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Conserved domains on  [gi|2055752556|ref|WP_216631457|]
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oxalate decarboxylase family bicupin [Bacillus amyloliquefaciens]

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 ...
 12-378 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: 650.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  12 GRKGATDEGPRNLPRDFQNPDMLVPPSTDAGTVQNLKFSFSDTHMRLEDGGWSREVTVRELPVSKNIAAVNMRLKPGAVR 91
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  92 ELHWHKEAEWGYVINGGVRLTAVDQNGRNFIDNVSEGDLWYFPSGIPHSIQGLEQGSEFLLVFDDGSFSENSTFSVTDWF 171
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLDEGCEFLLVFDDGNFSEDGTFLVTDWL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 172 AHTPRSVLEANFGVPGYELAYIHKKERYMFQLEPPPPIEQAAVSSPEGTVLEPFSYKLSRQEPLVTSGGRVKIVDSKTFK 251
Cdd:TIGR03404 161 AHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEVPGPFTYHLSEQKPKQVPGGTVRIADSTNFP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 252 VSKTIAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEGRARTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFL 331
Cdd:TIGR03404 241 VSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2055752556 332 EIFKSDRFEDVSLNQWLALTPQRFVEQTLNVSPAFARRLKKKKSPVV 378
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 ...
 12-378 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: 650.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  12 GRKGATDEGPRNLPRDFQNPDMLVPPSTDAGTVQNLKFSFSDTHMRLEDGGWSREVTVRELPVSKNIAAVNMRLKPGAVR 91
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  92 ELHWHKEAEWGYVINGGVRLTAVDQNGRNFIDNVSEGDLWYFPSGIPHSIQGLEQGSEFLLVFDDGSFSENSTFSVTDWF 171
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLDEGCEFLLVFDDGNFSEDGTFLVTDWL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 172 AHTPRSVLEANFGVPGYELAYIHKKERYMFQLEPPPPIEQAAVSSPEGTVLEPFSYKLSRQEPLVTSGGRVKIVDSKTFK 251
Cdd:TIGR03404 161 AHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEVPGPFTYHLSEQKPKQVPGGTVRIADSTNFP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 252 VSKTIAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEGRARTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFL 331
Cdd:TIGR03404 241 VSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2055752556 332 EIFKSDRFEDVSLNQWLALTPQRFVEQTLNVSPAFARRLKKKKSPVV 378
Cdd:TIGR03404 321 EVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 48-201 2.05e-97

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: 286.43  E-value: 2.05e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  48 KFSFSDTHMRLEDGGWSREVTVRELPVSKNIAAVNMRLKPGAVRELHWHKEAEWGYVINGGVRLTAVDQNGRNFIDNVSE 127
Cdd:cd20304     1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWHAAAEWAYVLSGRCRITAVDPEGRSFIDDVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055752556 128 GDLWYFPSGIPHSIQGLEQ-GSEFLLVFDDGSFSENSTFSVTDWFAHTPRSVLEANFGVPGYELAYIHKKERYMF 201
Cdd:cd20304    81 GDLWYFPRGHPHSIQGLGPdGCEFLLVFDDGNFSEFGTFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKKELYIF 155
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 255-352 2.98e-43

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: 146.26  E-value: 2.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 255 TIAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEGRARTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIF 334
Cdd:COG2140     2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81

                          90       100
                  ....*....|....*....|.
gi 2055752556 335 KSDRFED---VSLNQWLALTP 352
Cdd:COG2140    82 DDDAGSDygtISLSGWLAHTP 102
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 230-368 1.91e-31

