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Conserved domains on  [gi|1907079826|ref|XP_036012170|]
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transmembrane ascorbate-dependent reductase CYB561 isoform X2 [Mus musculus]

Protein Classification

cytochrome b family protein( domain architecture ID 581032)

cytochrome b family protein such as formate dehydrogenase subunit gamma or cytochrome b, a component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.

Gene Ontology:  GO:0046872|GO:0016491

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 ...
 53-194 1.08e-76

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 cd08763:

Pssm-ID: 474033  Cd Length: 143  Bit Score: 228.93  E-value: 1.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  53 WESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSW 132
Cdd:cd08763     1 WSGPLQFNVHPLCMVLGLVFLCGEALLVYRVFRNETKRSTKILHGLLHIMALVISLVGLVAVFDYHQANGYPDMYSLHSW 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907079826 133 CGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLF 194
Cdd:cd08763    81 CGILTFVLYFLQWLIGFSFFLFPGASFTLRSQYKPLHEFFGRALFLSSVGTSLLGLTEKLLF 142
 
Name Accession Description Interval E-value
Cyt_b561_CYB561 cd08763
Vertebrate cytochrome b(561), CYB561 gene product; Cytochrome b(561), as found in vertebrates, ...
 53-194 1.08e-76

Vertebrate cytochrome b(561), CYB561 gene product; 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. 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: 176493  Cd Length: 143  Bit Score: 228.93  E-value: 1.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  53 WESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSW 132
Cdd:cd08763     1 WSGPLQFNVHPLCMVLGLVFLCGEALLVYRVFRNETKRSTKILHGLLHIMALVISLVGLVAVFDYHQANGYPDMYSLHSW 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907079826 133 CGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLF 194
Cdd:cd08763    81 CGILTFVLYFLQWLIGFSFFLFPGASFTLRSQYKPLHEFFGRALFLSSVGTSLLGLTEKLLF 142
Cytochrom_B561 pfam03188
Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport ...
 61-195 1.50e-48

Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport protein. It is an integral membrane protein, that binds two heme groups non-covalently. This is a eukaryotic family. Members of the 'prokaryotic cytochrome b561' family can be found in Pfam: PF01292.


Pssm-ID: 427188  Cd Length: 137  Bit Score: 157.00  E-value: 1.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  61 VHPLCMVIGMIFLQGDALLVYRV--FRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVF 138
Cdd:pfam03188   1 WHPVLMVIGFIFLMGEAILVYRVnsTRRLSKKTKKLLHWILQALALILAVIGLVAVFKFHNLSGIPHFYSLHSWLGLLTV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907079826 139 VLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLFK 195
Cdd:pfam03188  81 ILYALQWVGGFVTFLFPGLSKRIRPLLLPLHVFFGLVIFVLAIVTALLGLLEKLIFQ 137
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
 61-188 1.82e-39

Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate for the generation of norepinephrine by dopamine-beta-hydroxylase in the chromaffin vesicles of the adrenal gland. It is a transmembrane heme protein with the two heme groups being bound to conserved histidine residues. A cytochrome b-561 homologue, termed Dcytb, is an iron-regulated ferric reductase in the duodenal mucosa. Other homologues of these are also likely to be ferric reductases. SDR2 is proposed to be important in regulating the metabolism of iron in the onset of neurodegenerative disorders.


Pssm-ID: 214769  Cd Length: 129  Bit Score: 133.51  E-value: 1.82e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826   61 VHPLCMVIGMIFLQGDALLVYR-VFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVFV 139
Cdd:smart00665   1 LHPVLMILGFGFLMGEAILVARpLTRFLSKPTWFLLHVVLQILALVLGVIGLLAIFISHNESGIANFYSLHSWLGLAAFV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907079826  140 LYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGL 188
Cdd:smart00665  81 LAGLQWLSGFLRPLPPGLPSKYRSYLNPYHRFVGLAAFILAIVTIFLGL 129
PLN02810 PLN02810
carbon-monoxide oxygenase
 37-231 1.10e-38

carbon-monoxide oxygenase


Pssm-ID: 178406  Cd Length: 231  Bit Score: 134.95  E-value: 1.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  37 VAVTGA-----WLGLYRGGIAWES---SLQFNVHPLCMVIGMIFLQGDALLVYRVFRREaKRTTKILHGLLHVFAFIIAL 108
Cdd:PLN02810   17 LAVIGAimvlvWSIYYRGGLAWEAtnkNLIFNLHPVLMLIGLIIIGGEAIMSYKSLPLK-KEVKKLIHLVLHAIALILGI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826 109 VGLVAVFDYHKKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGL 188
Cdd:PLN02810   96 FGICAAFKNHNESGIANLYSLHSWLGIGIISLYGIQWIYGFIVFFFPGGSTNLRSGSLPWHVLFGLFVYILAVGNAALGF 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907079826 189 KEALLFKLGSKYSTFEPEGVLANVLGLLLVCFGV-VVLYILAQA 231
Cdd:PLN02810  176 LEKLTFLESGGLDKYGSEALLVNFTAIITILYGAfVVLTALAQS 219
 
