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Conserved domains on  [gi|517077391|ref|WP_018266209|]
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cupin domain-containing protein [Methylosinus sp. LW4]

Protein Classification

cupin domain-containing protein( domain architecture ID 1562428)

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 32-402 0e+00

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.


The actual alignment was detected with superfamily member TIGR03404:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 367  Bit Score: 603.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391   32 NKASLTDPGPRSEAIGGQFPSAQFPPPTDVSDMPMFWASFNNAPKRVQNGGWARQVTQYDFAIAEEISGVDMRLTAGGIR 111
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  112 EMHWHLAAEWGYVSYGSCRITVLDDQGRAYVSDVKEGDIWYFPAGQPHSLQGLgPDGCEFLLCFDDGKATEYNTLLVTDW 191
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGL-DEGCEFLLVFDDGNFSEDGTFLVTDW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  192 IAHTPPEILAANFGLPAETFANIPLNQLYIFQGEVPGPLAADQASSAQGEgaPPYPYTFSLkGSAAAKKTKGGEVRVADS 271
Cdd:TIGR03404 160 LAHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGE--VPGPFTYHL-SEQKPKQVPGGTVRIADS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  272 DNFKVSSTIAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGPKAVTQDFHAGDIGYVKRAHGHYVQNVGDTE 351
Cdd:TIGR03404 237 TNFPVSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDET 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 517077391  352 LQFLEVFRAAHFRDVSLTDWLTHTPPAMVAQHLNIDEATIAKFPRGKPIVM 402
Cdd:TIGR03404 317 LVFLEVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
 
Name Accession Description Interval E-value
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 32-402 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: 603.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391   32 NKASLTDPGPRSEAIGGQFPSAQFPPPTDVSDMPMFWASFNNAPKRVQNGGWARQVTQYDFAIAEEISGVDMRLTAGGIR 111
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  112 EMHWHLAAEWGYVSYGSCRITVLDDQGRAYVSDVKEGDIWYFPAGQPHSLQGLgPDGCEFLLCFDDGKATEYNTLLVTDW 191
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGL-DEGCEFLLVFDDGNFSEDGTFLVTDW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  192 IAHTPPEILAANFGLPAETFANIPLNQLYIFQGEVPGPLAADQASSAQGEgaPPYPYTFSLkGSAAAKKTKGGEVRVADS 271
Cdd:TIGR03404 160 LAHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGE--VPGPFTYHL-SEQKPKQVPGGTVRIADS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  272 DNFKVSSTIAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGPKAVTQDFHAGDIGYVKRAHGHYVQNVGDTE 351
Cdd:TIGR03404 237 TNFPVSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDET 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 517077391  352 LQFLEVFRAAHFRDVSLTDWLTHTPPAMVAQHLNIDEATIAKFPRGKPIVM 402
Cdd:TIGR03404 317 LVFLEVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 68-222 6.02e-95

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: 281.04  E-value: 6.02e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  68 WASFNNAPKRVQNGGWARQVTQYDFAIAEEISGVDMRLTAGGIREMHWHLAAEWGYVSYGSCRITVLDDQGRAYVSDVKE 147
Cdd:cd20304    1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWHAAAEWAYVLSGRCRITAVDPEGRSFIDDVGP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517077391 148 GDIWYFPAGQPHSLQGLGPDGCEFLLCFDDGKATEYNTLLVTDWIAHTPPEILAANFGLPAETFANIPLNQLYIF 222
Cdd:cd20304   81 GDLWYFPRGHPHSIQGLGPDGCEFLLVFDDGNFSEFGTFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKKELYIF 155
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 279-393 6.68e-39

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: 135.48  E-value: 6.68e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 279 TIAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGPKAVTQDFHAGDIGYVKRAHGHYVQNVGDTELQFLEVF 358
Cdd:COG2140    2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 517077391 359 RAAHFRD---VSLTDWLTHTPPAMVAqhlnIDEATIAK 393
Cdd:COG2140   82 DDDAGSDygtISLSGWLAHTPPEVLA----VDNPRYDK 115
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 260-391 4.91e-27