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: 116.23  E-value: 1.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  230 SRQEPLVTS-GGRVKIVDSKTFKVSKT--IAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEG-RARTFNYQ 305
Cdd:smart00835   1 LEPRPDFSNeGGRLREADPTNFPALNGlgISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGnKVYDARLR 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055752556  306 AGDVGYVPFAMGHYVQNTGDTVLRFLEIFKSD---RFEDVSLNQWLALTPQRFVEQTLNVSPAFAR 368
Cdd:smart00835  81 EGDVFVVPQGHPHFQVNSGDENLEFVAFNTNDpnrRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 227-368 2.76e-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: 94.71  E-value: 2.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 227 YKLSRQEPLVTS-GGRVKIVDSKTFKVSKT--IAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKM-TVFAAEG-RART 301
Cdd:pfam00190   1 LNLLEPGPTYNPeGGRVTTVNSKNLPGLNTlgISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGnRVFH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055752556 302 FNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIFKSDRFEDVS----LNQWLALTPQRFVEQTLNVSPAFAR 368
Cdd:pfam00190  81 KVLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSilagGFSSLPALPPEVLAKAFQLAGEEVK 151
PRK04190 PRK04190
glucose-6-phosphate isomerase; Provisional
 272-337 3.82e-06

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179774  Cd Length: 191  Bit Score: 46.95  E-value: 3.82e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055752556 272 HWHPNTDEWQYY--LSGEAKMTVFAAEGRARTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIFKSD 337
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 ...
 12-378 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: 650.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  12 GRKGATDEGPRNLPRDFQNPDMLVPPSTDAGTVQNLKFSFSDTHMRLEDGGWSREVTVRELPVSKNIAAVNMRLKPGAVR 91
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  92 ELHWHKEAEWGYVINGGVRLTAVDQNGRNFIDNVSEGDLWYFPSGIPHSIQGLEQGSEFLLVFDDGSFSENSTFSVTDWF 171
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGLDEGCEFLLVFDDGNFSEDGTFLVTDWL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 172 AHTPRSVLEANFGVPGYELAYIHKKERYMFQLEPPPPIEQAAVSSPEGTVLEPFSYKLSRQEPLVTSGGRVKIVDSKTFK 251
Cdd:TIGR03404 161 AHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGEVPGPFTYHLSEQKPKQVPGGTVRIADSTNFP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 252 VSKTIAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEGRARTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFL 331
Cdd:TIGR03404 241 VSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDETLVFL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2055752556 332 EIFKSDRFEDVSLNQWLALTPQRFVEQTLNVSPAFARRLKKKKSPVV 378
Cdd:TIGR03404 321 EVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 48-201 2.05e-97

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: 286.43  E-value: 2.05e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  48 KFSFSDTHMRLEDGGWSREVTVRELPVSKNIAAVNMRLKPGAVRELHWHKEAEWGYVINGGVRLTAVDQNGRNFIDNVSE 127
Cdd:cd20304     1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWHAAAEWAYVLSGRCRITAVDPEGRSFIDDVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055752556 128 GDLWYFPSGIPHSIQGLEQ-GSEFLLVFDDGSFSENSTFSVTDWFAHTPRSVLEANFGVPGYELAYIHKKERYMF 201
Cdd:cd20304    81 GDLWYFPRGHPHSIQGLGPdGCEFLLVFDDGNFSEFGTFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKKELYIF 155
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 224-375 2.56e-97

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: 286.40  E-value: 2.56e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 224 PFSYKLSRQEPLVTS-GGRVKIVDSKTFKVSKTIAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEGRARTF 302
Cdd:cd20305     1 PHTFRLLAQPPIKVPaGGSVRIVDSKNFPISTTIAAALVTLEPGALRELHWHPNADEWQYYISGKARMTVFASGGRARTF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055752556 303 NYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIFKSDRFEDVSLNQWLALTPQRFVEQTLNVSPAFARRLKKKKS 375
Cdd:cd20305    81 DFQAGDVGYVPRGYGHYIENTGDEPLEFLEVFNSGRYQDISLSQWLALTPPDLVAAHLGLPDDTIAKLPKKKQ 153
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 232-374 3.61e-55

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: 178.44  E-value: 3.61e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 232 QEPLVTS-GGRVKIVDSKTFKVSKTIAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEGRARTFNYQAGDVG 310
Cdd:cd02240     2 SEPIEENaGGSVRIATVTNFPISKDLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRFETFNLGAGDVG 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055752556 311 YVPFAMGHYVQNTGDTVLRFLEIFKSDRFEDVSLNQWLALTPQRFVEQTLNVSPAFARRLKKKK 374
Cdd:cd02240    82 YVPSGSGHHIENIGDEDAEFLLIFDDGTFADVSLPWWLAMTPEEVLAATLDLGKFIDALPKAKH 145
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 53-185 7.57e-50

