYLFVIEGEVEVADTVLSKRDGAGFWDTDSIAIEVLKHATVLLMEV-PME 235
Cdd:COG1741  156 DALLYDIRLDAGATLTLPLP-PGREAYLYVIEGSVTVNGETLEAGDLAVLSDGDELTLTADEDARVLLLGGePLD 229
 
Name Accession Description Interval E-value
YhaK COG1741
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];
11-235 1.81e-69

Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];


Pssm-ID: 441347 [Multi-domain]  Cd Length: 253  Bit Score: 213.48  E-value: 1.81e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  11 RGYANHGWLKTHHTFSfanyyNPKRVHFGMLRVLNDDSIAP---GEGFDTHPHKNMEVISIPLKGYMCHGDSIRNSEVIT 87
Cdd:COG1741    1 RPTDLGGGLKVRRYLP-----SRDRRGFGPFRVLDHDGPAPpgyGAGFPPHPHRGMETVTYVLEGELEHRDSLGNGGVIR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  88 PGDIQVMSAGSGIFHSEFNDSGEEQLDLLQIWVF--PREENTEPHYKNY-DIRSVLKKNELGVMIA--PDG-SAPASINQ 161
Cdd:COG1741   76 PGDVQWMTAGSGIVHSERNPSEGGPLHGLQLWVNlpPADKGLAPRYQHIpDIPEVELGGGRLRVIAgpLDGvDGPVKIHQ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546445029 162 DAWFSMGTLDAGLVKEYKLHgKKNGVYLFVIEGEVEVADTVLSKRDGAGFWDTDSIAIEVLKHATVLLMEV-PME 235
Cdd:COG1741  156 DALLYDIRLDAGATLTLPLP-PGREAYLYVIEGSVTVNGETLEAGDLAVLSDGDELTLTADEDARVLLLGGePLD 229
cupin_Yhhw_N cd02910
Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, N-terminal cupin ...
 18-136 1.78e-67

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: 203.56  E-value: 1.78e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  18 WLKTHHTFSFANYYNPKRVHFGMLRVLNDDSIAPGEGFDTHPHKNMEVISIPLKGYMCHGDSIRNSEVITPGDIQVMSAG 97
Cdd:cd02910    1 WLKSRHTFSFADYYDPKNMGFGALRVINDDIVAPGTGFGTHPHRDMEIITYVLEGELTHRDSMGNKGVLKRGDVQRMSAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 546445029  98 SGIFHSEFNDSGEEQLDLLQIWVFPREENTEPHYKNYDI 136
Cdd:cd02910   81 TGIRHSEYNLSDTEPLRFLQIWILPDQRGLKPSYQQKRF 119
Pirin pfam02678
Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The ...
 5-120 1.80e-33

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: 116.58  E-value: 1.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029    5 VDKANTRGYAnhGWLKTHHTFSFANYYNPKRVHFGmlrvlnddsiaPGEGFDTHPHKNMEVISIPLKGYMCHGDSIRNSE 84
Cdd:pfam02678   2 FRVRRALGGA--GWLQSVDPFSFLDYFGPAEFGPG-----------YGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNHG 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 546445029   85 VITPGDIQVMSAGSGIFHSEFNDSGEEQLDLLQIWV 120
Cdd:pfam02678  69 VIRPGDVQWMTAGSGIVHSEMNPSEEGPLHGFQLWV 104
 
Name Accession Description Interval E-value
YhaK COG1741
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];
11-235 1.81e-69

Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];


Pssm-ID: 441347 [Multi-domain]  Cd Length: 253  Bit Score: 213.48  E-value: 1.81e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  11 RGYANHGWLKTHHTFSfanyyNPKRVHFGMLRVLNDDSIAP---GEGFDTHPHKNMEVISIPLKGYMCHGDSIRNSEVIT 87
Cdd:COG1741    1 RPTDLGGGLKVRRYLP-----SRDRRGFGPFRVLDHDGPAPpgyGAGFPPHPHRGMETVTYVLEGELEHRDSLGNGGVIR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  88 PGDIQVMSAGSGIFHSEFNDSGEEQLDLLQIWVF--PREENTEPHYKNY-DIRSVLKKNELGVMIA--PDG-SAPASINQ 161
Cdd:COG1741   76 PGDVQWMTAGSGIVHSERNPSEGGPLHGLQLWVNlpPADKGLAPRYQHIpDIPEVELGGGRLRVIAgpLDGvDGPVKIHQ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546445029 162 DAWFSMGTLDAGLVKEYKLHgKKNGVYLFVIEGEVEVADTVLSKRDGAGFWDTDSIAIEVLKHATVLLMEV-PME 235
Cdd:COG1741  156 DALLYDIRLDAGATLTLPLP-PGREAYLYVIEGSVTVNGETLEAGDLAVLSDGDELTLTADEDARVLLLGGePLD 229
cupin_Yhhw_N cd02910
Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, N-terminal cupin ...
 18-136 1.78e-67