Name Accession Description Interval E-value
Cyt_b561_CYB561 cd08763
Vertebrate cytochrome b(561), CYB561 gene product; Cytochrome b(561), as found in vertebrates, ...
 53-194 1.08e-76

Vertebrate cytochrome b(561), CYB561 gene product; 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. 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: 176493  Cd Length: 143  Bit Score: 228.93  E-value: 1.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  53 WESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSW 132
Cdd:cd08763     1 WSGPLQFNVHPLCMVLGLVFLCGEALLVYRVFRNETKRSTKILHGLLHIMALVISLVGLVAVFDYHQANGYPDMYSLHSW 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907079826 133 CGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLF 194
Cdd:cd08763    81 CGILTFVLYFLQWLIGFSFFLFPGASFTLRSQYKPLHEFFGRALFLSSVGTSLLGLTEKLLF 142
Cyt_b561_CG1275_like cd08764
Non-vertebrate eumetazoan cytochrome b(561); Cytochrome b(561), as found in non-vertebrate ...
 37-244 3.63e-72

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: 219.89  E-value: 3.63e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  37 VAVTGAWLGLYRGGIAW-ESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVF 115
Cdd:cd08764     1 VVLVGIWLGKFRGGFSWtGPGLQFNWHPLLMVLGLIFLYGNSILVYRVFRNTRKKRLKLLHAVLHLLAFILAVIGLKAVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826 116 DYH--KKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALL 193
Cdd:cd08764    81 DSHnlAKPPIPNMYSLHSWLGLTAVILFSLQWVGGFVSFLFPGLPETLRAAYLPLHVFFGLFIFVLAVATALLGITEKAF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907079826 194 FKLGsKYSTFEPEGVLANVLGLLLVCFGVVVLYILAQADWKRPSQAEEQAL 244
Cdd:cd08764   161 FSLN-KYSNLPAEGVLGNFIGIVLVIFGGLVVYLVTEPDYKRIELPEEEEL 210
Cytochrom_B561 pfam03188
Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport ...
 61-195 1.50e-48

Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport protein. It is an integral membrane protein, that binds two heme groups non-covalently. This is a eukaryotic family. Members of the 'prokaryotic cytochrome b561' family can be found in Pfam: PF01292.


Pssm-ID: 427188  Cd Length: 137  Bit Score: 157.00  E-value: 1.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  61 VHPLCMVIGMIFLQGDALLVYRV--FRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVF 138
Cdd:pfam03188   1 WHPVLMVIGFIFLMGEAILVYRVnsTRRLSKKTKKLLHWILQALALILAVIGLVAVFKFHNLSGIPHFYSLHSWLGLLTV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907079826 139 VLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLFK 195
Cdd:pfam03188  81 ILYALQWVGGFVTFLFPGLSKRIRPLLLPLHVFFGLVIFVLAIVTALLGLLEKLIFQ 137
Cyt_b561 cd08554
Eukaryotic cytochrome b(561); Cytochrome b(561) is a family of endosomal or secretory ...
 58-188 2.58e-46

Eukaryotic cytochrome b(561); Cytochrome b(561) is a family of endosomal or secretory vesicle-specific electron transport proteins. They are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments. This is an exclusively eukaryotic family. Members of the prokaryotic cytochrome b561 family are not deemed homologous.


Pssm-ID: 176489  Cd Length: 131  Bit Score: 150.90  E-value: 2.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  58 QFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILV 137
Cdd:cd08554     1 EFNWHPLLMVIGFVFLMGEALLVYRVFRLLTKRALKLLHAILHLLAFVLGLVGLLAVFLFHNAGGIANLYSLHSWLGLAT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907079826 138 FVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGL 188
Cdd:cd08554    81 VLLFLLQFLSGFVLFLLPLLRLSYRSSLLPFHRFFGLAIFVLAIATILLGI 131
Cyt_b561_ACYB-1_like cd08766
Plant cytochrome b(561), including the carbon monoxide oxygenase ACYB-1; Cytochrome b(561), as ...
 59-194 1.23e-43