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: 164.57  E-value: 7.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  53 DTHMRLE-DGGWSREVTVRELPVSKNIAAVNMRLKPGAVRELHWHK-EAEWGYVINGGVRLTAVDQNGRNFIDNVSEGDL 130
Cdd:cd02240     1 DSEPIEEnAGGSVRIATVTNFPISKDLSSALVRVAPGAMRELHWHPnTAEWQYVISGSARVTVFDEDGRFETFNLGAGDV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2055752556 131 WYFPSGIPHSIQGL-EQGSEFLLVFDDGSFsenSTFSVTDWFAHTPRSVLEANFGV 185
Cdd:cd02240    81 GYVPSGSGHHIENIgDEDAEFLLIFDDGTF---ADVSLPWWLAMTPEEVLAATLDL 133
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 255-352 2.98e-43

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: 146.26  E-value: 2.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 255 TIAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEGRARTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIF 334
Cdd:COG2140     2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81

                          90       100
                  ....*....|....*....|.
gi 2055752556 335 KSDRFED---VSLNQWLALTP 352
Cdd:COG2140    82 DDDAGSDygtISLSGWLAHTP 102
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 77-180 4.70e-34

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: 122.38  E-value: 4.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  77 NIAAVNMRLKPGAVRELHWH-KEAEWGYVINGGVRLTAVDQNGRNFIDNVSEGDLWYFPSGIPHSIQGL-EQGSEFLLVF 154
Cdd:COG2140     2 TLAGGLTVLEPGGVREEHWHpNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTgDEPLVFLAVF 81

                          90       100
                  ....*....|....*....|....*.
gi 2055752556 155 DDGSFSENSTFSVTDWFAHTPRSVLE 180
Cdd:COG2140    82 DDDAGSDYGTISLSGWLAHTPPEVLA 107
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 230-368 1.91e-31

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: 116.23  E-value: 1.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  230 SRQEPLVTS-GGRVKIVDSKTFKVSKT--IAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEG-RARTFNYQ 305
Cdd:smart00835   1 LEPRPDFSNeGGRLREADPTNFPALNGlgISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPNGnKVYDARLR 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055752556  306 AGDVGYVPFAMGHYVQNTGDTVLRFLEIFKSD---RFEDVSLNQWLALTPQRFVEQTLNVSPAFAR 368
Cdd:smart00835  81 EGDVFVVPQGHPHFQVNSGDENLEFVAFNTNDpnrRFFLAGRNSVLRGLPPEVLAAAFGVSAEEVR 146
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 224-367 3.41e-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: 113.07  E-value: 3.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 224 PFSYKLSRQEPLV-TSGGRVKIVDSKTFKVSKTIAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEGRARTF 302
Cdd:cd20306     1 PHLFSLEDSNPFFeSEGGSIRQATADQLPVLKGLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSLDTF 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055752556 303 NYQAGDVGYVPfaMG--HYVQNTGDTVLRFLEIFKSDRFEDVSLNQWLALTPQRFVEQTLNVSPAFA 367
Cdd:cd20306    81 TVKPGQVVFIP--QGwlHWIENVGDEEAHLLIFFNHETPEDIGLSDSLRATPPEVLGNTYGVDAFFA 145
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 227-373 1.22e-28

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: 109.24  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 227 YKLSRQEPLVTSGGRVKIVDSKTFKVSKTIAAALVEVEPGGMRELHWHpNTDEWQYYLSGEAKMTVFAAEGRARTFNYQA 306
Cdd:cd20304     2 FSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWH-AAAEWAYVLSGRCRITAVDPEGRSFIDDVGP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 307 GDVGYVPFAMGHYVQNTGDTVLRFLEIFKSDRFED---VSLNQWLALTPQRFVEQTLNVSPAFARRLKKK 373
Cdd:cd20304    81 GDLWYFPRGHPHSIQGLGPDGCEFLLVFDDGNFSEfgtFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKK 150
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 48-196 1.63e-24

