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Conserved domains on  [gi|21730352|pdb|1J58|A]
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Chain A, YVRK PROTEIN

Protein Classification

oxalate decarboxylase family bicupin( domain architecture ID 11496804)

oxalate decarboxylase family bicupin contains two cupin domains and is similar to Bacillus subtilis oxalate decarboxylases OxdC and OxdD that convert oxalate to formate and CO(2)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 13-379 0e+00

bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins as they have two copies of the cupin domain (pfam00190). Two different known activities for members of this family are oxalate decarboxylase (EC 4.1.1.2) and oxalate oxidase (EC 1.2.3.4), although the latter activity has more often been found in distantly related monocupin (germin) proteins.


:

Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 679.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A         13 GDKGATVKIPRNIERDRQNPD*LVPPETDHGTVSN*KFSFSDTHNRLEKGGYAREVTVRELPISENLASVN*RLKPGAIR 92
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A         93 ELHWHKEAEWAY*IYGSARVTIVDEKGRSFIDDVGEGDLWYFPSGLPHSIQALEEGAEFLLVFDDGSFSENSTFQLTDWL 172
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLDEGCEFLLVFDDGNFSEDGTFLVTDWL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A        173 AHTPKEVIAANFGVTKEEISNLPGKEKYIFENQLPGSLKDDIVEGPNGEVPYPFTYRLLEQEPIESEGGKVYIADSTNFK 252
Cdd:TIGR03404 161 AHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEVPGPFTYHLSEQKPKQVPGGTVRIADSTNFP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A        253 VSKTIASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFL 332
Cdd:TIGR03404 241 VSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
1J58_A        333 EIFKDDHYADVSLNQWLA*LPETFVQAHLDLGKDFTDVLSKEKHPVV 379
Cdd:TIGR03404 321 EVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
 
Name Accession Description Interval E-value
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 13-379 0e+00

bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins as they have two copies of the cupin domain (pfam00190). Two different known activities for members of this family are oxalate decarboxylase (EC 4.1.1.2) and oxalate oxidase (EC 1.2.3.4), although the latter activity has more often been found in distantly related monocupin (germin) proteins.


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 679.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A         13 GDKGATVKIPRNIERDRQNPD*LVPPETDHGTVSN*KFSFSDTHNRLEKGGYAREVTVRELPISENLASVN*RLKPGAIR 92
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A         93 ELHWHKEAEWAY*IYGSARVTIVDEKGRSFIDDVGEGDLWYFPSGLPHSIQALEEGAEFLLVFDDGSFSENSTFQLTDWL 172
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLDEGCEFLLVFDDGNFSEDGTFLVTDWL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A        173 AHTPKEVIAANFGVTKEEISNLPGKEKYIFENQLPGSLKDDIVEGPNGEVPYPFTYRLLEQEPIESEGGKVYIADSTNFK 252
Cdd:TIGR03404 161 AHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEVPGPFTYHLSEQKPKQVPGGTVRIADSTNFP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A        253 VSKTIASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFL 332
Cdd:TIGR03404 241 VSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
1J58_A        333 EIFKDDHYADVSLNQWLA*LPETFVQAHLDLGKDFTDVLSKEKHPVV 379
Cdd:TIGR03404 321 EVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 49-202 1.63e-100

Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380438  Cd Length: 155  Bit Score: 294.52  E-value: 1.63e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       49 KFSFSDTHNRLEKGGYAREVTVRELPISENLASVN*RLKPGAIRELHWHKEAEWAY*IYGSARVTIVDEKGRSFIDDVGE 128
Cdd:cd20304   1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWHAAAEWAYVLSGRCRITAVDPEGRSFIDDVGP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1J58_A      129 GDLWYFPSGLPHSIQALE-EGAEFLLVFDDGSFSENSTFQLTDWLAHTPKEVIAANFGVTKEEISNLPGKEKYIF 202
Cdd:cd20304  81 GDLWYFPRGHPHSIQGLGpDGCEFLLVFDDGNFSEFGTFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKKELYIF 155
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 256-354 9.49e-41

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 139.72  E-value: 9.49e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      256 TIASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEIF 335
Cdd:COG2140   2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81

                        90       100
                ....*....|....*....|..
1J58_A      336 KDDH---YADVSLNQWLA*LPE 354
Cdd:COG2140  82 DDDAgsdYGTISLSGWLAHTPP 103
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 231-363 2.40e-29

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 110.83  E-value: 2.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A         231 LEQEPI-ESEGGKVYIADSTNFKVSKT--IASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDG-HARTFNYQ 306
Cdd:smart00835   1 LEPRPDfSNEGGRLREADPTNFPALNGlgISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGnKVYDARLR 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
1J58_A         307 AGDVGYVPFA*GHYVENIGDEPLVFLeIFKDDHYADVSL----NQWLA*LPETFVQAHLDL 363
Cdd:smart00835  81 EGDVFVVPQGHPHFQVNSGDENLEFV-AFNTNDPNRRFFlagrNSVLRGLPPEVLAAAFGV 140
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 228-369 5.60e-28