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: 105.06  E-value: 4.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391   260 KTKGGEVRVADSDNFKVSST--IAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDA-GPKAVTQDFHAGDIGYV 336
Cdd:smart00835   8 SNEGGRLREADPTNFPALNGlgISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPnGNKVYDARLREGDVFVV 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 517077391   337 KRAHGHYVQNVGDTELQFLEVF---RAAHFRDVSLTDWLTHTPPAMVAQHLNIDEATI 391
Cdd:smart00835  88 PQGHPHFQVNSGDENLEFVAFNtndPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEV 145
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 260-391 1.76e-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: 90.09  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  260 KTKGGEVRVADSDNFKVSST--IAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGP--KAVTQDFHAGDIGY 335
Cdd:pfam00190  11 NPEGGRVTTVNSKNLPGLNTlgISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNgnRVFHKVLREGDVFV 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  336 VKRAHGHYVQNVGDTELQFLEVF----RAAHFRDVSLTDWLTHTPPAMVAQHLNIDEATI 391
Cdd:pfam00190  91 VPQGLPHFQYNIGDEPAVAFVAFdtnnPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEV 150
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 120-162 1.53e-03

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 39.13  E-value: 1.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 517077391 120 EWGYVSYGSCRITVLDDqGRAYVSDVKEGDIWYFPAGQPHSLQ 162
Cdd:PRK13264  56 EFFYQLEGDMYLKVQED-GKRRDVPIREGEMFLLPPHVPHSPQ 97
 
Name Accession Description Interval E-value
bicupin_oxalic TIGR03404
bicupin, oxalate decarboxylase family; Members of this protein family are defined as bicupins ...
 32-402 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: 603.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391   32 NKASLTDPGPRSEAIGGQFPSAQFPPPTDVSDMPMFWASFNNAPKRVQNGGWARQVTQYDFAIAEEISGVDMRLTAGGIR 111
Cdd:TIGR03404   1 GGLGATDPGPRNLARDKQNPDILAPPTTDHGSVPNLKWSFSDSHNRLENGGWAREVTVRDLPISTAIAGVNMRLEPGAIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  112 EMHWHLAAEWGYVSYGSCRITVLDDQGRAYVSDVKEGDIWYFPAGQPHSLQGLgPDGCEFLLCFDDGKATEYNTLLVTDW 191
Cdd:TIGR03404  81 ELHWHKEAEWAYVLYGSCRITAVDENGRNYIDDVGAGDLWYFPPGIPHSLQGL-DEGCEFLLVFDDGNFSEDGTFLVTDW 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  192 IAHTPPEILAANFGLPAETFANIPLNQLYIFQGEVPGPLAADQASSAQGEgaPPYPYTFSLkGSAAAKKTKGGEVRVADS 271
Cdd:TIGR03404 160 LAHTPKDVLAKNFGVPESAFDNLPLKELYIFPGTVPGPLDEEAVTGPAGE--VPGPFTYHL-SEQKPKQVPGGTVRIADS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  272 DNFKVSSTIAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGPKAVTQDFHAGDIGYVKRAHGHYVQNVGDTE 351
Cdd:TIGR03404 237 TNFPVSKTIAAAIVTVEPGAMRELHWHPNADEWQYFIQGQARMTVFAAGGNARTFDYQAGDVGYVPRNMGHYVENTGDET 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 517077391  352 LQFLEVFRAAHFRDVSLTDWLTHTPPAMVAQHLNIDEATIAKFPRGKPIVM 402
Cdd:TIGR03404 317 LVFLEVFKADRFADVSLNQWLALTPPQLVAAHLNLDDEVIDSLKKEKQPVV 367
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 68-222 6.02e-95