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: 98.05  E-value: 1.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  48 KFSFSDTHMRLE-DGGWSREVTVRELPVSKNIAAVNMRLKPGAVRELHWHKEA-EWGYVINGGVRLTAVDQNGR--NFId 123
Cdd:cd20306     3 LFSLEDSNPFFEsEGGSIRQATADQLPVLKGLSIYRLRLSPGGIREPHWHPNAnELGYVISGEARVSILDPTGSldTFT- 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055752556 124 nVSEGDLWYFPSGIPHSIQGL-EQGSEFLLVFDDGSFsenSTFSVTDWFAHTPRSVLEANFGVPGYELAYIHKK 196
Cdd:cd20306    82 -VKPGQVVFIPQGWLHWIENVgDEEAHLLIFFNHETP---EDIGLSDSLRATPPEVLGNTYGVDAFFAAPAFPT 151
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 60-190 1.77e-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: 214845 [Multi-domain]  Cd Length: 146  Bit Score: 95.04  E-value: 1.77e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556   60 DGGWSREVTVRELPVSK--NIAAVNMRLKPGAVRELHWHKEA-EWGYVINGGVRLTAVDQNG-RNFIDNVSEGDLWYFPS 135
Cdd:smart00835  10 EGGRLREADPTNFPALNglGISAARVNLEPGGMLPPHYHPRAtELLYVVRGEGRVGVVDPNGnKVYDARLREGDVFVVPQ 89

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2055752556  136 GIPHSIQGLEQGSEFLLVFDDGSFSENSTFS-VTDWFAHTPRSVLEANFGVPGYEL 190
Cdd:smart00835  90 GHPHFQVNSGDENLEFVAFNTNDPNRRFFLAgRNSVLRGLPPEVLAAAFGVSAEEV 145
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 227-368 2.76e-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: 94.71  E-value: 2.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 227 YKLSRQEPLVTS-GGRVKIVDSKTFKVSKT--IAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKM-TVFAAEG-RART 301
Cdd:pfam00190   1 LNLLEPGPTYNPeGGRVTTVNSKNLPGLNTlgISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVgFVVPGNGnRVFH 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2055752556 302 FNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIFKSDRFEDVS----LNQWLALTPQRFVEQTLNVSPAFAR 368
Cdd:pfam00190  81 KVLREGDVFVVPQGLPHFQYNIGDEPAVAFVAFDTNNPGNQSilagGFSSLPALPPEVLAKAFQLAGEEVK 151
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 60-185 6.31e-21

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: 88.16  E-value: 6.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  60 DGGWSREVTVRELPVSK--NIAAVNMRLKPGAVRELHWHKEA-EWGYVINGGVRLTAVDQNG--RNFIDNVSEGDLWYFP 134
Cdd:pfam00190  13 EGGRVTTVNSKNLPGLNtlGISAARVDLAPGGMNPPHWHPNAtEILYVLQGRGRVGFVVPGNgnRVFHKVLREGDVFVVP 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2055752556 135 SGIPHSIQ--GLEQGSEFLLVFDDGSFSENSTFSVTDWFAHTPRSVLEANFGV 185
Cdd:pfam00190  93 QGLPHFQYniGDEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQL 145
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 258-334 1.66e-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: 62.11  E-value: 1.66e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055752556 258 AALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEgrarTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIF 334
Cdd:cd02208     1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGE----TVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 259-334 2.41e-12

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: 61.89  E-value: 2.41e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2055752556 259 ALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVfaaEGRARTfnYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIF 334
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTV---DGEEVV--LKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 259-333 7.35e-12

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: 61.38  E-value: 7.35e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2055752556 259 ALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVfaaEGRARTFnyQAGDVGYVPFAMGHYVQNTGDTVLRFLEI 333
Cdd:cd02214    22 AHARVPPGESTLPHRLKGSEEVYYILEGEGTMEI---DGEPREV--GPGDAVLIPPGAVQRIENTGEEDLVFLCI 91
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
251-334 2.89e-11

