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Conserved domains on  [gi|15597514|ref|NP_251008|]
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hypothetical protein PA2318 [Pseudomonas aeruginosa PAO1]

Protein Classification

cupin domain-containing protein( domain architecture ID 10007407)

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
PubMed:  19478949|14697267|9573603
SCOP:  3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG3450 COG3450
Predicted enzyme of the cupin superfamily [General function prediction only];
20-117 1.56e-19

Predicted enzyme of the cupin superfamily [General function prediction only];


:

Pssm-ID: 442673  Cd Length: 108  Bit Score: 76.94  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597514  20 SVADLGSEILEGEVKAFGKMTAGAPTDPVSAAYFGTTAGKFRMTYPFSEQATVVSGEVRLTDEsTGQSTLYKAGDSWFVS 99
Cdd:COG3450  10 SDPPAPERILEGDPSARTWNLFTSPDGGVSAGVWECTPGKFRWDYDEDEFCYILEGRVTVTDD-DGEPVEFGAGDSFVFP 88

                        90
                ....*....|....*...
gi 15597514 100 KGTPVLWEVaDGGFVKHY 117
Cdd:COG3450  89 AGFKGTWEV-LETVRKHY 105
 
Name Accession Description Interval E-value
COG3450 COG3450
Predicted enzyme of the cupin superfamily [General function prediction only];
20-117 1.56e-19

Predicted enzyme of the cupin superfamily [General function prediction only];


Pssm-ID: 442673  Cd Length: 108  Bit Score: 76.94  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597514  20 SVADLGSEILEGEVKAFGKMTAGAPTDPVSAAYFGTTAGKFRMTYPFSEQATVVSGEVRLTDEsTGQSTLYKAGDSWFVS 99
Cdd:COG3450  10 SDPPAPERILEGDPSARTWNLFTSPDGGVSAGVWECTPGKFRWDYDEDEFCYILEGRVTVTDD-DGEPVEFGAGDSFVFP 88

                        90
                ....*....|....*...
gi 15597514 100 KGTPVLWEVaDGGFVKHY 117
Cdd:COG3450  89 AGFKGTWEV-LETVRKHY 105
cupin_TM1112-like cd02227
Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial ...
 49-120 2.88e-18

Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial and plant proteins homologous to TM1112, a Thermotoga maritima protein of unknown function with a cupin beta barrel domain. TM1112 (also known as DUF861) is a subfamily of RmlC-like cupins with a conserved "jelly roll-like" beta-barrel fold; structures indicate that a monomer is the biologically-relevant form.


Pssm-ID: 380356 [Multi-domain]  Cd Length: 69  Bit Score: 72.61  E-value: 2.88e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597514  49 SAAYFGTTAGKFRMTYPFSEQATVVSGEVRLTDEsTGQSTLYKAGDSWFVSKGTPVLWEVAdgGFVKHYYAV 120
Cdd:cd02227   1 SWGIWECTPGKFPWNYDEDEFCYILEGEVRVTPE-DGEPVTFKAGDLVVFPAGFSGTWEVL--EPVRKHYVF 69
Cupin_3 pfam05899
EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly ...
 42-117 5.89e-18

EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly roll-like beta-barrel fold capable of homodimerization found in bacteria, plant and fungi. It is present in EutQ family from the eut operon, involved in ethanolamine degradation. EutQ is essential during anoxic growth and has acetate kinase activity. The cupin domain from EutQ does not possess the His residues responsible for metal coordination in other classes of cupins. This domain is also found in (S)-ureidoglycine aminohydrolase (UGlyAH) from E.coli, which is involved in the anaerobic nitrogen utilization via the assimilation of allantoin. It catalyzes the deamination of allantoin to produce S-ureidoglycolate and ammonia from S-ureidoglycine.


Pssm-ID: 399116 [Multi-domain]  Cd Length: 74  Bit Score: 71.94  E-value: 5.89e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597514    42 GAPTDPVSAAYFGTTAGKFRMTYPFSEQATVVSGEVRLTDEsTGQSTLYKAGDSWFVSKGTPVLWEVADgGFVKHY 117
Cdd:pfam05899   1 LSPLGVFSWGIWECTPGKFRWTYEEDETCYILSGEVTVTPE-GGKTVTLRAGDLVVLPKGLSGTWDVLE-TVRKHY 74
 
Name Accession Description Interval E-value
COG3450 COG3450
Predicted enzyme of the cupin superfamily [General function prediction only];
20-117 1.56e-19