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: 203.56  E-value: 1.78e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  18 WLKTHHTFSFANYYNPKRVHFGMLRVLNDDSIAPGEGFDTHPHKNMEVISIPLKGYMCHGDSIRNSEVITPGDIQVMSAG 97
Cdd:cd02910    1 WLKSRHTFSFADYYDPKNMGFGALRVINDDIVAPGTGFGTHPHRDMEIITYVLEGELTHRDSMGNKGVLKRGDVQRMSAG 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 546445029  98 SGIFHSEFNDSGEEQLDLLQIWVFPREENTEPHYKNYDI 136
Cdd:cd02910   81 TGIRHSEYNLSDTEPLRFLQIWILPDQRGLKPSYQQKRF 119
Pirin pfam02678
Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The ...
 5-120 1.80e-33

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: 116.58  E-value: 1.80e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029    5 VDKANTRGYAnhGWLKTHHTFSFANYYNPKRVHFGmlrvlnddsiaPGEGFDTHPHKNMEVISIPLKGYMCHGDSIRNSE 84
Cdd:pfam02678   2 FRVRRALGGA--GWLQSVDPFSFLDYFGPAEFGPG-----------YGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNHG 68

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 546445029   85 VITPGDIQVMSAGSGIFHSEFNDSGEEQLDLLQIWV 120
Cdd:pfam02678  69 VIRPGDVQWMTAGSGIVHSEMNPSEEGPLHGFQLWV 104
Pirin_C_2 pfam17954
Quercetinase C-terminal cupin domain; Experiments on the YhhW protein show that is has ...
 147-232 4.24e-27

Quercetinase C-terminal cupin domain; Experiments on the YhhW protein show that is has quercetinase activity. This entry represents the C-terminal cupin domain from the two cupin domains that make up the protein. This domain is usually associated with pfam02678.


Pssm-ID: 465583  Cd Length: 86  Bit Score: 99.46  E-value: 4.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  147 VMIAPDGS-APASINQDAWFSMGTLDAGLVKEYKLHgKKNGVYLFVIEGEVEVADTVLSKRDGAGFWDTDSIAIEVLKHA 225
Cdd:pfam17954   1 LIASPDGRdGSLKIHQDARLYAGLLDAGESLEYTLK-PGRGAYLQVARGSVEVNGQELEAGDGAAISDEDSLTITALEDA 79


                  ....*..
gi 546445029  226 TVLLMEV 232
Cdd:pfam17954  80 EVLLFDL 86
cupin_pirin-like_N cd20287
pirin-like, N-terminal cupin domain; This family contains the N-terminal cupin domain of pirin ...
 41-120 2.40e-23

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: 89.57  E-value: 2.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  41 LRVLNDDSIAPGEGFDTHPHKNMEVISIPLKGYMCHGDSIRNSEVITPGDIQVMSAGSGIFHSEFNDSGEEQLDLLQIWV 120
Cdd:cd20287    1 LRVFNEFVGGRGGGFPDHPHRGFEILSYLLEGS*EHEDSCGNTGQ*NAGELQW*SAGRGILHSE*NCSEDEPLHGLQLWV 80
cupin_pirin_N cd02909
pirin, N-terminal cupin domain; This family contains the N-terminal domain of pirin, a nuclear ...
 37-120 1.89e-21

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: 85.28  E-value: 1.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546445029  37 HFGMlrvlnDDSIAPGEGFDTHPHKNMEVISIPLKGYMCHGDSIRNSEVITPGDIQVMSAGSGIFHSEFNDSGEEQLDLL 116
Cdd:cd02909   23 HFGP-----VKPEPYGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNKGVIRPGDVQWMTAGRGIVHSEMPPEEGGPLHGL 97


                 ....
gi 546445029 117 QIWV 120
Cdd:cd02909   98 QLWV 101
cupin_Yhhw_C cd20311
Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, C-terminal cupin ...
 163-229 3.29e-04

Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, C-terminal cupin domain; This family includes the C-terminal domain 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 C-terminal cupin-like domain has diverged considerably and has closer alignment with C-terminal pirin, while the N-terminal cupin domain of YhhW has a metal coordination site and is thought to have catalytic activity. 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: 380445  Cd Length: 70  Bit Score: 37.90  E-value: 3.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546445029 163 AWFSMGTLDAGlVKEYKLHGKKNGVYLFVIEGEVEVADTVLSKRDGAGFWDTDSIAIEVLKHATVLL 229
Cdd:cd20311    1 AWLYASVLDKG-EASVHLLAGGRRAWLQVVRGTVTVNGVALKTGDGAAISDETALTLTADSDAEVLL 66
 
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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