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 395138  Cd Length: 151  Bit Score: 107.42  E-value: 5.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A        228 YRLLEQEP-IESEGGKVYIADSTNFKVSKT--IASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTFN 304
Cdd:pfam00190   1 LNLLEPGPtYNPEGGRVTTVNSKNLPGLNTlgISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNGNRVFH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1J58_A        305 --YQAGDVGYVPFA*GHYVENIGDEPLVFLEIFKDDHYADVS----LNQWLA*LPETFVQAHLDLGKDFTD 369
Cdd:pfam00190  81 kvLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSilagGFSSLPALPPEVLAKAFQLAGEEVK 151
PRK04190 PRK04190
glucose-6-phosphate isomerase; Provisional
 273-338 5.43e-04

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179774  Cd Length: 191  Bit Score: 40.78  E-value: 5.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1J58_A       273 HWH--PNTHEWQYYISGKAR*TVFASDGHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEIFKDD 338
Cdd:PRK04190  90 HFHakADRAEIYYGLKGKGLMLLQDPEGEARWIEMEPGTVVYVPPYWAHRSVNTGDEPLVFLACYPAD 157
 
Name Accession Description Interval E-value
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 13-379 0e+00

bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins as they have two copies of the cupin domain (pfam00190). Two different known activities for members of this family are oxalate decarboxylase (EC 4.1.1.2) and oxalate oxidase (EC 1.2.3.4), although the latter activity has more often been found in distantly related monocupin (germin) proteins.


Pssm-ID: 274565 [Multi-domain]  Cd Length: 367  Bit Score: 679.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A         13 GDKGATVKIPRNIERDRQNPD*LVPPETDHGTVSN*KFSFSDTHNRLEKGGYAREVTVRELPISENLASVN*RLKPGAIR 92
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A         93 ELHWHKEAEWAY*IYGSARVTIVDEKGRSFIDDVGEGDLWYFPSGLPHSIQALEEGAEFLLVFDDGSFSENSTFQLTDWL 172
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLDEGCEFLLVFDDGNFSEDGTFLVTDWL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A        173 AHTPKEVIAANFGVTKEEISNLPGKEKYIFENQLPGSLKDDIVEGPNGEVPYPFTYRLLEQEPIESEGGKVYIADSTNFK 252
Cdd:TIGR03404 161 AHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEVPGPFTYHLSEQKPKQVPGGTVRIADSTNFP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A        253 VSKTIASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFL 332
Cdd:TIGR03404 241 VSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
1J58_A        333 EIFKDDHYADVSLNQWLA*LPETFVQAHLDLGKDFTDVLSKEKHPVV 379
Cdd:TIGR03404 321 EVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 49-202 1.63e-100

Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380438  Cd Length: 155  Bit Score: 294.52  E-value: 1.63e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       49 KFSFSDTHNRLEKGGYAREVTVRELPISENLASVN*RLKPGAIRELHWHKEAEWAY*IYGSARVTIVDEKGRSFIDDVGE 128
Cdd:cd20304   1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWHAAAEWAYVLSGRCRITAVDPEGRSFIDDVGP 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1J58_A      129 GDLWYFPSGLPHSIQALE-EGAEFLLVFDDGSFSENSTFQLTDWLAHTPKEVIAANFGVTKEEISNLPGKEKYIF 202
Cdd:cd20304  81 GDLWYFPRGHPHSIQGLGpDGCEFLLVFDDGNFSEFGTFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKKELYIF 155
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 225-376 7.91e-95

Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380439 [Multi-domain]  Cd Length: 153  Bit Score: 279.85  E-value: 7.91e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      225 PFTYRLLEQEPI-ESEGGKVYIADSTNFKVSKTIASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTF 303
Cdd:cd20305   1 PHTFRLLAQPPIkVPAGGSVRIVDSKNFPISTTIAAALVTLEPGALRELHWHPNADEWQYYISGKARMTVFASGGRARTF 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1J58_A      304 NYQAGDVGYVPFA*GHYVENIGDEPLVFLEIFKDDHYADVSLNQWLA*LPETFVQAHLDLGKDFTDVLSKEKH 376
Cdd:cd20305  81 DFQAGDVGYVPRGYGHYIENTGDEPLEFLEVFNSGRYQDISLSQWLALTPPDLVAAHLGLPDDTIAKLPKKKQ 153
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 232-376 1.55e-71

Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380367 [Multi-domain]  Cd Length: 145  Bit Score: 220.43  E-value: 1.55e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      232 EQEPI-ESEGGKVYIADSTNFKVSKTIASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTFNYQAGDV 310
Cdd:cd02240   1 DSEPIeENAGGSVRIATVTNFPISKDLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRFETFNLGAGDV 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1J58_A      311 GYVPFA*GHYVENIGDEPLVFLEIFKDDHYADVSLNQWLA*LPETFVQAHLDLGKdFTDVLSKEKH 376
Cdd:cd02240  81 GYVPSGSGHHIENIGDEDAEFLLIFDDGTFADVSLPWWLAMTPEEVLAATLDLGK-FIDALPKAKH 145
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 54-199 2.04e-64

Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds and both domains are included in this alignment. Each OxDC cupin domain contains one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380367 [Multi-domain]  Cd Length: 145  Bit Score: 201.94  E-value: 2.04e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       54 DTHNRLE-KGGYAREVTVRELPISENLASVN*RLKPGAIRELHWHK-EAEWAY*IYGSARVTIVDEKGRSFIDDVGEGDL 131
Cdd:cd02240   1 DSEPIEEnAGGSVRIATVTNFPISKDLSSALVRVAPGAMRELHWHPnTAEWQYVISGSARVTVFDEDGRFETFNLGAGDV 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1J58_A      132 WYFPSGLPHSIQAL-EEGAEFLLVFDDGSFsenSTFQLTDWLAHTPKEVIAANFGVTKeEISNLPGKEK 199
Cdd:cd02240  81 GYVPSGSGHHIENIgDEDAEFLLIFDDGTF---ADVSLPWWLAMTPEEVLAATLDLGK-FIDALPKAKH 145
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 256-354 9.49e-41

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 139.72  E-value: 9.49e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      256 TIASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEIF 335
Cdd:COG2140   2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81

                        90       100
                ....*....|....*....|..
1J58_A      336 KDDH---YADVSLNQWLA*LPE 354
Cdd:COG2140  82 DDDAgsdYGTISLSGWLAHTPP 103
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 78-181 1.98e-35

Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 441743 [Multi-domain]  Cd Length: 115  Bit Score: 125.85  E-value: 1.98e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       78 NLASVN*RLKPGAIRELHWH-KEAEWAY*IYGSARVTIVDEKGRSFIDDVGEGDLWYFPSGLPHSIQAL-EEGAEFLLVF 155
Cdd:COG2140   2 TLAGGLTVLEPGGVREEHWHpNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTgDEPLVFLAVF 81

                        90       100
                ....*....|....*....|....*.
1J58_A      156 DDGSFSENSTFQLTDWLAHTPKEVIA 181
Cdd:COG2140  82 DDDAGSDYGTISLSGWLAHTPPEVLA 107
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 49-190 9.50e-30

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 111.91  E-value: 9.50e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       49 KFSFSDTHNRLEK-GGYAREVTVRELPISENLASVN*RLKPGAIRELHWHKEA-EWAY*IYGSARVTIVDEKGR--SFid 124
Cdd:cd20306   3 LFSLEDSNPFFESeGGSIRQATADQLPVLKGLSIYRLRLSPGGIREPHWHPNAnELGYVISGEARVSILDPTGSldTF-- 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1J58_A      125 DVGEGDLWYFPSGLPHSIQAL-EEGAEFLLVFDDGSFsenSTFQLTDWLAHTPKEVIAANFGVTKEE 190
Cdd:cd20306  81 TVKPGQVVFIPQGWLHWIENVgDEEAHLLIFFNHETP---EDIGLSDSLRATPPEVLGNTYGVDAFF 144
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 231-363 2.40e-29

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 110.83  E-value: 2.40e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A         231 LEQEPI-ESEGGKVYIADSTNFKVSKT--IASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDG-HARTFNYQ 306
Cdd:smart00835   1 LEPRPDfSNEGGRLREADPTNFPALNGlgISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGnKVYDARLR 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
1J58_A         307 AGDVGYVPFA*GHYVENIGDEPLVFLeIFKDDHYADVSL----NQWLA*LPETFVQAHLDL 363
Cdd:smart00835  81 EGDVFVVPQGHPHFQVNSGDENLEFV-AFNTNDPNRRFFlagrNSVLRGLPPEVLAAAFGV 140
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 225-335 7.34e-29

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 109.60  E-value: 7.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      225 PFTYRLLEQEP-IESEGGKVYIADSTNFKVSKTIASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTF 303
Cdd:cd20306   1 PHLFSLEDSNPfFESEGGSIRQATADQLPVLKGLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSLDTF 80

                        90       100       110
                ....*....|....*....|....*....|..
1J58_A      304 NYQAGDVGYVPFA*GHYVENIGDEPLVFLEIF 335
Cdd:cd20306  81 TVKPGQVVFIPQGWLHWIENVGDEEAHLLIFF 112
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 228-369 5.60e-28

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 395138  Cd Length: 151  Bit Score: 107.42  E-value: 5.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A        228 YRLLEQEP-IESEGGKVYIADSTNFKVSKT--IASALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVFASDGHARTFN 304
Cdd:pfam00190   1 LNLLEPGPtYNPEGGRVTTVNSKNLPGLNTlgISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNGNRVFH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1J58_A        305 --YQAGDVGYVPFA*GHYVENIGDEPLVFLEIFKDDHYADVS----LNQWLA*LPETFVQAHLDLGKDFTD 369
Cdd:pfam00190  81 kvLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSilagGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 61-191 9.75e-25

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 98.51  E-value: 9.75e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A          61 KGGYAREVTVRELPISE--NLASVN*RLKPGAIRELHWHKEA-EWAY*IYGSARVTIVDEKGRS-FIDDVGEGDLWYFPS 136
Cdd:smart00835  10 EGGRLREADPTNFPALNglGISAARVNLEPGGMLPPHYHPRAtELLYVVRGEGRVGVVDPNGNKvYDARLREGDVFVVPQ 89

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
1J58_A         137 GLPHSIQALEEGAEFLLVFDDGSFSENST-FQLTDWLAHTPKEVIAANFGVTKEEI 191
Cdd:smart00835  90 GHPHFQVNSGDENLEFVAFNTNDPNRRFFlAGRNSVLRGLPPEVLAAAFGVSAEEV 145
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 61-191 1.33e-23

Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel). This family contains 11S and 7S plant seed storage proteins, and germins. Plant seed storage proteins provide the major nitrogen source for the developing plant.