Plant cytochrome b(561), including the carbon monoxide oxygenase ACYB-1; Cytochrome b(561), as found in plants, similar to the Arabidopsis thaliana ACYB-1 gene product, a cytochrome b561 isoform localized to the tonoplast. This protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), and might be capable of trans-membrane electron transport from intracellular ascorbate to extracellular ferric chelates. 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: 176496  Cd Length: 144  Bit Score: 144.76  E-value: 1.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  59 FNVHPLCMVIGMIFLQGDALLVYRVFRREaKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVF 138
Cdd:cd08766     8 FNVHPVLMVIGFIFLAGEAILAYKTVPGS-REVQKAVHLTLHLVALVLGIVGIYAAFKFHNEVGIPNLYSLHSWLGIGTI 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907079826 139 VLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLF 194
Cdd:cd08766    87 SLFGLQWLFGFVTFWFPGASRNTRAALLPWHVFLGLAIYYLAIATAETGLLEKLTF 142
Cyt_b561_CYBASC3 cd08762
Vertebrate cytochrome b(561), CYBASC3 gene product; Cytochrome b ascorbate-dependent 3, as ...
 27-196 2.91e-41

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: 140.00  E-value: 2.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  27 AFSQLLGLTVVAVTGAWLGLYRGGIAWE-SSLQFNVHPLCMVIGMIFLQGDALLVYRVFRR--EAKRTTKILHGLLHVFA 103
Cdd:cd08762     2 LLLGILGIACVVLVVHWNQMWRGGFAWDgSSKNFNWHPVLMVTGMVVLYGNAALVYRIPLTwgGPKLPWKLLHAGLLLLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826 104 FIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGT 183
Cdd:cd08762    82 FILTVIGLCAVFNFHNVHHTANLYSLHSWVGICTVALFTCQWVMGFTSFLLPWAPMWLRALVKPIHVFFGAMILVLSIAS 161

                         170
                  ....*....|...
gi 1907079826 184 ALLGLKEALLFKL 196
Cdd:cd08762   162 CISGINEKLFFSL 174
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
 61-188 1.82e-39

Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate for the generation of norepinephrine by dopamine-beta-hydroxylase in the chromaffin vesicles of the adrenal gland. It is a transmembrane heme protein with the two heme groups being bound to conserved histidine residues. A cytochrome b-561 homologue, termed Dcytb, is an iron-regulated ferric reductase in the duodenal mucosa. Other homologues of these are also likely to be ferric reductases. SDR2 is proposed to be important in regulating the metabolism of iron in the onset of neurodegenerative disorders.


Pssm-ID: 214769  Cd Length: 129  Bit Score: 133.51  E-value: 1.82e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826   61 VHPLCMVIGMIFLQGDALLVYR-VFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVFV 139
Cdd:smart00665   1 LHPVLMILGFGFLMGEAILVARpLTRFLSKPTWFLLHVVLQILALVLGVIGLLAIFISHNESGIANFYSLHSWLGLAAFV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907079826  140 LYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGL 188
Cdd:smart00665  81 LAGLQWLSGFLRPLPPGLPSKYRSYLNPYHRFVGLAAFILAIVTIFLGL 129
PLN02810 PLN02810
carbon-monoxide oxygenase
 37-231 1.10e-38

carbon-monoxide oxygenase


Pssm-ID: 178406  Cd Length: 231  Bit Score: 134.95  E-value: 1.10e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  37 VAVTGA-----WLGLYRGGIAWES---SLQFNVHPLCMVIGMIFLQGDALLVYRVFRREaKRTTKILHGLLHVFAFIIAL 108
Cdd:PLN02810   17 LAVIGAimvlvWSIYYRGGLAWEAtnkNLIFNLHPVLMLIGLIIIGGEAIMSYKSLPLK-KEVKKLIHLVLHAIALILGI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826 109 VGLVAVFDYHKKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGL 188
Cdd:PLN02810   96 FGICAAFKNHNESGIANLYSLHSWLGIGIISLYGIQWIYGFIVFFFPGGSTNLRSGSLPWHVLFGLFVYILAVGNAALGF 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907079826 189 KEALLFKLGSKYSTFEPEGVLANVLGLLLVCFGV-VVLYILAQA 231
Cdd:PLN02810  176 LEKLTFLESGGLDKYGSEALLVNFTAIITILYGAfVVLTALAQS 219
PLN02680 PLN02680
carbon-monoxide oxygenase
 16-234 1.24e-38

carbon-monoxide oxygenase


Pssm-ID: 215365  Cd Length: 232  Bit Score: 134.54  E-value: 1.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  16 ASVPAALPYYVAFSQLLGLTVVAVTGAWLGLYRGGIAWES---SLQFNVHPLCMVIGMIFLQGDALLVYRVFRrEAKRTT 92
Cdd:PLN02680    1 MAVPVIRFPIFMLVRLLGVIVAALVLTWTVHYRGGLALSSdnkDLIFNVHPVLMVIGLVLLNGEAMLAYKTVP-GTKNLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  93 KILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFF 172
Cdd:PLN02680   80 KLVHLTLQFLAFCLSLIGVWAALKFHNEKGIDNFYSLHSWLGLACLFLFSLQWAAGFVTFWYPGGSRNSRASLLPWHVFF 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907079826 173 GATIFLFSVGTALLGLKEALLF----KLGSKYSTfepEGVLANVLGLLLVCF-GVVVLYILAQADWK 234
Cdd:PLN02680  160 GIYIYALAVATATTGILEKATFlqsnKVISRYST---EAMLVNSLGILIVVLgGFVILAIVTPLNGK 223
Cyt_b561_CYBRD1 cd08765
Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate ...
 50-198 9.19e-36