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: 281.04  E-value: 6.02e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  68 WASFNNAPKRVQNGGWARQVTQYDFAIAEEISGVDMRLTAGGIREMHWHLAAEWGYVSYGSCRITVLDDQGRAYVSDVKE 147
Cdd:cd20304    1 KFSFSDSHNRLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWHAAAEWAYVLSGRCRITAVDPEGRSFIDDVGP 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517077391 148 GDIWYFPAGQPHSLQGLGPDGCEFLLCFDDGKATEYNTLLVTDWIAHTPPEILAANFGLPAETFANIPLNQLYIF 222
Cdd:cd20304   81 GDLWYFPRGHPHSIQGLGPDGCEFLLVFDDGNFSEFGTFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKKELYIF 155
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 247-399 5.98e-89

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: 265.60  E-value: 5.98e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 247 PYTFSLKGSAAAKKTKGGEVRVADSDNFKVSSTIAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGPKAVTQ 326
Cdd:cd20305    1 PHTFRLLAQPPIKVPAGGSVRIVDSKNFPISTTIAAALVTLEPGALRELHWHPNADEWQYYISGKARMTVFASGGRARTF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517077391 327 DFHAGDIGYVKRAHGHYVQNVGDTELQFLEVFRAAHFRDVSLTDWLTHTPPAMVAQHLNIDEATIAKFPRGKP 399
Cdd:cd20305   81 DFQAGDVGYVPRGYGHYIENTGDEPLEFLEVFNSGRYQDISLSQWLALTPPDLVAAHLGLPDDTIAKLPKKKQ 153
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 261-392 4.55e-45

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: 152.63  E-value: 4.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 261 TKGGEVRVADSDNFKVSSTIAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGPKAVTQDFHAGDIGYVKRAH 340
Cdd:cd02240    8 NAGGSVRIATVTNFPISKDLSSALVRVAPGAMRELHWHPNTAEWQYVISGSARVTVFDEDGRFETFNLGAGDVGYVPSGS 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517077391 341 GHYVQNVGDTELQFLEVFRAAHFRDVSLTDWLTHTPPAMVAQHLNIDEATIA 392
Cdd:cd02240   88 GHHIENIGDEDAEFLLIFDDGTFADVSLPWWLAMTPEEVLAATLDLGKFIDA 139
cupin_OxDC cd02240
Oxalate decarboxylase (OxDC), cupin domain; Oxalate decarboxylase (OxDC; EC 4.1.1.2) is a ...
 81-212 8.86e-42

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: 144.16  E-value: 8.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  81 GGWARQVTQYDFAIAEEISGVDMRLTAGGIREMHWH-LAAEWGYVSYGSCRITVLDDQGRAYVSDVKEGDIWYFPAGQPH 159
Cdd:cd02240   10 GGSVRIATVTNFPISKDLSSALVRVAPGAMRELHWHpNTAEWQYVISGSARVTVFDEDGRFETFNLGAGDVGYVPSGSGH 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 517077391 160 SLQGLGPDGCEFLLCFDDGKateYNTLLVTDWIAHTPPEILAANFGLPAETFA 212
Cdd:cd02240   90 HIENIGDEDAEFLLIFDDGT---FADVSLPWWLAMTPEEVLAATLDLGKFIDA 139
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 279-393 6.68e-39

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: 135.48  E-value: 6.68e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 279 TIAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGPKAVTQDFHAGDIGYVKRAHGHYVQNVGDTELQFLEVF 358
Cdd:COG2140    2 TLAGGLTVLEPGGVREEHWHPNAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 517077391 359 RAAHFRD---VSLTDWLTHTPPAMVAqhlnIDEATIAK 393
Cdd:COG2140   82 DDDAGSDygtISLSGWLAHTPPEVLA----VDNPRYDK 115
cupin_OxDC_C cd20305
Oxalate decarboxylase (OxDC), C-terminal cupin domain; This model represents the C-terminal ...
 74-215 7.75e-39