Pssm-ID: 395138  Cd Length: 151  Bit Score: 95.48  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A         61 KGGYAREVTVRELPI--SENLASVN*RLKPGAIRELHWHKEA-EWAY*IYGSARVTIVDEKG--RSFIDDVGEGDLWYFP 135
Cdd:pfam00190  13 EGGRVTTVNSKNLPGlnTLGISAARVDLAPGGMNPPHWHPNAtEILYVLQGRGRVGFVVPGNgnRVFHKVLREGDVFVVP 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
1J58_A        136 SGLPHSIQAL--EEGAEFLLVFDDGSFSENSTFQLTDWLAHTPKEVIAANFGVTKEEI 191
Cdd:pfam00190  93 QGLPHFQYNIgdEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEV 150
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 227-353 2.39e-23

Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal cupin domain of oxalate decarboxylase (OxDC; EC 4.1.1.2), a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380438  Cd Length: 155  Bit Score: 94.98  E-value: 2.39e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      227 TYRLLEQEPIESEGGKVYIADSTNFKVSKTIASALVTVEPGA*RELHWHpNTHEWQYYISGKAR*TVFASDGHARTFNYQ 306
Cdd:cd20304   1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWH-AAAEWAYVLSGRCRITAVDPEGRSFIDDVG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
1J58_A      307 AGDVGYVPFA*GHYVENIGDEPLVFLEIFKDDHYAD---VSLNQWLA*LP 353
Cdd:cd20304  80 PGDLWYFPRGHPHSIQGLGPDGCEFLLVFDDGNFSEfgtFSITDWLAHTP 129
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 261-335 3.88e-12

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.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 61.34  E-value: 3.88e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1J58_A      261 LVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVfasdGHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEIF 335
Cdd:cd02208   3 VVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTL----DDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 260-335 1.08e-11

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 59.96  E-value: 1.08e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1J58_A        260 ALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVfasDGHARTfnYQAGDVGYVPFA*GHYVENIGDEPLVFLEIF 335
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTV---DGEEVV--LKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 54-190 2.71e-11

11S legumin seed storage globulin, C-terminal cupin domain; This family contains the C-terminal domains of 11S legumin seed storage proteins that supply nutrition for seed germination, such as glycinin and legumin, including many common food allergens such as the peanut major allergen Ara h 3, almond allergen Pru du 6, Pecan allergen Car i 4, hazelnut nut allergen Cor a 9, Brazil nut allergen Ber e 2, cashew allergen Ana o 2, pistachio allergen Pis v 2/5, and walnut allergen Jug n/r 4. These plant seed storage globulins have tandem cupin-like beta-barrel folds (referred to as a bicupin). They are synthesized as propeptides in the endoplasmic reticulum and transported to the secretory vesicles as a homotrimer. The propeptides are processed as they are sorted in the secretory vesicles. The homotrimer binds another homotrimer to form a homohexamer with 32-point symmetry formed by a face-to-face stacking of the two trimers. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380370  Cd Length: 155  Bit Score: 61.34  E-value: 2.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       54 DTHNRleKGGYAREVTVRELPISENLA-SVN-*RLKPGAIRELHWHKEA-EWAY*IYGSARVTIVDEKGRSFIDD-VGEG 129
Cdd:cd02243   1 DVYVP--RGGRITTLNSFKLPILRFVGlSAErVKLEPNAMFAPHWNANAhQVIYVTRGSGRVQVVGDNGKRVLDGeVREG 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1J58_A      130 DLWYFPSGLPHSIQALEEGAEFLlvfddgSF--SENSTF-QL---TDWLAHTPKEVIAANFGVTKEE 190
Cdd:cd02243  79 QLLVVPQFFAVAKIAGEEGFEWV------SFktSDNPIFsELagrTSVLRALPPEVLANSYNISPEE 139
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 260-334 1.52e-10

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 57.53  E-value: 1.52e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1J58_A      260 ALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVfasDGhaRTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEI 334
Cdd:cd02214  22 AHARVPPGESTLPHRLKGSEEVYYILEGEGTMEI---DG--EPREVGPGDAVLIPPGAVQRIENTGEEDLVFLCI 91
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
260-335 2.62e-10

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 57.46  E-value: 2.62e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1J58_A      260 ALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVfasDGhaRTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEIF 335
Cdd:COG0662  30 KRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTI---GD--EEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEVQ 100
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 260-332 3.06e-08

Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial proteins homologous to TM1287 decarboxylase, a Thermotoga maritima manganese-containing cupin thought to catalyze the conversion of oxalate to formate and carbon dioxide, due to its similarity to oxalate decarboxylase (OXDC) from Bacillus subtilis. TM1287 shows a cupin fold with a conserved "jelly roll-like" beta-barrel fold and forms a homodimer.