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 60.16  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 251 KVSKTIAAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVfaaegRARTFNYQAGDVGYVPFAMGHYVQNTGDTVLRF 330
Cdd:COG0662    22 EGGERLSVKRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTI-----GDEEVELKAGDSVYIPAGVPHRLRNPGDEPLEL 96


                  ....
gi 2055752556 331 LEIF 334
Cdd:COG0662    97 LEVQ 100
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
56-154 4.11e-09

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 53.31  E-value: 4.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  56 MRLEDGGWSREVTVRELPVSKNIAAVNMRLKPGAVRELHWHKEAEWGYVINGGVRLTAvdqNGRNFIdnVSEGDLWYFPS 135
Cdd:COG1917     1 MRLAEIALTGVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEV---GGEEYE--LKPGDVVFIPP 75

                          90
                  ....*....|....*....
gi 2055752556 136 GIPHSIQGLEQGSEFLLVF 154
Cdd:COG1917    76 GVPHAFRNLGDEPAVLLVV 94
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 83-139 3.75e-08

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: 49.95  E-value: 3.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2055752556  83 MRLKPGAVRELHWHK-EAEWGYVINGGVRLTavdQNGRNFIdnVSEGDLWYFPSGIPH 139
Cdd:pfam07883   3 VTLPPGESSPPHRHPgEDEFFYVLEGEGELT---VDGEEVV--LKAGDSVYFPAGVPH 55
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 83-154 4.02e-08

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: 49.79  E-value: 4.02e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055752556  83 MRLKPGAVRELHWHKEA-EWGYVINGGVRLTAVDQNGRNfidnVSEGDLWYFPSGIPHSIQGLE-QGSEFLLVF 154
Cdd:cd02208     4 VTLPPGTSSPPHWHPEQdEIFYVLSGEGELTLDDGETVE----LKAGDIVLIPPGVPHSFVNTSdEPAVFLVVS 73
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
254-333 1.05e-07

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 50.02  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 254 KTIAAALVEVEPGGM-RELHWHPNTDEWQYYLSGEAKMTVFAAEGRARtfnyqAGDVGYVPFAMGHYVQNTGDTVLRFLE 332
Cdd:COG3837    26 TRLGVNLITLPPGASsSPYHAHSAEEEFVYVLEGELTLRIGGEEYVLE-----PGDSVGFPAGVPHRLRNRGDEPARYLV 100


                  .
gi 2055752556 333 I 333
Cdd:COG3837   101 V 101
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
58-141 2.12e-07

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 48.98  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  58 LEDGGWSREVTVRElpVSKNIAAVNMRLKPGAVRELHWH-KEAEWGYVINGGVRLTavdQNGRNFIdnVSEGDLWYFPSG 136
Cdd:COG0662     9 LKAIGWGSYEVLGE--GGERLSVKRITVPPGAELSLHVHpHRDEFFYVLEGTGEVT---IGDEEVE--LKAGDSVYIPAG 81


                  ....*
gi 2055752556 137 IPHSI 141
Cdd:COG0662    82 VPHRL 86
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 239-337 2.30e-07

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: 50.67  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 239 GGRVKIVDSKTFKVSKT--IAAALVEVEPGGMRELHWHPNTDEWQYYLSGEakMTV-FAAEGRARTFN--YQAGDVGYVP 313
Cdd:cd02241    51 GGSVTLANVANFPALNGlgISMARGDLAPCGVNPPHTHPRATELLYVVEGT--LYVgFVDENGNRLFTktLNPGDVFVFP 128

                          90       100
                  ....*....|....*....|....
gi 2055752556 314 FAMGHYVQNTGDTVLRFLEIFKSD 337
Cdd:cd02241   129 QGLIHFQFNPGCEPAVFVAAFNSE 152
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 254-333 6.43e-07

