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Conserved domains on  [gi|1907199579|ref|XP_036011087|]
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phosphopantothenoylcysteine decarboxylase isoform X5 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Flavoprotein super family cl19190
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 19-42 1.43e-03

Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes epidermin biosynthesis protein, EpiD, which has been shown to be a flavoprotein that binds FMN. This enzyme catalyzes the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond. This family also includes the B chain of dipicolinate synthase a small polar molecule that accumulates to high concentrations in bacterial endospores, and is thought to play a role in spore heat resistance, or the maintenance of heat resistance. dipicolinate synthase catalyzes the formation of dipicolinic acid from dihydroxydipicolinic acid. This family also includes phenyl-acrylic acid decarboxylase (EC:4.1.1.-).


The actual alignment was detected with superfamily member pfam02441:

Pssm-ID: 450266 [Multi-domain]  Cd Length: 177  Bit Score: 34.66  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|....
gi 1907199579  19 RVLVGVTGSVAALKLPLLVSKLLD 42
Cdd:pfam02441   2 RILVGITGSSAAIKALRLLEELKK 25
 
Name Accession Description Interval E-value
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 19-42 1.43e-03

Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes epidermin biosynthesis protein, EpiD, which has been shown to be a flavoprotein that binds FMN. This enzyme catalyzes the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond. This family also includes the B chain of dipicolinate synthase a small polar molecule that accumulates to high concentrations in bacterial endospores, and is thought to play a role in spore heat resistance, or the maintenance of heat resistance. dipicolinate synthase catalyzes the formation of dipicolinic acid from dihydroxydipicolinic acid. This family also includes phenyl-acrylic acid decarboxylase (EC:4.1.1.-).


Pssm-ID: 426775 [Multi-domain]  Cd Length: 177  Bit Score: 34.66  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|....
gi 1907199579  19 RVLVGVTGSVAALKLPLLVSKLLD 42
Cdd:pfam02441   2 RILVGITGSSAAIKALRLLEELKK 25
 
Name Accession Description Interval E-value
Flavoprotein pfam02441
Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes ...
 19-42 1.43e-03

Flavoprotein; This family contains diverse flavoprotein enzymes. This family includes epidermin biosynthesis protein, EpiD, which has been shown to be a flavoprotein that binds FMN. This enzyme catalyzes the removal of two reducing equivalents from the cysteine residue of the C-terminal meso-lanthionine of epidermin to form a --C==C-- double bond. This family also includes the B chain of dipicolinate synthase a small polar molecule that accumulates to high concentrations in bacterial endospores, and is thought to play a role in spore heat resistance, or the maintenance of heat resistance. dipicolinate synthase catalyzes the formation of dipicolinic acid from dihydroxydipicolinic acid. This family also includes phenyl-acrylic acid decarboxylase (EC:4.1.1.-).


Pssm-ID: 426775 [Multi-domain]  Cd Length: 177  Bit Score: 34.66  E-value: 1.43e-03
                          10        20
                  ....*....|....*....|....
gi 1907199579  19 RVLVGVTGSVAALKLPLLVSKLLD 42
Cdd:pfam02441   2 RILVGITGSSAAIKALRLLEELKK 25
 
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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