Predicted enzyme of the cupin superfamily [General function prediction only];


Pssm-ID: 442673  Cd Length: 108  Bit Score: 76.94  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597514  20 SVADLGSEILEGEVKAFGKMTAGAPTDPVSAAYFGTTAGKFRMTYPFSEQATVVSGEVRLTDEsTGQSTLYKAGDSWFVS 99
Cdd:COG3450  10 SDPPAPERILEGDPSARTWNLFTSPDGGVSAGVWECTPGKFRWDYDEDEFCYILEGRVTVTDD-DGEPVEFGAGDSFVFP 88

                        90
                ....*....|....*...
gi 15597514 100 KGTPVLWEVaDGGFVKHY 117
Cdd:COG3450  89 AGFKGTWEV-LETVRKHY 105
cupin_TM1112-like cd02227
Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial ...
 49-120 2.88e-18

Thermotoga maritima TM1112 and related proteins, cupin domain; This family includes bacterial and plant proteins homologous to TM1112, a Thermotoga maritima protein of unknown function with a cupin beta barrel domain. TM1112 (also known as DUF861) is a subfamily of RmlC-like cupins with a conserved "jelly roll-like" beta-barrel fold; structures indicate that a monomer is the biologically-relevant form.


Pssm-ID: 380356 [Multi-domain]  Cd Length: 69  Bit Score: 72.61  E-value: 2.88e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597514  49 SAAYFGTTAGKFRMTYPFSEQATVVSGEVRLTDEsTGQSTLYKAGDSWFVSKGTPVLWEVAdgGFVKHYYAV 120
Cdd:cd02227   1 SWGIWECTPGKFPWNYDEDEFCYILEGEVRVTPE-DGEPVTFKAGDLVVFPAGFSGTWEVL--EPVRKHYVF 69
Cupin_3 pfam05899
EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly ...
 42-117 5.89e-18

EutQ-like cupin domain; This entry represents the cupin domain, with a conserved jelly roll-like beta-barrel fold capable of homodimerization found in bacteria, plant and fungi. It is present in EutQ family from the eut operon, involved in ethanolamine degradation. EutQ is essential during anoxic growth and has acetate kinase activity. The cupin domain from EutQ does not possess the His residues responsible for metal coordination in other classes of cupins. This domain is also found in (S)-ureidoglycine aminohydrolase (UGlyAH) from E.coli, which is involved in the anaerobic nitrogen utilization via the assimilation of allantoin. It catalyzes the deamination of allantoin to produce S-ureidoglycolate and ammonia from S-ureidoglycine.


Pssm-ID: 399116 [Multi-domain]  Cd Length: 74  Bit Score: 71.94  E-value: 5.89e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597514    42 GAPTDPVSAAYFGTTAGKFRMTYPFSEQATVVSGEVRLTDEsTGQSTLYKAGDSWFVSKGTPVLWEVADgGFVKHY 117
Cdd:pfam05899   1 LSPLGVFSWGIWECTPGKFRWTYEEDETCYILSGEVTVTPE-GGKTVTLRAGDLVVLPKGLSGTWDVLE-TVRKHY 74
cupin_EutQ cd02228
Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial ...
 47-110 3.93e-04

Clostridium difficile EutQ and related proteins, cupin domain; This family includes bacterial and fungal proteins homologous to ethanolamine utilization protein EutQ found in Clostridium difficile, as well as in other bacteria, including the enteric pathogens Salmonella enterica and Enterococcus faecalis. EutQ is encoded by the eutQ gene which is part of the eut (ethanolamine utilization) operon found to be essential during anoxic growth of S. enterica on ethanolamine and tetrathionate. In C. difficile, inability to utilize ethanolamine results in greater virulence and a shorter time to morbidity in the animal model, suggesting that, in contrast to other intestinal pathogens, the metabolism of ethanolamine can delay the onset of disease. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization. In contrast to the metal-binding catalytic cupins, the EutQ family does not possess the histidine residues that are responsible for metal coordination in the oxidoreductase and epimerase classes of cupins.


Pssm-ID: 380357 [Multi-domain]  Cd Length: 84  Bit Score: 36.72  E-value: 3.93e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597514  47 PVSAAYFGTTAGKFRMTYPFSEQATVVSGEVRLTDEstGQSTLYKAGDSWFVSKGTPVLWEVAD 110
Cdd:cd02228  14 PMSAGFMELEKKSFPWTLTYDEIKYVLEGELEITDD--GQTVTAKPGDVLFIPKGSKITFSTPD 75
 
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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