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: 136.56  E-value: 7.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  74 APKRVQNGGWARQVTQYDFAIAEEISGVDMRLTAGGIREMHWH-LAAEWGYVSYGSCRITVLDDQGRAYVSDVKEGDIWY 152
Cdd:cd20305   10 PPIKVPAGGSVRIVDSKNFPISTTIAAALVTLEPGALRELHWHpNADEWQYYISGKARMTVFASGGRARTFDFQAGDVGY 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517077391 153 FPAGQPHSLQGLGPDGCEFLLCFDDGKateYNTLLVTDWIAHTPPEILAANFGLPAETFANIP 215
Cdd:cd20305   90 VPRGYGHYIENTGDEPLEFLEVFNSGR---YQDISLSQWLALTPPDLVAAHLGLPDDTIAKLP 149
OxdD COG2140
Oxalate decarboxylase/archaeal phosphoglucose isomerase, cupin superfamily [Carbohydrate ...
 97-201 4.30e-36

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: 128.16  E-value: 4.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  97 EISGVDMRLTAGGIREMHWHL-AAEWGYVSYGSCRITVLDDQGRAYVSDVKEGDIWYFPAGQPHSLQGLGPDGCEFLLCF 175
Cdd:COG2140    2 TLAGGLTVLEPGGVREEHWHPnAAEWYYVLSGEARMTVQDPPGRARTVDVGPGDVVYVPPGYGHYIINTGDEPLVFLAVF 81

                         90       100
                 ....*....|....*....|....*.
gi 517077391 176 DDGKATEYNTLLVTDWIAHTPPEILA 201
Cdd:COG2140   82 DDDAGSDYGTISLSGWLAHTPPEVLA 107
cupin_OxDC_N cd20304
Oxalate decarboxylase (OxDC), N-terminal cupin domain; This model represents the N-terminal ...
 249-397 9.92e-34

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: 123.10  E-value: 9.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 249 TFSLKGSAAaKKTKGGEVRVADSDNFKVSSTIAAALVTLAPGALREMHWHpNGDEWQYWIKGHGRMTLFDAGPKAVTQDF 328
Cdd:cd20304    1 KFSFSDSHN-RLESGGWAREVTVRDLPISTGIAGVNMRLEPGAIRELHWH-AAAEWAYVLSGRCRITAVDPEGRSFIDDV 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517077391 329 HAGDIGYVKRAHGHYVQNVGDTELQFLEVFRAAHFRD---VSLTDWLTHTPPAMVAQHLNIDEATIAKFPRG 397
Cdd:cd20304   79 GPGDLWYFPRGHPHSIQGLGPDGCEFLLVFDDGNFSEfgtFSITDWLAHTPKEVLAKNFGVPAEAFDNLPKK 150
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 247-396 5.00e-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: 5.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 247 PYTFSLKGSAAAKKTKGGEVRVADSDNFKVSSTIAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGPKAVTQ 326
Cdd:cd20306    1 PHLFSLEDSNPFFESEGGSIRQATADQLPVLKGLSIYRLRLSPGGIREPHWHPNANELGYVISGEARVSILDPTGSLDTF 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517077391 327 DFHAGDIGYVKRAHGHYVQNVGDTELQFLEVFRAAHFRDVSLTDWLTHTPPAMVAQHLNIDE-ATIAKFPR 396
Cdd:cd20306   81 TVKPGQVVFIPQGWLHWIENVGDEEAHLLIFFNHETPEDIGLSDSLRATPPEVLGNTYGVDAfFAAPAFPT 151
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 70-212 2.13e-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: 111.53  E-value: 2.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  70 SFNNAPKRVQN-GGWARQVTQYDFAIAEEISGVDMRLTAGGIREMHWH-LAAEWGYVSYGSCRITVLDDQGRAYVSDVKE 147
Cdd:cd20306    5 SLEDSNPFFESeGGSIRQATADQLPVLKGLSIYRLRLSPGGIREPHWHpNANELGYVISGEARVSILDPTGSLDTFTVKP 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517077391 148 GDIWYFPAGQPHSLQGLGPDGCEFLLCFDDGKAteyNTLLVTDWIAHTPPEILAANFGLPAETFA 212
Cdd:cd20306   85 GQVVFIPQGWLHWIENVGDEEAHLLIFFNHETP---EDIGLSDSLRATPPEVLGNTYGVDAFFAA 146
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 260-391 4.91e-27

