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Conserved domains on  [gi|1695530100|gb|QDG62879|]
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pirin family protein [Pseudarthrobacter sp. NIBRBAC000502771]

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
Gene Ontology:  GO:0046872
PubMed:  14697267|19478949
SCOP:  4000967

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];
32-288 6.78e-100

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


:

Pssm-ID: 441347 [Multi-domain]  Cd Length: 253  Bit Score: 294.76  E-value: 6.78e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100  32 REVPLGGvrAMNVKRTLPQRGLPTIGAWCFLDSFGPDRTA--MSVLPHPHIGLQTVTWPLAGHIRHRDSVGSDVVVRPGE 109
Cdd:COG1741     1 RPTDLGG--GLKVRRYLPSRDRRGFGPFRVLDHDGPAPPGygAGFPPHPHRGMETVTYVLEGELEHRDSLGNGGVIRPGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100 110 LNIMTAGRGVSHSEFAvlPADGGELpvqRGLQLWVALPGGDRHREPEFEQHRELPRAAGPGFTVTVMVGEFAGVASPATV 189
Cdd:COG1741    79 VQWMTAGSGIVHSERN--PSEGGPL---HGLQLWVNLPPADKGLAPRYQHIPDIPEVELGGGRLRVIAGPLDGVDGPVKI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100 190 FSPIVGADISCE--GEAALPLNPGFEHGILVLDGALAVDGQDLPAGPLGYLGTGRsELRVAALPGTRFLLIGGEPFAEEL 267
Cdd:COG1741   154 HQDALLYDIRLDagATLTLPLPPGREAYLYVIEGSVTVNGETLEAGDLAVLSDGD-ELTLTADEDARVLLLGGEPLDEPI 232

                         250       260
                  ....*....|....*....|.
gi 1695530100 268 LMWWNFVGRTHDEVEKARDDW 288
Cdd:COG1741   233 VMWGPFVMNTKEEIEQAKEDW 253
 
Name Accession Description Interval E-value
YhaK COG1741
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];
32-288 6.78e-100

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


Pssm-ID: 441347 [Multi-domain]  Cd Length: 253  Bit Score: 294.76  E-value: 6.78e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100  32 REVPLGGvrAMNVKRTLPQRGLPTIGAWCFLDSFGPDRTA--MSVLPHPHIGLQTVTWPLAGHIRHRDSVGSDVVVRPGE 109
Cdd:COG1741     1 RPTDLGG--GLKVRRYLPSRDRRGFGPFRVLDHDGPAPPGygAGFPPHPHRGMETVTYVLEGELEHRDSLGNGGVIRPGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100 110 LNIMTAGRGVSHSEFAvlPADGGELpvqRGLQLWVALPGGDRHREPEFEQHRELPRAAGPGFTVTVMVGEFAGVASPATV 189
Cdd:COG1741    79 VQWMTAGSGIVHSERN--PSEGGPL---HGLQLWVNLPPADKGLAPRYQHIPDIPEVELGGGRLRVIAGPLDGVDGPVKI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100 190 FSPIVGADISCE--GEAALPLNPGFEHGILVLDGALAVDGQDLPAGPLGYLGTGRsELRVAALPGTRFLLIGGEPFAEEL 267
Cdd:COG1741   154 HQDALLYDIRLDagATLTLPLPPGREAYLYVIEGSVTVNGETLEAGDLAVLSDGD-ELTLTADEDARVLLLGGEPLDEPI 232

                         250       260
                  ....*....|....*....|.
gi 1695530100 268 LMWWNFVGRTHDEVEKARDDW 288
Cdd:COG1741   233 VMWGPFVMNTKEEIEQAKEDW 253
cupin_pirin_N cd02909
pirin, N-terminal cupin domain; This family contains the N-terminal domain of pirin, a nuclear ...
 42-147 1.78e-33

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: 119.18  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100  42 MNVKRTLPQRGLPTIGAWCFLDSFGPDRTAMSVL---PHPHIGLQTVTWPLAGHIRHRDSVGSDVVVRPGELNIMTAGRG 118
Cdd:cd02909     1 ARVRRVLPTPELRNLDPFLLLDHFGPVKPEPYGAgfpPHPHRGFETVTYLLEGEVEHRDSLGNKGVIRPGDVQWMTAGRG 80

                          90       100
                  ....*....|....*....|....*....
gi 1695530100 119 VSHSEfaVLPADGGELpvqRGLQLWVALP 147
Cdd:cd02909    81 IVHSE--MPPEEGGPL---HGLQLWVNLP 104
Pirin pfam02678
Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The ...
 38-144 1.22e-27

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: 103.87  E-value: 1.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100  38 GVRAMNVKRTLPQrgLPTIGAWCFLDSFGPDRTA----MSVLPHPHIGLQTVTWPLAGHIRHRDSVGSDVVVRPGELNIM 113
Cdd:pfam02678   1 GFRVRRALGGAGW--LQSVDPFSFLDYFGPAEFGpgygAGFPPHPHRGFETVTYLLEGEVEHRDSLGNHGVIRPGDVQWM 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1695530100 114 TAGRGVSHSEFAvlPADGGELpvqRGLQLWV 144
Cdd:pfam02678  79 TAGSGIVHSEMN--PSEEGPL---HGFQLWV 104
 
Name Accession Description Interval E-value
YhaK COG1741
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];
32-288 6.78e-100