Pssm-ID: 380350 [Multi-domain]  Cd Length: 93  Bit Score: 50.93  E-value: 3.06e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1J58_A      260 ALVTVEPGA*RELHWHPNTHEwQYYI-SGKAr*tVFASDGhaRTFNYQAGDVGYVPFA*GHYVENIGDEPLVFL 332
Cdd:cd02221  22 ARVTLPPGSSIGYHQHEGEFE-IYYIlSGEG---LYTDNG--KEYEVKAGDVTFTRDGESHGIENTGDEDLVFI 89
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
55-158 5.20e-08

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 50.23  E-value: 5.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       55 THNRLEKGGYAREVTVRElpiSENLASVN*RLKPGAIRELHWHKEAEWAY*IYGSARVTIVDEKGRsfiddVGEGDLWYF 134
Cdd:COG1917   2 RLAEIALTGVSVRVLADG---EDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEVGGEEYE-----LKPGDVVFI 73

                        90       100
                ....*....|....*....|....*
1J58_A      135 PSGLPHSIQALE-EGAEFLLVFDDG 158
Cdd:COG1917  74 PPGVPHAFRNLGdEPAVLLVVFSPG 98
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
260-335 1.21e-07

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 49.46  E-value: 1.21e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1J58_A      260 ALVTVEPGA*RELHWHPnTHEWQYYISGKAR*TVfasDGHarTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEIF 335
Cdd:COG1917  26 VRVTFEPGARTPWHSHP-GEELIYVLEGEGEVEV---GGE--EYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 68-148 1.22e-07

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 49.39  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       68 VTVRELPISENLASVN*RLKPGAIRELHWHKEAEWAY*IYGSARVTIVDEKgrsfiDDVGEGDLWYFPSGLPHSIQALEE 147
Cdd:cd02238  16 VRRKILAGGEKLMLVEVRFEKGAVVPLHSHPHEQIGYVLSGRFEFTIGGET-----RILKPGDSYYIPPNVPHGAEALED 90


                .
1J58_A      148 G 148
Cdd:cd02238  91 S 91
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 85-155 3.31e-07

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.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 47.48  E-value: 3.31e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1J58_A       85 RLKPGAIRELHWHKEA-EWAY*IYGSARVTIVDEKGRsfidDVGEGDLWYFPSGLPHSIQALE-EGAEFLLVF 155
Cdd:cd02208   5 TLPPGTSSPPHWHPEQdEIFYVLSGEGELTLDDGETV----ELKAGDIVLIPPGVPHSFVNTSdEPAVFLVVS 73
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 261-332 3.78e-07

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 47.44  E-value: 3.78e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1J58_A      261 LVTVEPGA*RELHWHPNTHEwQYYISGKAR*TVfasDGHARTFnyQAGDVGYVPFA*GHYVENIGDEPLVFL 332
Cdd:cd02222  21 YFEIEPGGHTPLHTHPWEHE-VYVLRGKGVVVI---GGEEYPV--KPGDVVYIPPNEPHQFRNTGDEPLGFL 86
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 245-334 7.79e-07

Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal cupin domain of mannose-6-phosphate isomerases (MPIs) which have been classified broadly into two groups, type I and type II, based on domain organization. This family contains type II phosphomannose isomerase (also known as PMI-GDP, phosphomannose isomerase/GDP-D-mannose pyrophosphorylase), a bifunctional enzyme with two domains that catalyze the first and third steps in the GDP-mannose pathway in which fructose 6-phosphate is converted to GDP-D-mannose. The N-terminal domain catalyzes the first and rate-limiting step, the isomerization from D-fructose-6-phosphate to D-mannose-6-phosphate, while the C-terminal cupin domain (represented in this alignment model) converts mannose 1-phosphate to GDP-D-mannose in the final step of the reaction. Although these two domains occur together in one protein in most organisms, they occur as separate proteins in certain cyanobacterial organisms. Also, although type I and type II MPIs have no overall sequence similarity, they share a conserved catalytic motif.


