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Conserved domains on  [gi|499598351|ref|WP_011279085|]
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pirin family protein [Sulfolobus acidocaldarius]

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];
12-276 2.54e-101

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


:

Pssm-ID: 441347 [Multi-domain]  Cd Length: 253  Bit Score: 296.68  E-value: 2.54e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  12 KSTMDGAGVKLYRVFGGMHTVEYtDPFLLLDFFGSSNPsDYLAGFPWHPHRGIETVTLLYKGKVEHQDSEGNKGVIYPGQ 91
Cdd:COG1741    1 RPTDLGGGLKVRRYLPSRDRRGF-GPFRVLDHDGPAPP-GYGAGFPPHPHRGMETVTYVLEGELEHRDSLGNGGVIRPGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  92 SQWMTAGSGIFHQEMPRPlegteiarynqKPEDMYGLQLWVNLPSNMKMSDPVYRDVKQLPKERFDFGEVQILSGKFMGI 171
Cdd:COG1741   79 VQWMTAGSGIVHSERNPS-----------EGGPLHGLQLWVNLPPADKGLAPRYQHIPDIPEVELGGGRLRVIAGPLDGV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351 172 DGPVRVKSPVdpTYLDVLLD--GEVKIPVKNGYTVLVYVVDGKIkTVNTPYIDSGNLIIFDrEGDEVDLSGNG--RFILI 247
Cdd:COG1741  148 DGPVKIHQDA--LLYDIRLDagATLTLPLPPGREAYLYVIEGSV-TVNGETLEAGDLAVLS-DGDELTLTADEdaRVLLL 223

                        250       260
                 ....*....|....*....|....*....
gi 499598351 248 SGRPLNEPVYWYGPIVMNSEEQILEALND 276
Cdd:COG1741  224 GGEPLDEPIVMWGPFVMNTKEEIEQAKED 252
 
Name Accession Description Interval E-value
YhaK COG1741
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];
12-276 2.54e-101

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


Pssm-ID: 441347 [Multi-domain]  Cd Length: 253  Bit Score: 296.68  E-value: 2.54e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  12 KSTMDGAGVKLYRVFGGMHTVEYtDPFLLLDFFGSSNPsDYLAGFPWHPHRGIETVTLLYKGKVEHQDSEGNKGVIYPGQ 91
Cdd:COG1741    1 RPTDLGGGLKVRRYLPSRDRRGF-GPFRVLDHDGPAPP-GYGAGFPPHPHRGMETVTYVLEGELEHRDSLGNGGVIRPGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  92 SQWMTAGSGIFHQEMPRPlegteiarynqKPEDMYGLQLWVNLPSNMKMSDPVYRDVKQLPKERFDFGEVQILSGKFMGI 171
Cdd:COG1741   79 VQWMTAGSGIVHSERNPS-----------EGGPLHGLQLWVNLPPADKGLAPRYQHIPDIPEVELGGGRLRVIAGPLDGV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351 172 DGPVRVKSPVdpTYLDVLLD--GEVKIPVKNGYTVLVYVVDGKIkTVNTPYIDSGNLIIFDrEGDEVDLSGNG--RFILI 247
Cdd:COG1741  148 DGPVKIHQDA--LLYDIRLDagATLTLPLPPGREAYLYVIEGSV-TVNGETLEAGDLAVLS-DGDELTLTADEdaRVLLL 223

                        250       260
                 ....*....|....*....|....*....
gi 499598351 248 SGRPLNEPVYWYGPIVMNSEEQILEALND 276
Cdd:COG1741  224 GGEPLDEPIVMWGPFVMNTKEEIEQAKED 252
cupin_pirin_N cd02909
pirin, N-terminal cupin domain; This family contains the N-terminal domain of pirin, a nuclear ...
 20-135 5.78e-54

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: 170.79  E-value: 5.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  20 VKLYRVFGGmHTVEYTDPFLLLDFFGSSNPSDYLAGFPWHPHRGIETVTLLYKGKVEHQDSEGNKGVIYPGQSQWMTAGS 99
Cdd:cd02909    1 ARVRRVLPT-PELRNLDPFLLLDHFGPVKPEPYGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNKGVIRPGDVQWMTAGR 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499598351 100 GIFHQEMPRPLEGTeiarynqkpedMYGLQLWVNLP 135
Cdd:cd02909   80 GIVHSEMPPEEGGP-----------LHGLQLWVNLP 104
Pirin pfam02678
Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The ...
 19-132 6.09e-46

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: 150.09  E-value: 6.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351   19 GVKLYRVFGGMHTVEYTDPFLLLDFFGSSN-PSDYLAGFPWHPHRGIETVTLLYKGKVEHQDSEGNKGVIYPGQSQWMTA 97
Cdd:pfam02678   1 GFRVRRALGGAGWLQSVDPFSFLDYFGPAEfGPGYGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNHGVIRPGDVQWMTA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499598351   98 GSGIFHQEMPRPLEGTeiarynqkpedMYGLQLWV 132
Cdd:pfam02678  81 GSGIVHSEMNPSEEGP-----------LHGFQLWV 104
 
Name Accession Description Interval E-value
YhaK COG1741
Redox-sensitive bicupin YhaK, pirin superfamily [General function prediction only];
12-276 2.54e-101