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: 105.06  E-value: 4.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391   260 KTKGGEVRVADSDNFKVSST--IAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDA-GPKAVTQDFHAGDIGYV 336
Cdd:smart00835   8 SNEGGRLREADPTNFPALNGlgISAARVNLEPGGMLPPHYHPRATELLYVVRGEGRVGVVDPnGNKVYDARLREGDVFVV 87

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 517077391   337 KRAHGHYVQNVGDTELQFLEVF---RAAHFRDVSLTDWLTHTPPAMVAQHLNIDEATI 391
Cdd:smart00835  88 PQGHPHFQVNSGDENLEFVAFNtndPNRRFFLAGRNSVLRGLPPEVLAAAFGVSAEEV 145
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 260-391 1.76e-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: 90.09  E-value: 1.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  260 KTKGGEVRVADSDNFKVSST--IAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGP--KAVTQDFHAGDIGY 335
Cdd:pfam00190  11 NPEGGRVTTVNSKNLPGLNTlgISAARVDLAPGGMNPPHWHPNATEILYVLQGRGRVGFVVPGNgnRVFHKVLREGDVFV 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  336 VKRAHGHYVQNVGDTELQFLEVF----RAAHFRDVSLTDWLTHTPPAMVAQHLNIDEATI 391
Cdd:pfam00190  91 VPQGLPHFQYNIGDEPAVAFVAFdtnnPGNQSILAGGFSSLPALPPEVLAKAFQLAGEEV 150
Cupin_1 smart00835
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 80-211 1.04e-20

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: 87.72  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391    80 NGGWARQVTQYDFAIAE--EISGVDMRLTAGGIREMHWHL-AAEWGYVSYGSCRITVLDDQG-RAYVSDVKEGDIWYFPA 155
Cdd:smart00835  10 EGGRLREADPTNFPALNglGISAARVNLEPGGMLPPHYHPrATELLYVVRGEGRVGVVDPNGnKVYDARLREGDVFVVPQ 89

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 517077391   156 GQPHSLQGLGPDGCEFlLCFDDGKATEYNTLL-VTDWIAHTPPEILAANFGLPAETF 211
Cdd:smart00835  90 GHPHFQVNSGDENLEF-VAFNTNDPNRRFFLAgRNSVLRGLPPEVLAAAFGVSAEEV 145
Cupin_1 pfam00190
Cupin; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' ...
 80-210 1.58e-15

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: 73.14  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391   80 NGGWARQVTQYDFAI--AEEISGVDMRLTAGGIREMHWHL-AAEWGYVSYGSCR--ITVLDDQGRAYVSDVKEGDIWYFP 154
Cdd:pfam00190  13 EGGRVTTVNSKNLPGlnTLGISAARVDLAPGGMNPPHWHPnATEILYVLQGRGRvgFVVPGNGNRVFHKVLREGDVFVVP 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 517077391  155 AGQPHSLQGLG-PDGCEFLLCFDDGKATEYNTLLVTDWIAHTPPEILAANFGLPAET 210
Cdd:pfam00190  93 QGLPHFQYNIGdEPAVAFVAFDTNNPGNQSILAGGFSSLPALPPEVLAKAFQLAGEE 149
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 283-358 3.33e-10

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: 55.73  E-value: 3.33e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517077391  283 ALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDagpkaVTQDFHAGDIGYVKRAHGHYVQNVGDTELQFLEVF 358
Cdd:pfam07883   1 GLVTLPPGESSPPHRHPGEDEFFYVLEGEGELTVDG-----EEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDVY 71
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
265-365 7.57e-10

