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Conserved domains on  [gi|1510971121|ref|WP_122966626|]
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MULTISPECIES: cupin domain-containing protein [Brevibacillus]

Protein Classification

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

CATH:  2.60.120.10
Gene Ontology:  GO:0046872
SCOP:  3001825

Graphical summary

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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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971121  21 GAVFSRILRTKDAVSIGCIHVKAGGVVGYHPAVCPQLFLVVNGEGWVRgEDDERIPIQAGQAAFWQAGEGHESGTESGMT 100
Cdd:COG1917    10 GVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVE-VGGEEYELKPGDVVFIPPGVPHAFRNLGDEP 88

                  ....
gi 1510971121 101 AIVI 104
Cdd:COG1917    89 AVLL 92
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971121  21 GAVFSRILRTKDAVSIGCIHVKAGGVVGYHPAVCPQLFLVVNGEGWVRgEDDERIPIQAGQAAFWQAGEGHESGTESGMT 100
Cdd:COG1917    10 GVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVE-VGGEEYELKPGDVVFIPPGVPHAFRNLGDEP 88

                  ....
gi 1510971121 101 AIVI 104
Cdd:COG1917    89 AVLL 92
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
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1510971121  57 LFLVVNGEGWVRGeDDERIPIQAGQAAFWQAGEGH 91
Cdd:cd06988    25 IFIVISGKGIVVV-DGEREPVKAGDVVYIPPGTEH 58
 
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971121  21 GAVFSRILRTKDAVSIGCIHVKAGGVVGYHPAVCPQLFLVVNGEGWVRgEDDERIPIQAGQAAFWQAGEGHESGTESGMT 100
Cdd:COG1917    10 GVSVRVLADGEDELEVVRVTFEPGARTPWHSHPGEELIYVLEGEGEVE-VGGEEYELKPGDVVFIPPGVPHAFRNLGDEP 88

                  ....
gi 1510971121 101 AIVI 104
Cdd:COG1917    89 AVLL 92
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971121  39 IHVKAGGVVG---YHPAVCpQLFLVVNGEGWVRgEDDERIPIQAGQAAFWQAGEGH--ESGTESGMTAIVIEGEELDPDS 113
Cdd:COG3837    33 ITLPPGASSSpyhAHSAEE-EFVYVLEGELTLR-IGGEEYVLEPGDSVGFPAGVPHrlRNRGDEPARYLVVGTRAPYPDS 110

                  .
gi 1510971121 114 F 114
Cdd:COG3837   111 F 111
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
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1510971121  57 LFLVVNGEGWVRGeDDERIPIQAGQAAFWQAGEGH 91
Cdd:cd06988    25 IFIVISGKGIVVV-DGEREPVKAGDVVYIPPGTEH 58
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
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971121   1 MRRFRFDEQAGREIERFDSVGavfsrilRTKDAVSIGCIHVKAGGVVGYHP-AVCPQLFLVVNGEGWVRgEDDERIPIQA 79
Cdd:COG0662     1 MQDVNIEELKAIGWGSYEVLG-------EGGERLSVKRITVPPGAELSLHVhPHRDEFFYVLEGTGEVT-IGDEEVELKA 72
                          90
                  ....*....|..
gi 1510971121  80 GQAAFWQAGEGH 91
Cdd:COG0662    73 GDSVYIPAGVPH 84
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
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1510971121  36 IGCIHVKAGGVVGYHP-AVCPQLFLVVNGEGWVRGEDDERIPIQAGQAAFWQAGEGHESGTESGMTAIVI 104
Cdd:cd02208     1 ISVVTLPPGTSSPPHWhPEQDEIFYVLSGEGELTLDDGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFL 70
 
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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