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


Pssm-ID: 441347 [Multi-domain]  Cd Length: 253  Bit Score: 296.68  E-value: 2.54e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  12 KSTMDGAGVKLYRVFGGMHTVEYtDPFLLLDFFGSSNPsDYLAGFPWHPHRGIETVTLLYKGKVEHQDSEGNKGVIYPGQ 91
Cdd:COG1741    1 RPTDLGGGLKVRRYLPSRDRRGF-GPFRVLDHDGPAPP-GYGAGFPPHPHRGMETVTYVLEGELEHRDSLGNGGVIRPGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  92 SQWMTAGSGIFHQEMPRPlegteiarynqKPEDMYGLQLWVNLPSNMKMSDPVYRDVKQLPKERFDFGEVQILSGKFMGI 171
Cdd:COG1741   79 VQWMTAGSGIVHSERNPS-----------EGGPLHGLQLWVNLPPADKGLAPRYQHIPDIPEVELGGGRLRVIAGPLDGV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351 172 DGPVRVKSPVdpTYLDVLLD--GEVKIPVKNGYTVLVYVVDGKIkTVNTPYIDSGNLIIFDrEGDEVDLSGNG--RFILI 247
Cdd:COG1741  148 DGPVKIHQDA--LLYDIRLDagATLTLPLPPGREAYLYVIEGSV-TVNGETLEAGDLAVLS-DGDELTLTADEdaRVLLL 223

                        250       260
                 ....*....|....*....|....*....
gi 499598351 248 SGRPLNEPVYWYGPIVMNSEEQILEALND 276
Cdd:COG1741  224 GGEPLDEPIVMWGPFVMNTKEEIEQAKED 252
cupin_pirin_N cd02909
pirin, N-terminal cupin domain; This family contains the N-terminal domain of pirin, a nuclear ...
 20-135 5.78e-54

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: 170.79  E-value: 5.78e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  20 VKLYRVFGGmHTVEYTDPFLLLDFFGSSNPSDYLAGFPWHPHRGIETVTLLYKGKVEHQDSEGNKGVIYPGQSQWMTAGS 99
Cdd:cd02909    1 ARVRRVLPT-PELRNLDPFLLLDHFGPVKPEPYGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNKGVIRPGDVQWMTAGR 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499598351 100 GIFHQEMPRPLEGTeiarynqkpedMYGLQLWVNLP 135
Cdd:cd02909   80 GIVHSEMPPEEGGP-----------LHGLQLWVNLP 104
Pirin pfam02678
Pirin; This family consists of Pirin proteins from both eukaryotes and prokaryotes. The ...
 19-132 6.09e-46

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: 150.09  E-value: 6.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351   19 GVKLYRVFGGMHTVEYTDPFLLLDFFGSSN-PSDYLAGFPWHPHRGIETVTLLYKGKVEHQDSEGNKGVIYPGQSQWMTA 97
Cdd:pfam02678   1 GFRVRRALGGAGWLQSVDPFSFLDYFGPAEfGPGYGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNHGVIRPGDVQWMTA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 499598351   98 GSGIFHQEMPRPLEGTeiarynqkpedMYGLQLWV 132
Cdd:pfam02678  81 GSGIVHSEMNPSEEGP-----------LHGFQLWV 104
Pirin_C pfam05726
Pirin C-terminal cupin domain; This region is found the C-terminal half of the Pirin protein.
 185-283 2.49e-31

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: 112.69  E-value: 2.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  185 YLDVLLD--GEVKIPVKNGYTVLVYVVDGKIKTVNTPYIDSGNLIIFDREGDEVDLSGNG--RFILISGRPLNEPVYWYG 260
Cdd:pfam05726   1 YVDLTLEagAEFTLPLPEGWNRALYVLEGSLEVGGEDAIEEHQLAVLGPPGDDLVVRAEApaRFLLLGGEPLGEPVVQYG 80

                          90       100
                  ....*....|....*....|...
gi 499598351  261 PIVMNSEEQILEALNDLRNGTFV 283
Cdd:pfam05726  81 PFVMNTKEEIEQAKEDWRNGRFG 103
cupin_Yhhw_N cd02910
Escherichia coli YhhW and YhaK and related proteins, pirin-like bicupin, N-terminal cupin ...
 54-132 9.01e-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: 9.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  54 AGFPWHPHRGIETVTLLYKGKVEHQDSEGNKGVIYPGQSQWMTAGSGIFHQEmprplegteiarYN-QKPEDMYGLQLWV 132
Cdd:cd02910   36 TGFGTHPHRDMEIITYVLEGELTHRDSMGNKGVLKRGDVQRMSAGTGIRHSE------------YNlSDTEPLRFLQIWI 103
cupin_pirin-like_N cd20287
pirin-like, N-terminal cupin domain; This family contains the N-terminal cupin domain of pirin ...
 38-133 1.37e-19

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: 81.10  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499598351  38 FLLLDFFGSSNPsdylAGFPWHPHRGIETVTLLYKGKVEHQDSEGNKGVIYPGQSQWMTAGSGIFHQEMPRplegteiar 117
Cdd:cd20287    1 LRVFNEFVGGRG----GGFPDHPHRGFEILSYLLEGS*EHEDSCGNTGQ*NAGELQW*SAGRGILHSE*NC--------- 67

                         90
                 ....*....|....*.
gi 499598351 118 ynQKPEDMYGLQLWVN 133
Cdd:cd20287   68 --SEDEPLHGLQLWVN 81
cupin_pirin_C cd02247
pirin, C-terminal cupin domain; This family contains the C-terminal domain of pirin, a nuclear ...
 182-251 4.39e-11

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: 57.63  E-value: 4.39e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499598351 182 DPTYLDVLLD--GEVKIPVKNGYTVLVYVVDGKIkTVNTPYI--DSGNLIIFDREGDEVDL---SGNGRFILISGRP 251
Cdd:cd02247    1 PVLYLDITLEpgAKFTQPVPAGWNAFIYVLEGEA-TIGGEEVeaEAGHLAVLGPGGDGVELeakEEGARFLLIAGEP 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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