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: 47.48  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 254 KTIAAALVEVEPGGMR-ELHWHPNTDEWQYYLSGEAKMTVfaaEGRARTFnyQAGDvgYVPF----AMGHYVQNTGDTVL 328
Cdd:cd02224    15 TQLGVNLERLPPGARSsPRHWHSAEEEFVYVLSGEGTLRL---DGEEVLP--RPGD--FVGFpagtGVAHQLINRSDEPL 87


                  ....*
gi 2055752556 329 RFLEI 333
Cdd:cd02224    88 VYLVV 92
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 67-154 1.23e-06

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: 46.69  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  67 VTVRELPVSKNIAAVNMRLKPGAVRELHWHKEAEWGYVINGGVRLTAvdqNGRNFIdnVSEGDLWYFPSGIPHSIQGLEq 146
Cdd:cd02238    16 VRRKILAGGEKLMLVEVRFEKGAVVPLHSHPHEQIGYVLSGRFEFTI---GGETRI--LKPGDSYYIPPNVPHGAEALE- 89


                  ....*...
gi 2055752556 147 GSEFLLVF 154
Cdd:cd02238    90 DSVLLDVF 97
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
256-334 1.57e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 46.00  E-value: 1.57e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055752556 256 IAAALVEVEPGGMRELHWHPnTDEWQYYLSGEAKMTVfaaEGraRTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIF 334
Cdd:COG1917    23 LEVVRVTFEPGARTPWHSHP-GEELIYVLEGEGEVEV---GG--EEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 260-331 2.08e-06

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: 45.52  E-value: 2.08e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055752556 260 LVEVEPGGMRELHWHPNTDEwQYYLSGEAKMTVfaaEGRARTFnyQAGDVGYVPFAMGHYVQNTGDTVLRFL 331
Cdd:cd02222    21 YFEIEPGGHTPLHTHPWEHE-VYVLRGKGVVVI---GGEEYPV--KPGDVVYIPPNEPHQFRNTGDEPLGFL 86
PRK04190 PRK04190
glucose-6-phosphate isomerase; Provisional
 272-337 3.82e-06

glucose-6-phosphate isomerase; Provisional


Pssm-ID: 179774  Cd Length: 191  Bit Score: 46.95  E-value: 3.82e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055752556 272 HWHPNTDEWQYY--LSGEAKMTVFAAEGRARTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIFKSD 337
Cdd:PRK04190   90 HFHAKADRAEIYygLKGKGLMLLQDPEGEARWIEMEPGTVVYVPPYWAHRSVNTGDEPLVFLACYPAD 157
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 236-373 4.22e-06

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: 46.31  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 236 VTSGGRVKIVDSKTFKVSKTI--AAALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVFAAEGRaRTFN--YQAGDVGY 311
Cdd:cd02243     4 VPRGGRITTLNSFKLPILRFVglSAERVKLEPNAMFAPHWNANAHQVIYVTRGSGRVQVVGDNGK-RVLDgeVREGQLLV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2055752556 312 VP--FAMghyVQNTGDTVLRFLEIFKSDR--FEDVSLNQ--WLALTPQrFVEQTLNVSPAFARRLKKK 373
Cdd:cd02243    83 VPqfFAV---AKIAGEEGFEWVSFKTSDNpiFSELAGRTsvLRALPPE-VLANSYNISPEEAKQLKSN 146
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 240-333 1.79e-05

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: 43.70  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 240 GRVKIVD-SKTFKVSKtiaaalVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVfaaegRARTFNYQAGDVGYVPFAMGH 318
Cdd:cd02213    29 GSYEVLDeGEGYKVKR------LTVNPGKRLSLQRHHHRSEHWVVVSGTAEVTL-----DGKEKLLKEGESIYIPKGTKH 97

                          90
                  ....*....|....*
gi 2055752556 319 YVQNTGDTVLRFLEI 333
Cdd:cd02213    98 RLENPGKIPLEIIEV 112
cupin_PGI cd02218
cupin-type phosphoglucose isomerase; The cupin-type phosphoglucose isomerase (also called ...
 272-337 1.79e-05

