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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232679958  17 WLKSRHTFSFAEYYDPEFMGFGSLRVINEDRIQGGTGFGTHPHKDMEIISYVISGALQHKDSMGNVAVIKPGEIQRMSAG 96
Cdd:cd02910     1 WLKSRHTFSFADYYDPKNMGFGALRVINDDIVAPGTGFGTHPHRDMEIITYVLEGELTHRDSMGNKGVLKRGDVQRMSAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1232679958  97 TGVAHSEYNDEKSKETHFFQIWISPDHRGGKPGYGQKSF 135
Cdd:cd02910    81 TGIRHSEYNLSDTEPLRFLQIWILPDQRGLKPSYQQKRF 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232679958  17 WLKSRHTFSFAEYYDPEFMGFGSLRVINEDRIQGGTGFGTHPHKDMEIISYVISGALQHKDSMGNVAVIKPGEIQRMSAG 96
Cdd:cd02910     1 WLKSRHTFSFADYYDPKNMGFGALRVINDDIVAPGTGFGTHPHRDMEIITYVLEGELTHRDSMGNKGVLKRGDVQRMSAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1232679958  97 TGVAHSEYNDEKSKETHFFQIWISPDHRGGKPGYGQKSF 135
Cdd:cd02910    81 TGIRHSEYNLSDTEPLRFLQIWILPDQRGLKPSYQQKRF 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232679958  16 GWLKSRHTFSFAEYYDPEFMGFGslrvinedriqGGTGFGTHPHKDMEIISYVISGALQHKDSMGNVAVIKPGEIQRMSA 95
Cdd:pfam02678  12 GWLQSVDPFSFLDYFGPAEFGPG-----------YGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNHGVIRPGDVQWMTA 80

                          90       100
                  ....*....|....*....|....
gi 1232679958  96 GTGVAHSEYNDEKSKETHFFQIWI 119
Cdd:pfam02678  81 GSGIVHSEMNPSEEGPLHGFQLWV 104

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232679958 163 ANMYISRLKK-SEALDYKLNkGRKLWIQLIKGTVKVNDNEIETGDAIAAIDIGTVKIEVKDDSEMIIFDLV 232
Cdd:cd20311     1 AWLYASVLDKgEASVHLLAG-GRRAWLQVVRGTVTVNGVALKTGDGAAISDETALTLTADSDAEVLLFDLP 70

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232679958  17 WLKSRHTFSFAEYYDPEFMGFGSLRVINEDRIQGGTGFGTHPHKDMEIISYVISGALQHKDSMGNVAVIKPGEIQRMSAG 96
Cdd:cd02910     1 WLKSRHTFSFADYYDPKNMGFGALRVINDDIVAPGTGFGTHPHRDMEIITYVLEGELTHRDSMGNKGVLKRGDVQRMSAG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1232679958  97 TGVAHSEYNDEKSKETHFFQIWISPDHRGGKPGYGQKSF 135
Cdd:cd02910    81 TGIRHSEYNLSDTEPLRFLQIWILPDQRGLKPSYQQKRF 119

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232679958  16 GWLKSRHTFSFAEYYDPEFMGFGslrvinedriqGGTGFGTHPHKDMEIISYVISGALQHKDSMGNVAVIKPGEIQRMSA 95
Cdd:pfam02678  12 GWLQSVDPFSFLDYFGPAEFGPG-----------YGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNHGVIRPGDVQWMTA 80

                          90       100
                  ....*....|....*....|....
gi 1232679958  96 GTGVAHSEYNDEKSKETHFFQIWI 119
Cdd:pfam02678  81 GSGIVHSEMNPSEEGPLHGFQLWV 104

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232679958  19 KSRHTFSFAE--YYDPeFMGFGSLRVINEDriQGGTGFGTHPHKDMEIISYVISGALQHKDSMGNVAVIKPGEIQRMSAG 96
Cdd:cd02909     2 RVRRVLPTPElrNLDP-FLLLDHFGPVKPE--PYGAGFPPHPHRGFETVTYLLEGEVEHRDSLGNKGVIRPGDVQWMTAG 78

                          90       100
                  ....*....|....*....|...
gi 1232679958  97 TGVAHSEYNDEKSKETHFFQIWI 119
Cdd:cd02909    79 RGIVHSEMPPEEGGPLHGLQLWV 101

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.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232679958 163 ANMYISRLKK-SEALDYKLNkGRKLWIQLIKGTVKVNDNEIETGDAIAAIDIGTVKIEVKDDSEMIIFDLV 232
Cdd:cd20311     1 AWLYASVLDKgEASVHLLAG-GRRAWLQVVRGTVTVNGVALKTGDGAAISDETALTLTADSDAEVLLFDLP 70

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232679958  47 RIQGGTGFGTHPHKDMEIISYVISGALQHKDSMGNVAVIKPGEIQRMSAgtGVAHSEYNDEkSKETHFFQIW 118
Cdd:cd02208     5 TLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGETVELKAGDIVLIPP--GVPHSFVNTS-DEPAVFLVVS 73