Pssm-ID: 380343 [Multi-domain]  Cd Length: 126  Bit Score: 47.55  E-value: 7.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      245 IADSTNFKVSKtiasalVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVfasDGhaRTFNYQAGDVGYVPFA*GHYVENI 324
Cdd:cd02213  34 LDEGEGYKVKR------LTVNPGKRLSLQRHHHRSEHWVVVSGTAEVTL---DG--KEKLLKEGESIYIPKGTKHRLENP 102

                        90
                ....*....|
1J58_A      325 GDEPLVFLEI 334
Cdd:cd02213 103 GKIPLEIIEV 112
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 259-337 9.54e-07

Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to dimethylsulfoniopropionate lyase DddK from marine bacterium Pelagibacter. DddK cleaves dimethylsulfoniopropionate (DMSP), the organic osmolyte and antioxidant produced in marine environments, and yields acrylate and the climate-active gas dimethyl sulfide (DMS). DddK contains a double-stranded beta-helical motif which utilizes various divalent metal ions as cofactors for catalytic activity; however, nickel, an abundant metal ion in marine environments, confers the highest DMSP lyase activity. Also included in this family is Plu4264, a Photorhabdus luminescens manganese-containing cupin shown to have similar metal binding site to TM1287 decarboxylase, but two very different substrate binding pockets. The Plu4264 binding pocket shows a cavity and substrate entry point more than twice as large as and more hydrophobic than TM1287, suggesting that Plu4264 accepts a substrate that is significantly larger than that of TM1287, a putative oxalate decarboxylase. Thus, the function of Plu4264 could be similar to that of TM1287 but with a larger, less charged substrate. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380393 [Multi-domain]  Cd Length: 76  Bit Score: 46.07  E-value: 9.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      259 SALVTVEPGA*RELHWHpntHEWQYYI--SGKAR*TVfasDGHARTFnyQAGDVGYVPFA*GHYVENIGDEPLVFLEIFK 336
Cdd:cd06988   4 GAWCVVRPGTTSTPHSH---HEYEIFIviSGKGIVVV---DGEREPV--KAGDVVYIPPGTEHYVKNDGDEDFEFYSIWW 75


                .
1J58_A      337 D 337
Cdd:cd06988  76 D 76
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
261-342 1.40e-06

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 46.55  E-value: 1.40e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      261 LVTVEPGA*-RELHWHPNTHEWQYYISGKAR*TVfasDGHARTFnyQAGDVGYVPFA*GHYVENIGDEPLVFLEIFKDDH 339
Cdd:COG3837  32 LITLPPGASsSPYHAHSAEEEFVYVLEGELTLRI---GGEEYVL--EPGDSVGFPAGVPHRLRNRGDEPARYLVVGTRAP 106


                ...
1J58_A      340 YAD 342
Cdd:COG3837 107 YPD 109
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 85-155 1.63e-06

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 45.33  E-value: 1.63e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1J58_A         85 RLKPGAIRELHWHK-EAEWAY*IYGSARVTIVDEKgrsfiDDVGEGDLWYFPSGLPHSIQAL-EEGAEFLLVF 155
Cdd:pfam07883   4 TLPPGESSPPHRHPgEDEFFYVLEGEGELTVDGEE-----VVLKAGDSVYFPAGVPHRFRNTgDEPARLLDVY 71
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
85-155 6.79e-06

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 44.75  E-value: 6.79e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1J58_A       85 RLKPGAIRELHWH-KEAEWAY*IYGSARVTIVDEKGrsfidDVGEGDLWYFPSGLPHSIQAL-EEGAEFLLVF 155
Cdd:COG0662  33 TVPPGAELSLHVHpHRDEFFYVLEGTGEVTIGDEEV-----ELKAGDSVYIPAGVPHRLRNPgDEPLELLEVQ 100
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 36-197 7.85e-06

Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380368  Cd Length: 191  Bit Score: 46.05  E-value: 7.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       36 VPPETDHGTVSN*KFSFSDTHNRLE----KGGYAREVTVRELP--ISENLASVN*RLKPGAIRELHWHKEA-EWAY*IYG 108
Cdd:cd02241  21 GYPCKDPALVTADDFVFDFLNPPGNtsnpLGGSVTLANVANFPalNGLGISMARGDLAPCGVNPPHTHPRAtELLYVVEG 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      109 SARVTIVDEKGRSFID-DVGEGDLWYFPSGLPHSIQAL-EEGAEFLLVFDdgsfSEN--------STFQLTDwlahtPKE 178
Cdd:cd02241 101 TLYVGFVDENGNRLFTkTLNPGDVFVFPQGLIHFQFNPgCEPAVFVAAFN----SEDpgtqqiaqALFGLPP-----PDD 171

                       170
                ....*....|....*....
1J58_A      179 VIAANFGVTKEEISNLPGK 197
Cdd:cd02241 172 VLAAAFGLDGAQVEKLKSK 190
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 261-334 1.41e-05

Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase with a cupin domain; This family includes proteins similar to sugar phosphate isomerase SPO2919 from Silicibacter pomeroyi and Afe_0303 from Acidithiobacillus ferrooxidans, but are as yet uncharacterized. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380353 [Multi-domain]  Cd Length: 105  Bit Score: 43.63  E-value: 1.41e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1J58_A      261 LVTVEPGA*R-ELHWHPNTHEWQYYISGKAR*TVfasDGHARTFnyQAGDvgYVPF----A*GHYVENIGDEPLVFLEI 334
Cdd:cd02224  21 LERLPPGARSsPRHWHSAEEEFVYVLSGEGTLRL---DGEEVLP--RPGD--FVGFpagtGVAHQLINRSDEPLVYLVV 92
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 85-152 7.35e-05

