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Conserved domains on  [gi|159489725|ref|XP_001702847|]
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C-8,7 sterol isomerase [Chlamydomonas reinhardtii]

Protein Classification

EBP domain-containing protein (domain architecture ID 10526086)

EBP domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
EBP pfam05241
Emopamil binding protein; Emopamil binding protein (EBP) is as a gene that encodes a ...
30-208 1.87e-67

Emopamil binding protein; Emopamil binding protein (EBP) is as a gene that encodes a non-glycosylated type I integral membrane protein of endoplasmic reticulum and shows high level expression in epithelial tissues. The EBP protein has emopamil binding domains, including the sterol acceptor site and the catalytic centre, which show Delta8-Delta7 sterol isomerase activity. Human sterol isomerase, a homolog of mouse EBP, is suggested not only to play a role in cholesterol biosynthesis, but also to affect lipoprotein internalisation. In humans, mutations of EBP are known to cause the genetic disorder of X-linked dominant chondrodysplasia punctata (CDPX2). This syndrome of humans is lethal in most males, and affected females display asymmetric hyperkeratotic skin and skeletal abnormalities.


:

Pssm-ID: 310099  Cd Length: 179  Bit Score: 208.13  E-value: 1.87e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159489725   30 FFGSSALVVIFMFLLTGRFK-YLSSVERLWAGWWMVTGIIHFVIEGTVVANANFYKDTTgNILNEIWKEYAKADSRYATR 108
Cdd:pfam05241   1 FLAACAAVLLAAYLLSRRLLpKLSTADRLLFLWFAFDGLIHLFLEGYFLYNHRTLAGSQ-SFFAQLWKEYAKADSRYLTA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159489725  109 DAFIVQMEGVTAFIWGPICFAIVYGILHRKAWRFTAMLLVSLGQLYGDVLYYLTCFHIGVEKHTRPEPLYFWGYFVGANA 188
Cdd:pfam05241  80 DPFVVSMELITVFLWGPLCLLIAYAIAKRKPLRHPLQIVVSTGQLYGGVLYFATEWLDGGLNLSRPEPLYFWVYLVFFNA 159
                         170       180
                  ....*....|....*....|
gi 159489725  189 IWIVVPVTCIIYCARHVNSA 208
Cdd:pfam05241 160 LWVVIPLWLLWQSWKEIAAA 179
 
Name Accession Description Interval E-value
EBP pfam05241
Emopamil binding protein; Emopamil binding protein (EBP) is as a gene that encodes a ...
30-208 1.87e-67

Emopamil binding protein; Emopamil binding protein (EBP) is as a gene that encodes a non-glycosylated type I integral membrane protein of endoplasmic reticulum and shows high level expression in epithelial tissues. The EBP protein has emopamil binding domains, including the sterol acceptor site and the catalytic centre, which show Delta8-Delta7 sterol isomerase activity. Human sterol isomerase, a homolog of mouse EBP, is suggested not only to play a role in cholesterol biosynthesis, but also to affect lipoprotein internalisation. In humans, mutations of EBP are known to cause the genetic disorder of X-linked dominant chondrodysplasia punctata (CDPX2). This syndrome of humans is lethal in most males, and affected females display asymmetric hyperkeratotic skin and skeletal abnormalities.


Pssm-ID: 310099  Cd Length: 179  Bit Score: 208.13  E-value: 1.87e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159489725   30 FFGSSALVVIFMFLLTGRFK-YLSSVERLWAGWWMVTGIIHFVIEGTVVANANFYKDTTgNILNEIWKEYAKADSRYATR 108
Cdd:pfam05241   1 FLAACAAVLLAAYLLSRRLLpKLSTADRLLFLWFAFDGLIHLFLEGYFLYNHRTLAGSQ-SFFAQLWKEYAKADSRYLTA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159489725  109 DAFIVQMEGVTAFIWGPICFAIVYGILHRKAWRFTAMLLVSLGQLYGDVLYYLTCFHIGVEKHTRPEPLYFWGYFVGANA 188
Cdd:pfam05241  80 DPFVVSMELITVFLWGPLCLLIAYAIAKRKPLRHPLQIVVSTGQLYGGVLYFATEWLDGGLNLSRPEPLYFWVYLVFFNA 159
                         170       180
                  ....*....|....*....|
gi 159489725  189 IWIVVPVTCIIYCARHVNSA 208
Cdd:pfam05241 160 LWVVIPLWLLWQSWKEIAAA 179
 
Name Accession Description Interval E-value
EBP pfam05241
Emopamil binding protein; Emopamil binding protein (EBP) is as a gene that encodes a ...
30-208 1.87e-67

Emopamil binding protein; Emopamil binding protein (EBP) is as a gene that encodes a non-glycosylated type I integral membrane protein of endoplasmic reticulum and shows high level expression in epithelial tissues. The EBP protein has emopamil binding domains, including the sterol acceptor site and the catalytic centre, which show Delta8-Delta7 sterol isomerase activity. Human sterol isomerase, a homolog of mouse EBP, is suggested not only to play a role in cholesterol biosynthesis, but also to affect lipoprotein internalisation. In humans, mutations of EBP are known to cause the genetic disorder of X-linked dominant chondrodysplasia punctata (CDPX2). This syndrome of humans is lethal in most males, and affected females display asymmetric hyperkeratotic skin and skeletal abnormalities.


Pssm-ID: 310099  Cd Length: 179  Bit Score: 208.13  E-value: 1.87e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159489725   30 FFGSSALVVIFMFLLTGRFK-YLSSVERLWAGWWMVTGIIHFVIEGTVVANANFYKDTTgNILNEIWKEYAKADSRYATR 108
Cdd:pfam05241   1 FLAACAAVLLAAYLLSRRLLpKLSTADRLLFLWFAFDGLIHLFLEGYFLYNHRTLAGSQ-SFFAQLWKEYAKADSRYLTA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159489725  109 DAFIVQMEGVTAFIWGPICFAIVYGILHRKAWRFTAMLLVSLGQLYGDVLYYLTCFHIGVEKHTRPEPLYFWGYFVGANA 188
Cdd:pfam05241  80 DPFVVSMELITVFLWGPLCLLIAYAIAKRKPLRHPLQIVVSTGQLYGGVLYFATEWLDGGLNLSRPEPLYFWVYLVFFNA 159
                         170       180
                  ....*....|....*....|
gi 159489725  189 IWIVVPVTCIIYCARHVNSA 208
Cdd:pfam05241 160 LWVVIPLWLLWQSWKEIAAA 179
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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