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: 124.62  E-value: 9.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  50 GIAWE-SSLQFNVHPLCMVIGMIFLQGDALLVYRV--FRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADL 126
Cdd:cd08765     2 GLGWDgGAAEFNWHPVLMVIGFIFIQGIAIIVYRLpwTWKCSKLLMKLIHAGLHILAFILAIISVVAVFVFHNAKNIPNM 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907079826 127 YSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLFKLGS 198
Cdd:cd08765    82 YSLHSWVGLAAVILYPLQLVLGISVYLLPVAPVRLRAALMPLHVYSGLFIFGTVIATALMGITEKLIFSLKS 153
PLN02351 PLN02351
cytochromes b561 family protein
 15-252 1.53e-21

cytochromes b561 family protein


Pssm-ID: 215201  Cd Length: 242  Bit Score: 89.97  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  15 SASVPAALPYYVAFSQLLGLTVVAVTGAWLGLYRGGIAWESSLQFNV-----HPLCMVIGMIFLQGDALLVYRvFRREAK 89
Cdd:PLN02351    2 ATVDSSSLLPLLLFARLSGLVVAVLVLYWALFFKSSFLPQSTSQEDLvyavlHPLLMVIGFILISGEAILVHR-WLPGSR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  90 RTTKILHGLLHVFAFIIALVGLVAVFdyHKKKG-YADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQ 168
Cdd:PLN02351   81 KTKKSVHLWLQGLALASGVFGIWTKF--HGQDGiVANFYSLHSWMGLICVSLFGAQWLTGFMSFWHRGEMRTTRTTVLPW 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826 169 HIFFGATIFLFSVGTALLGLKEALLFKLGSK-YSTFEPEGVLANVLGLLLVCFGVVVlyILAQADWKRPSQAEEQALSMD 247
Cdd:PLN02351  159 HVFLGLYTYGLAVATAETGLLEKLTFLQTKRnVSKHGSESMVVNGLGLGLALLSGIV--ILAAVLPKYQSHSSKLVYSSQ 236


                  ....*
gi 1907079826 248 FKTLT 252
Cdd:PLN02351  237 DKCLS 241
Cyt_b561_CYB561D2_like cd08761
Eukaryotic cytochrome b(561), including the CYB561D2 gene product; Cytochrome b(561), as found ...
 49-190 3.84e-12

Eukaryotic cytochrome b(561), including the CYB561D2 gene product; Cytochrome b(561), as found in eukaryotes, similar to and including the human CYB561D2 gene product. CYB561D2 is a candidate tumor suppressor. The 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: 176491  Cd Length: 183  Bit Score: 63.08  E-value: 3.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  49 GGIAWESSLQFNVHPLCMVIGMIFLQGDALLVYR---VFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYAD 125
Cdd:cd08761    11 LYIARPGTSLFSWHPLLMSLGFLLLMTEALLLLQptsSLTKLARKTKVRLHWILQLLALLCILAGLVAIYYNKERNGKPH 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907079826 126 LYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLR--SRYRPQHIFFGATIFLFSVGTALLGLKE 190
Cdd:cd08761    91 FTSWHGILGLVTVILIVLQALGGLALLYPPGLRRGESkaKKLKKYHRLSGYVAYLLGLATLVLGLET 157
Cyt_b561_FRRS1_like cd08760
Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in ...
 37-189 1.53e-09

Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in eukaryotes, similar to and including the human FRRS1 gene product (ferric-chelate reductase 1), also called SDR-2 (stromal cell-derived receptor 2). This family comprises a variety of domain architectures, many of which contain dopamine beta-monooxygenase (DOMON) domains. The 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: 176490  Cd Length: 191  Bit Score: 55.81  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907079826  37 VAVTGAWLGLYRGGIAWESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRReAKRTTKILHGLLHVFAFIIALVGLVAVFd 116
Cdd:cd08760    14 SSSGGSPFLLPNGSSVGSSDTLIKAHGVLMAIAWGILMPIGALLARYFLL-GDPVWFYLHAGLQLLAVLLAIAGFVLGI- 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907079826 117 YHKKKGYADLYSLHSWCGILVFVLYFVQWLVGfsfFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLK 189
Cdd:cd08760    92 VLVQGGGGSLNNAHAILGIIVLALAILQPLLG---LLRPHPGSKKRSIWNWAHRWLGRAALILAIVNIFLGLD 161
 
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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