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 41.35  E-value: 7.35e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       85 RLKPGAIRELHWHKEAEWAY*I-YGSARVTIVDEKgrsfiDDVGEGDLWYFPSGLPHSIQALEEGA-EFL 152
Cdd:cd02214  25 RVPPGESTLPHRLKGSEEVYYIlEGEGTMEIDGEP-----REVGPGDAVLIPPGAVQRIENTGEEDlVFL 89
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 260-331 2.54e-04

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 39.97  E-value: 2.54e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1J58_A      260 ALVTVEPGA*RELHWHPNTHEWQYYISGKAR*TVfasDGHarTFNYQAGDVGYVPFA*GHYVENIGDEP--LVF 331
Cdd:cd06991  22 GTLTLAPGERVSEHYHPYSEEFLYVVRGRLVVRV---DGE--PVVLEAGEALLVPRGVRHRLENAGDEParLVF 90
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
85-154 3.37e-04

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 40.00  E-value: 3.37e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1J58_A       85 RLKPGA-IRELHWH-KEAEWAY*IYGSARVTIVDEKGRsfiddVGEGDLWYFPSGLPHSIQAL-EEGAEFLLV 154
Cdd:COG3837  34 TLPPGAsSSPYHAHsAEEEFVYVLEGELTLRIGGEEYV-----LEPGDSVGFPAGVPHRLRNRgDEPARYLVV 101
cupin_PGI cd02218
cupin-type phosphoglucose isomerase; The cupin-type phosphoglucose isomerase (also called ...
 273-338 3.81e-04

cupin-type phosphoglucose isomerase; The cupin-type phosphoglucose isomerase (also called cupin-like glucose-6-phosphate isomerase or cPGI; EC 5.3.1.9) family is found in archaea and certain prokaryotes where they catalyze the reversible aldose-ketose isomerization of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) as part of a unique variation of the Embden-Meyerhof glycolytic pathway. Cupin-PGIs represent a separate lineage in the evolution of phosphoglucose isomerases. Pyrococcus furiosus phosphoglucose isomerase (PfPGI) has been shown to be a metal-containing enzyme which catalyzes the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). These domains have a cupin beta-barrel fold capable of homodimerization.


Pssm-ID: 380347  Cd Length: 168  Bit Score: 40.62  E-value: 3.81e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1J58_A      273 HWHPNTHEWQYY--ISGKAr*tVF----ASDGHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEIFKDD 338
Cdd:cd02218  67 HYHAKRDYPEVYevLSGEG---LLllqkEDVGEVILVEAKPGDKVYIPPGYAHRTINTGDEPLVFANWWPSD 135
PRK04190 PRK04190
glucose-6-phosphate isomerase; Provisional
 273-338 5.43e-04

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179774  Cd Length: 191  Bit Score: 40.78  E-value: 5.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1J58_A       273 HWH--PNTHEWQYYISGKAR*TVFASDGHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEIFKDD 338
Cdd:PRK04190  90 HFHakADRAEIYYGLKGKGLMLLQDPEGEARWIEMEPGTVVYVPPYWAHRSVNTGDEPLVFLACYPAD 157
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
 257-335 1.34e-03

Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes mostly bacterial proteins homologous to CV2614, a Chromobacterium violaceum protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380364 [Multi-domain]  Cd Length: 102  Bit Score: 37.86  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      257 IASALVTVEPGA*RELHWH--PNtheWQYYISGKar*TVFASDGHARTFNyqAGDVgyvpFA*G----HYVENIGDEPLV 330
Cdd:cd02236  22 ITVLRITIPPGAELPWHTHpvPN---AGYVLSGE--LTVEYEDGKKRTFK--AGDA----FVEAvntwHRGRNGGDEPVE 90


                ....*
1J58_A      331 FLEIF 335
Cdd:cd02236  91 LLVFY 95
cupin_DAD_ChrR cd02237
2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR, and similar proteins; ...
 68-156 2.40e-03

2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR, and similar proteins; cupin domain; This family includes the proteins 2,4'-Dihydroxyacetophenone dioxygenase (DAD) and anti-sigma factor ChrR. DAD catalyzes the oxidation of 2,4'-dihydroxyacetophenone to 4-hydroxybenzoate and formate as part of the 4-hydroxyacetophenone catabolic pathway. The enzyme is a homotetramer containing one iron per molecule of enzyme. Anti-sigma factor ChrR is a member of the ZAS (Zn2+ anti-sigma) subfamily of group IV anti-sigmas. It inhibits transcriptional activity by binding to the Rsp extra cytoplasmic function (ECF) sigma factor E (sigmaE). Some ChrR members contain tandem repeats of two distinct homologous functional domains. Members of this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380365 [Multi-domain]  Cd Length: 82  Bit Score: 36.60  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A       68 VTVRELPIS--ENLASVN*RLKPGAIRELHWHKEAEWAY*IYGSarvtIVDEKGRsfiddVGEGDLWYFPSGLPHSIQAL 145
Cdd:cd02237   1 VEQRPLLIDpnTGLITAILRMAPGARLPDHEHVGGEEFYVLDGA----LTDEDGT-----AGAGDFVREPPGSRHSAVAP 71