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 55.92  E-value: 7.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 265 EVRVADSDNFKVsstiaaALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDagpkaVTQDFHAGDIGYVKRAHGHYV 344
Cdd:COG0662   18 EVLGEGGERLSV------KRITVPPGAELSLHVHPHRDEFFYVLEGTGEVTIGD-----EEVELKAGDSVYIPAGVPHRL 86

                         90       100
                 ....*....|....*....|.
gi 517077391 345 QNVGDTELQFLEVFRAAHFRD 365
Cdd:COG0662   87 RNPGDEPLELLEVQAPAYLGE 107
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 282-358 3.05e-09

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: 53.26  E-value: 3.05e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517077391 282 AALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDAGpkavTQDFHAGDIGYVKRAHGHYVQNVGDTELQFLEVF 358
Cdd:cd02208    1 ISVVTLPPGTSSPPHWHPEQDEIFYVLSGEGELTLDDGE----TVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
96-179 4.26e-09

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 53.70  E-value: 4.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  96 EEISGVDMRLTAGGIREMHWHLAAEWGYVSYGSCRITVlddQGRAYVsdVKEGDIWYFPAGQPHSLQGLGPDGCEFLLCF 175
Cdd:COG1917   21 DELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVEV---GGEEYE--LKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95


                 ....
gi 517077391 176 DDGK 179
Cdd:COG1917   96 SPGL 99
cupin_OxOx cd02241
Oxalate oxidase (germin), cupin domain; Oxalate oxidase (OxOx, also known as germin; EC 1.2.3. ...
 248-394 4.10e-08

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: 52.98  E-value: 4.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 248 YTFS-LKGSAAAKKTKGGEVRVADSDNFKVSST--IAAALVTLAPGALREMHWHPNGDEWQYWIKGhgrmTLF-----DA 319
Cdd:cd02241   35 FVFDfLNPPGNTSNPLGGSVTLANVANFPALNGlgISMARGDLAPCGVNPPHTHPRATELLYVVEG----TLYvgfvdEN 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517077391 320 GPKAVTQDFHAGDIGYVKRAHGHYVQNVGDTELQFLEVFRAAHFRDVSLTDWLTHTPP--AMVAQHLNIDEATIAKF 394
Cdd:cd02241  111 GNRLFTKTLNPGDVFVFPQGLIHFQFNPGCEPAVFVAAFNSEDPGTQQIAQALFGLPPpdDVLAAAFGLDGAQVEKL 187
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 103-175 1.57e-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: 48.25  E-value: 1.57e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517077391 103 MRLTAGGIREMHWH-LAAEWGYVSYGSCRITVldDQGRAYVsdVKEGDIWYFPAGQPHSLQGLGPDGCEFLLCF 175
Cdd:cd02208    4 VTLPPGTSSPPHWHpEQDEIFYVLSGEGELTL--DDGETVE--LKAGDIVLIPPGVPHSFVNTSDEPAVFLVVS 73
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
103-172 6.10e-07

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 47.83  E-value: 6.10e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517077391 103 MRLTAGGIREMHWHLA-AEWGYVSYGSCRITVlDDQgrayVSDVKEGDIWYFPAGQPHSLQGLGPDGCEFL 172
Cdd:COG0662   32 ITVPPGAELSLHVHPHrDEFFYVLEGTGEVTI-GDE----EVELKAGDSVYIPAGVPHRLRNPGDEPLELL 97
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
280-358 1.38e-06

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 46.38  E-value: 1.38e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517077391 280 IAAALVTLAPGALREMHWHPnGDEWQYWIKGHGRMTLfdAGPkavTQDFHAGDIGYVKRAHGHYVQNVGDTELQFLEVF 358
Cdd:COG1917   23 LEVVRVTFEPGARTPWHSHP-GEELIYVLEGEGEVEV--GGE---EYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVVF 95
cupin_TM1287-like cd02221
Thermotoga maritima TM1287 decarboxylase, cupin domain; This family includes bacterial ...
 283-355 1.83e-06