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: 44.47  E-value: 1.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2055752556 272 HWHPNTDEWQYY--LSGEAKM-TVFAAEGRARTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEIFKSD 337
Cdd:cd02218    67 HYHAKRDYPEVYevLSGEGLLlLQKEDVGEVILVEAKPGDKVYIPPGYAHRTINTGDEPLVFANWWPSD 135
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 60-185 2.73e-05

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: 44.00  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  60 DGGWSREVTVRELPVSKNI--AAVNMRLKPGAVRELHWHKEA-EWGYVINGGVRLTAVDQNGRN-FIDNVSEGDLWYFPS 135
Cdd:cd02243     6 RGGRITTLNSFKLPILRFVglSAERVKLEPNAMFAPHWNANAhQVIYVTRGSGRVQVVGDNGKRvLDGEVREGQLLVVPQ 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2055752556 136 GIPHSIQGLEQGSEFLlvfddgSF--SENSTFSV----TDWFAHTPRSVLEANFGV 185
Cdd:cd02243    86 FFAVAKIAGEEGFEWV------SFktSDNPIFSElagrTSVLRALPPEVLANSYNI 135
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 87-142 7.83e-05

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 42.04  E-value: 7.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2055752556  87 PGAVRELHWHKEAEWGYVINGGVRLTAvdqNGRNFidNVSEGDLWYFPSGIPHSIQ 142
Cdd:pfam02311  12 PGHSFPPHVHDFYVIGYIERGVGRFRL---NGRTY--HLGPGDLFLLPPGEPHDYE 62
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
76-141 1.19e-04

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 41.16  E-value: 1.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2055752556  76 KNIAAVNMRLKPGA-VRELHWH-KEAEWGYVINGGVRLTavdqngrnfIDN----VSEGDLWYFPSGIPHSI 141
Cdd:COG3837    26 TRLGVNLITLPPGAsSSPYHAHsAEEEFVYVLEGELTLR---------IGGeeyvLEPGDSVGFPAGVPHRL 88
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 258-334 1.52e-04

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: 39.91  E-value: 1.52e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2055752556 258 AALVEVEPGGMRELHWHpNTDEWQYYLSGEAKMTVfaaEGRARTFnyQAGDVGYVPFAMGHYVQNTGDTVLRFLEIF 334
Cdd:cd06988     4 GAWCVVRPGTTSTPHSH-HEYEIFIVISGKGIVVV---DGEREPV--KAGDVVYIPPGTEHYVKNDGDEDFEFYSIW 74
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 259-331 1.58e-04

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: 40.14  E-value: 1.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055752556 259 ALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVfaaEGRARTFNyqAGDVGYVPFAMGHYVQNTGDTVLRFL 331
Cdd:cd02221    22 ARVTLPPGSSIGYHQHEGEFEIYYILSGEGLYTD---NGKEYEVK--AGDVTFTRDGESHGIENTGDEDLVFI 89
cupin_BacB cd06975
Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as ...
 87-140 2.06e-04

Bacillus subtilis bacilysin and related proteins, cupin domain; Bacilysin (BacB, also known as AerE in Microcystis aeruginosa) is a non-ribosomally synthesized dipeptide antibiotic that is produced and excreted by certain strains of Bacillus subtilis. It is an oxidase that catalyzes the synthesis of 2-oxo-3-(4-oxocyclohexa-2,5-dienyl)propanoic acid, a precursor to L-anticapsin. Each bacilysin monomer has two tandem cupin domains. It is active against a wide range of bacteria and some fungi. The antimicrobial activity of bacilysin is antagonized by glucosamine and N-acetyl glucosamine, indicating that bacilysin interferes with glucosamine synthesis, and thus, with the synthesis of microbial cell walls. AerE is thought to be involved in the formation of the 2-carboxy-6-hydroxyoctahydroindole (Choi) moiety found on all aeruginosin tetrapeptides, based on gene knock-out experiments. It is encoded by the aerE gene of the aerABCDEF aeruginosin biosynthesis gene cluster in Microcystis aeruginosa.


