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Conserved domains on  [gi|188497708|ref|NP_001120855|]
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plasma membrane ascorbate-dependent reductase CYBRD1 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cytochrome_b_N super family cl23723
Cytochrome b (N-terminus)/b6/petB: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit ...
36-65 7.18e-14

Cytochrome b (N-terminus)/b6/petB: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit mitochondrial respiratory enzyme. Cytochrome b spans the mitochondrial membrane with 8 transmembrane helices (A-H) in eukaryotes. In plants and cyanobacteria, cytochrome b6 is analogous to eukaryote cytochrome b, containing two chains: helices A-D are encoded by the petB gene and helices E-H are encoded by the petD gene in these organisms. Cytochrome b/b6 contains two bound hemes and two ubiquinol/ubiquinone binding sites. The C-terminal portion of cytochrome b is described in a separate CD.


The actual alignment was detected with superfamily member cd08765:

Pssm-ID: 474033  Cd Length: 153  Bit Score: 64.92  E-value: 7.18e-14
                         10        20        30
                 ....*....|....*....|....*....|
gi 188497708  36 EGLGWDGSALEFNWHPVLMVTGFVFIQGIA 65
Cdd:cd08765    1 EGLGWDGGAAEFNWHPVLMVIGFIFIQGIA 30
 
Name Accession Description Interval E-value
Cyt_b561_CYBRD1 cd08765
Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate ...
36-65 7.18e-14

Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate reductase 3, a cytochrome b(561), as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. This protein is expressed at the brush border of duodenal enterocytes and may play a role in the uptake of dietary Fe(3+), facilitating its transport into the mucosal cells. It may also be involved in the recycling of extracellular ascorbate in erythrocyte membranes, and act as a ferrireductase in epithelial cells of the respiratory system. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176495  Cd Length: 153  Bit Score: 64.92  E-value: 7.18e-14
                         10        20        30
                 ....*....|....*....|....*....|
gi 188497708  36 EGLGWDGSALEFNWHPVLMVTGFVFIQGIA 65
Cdd:cd08765    1 EGLGWDGGAAEFNWHPVLMVIGFIFIQGIA 30
PLN02810 PLN02810
carbon-monoxide oxygenase
1-73 1.11e-07

carbon-monoxide oxygenase


Pssm-ID: 178406  Cd Length: 231  Bit Score: 49.43  E-value: 1.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188497708   1 MAMEGYWRFLALLGSALLVgfLSVIFALVWVLHYREGLGWDGS--ALEFNWHPVLMVTGFVFIQGIASFRFFSLS 73
Cdd:PLN02810   1 MAVGINALPLTFVAHALAV--IGAIMVLVWSIYYRGGLAWEATnkNLIFNLHPVLMLIGLIIIGGEAIMSYKSLP 73
 
Name Accession Description Interval E-value
Cyt_b561_CYBRD1 cd08765
Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate ...
36-65 7.18e-14

Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate reductase 3, a cytochrome b(561), as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. This protein is expressed at the brush border of duodenal enterocytes and may play a role in the uptake of dietary Fe(3+), facilitating its transport into the mucosal cells. It may also be involved in the recycling of extracellular ascorbate in erythrocyte membranes, and act as a ferrireductase in epithelial cells of the respiratory system. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176495  Cd Length: 153  Bit Score: 64.92  E-value: 7.18e-14
                         10        20        30
                 ....*....|....*....|....*....|
gi 188497708  36 EGLGWDGSALEFNWHPVLMVTGFVFIQGIA 65
Cdd:cd08765    1 EGLGWDGGAAEFNWHPVLMVIGFIFIQGIA 30
Cyt_b561_CG1275_like cd08764
Non-vertebrate eumetazoan cytochrome b(561); Cytochrome b(561), as found in non-vertebrate ...
24-70 1.04e-11

Non-vertebrate eumetazoan cytochrome b(561); Cytochrome b(561), as found in non-vertebrate eumetazoans, similar to the Drosophila melanogaster CG1275 gene product. This protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176494  Cd Length: 214  Bit Score: 60.04  E-value: 1.04e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 188497708  24 VIFALVWVLHYREGLGWDGSALEFNWHPVLMVTGFVFI--QGIASFRFF 70
Cdd:cd08764    1 VVLVGIWLGKFRGGFSWTGPGLQFNWHPLLMVLGLIFLygNSILVYRVF 49
Cyt_b561_CYBASC3 cd08762
Vertebrate cytochrome b(561), CYBASC3 gene product; Cytochrome b ascorbate-dependent 3, as ...
17-66 4.90e-10

Vertebrate cytochrome b(561), CYBASC3 gene product; Cytochrome b ascorbate-dependent 3, as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176492  Cd Length: 179  Bit Score: 55.26  E-value: 4.90e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 188497708  17 LLVGFLSVIFALVWVLHYREGLGWDGSALEFNWHPVLMVTGFVFIQGIAS 66
Cdd:cd08762    5 GILGIACVVLVVHWNQMWRGGFAWDGSSKNFNWHPVLMVTGMVVLYGNAA 54
PLN02810 PLN02810
carbon-monoxide oxygenase
1-73 1.11e-07

carbon-monoxide oxygenase


Pssm-ID: 178406  Cd Length: 231  Bit Score: 49.43  E-value: 1.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188497708   1 MAMEGYWRFLALLGSALLVgfLSVIFALVWVLHYREGLGWDGS--ALEFNWHPVLMVTGFVFIQGIASFRFFSLS 73
Cdd:PLN02810   1 MAVGINALPLTFVAHALAV--IGAIMVLVWSIYYRGGLAWEATnkNLIFNLHPVLMLIGLIIIGGEAIMSYKSLP 73
PLN02680 PLN02680
carbon-monoxide oxygenase
18-65 3.78e-06

carbon-monoxide oxygenase


Pssm-ID: 215365  Cd Length: 232  Bit Score: 44.79  E-value: 3.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 188497708  18 LVGFLSVIFALVWVLHYREGLGW--DGSALEFNWHPVLMVTGFVFIQGIA 65
Cdd:PLN02680  16 LLGVIVAALVLTWTVHYRGGLALssDNKDLIFNVHPVLMVIGLVLLNGEA 65
 
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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