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: 45.92  E-value: 1.83e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517077391 283 ALVTLAPGALREMHWHpNGDEWQYWI-KGHGRMTlfDAGpkaVTQDFHAGDIGYVKRAHGHYVQNVGDTELQFL 355
Cdd:cd02221   22 ARVTLPPGSSIGYHQH-EGEFEIYYIlSGEGLYT--DNG---KEYEVKAGDVTFTRDGESHGIENTGDEDLVFI 89
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 103-172 4.14e-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: 44.17  E-value: 4.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517077391  103 MRLTAGGIREMHWH-LAAEWGYVSYGSCRITVlDDQgrayVSDVKEGDIWYFPAGQPHSLQGLGPDGCEFL 172
Cdd:pfam07883   3 VTLPPGESSPPHRHpGEDEFFYVLEGEGELTV-DGE----EVVLKAGDSVYFPAGVPHRFRNTGDEPARLL 68
cupin_SPO2919-like cd02224
Silicibacter pomeroyi SPO2919 and related proteins, uncharacterized sugar phosphate isomerase ...
 280-357 6.82e-06

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: 44.40  E-value: 6.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 280 IAAALVTLAPGAlR--EMHWHPNGDEWQYWIKGHGRMTLFDAgpkavTQDFHAGD-IGYVK-RAHGHYVQNVGDTELQFL 355
Cdd:cd02224   17 LGVNLERLPPGA-RssPRHWHSAEEEFVYVLSGEGTLRLDGE-----EVLPRPGDfVGFPAgTGVAHQLINRSDEPLVYL 90


                 ..
gi 517077391 356 EV 357
Cdd:cd02224   91 VV 92
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
280-357 8.96e-06

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 44.62  E-value: 8.96e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517077391 280 IAAALVTLAPGA-LREMHWHPNGDEWQYWIKGHGRMTlFDAGPKAVTqdfhAGDIGYVKRAHGHYVQNVGDTELQFLEV 357
Cdd:COG3837   28 LGVNLITLPPGAsSSPYHAHSAEEEFVYVLEGELTLR-IGGEEYVLE----PGDSVGFPAGVPHRLRNRGDEPARYLVV 101
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 283-355 5.04e-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: 41.73  E-value: 5.04e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517077391 283 ALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLFDagpkaVTQDFHAGDIGYVKRAHGHYVQNVGDTELQFL 355
Cdd:cd02214   22 AHARVPPGESTLPHRLKGSEEVYYILEGEGTMEIDG-----EPREVGPGDAVLIPPGAVQRIENTGEEDLVFL 89
cupin_11S_legumin_C cd02243
11S legumin seed storage globulin, C-terminal cupin domain; This family contains the ...
 78-209 1.46e-04

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: 41.69  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  78 VQNGGWARQVTQYDFAIAEEI--SGVDMRLTAGGIREMHWHLAA-EWGYVSYGSCRITVLDDQG-RAYVSDVKEGDIWYF 153
Cdd:cd02243    4 VPRGGRITTLNSFKLPILRFVglSAERVKLEPNAMFAPHWNANAhQVIYVTRGSGRVQVVGDNGkRVLDGEVREGQLLVV 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517077391 154 PAGQPHSLQGlGPDGCEF---------LLCFDDGKATEYNTLlvtdwiahtPPEILAANFGLPAE 209
Cdd:cd02243   84 PQFFAVAKIA-GEEGFEWvsfktsdnpIFSELAGRTSVLRAL---------PPEVLANSYNISPE 138
cupin_DddK cd06988
Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ...
 282-358 2.20e-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: 39.53  E-value: 2.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517077391 282 AALVTLAPGALREMHWHpngDEWQYWI--KGHGRMTLFDagpkaVTQDFHAGDIGYVKRAHGHYVQNVGDTELQFLEVF 358
Cdd:cd06988    4 GAWCVVRPGTTSTPHSH---HEYEIFIviSGKGIVVVDG-----EREPVKAGDVVYIPPGTEHYVKNDGDEDFEFYSIW 74
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
103-172 2.56e-04

