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Conserved domains on  [gi|818325201|gb|KKQ08198|]
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MAG: Lycopene cyclase [Parcubacteria group bacterium GW2011_GWB1_36_5]

Protein Classification

lycopene cyclase domain-containing protein( domain architecture ID 10022454)

lycopene cyclase domain-containing protein includes lycopene beta-cyclase which catalyzes the cyclization of both ends of lycopene to form beta-carotene, a retinal precursor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CarR_dom_SF TIGR03462
lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as ...
 2-91 4.87e-08

lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as is observed in Archaea, Thermus, Sphingobacteria and Fungi. In the fungal sequences, this tandem domain pair is observed as the N-terminal half of a bifunctional protein, where it has been characterized as a lycopene beta-cyclase and the C-terminal half is a phytoene synthetase. In Myxococcus and Actinobacterial genomes this domain appears as a single polypeptide, tandemly repeated and usually in a genomic context consistent with a role in carotenoid biosynthesis. It is unclear whether any of the sequences in this family truly encode lycopene epsilon cyclases. However a number are annotated as such. The domain is generally hydrophobic with a number of predicted membrane spanning segments and contains a distinctive motif (hPhEEhhhhhh). In certain sequences one of either the proline or glutamates may vary, but always one of the tandem pair appear to match this canonical sequence exactly.


:

Pssm-ID: 274590  Cd Length: 89  Bit Score: 46.06  E-value: 4.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818325201   2 PEYLTILLVVLIVTVFIEFKYHIHLYHSRKeRLFVTLNIFLFGMFWDYFAVYRQHWIFPGDGLIGIRIFGLPIEEFLFFL 81
Cdd:TIGR03462  1 YLYLGVLLVWALPVLALLWVFRGPFLRLRA-LALALLIALPTFLVWDNLAIRRGVWTYNPRYILGIRLGDLPIEEFLFFL 79

                         90
                 ....*....|
gi 818325201  82 IIPYAALVMY 91
Cdd:TIGR03462 80 LTPLLTVLWL 89
 
Name Accession Description Interval E-value
CarR_dom_SF TIGR03462
lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as ...
 2-91 4.87e-08

lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as is observed in Archaea, Thermus, Sphingobacteria and Fungi. In the fungal sequences, this tandem domain pair is observed as the N-terminal half of a bifunctional protein, where it has been characterized as a lycopene beta-cyclase and the C-terminal half is a phytoene synthetase. In Myxococcus and Actinobacterial genomes this domain appears as a single polypeptide, tandemly repeated and usually in a genomic context consistent with a role in carotenoid biosynthesis. It is unclear whether any of the sequences in this family truly encode lycopene epsilon cyclases. However a number are annotated as such. The domain is generally hydrophobic with a number of predicted membrane spanning segments and contains a distinctive motif (hPhEEhhhhhh). In certain sequences one of either the proline or glutamates may vary, but always one of the tandem pair appear to match this canonical sequence exactly.


Pssm-ID: 274590  Cd Length: 89  Bit Score: 46.06  E-value: 4.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818325201   2 PEYLTILLVVLIVTVFIEFKYHIHLYHSRKeRLFVTLNIFLFGMFWDYFAVYRQHWIFPGDGLIGIRIFGLPIEEFLFFL 81
Cdd:TIGR03462  1 YLYLGVLLVWALPVLALLWVFRGPFLRLRA-LALALLIALPTFLVWDNLAIRRGVWTYNPRYILGIRLGDLPIEEFLFFL 79

                         90
                 ....*....|
gi 818325201  82 IIPYAALVMY 91
Cdd:TIGR03462 80 LTPLLTVLWL 89
 
Name Accession Description Interval E-value
CarR_dom_SF TIGR03462
lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as ...
 2-91 4.87e-08

lycopene cyclase domain; This domain is often repeated twice within the same polypeptide, as is observed in Archaea, Thermus, Sphingobacteria and Fungi. In the fungal sequences, this tandem domain pair is observed as the N-terminal half of a bifunctional protein, where it has been characterized as a lycopene beta-cyclase and the C-terminal half is a phytoene synthetase. In Myxococcus and Actinobacterial genomes this domain appears as a single polypeptide, tandemly repeated and usually in a genomic context consistent with a role in carotenoid biosynthesis. It is unclear whether any of the sequences in this family truly encode lycopene epsilon cyclases. However a number are annotated as such. The domain is generally hydrophobic with a number of predicted membrane spanning segments and contains a distinctive motif (hPhEEhhhhhh). In certain sequences one of either the proline or glutamates may vary, but always one of the tandem pair appear to match this canonical sequence exactly.


Pssm-ID: 274590  Cd Length: 89  Bit Score: 46.06  E-value: 4.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818325201   2 PEYLTILLVVLIVTVFIEFKYHIHLYHSRKeRLFVTLNIFLFGMFWDYFAVYRQHWIFPGDGLIGIRIFGLPIEEFLFFL 81
Cdd:TIGR03462  1 YLYLGVLLVWALPVLALLWVFRGPFLRLRA-LALALLIALPTFLVWDNLAIRRGVWTYNPRYILGIRLGDLPIEEFLFFL 79

                         90
                 ....*....|
gi 818325201  82 IIPYAALVMY 91
Cdd:TIGR03462 80 LTPLLTVLWL 89
 
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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