Pssm-ID: 380380 [Multi-domain]  Cd Length: 93  Bit Score: 39.87  E-value: 2.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2055752556  87 PGAVRELHWHKEAEWGYVINGGVRLTaVDQNGRNFIDnvsEGDLWYFPSGIPHS 140
Cdd:cd06975    28 PGAKMPLHQHREEQIGMILNGELEMT-VGGEEQELEP---LGDVYYAPPNVPHG 77
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 261-328 3.95e-04

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: 39.94  E-value: 3.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2055752556 261 VEV-EPGGMRELHWHPNTDEWQYYLSGeakmtvfaaEGRAR----TFNYQAGDVGYVPFAMGHYVQNTGDTVL 328
Cdd:cd06987    32 VEIfDPGGRTPPNTHPAAHEMFFVLAG---------EGRAYcdgqRVPLRPGDALVVPPGSEHVIENTGSGRL 95
cupin_BLL4011-like cd02235
Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes ...
 259-331 1.02e-03

Bradyrhizobium diazoefficiens BLL4011 and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to BLL4011, a Bradyrhizobium diazoefficiens 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: 380363 [Multi-domain]  Cd Length: 100  Bit Score: 37.94  E-value: 1.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2055752556 259 ALVEVEPGGMRELHWHPNtDEWQYYLSGEAKMTVfaaEGRA-RTFNyqAGDVGYVPFAMGHYVQNTGDTVLRFL 331
Cdd:cd02235    22 VRVEIPPGAVAGRHTHPG-EESGYVLEGSLELEV---DGQPpVTLK--AGDSFFIPAGTVHNAKNVGSGPAKLL 89
cupin_CV2614-like cd02236
Chromobacterium violaceum CV2614 and related proteins, cupin domain; This family includes ...
 256-334 1.09e-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: 38.24  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 256 IAAALVEVEPGGMRELHWH--PNtdeWQYYLSGEakMTVFAAEGRARTFNyqAGDVgyVPFAMG--HYVQNTGDTVLRFL 331
Cdd:cd02236    22 ITVLRITIPPGAELPWHTHpvPN---AGYVLSGE--LTVEYEDGKKRTFK--AGDA--FVEAVNtwHRGRNGGDEPVELL 92


                  ...
gi 2055752556 332 EIF 334
Cdd:cd02236    93 VFY 95
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 68-151 2.64e-03

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: 37.11  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556  68 TVRELPVSKNIAAVNM-----RLKPGAVRELHWHKEAEWGYVINGGvrltavdqNGRNFIDN----VSEGDLWYFPSGIP 138
Cdd:cd02214     4 LIRELLHPDNDGDPRYslahaRVPPGESTLPHRLKGSEEVYYILEG--------EGTMEIDGepreVGPGDAVLIPPGAV 75

                          90
                  ....*....|....
gi 2055752556 139 HSIQGLEQGS-EFL 151
Cdd:cd02214    76 QRIENTGEEDlVFL 89
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 239-326 4.00e-03

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: 36.50  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 239 GGRVKIVDSktfkvSKTIAA-----ALVEVEPGGMRELHWHPNTDEWQYYLSGEAKMTVfaaEGraRTFNYQAGDVGYVP 313
Cdd:cd06991     2 GGDLRILLS-----PKTVGAtsgfmGTLTLAPGERVSEHYHPYSEEFLYVVRGRLVVRV---DG--EPVVLEAGEALLVP 71

                          90
                  ....*....|...
gi 2055752556 314 FAMGHYVQNTGDT 326
Cdd:cd06991    72 RGVRHRLENAGDE 84
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
255-342 6.19e-03

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 37.88  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2055752556 255 TIAAALVEVEPGGMRELHWHPNTDE-WQYYLSGEAKMTVfaaEGRarTFNYQAGDVGYVPFAMGHYVQNTGDTVLRFLEI 333
Cdd:COG3257    58 TFSQYIVEVAPGGGSDRPEPDPGAEtFLFVLEGEVTLTL---GGE--THELTPGGYAYLPPGTPWTLRNAGDEPARFHWI 132


                  ....*....
gi 2055752556 334 FKsdRFEDV 342
Cdd:COG3257   133 RK--RYEPV 139
 
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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