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 40.39  E-value: 2.56e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517077391 103 MRLTAGG-IREMHWHLAA-EWGYVSYGSCRITVlddQGRAYVsdVKEGDIWYFPAGQPHSLQGLGPDGCEFL 172
Cdd:COG3837   33 ITLPPGAsSSPYHAHSAEeEFVYVLEGELTLRI---GGEEYV--LEPGDSVGFPAGVPHRLRNRGDEPARYL 99
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 269-357 2.88e-04

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: 40.23  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 269 ADSDNFKVSStiaaalVTLAPGALREMHWHPNGDEwqYWI--KGHGRMTLFDagpkaVTQDFHAGDIGYVKRAHGHYVQN 346
Cdd:cd02213   35 DEGEGYKVKR------LTVNPGKRLSLQRHHHRSE--HWVvvSGTAEVTLDG-----KEKLLKEGESIYIPKGTKHRLEN 101

                         90
                 ....*....|.
gi 517077391 347 VGDTELQFLEV 357
Cdd:cd02213  102 PGKIPLEIIEV 112
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 263-351 3.19e-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: 3.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391 263 GGEVRVADSDNFKVSSTIAAALVTLAPGALREMHWHPNGDEWQYWIKGHGRMTLfDAGPKAVTqdfhAGDIGYVKRAHGH 342
Cdd:cd06991    2 GGDLRILLSPKTVGATSGFMGTLTLAPGERVSEHYHPYSEEFLYVVRGRLVVRV-DGEPVVLE----AGEALLVPRGVRH 76


                 ....*....
gi 517077391 343 YVQNVGDTE 351
Cdd:cd06991   77 RLENAGDEP 85
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 111-171 5.09e-04

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: 39.73  E-value: 5.09e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517077391  111 REMHWHLAAEWGYVSYGSCRITVlddQGRAYvsDVKEGDIWYFPAGQPHSLQGLGPDGCEF 171
Cdd:pfam02311  16 FPPHVHDFYVIGYIERGVGRFRL---NGRTY--HLGPGDLFLLPPGEPHDYEPESEDGWRY 71
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 87-166 1.44e-03

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: 37.83  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517077391  87 VTQYDFAIAEEISGVDMRLTAGGIREMHWHLAAEWGYVSYGSCRITVlDDQGRayvsDVKEGDIWYFPAGQPHSLQGLGP 166
Cdd:cd02238   16 VRRKILAGGEKLMLVEVRFEKGAVVPLHSHPHEQIGYVLSGRFEFTI-GGETR----ILKPGDSYYIPPNVPHGAEALED 90
PRK13264 PRK13264
3-hydroxyanthranilate 3,4-dioxygenase; Provisional
 120-162 1.53e-03

3-hydroxyanthranilate 3,4-dioxygenase; Provisional


Pssm-ID: 183930  Cd Length: 177  Bit Score: 39.13  E-value: 1.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 517077391 120 EWGYVSYGSCRITVLDDqGRAYVSDVKEGDIWYFPAGQPHSLQ 162
Cdd:PRK13264  56 EFFYQLEGDMYLKVQED-GKRRDVPIREGEMFLLPPHVPHSPQ 97
cupin_PMI_typeII_C cd02213
Phosphomannose isomerase type II, C-terminal cupin domain; This family includes the C-terminal ...
 111-172 4.56e-03

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: 36.77  E-value: 4.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517077391 111 REMHWhlaaewgYVSYGSCRITVLDDqgrayVSDVKEGDIWYFPAGQPHSLQGLGPDGCEFL 172
Cdd:cd02213   61 RSEHW-------VVVSGTAEVTLDGK-----EKLLKEGESIYIPKGTKHRLENPGKIPLEII 110
 
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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