MULTISPECIES: cupin domain-containing protein [Brevibacillus]
cupin domain-containing protein( domain architecture ID 10004899)
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
List of domain hits
Name | Accession | Description | Interval | E-value | |||
QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
21-104 | 3.29e-06 | |||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; : Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 42.53 E-value: 3.29e-06
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Name | Accession | Description | Interval | E-value | |||
QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
21-104 | 3.29e-06 | |||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 42.53 E-value: 3.29e-06
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cupin_DddK | cd06988 | Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ... |
57-91 | 2.72e-03 | |||
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: 34.13 E-value: 2.72e-03
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Name | Accession | Description | Interval | E-value | |||
QdoI | COG1917 | Cupin domain protein related to quercetin dioxygenase [General function prediction only]; |
21-104 | 3.29e-06 | |||
Cupin domain protein related to quercetin dioxygenase [General function prediction only]; Pssm-ID: 441521 [Multi-domain] Cd Length: 99 Bit Score: 42.53 E-value: 3.29e-06
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COG3837 | COG3837 | Uncharacterized conserved protein, cupin superfamily [Function unknown]; |
39-114 | 4.96e-04 | |||
Uncharacterized conserved protein, cupin superfamily [Function unknown]; Pssm-ID: 443048 [Multi-domain] Cd Length: 115 Bit Score: 36.92 E-value: 4.96e-04
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cupin_DddK | cd06988 | Dimethylsulfoniopropionate lyase DddK and related proteins, cupin domain; This family includes ... |
57-91 | 2.72e-03 | |||
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: 34.13 E-value: 2.72e-03
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ManC | COG0662 | Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; |
1-91 | 3.54e-03 | |||
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 440426 [Multi-domain] Cd Length: 114 Bit Score: 34.73 E-value: 3.54e-03
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cupin_RmlC-like | cd02208 | RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ... |
36-104 | 6.83e-03 | |||
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: 33.23 E-value: 6.83e-03
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Blast search parameters | ||||
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