                        90
                ....*....|.
1J58_A      146 EEGAEFLLVFD 156
Cdd:cd02237  72 REGCLILVILQ 82
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 265-329 2.41e-03

Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to MAE_RS03005, a Microcystis aeruginosa protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380392 [Multi-domain]  Cd Length: 122  Bit Score: 37.63  E-value: 2.41e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1J58_A      265 EPGA*RELHWHPNTHEWQYYISGKAR*TVfasDGHarTFNYQAGDVGYVPFA*GHYVENIGDEPL 329
Cdd:cd06987  36 DPGGRTPPNTHPAAHEMFFVLAGEGRAYC---DGQ--RVPLRPGDALVVPPGSEHVIENTGSGRL 95
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 88-143 3.03e-03

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 38.36  E-value: 3.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
1J58_A        88 PGAIRELHWHKEAEWAY*IYGSARVTIVDEKGRSFIDdVGEGDLWYFPSGLPHSIQ 143
Cdd:PRK13264  43 PNARTDFHYDPGEEFFYQLEGDMYLKVQEDGKRRDVP-IREGEMFLLPPHVPHSPQ 97
cupin_yp_001338853-like cd07008
Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes ...
 232-334 3.92e-03

Klebsiella pneumoniae yp_001338853.1 and related proteins, cupin domain; This family includes bacterial proteins homologous to Klebsiella pneumoniae yp_001338853.1, an uncharacterized conserved protein with double-stranded beta-helix domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380411 [Multi-domain]  Cd Length: 101  Bit Score: 36.46  E-value: 3.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      232 EQEPIESEggkVYIADSTnfkvsktiASALVTVEPGA*RELHWHPN-THEWqYYISGKAr*TVFASDGHARTFNyqAGDV 310
Cdd:cd07008  13 DEEPIRSV---ITETDDS--------AIVVWHVKPGQEIAAHIHPHgQDTW-IVLSGEG--EYLLGDGQTVPIK--AGDI 76

                        90       100
                ....*....|....*....|....
1J58_A      311 GYVPFA*GHYVENIGDEPLVFLEI 334
Cdd:cd07008  77 VIAPAGQVHGARNTGDEPLVFVSV 100
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 108-154 4.34e-03

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 35.95  E-value: 4.34e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
1J58_A      108 GSARVTIVDEKGRsfiddVGEGDLWYFPSGLPHSIQALEEgAEFLLV 154
Cdd:cd02230  40 GEAEFTIGGETVT-----LKAGELIVMPANVPHALKAEED-FKMLLT 80
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 226-335 4.35e-03

Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3.4) catalyzes the manganese-dependent oxidative decarboxylation of oxalate to carbon dioxide and hydrogen peroxide (H2O2). It is widespread in fungi and various plant tissues and may play a role in plant signaling and defense. This enzyme has been employed in a widely used assay for detecting urinary oxalate levels. Also, the gene encoding OxOx from barley roots has been expressed in oilseed rape in order to provide a defense against externally supplied oxalic acid. In germin, the predominant protein produced during the early phase of wheat germination, it is believed that H2O2 production is employed as a defense mechanism in response to infection by pathogens. Germin is also a marker of growth onset in cell walls in germinating cereals. The H2O2 produced by OxOx, together with the Ca2+ released by degradation of calcium oxalate, are thought to mediate cell wall cross-linking at high concentrations. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380368  Cd Length: 191  Bit Score: 37.96  E-value: 4.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1J58_A      226 FTYRLLEQEPIES--EGGKVYIADSTNFKVSKT--IASALVTVEPGA*RELHWHPNTHEWQYYISGkar*TVFA----SD 297
Cdd:cd02241  35 FVFDFLNPPGNTSnpLGGSVTLANVANFPALNGlgISMARGDLAPCGVNPPHTHPRATELLYVVEG----TLYVgfvdEN 110

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1J58_A      298 GhARTFN--YQAGDVgyVPFA*G--HYVENIGDEPLVFLEIF 335
Cdd:cd02241 111 G-NRLFTktLNPGDV--FVFPQGliHFQFNPGCEPAVFVAAF 149
MannoseP_isomer pfam01050
Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the ...
 262-334 6.57e-03

Mannose-6-phosphate isomerase; All of the members of this Pfam entry belong to family 2 of the mannose-6-phosphate isomerases. The type II phosphomannose isomerases are bifunctional enzymes. This Pfam entry covers the isomerase domain. The guanosine diphospho-D-mannose pyrophosphorylase domain is in another Pfam entry, see pfam00483.


Pssm-ID: 426015 [Multi-domain]  Cd Length: 151  Bit Score: 37.01  E-value: 6.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1J58_A        262 VTVEPGA*RELHWHPNTHEWQYYISGKAR*TVfasdgHARTFNYQAGDVGYVPFA*GHYVENIGDEPLVFLEI 334
Cdd:pfam01050  68 ITVKPGARLSLQMHHHRAEHWIVVSGTARVTK-----GGETFLLTENESTYIPLGTIHRLENPGKIPLELIEV 135
 
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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