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


Pssm-ID: 441347 [Multi-domain]  Cd Length: 253  Bit Score: 294.76  E-value: 6.78e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100  32 REVPLGGvrAMNVKRTLPQRGLPTIGAWCFLDSFGPDRTA--MSVLPHPHIGLQTVTWPLAGHIRHRDSVGSDVVVRPGE 109
Cdd:COG1741     1 RPTDLGG--GLKVRRYLPSRDRRGFGPFRVLDHDGPAPPGygAGFPPHPHRGMETVTYVLEGELEHRDSLGNGGVIRPGD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100 110 LNIMTAGRGVSHSEFAvlPADGGELpvqRGLQLWVALPGGDRHREPEFEQHRELPRAAGPGFTVTVMVGEFAGVASPATV 189
Cdd:COG1741    79 VQWMTAGSGIVHSERN--PSEGGPL---HGLQLWVNLPPADKGLAPRYQHIPDIPEVELGGGRLRVIAGPLDGVDGPVKI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100 190 FSPIVGADISCE--GEAALPLNPGFEHGILVLDGALAVDGQDLPAGPLGYLGTGRsELRVAALPGTRFLLIGGEPFAEEL 267
Cdd:COG1741   154 HQDALLYDIRLDagATLTLPLPPGREAYLYVIEGSVTVNGETLEAGDLAVLSDGD-ELTLTADEDARVLLLGGEPLDEPI 232

                         250       260
                  ....*....|....*....|.
gi 1695530100 268 LMWWNFVGRTHDEVEKARDDW 288
Cdd:COG1741   233 VMWGPFVMNTKEEIEQAKEDW 253
cupin_pirin_N cd02909
pirin, N-terminal cupin domain; This family contains the N-terminal domain of pirin, a nuclear ...
 42-147 1.78e-33

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: 119.18  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100  42 MNVKRTLPQRGLPTIGAWCFLDSFGPDRTAMSVL---PHPHIGLQTVTWPLAGHIRHRDSVGSDVVVRPGELNIMTAGRG 118
Cdd:cd02909     1 ARVRRVLPTPELRNLDPFLLLDHFGPVKPEPYGAgfpPHPHRGFETVTYLLEGEVEHRDSLGNKGVIRPGDVQWMTAGRG 80

                          90       100
                  ....*....|....*....|....*....
gi 1695530100 119 VSHSEfaVLPADGGELpvqRGLQLWVALP 147
Cdd:cd02909    81 IVHSE--MPPEEGGPL---HGLQLWVNLP 104
Pirin pfam02678
Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The ...
 38-144 1.22e-27

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: 103.87  E-value: 1.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100  38 GVRAMNVKRTLPQrgLPTIGAWCFLDSFGPDRTA----MSVLPHPHIGLQTVTWPLAGHIRHRDSVGSDVVVRPGELNIM 113
Cdd:pfam02678   1 GFRVRRALGGAGW--LQSVDPFSFLDYFGPAEFGpgygAGFPPHPHRGFETVTYLLEGEVEHRDSLGNHGVIRPGDVQWM 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1695530100 114 TAGRGVSHSEFAvlPADGGELpvqRGLQLWV 144
Cdd:pfam02678  79 TAGSGIVHSEMN--PSEEGPL---HGFQLWV 104
Pirin_C pfam05726
Pirin C-terminal cupin domain; This region is found the C-terminal half of the Pirin protein.
 196-290 5.82e-20

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: 83.42  E-value: 5.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100 196 ADISCE--GEAALPLNPGFEHGILVLDGALAVDGQD-LPAGPLGYLGTGRSELRVAALPGTRFLLIGGEPFAEELLMWWN 272
Cdd:pfam05726   2 VDLTLEagAEFTLPLPEGWNRALYVLEGSLEVGGEDaIEEHQLAVLGPPGDDLVVRAEAPARFLLLGGEPLGEPVVQYGP 81

                          90
                  ....*....|....*...
gi 1695530100 273 FVGRTHDEVEKARDDWEA 290
Cdd:pfam05726  82 FVMNTKEEIEQAKEDWRN 99
cupin_Yhhw_N cd02910
Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, N-terminal cupin ...
 76-161 4.19e-16

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: 73.36  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1695530100  76 PHPHIGLQTVTWPLAGHIRHRDSVGSDVVVRPGELNIMTAGRGVSHSEFAvlPADGGELpvqRGLQLWVaLPgGDRHREP 155
Cdd:cd02910    40 THPHRDMEIITYVLEGELTHRDSMGNKGVLKRGDVQRMSAGTGIRHSEYN--LSDTEPL---RFLQIWI-LP-DQRGLKP 112


                  ....*.
gi 1695530100 156 EFEQHR 161
Cdd:cd02910   113 SYQQKR 118
cupin_pirin-like_N cd20287
pirin-like, N-terminal cupin domain; This family contains the N-terminal cupin domain of pirin ...
 76-144 2.43e-10

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: 56.06  E-value: 2.43e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1695530100  76 PHPHIGLQTVTWPLAGHIRHRDSVGSDVVVRPGELNIMTAGRGVSHSEFAVlpadgGELPVQRGLQLWV 144
Cdd:cd20287    17 DHPHRGFEILSYLLEGS*EHEDSCGNTGQ*NAGELQW*SAGRGILHSE*NC-----SEDEPLHGLQLWV 80
cupin_pirin_C cd02247
pirin, C-terminal cupin domain; This family contains the C-terminal domain of pirin, a nuclear ...
 192-262 1.06e-06

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: 45.69  E-value: 1.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1695530100 192 PIVGADISCE--GEAALPLNPGFEHGILVLDGALAVDGQD--LPAGPLGYLGTGRSELRVAALP-GTRFLLIGGEP 262
Cdd:cd02247     1 PVLYLDITLEpgAKFTQPVPAGWNAFIYVLEGEATIGGEEveAEAGHLAVLGPGGDGVELEAKEeGARFLLIAGEP 76
 
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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