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Conserved domains on  [gi|25453427|sp|Q60720|]
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RecName: Full=Transmembrane ascorbate-dependent reductase CYB561; AltName: Full=Chromaffin granule Cyt b561; Short=CGCytb; AltName: Full=Cytochrome b-561; AltName: Full=Cytochrome b561

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 ...
 43-184 4.96e-77

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: 229.32  E-value: 4.96e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  43 WESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSW 122
Cdd:cd08763   1 WSGPLQFNVHPLCMVLGLVFLCGEALLVYRVFRNETKRSTKILHGLLHIMALVISLVGLVAVFDYHQANGYPDMYSLHSW 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453427 123 CGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLF 184
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, ...
 43-184 4.96e-77

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: 229.32  E-value: 4.96e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  43 WESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSW 122
Cdd:cd08763   1 WSGPLQFNVHPLCMVLGLVFLCGEALLVYRVFRNETKRSTKILHGLLHIMALVISLVGLVAVFDYHQANGYPDMYSLHSW 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453427 123 CGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLF 184
Cdd:cd08763  81 CGILTFVLYFLQWLIGFSFFLFPGASFTLRSQYKPLHEFFGRALFLSSVGTSLLGLTEKLLF 142
Cytochrom_B561 pfam03188
Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport ...
 51-185 4.95e-49

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: 157.77  E-value: 4.95e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427    51 VHPLCMVIGMIFLQGDALLVYRV--FRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVF 128
Cdd:pfam03188   1 WHPVLMVIGFIFLMGEAILVYRVnsTRRLSKKTKKLLHWILQALALILAVIGLVAVFKFHNLSGIPHFYSLHSWLGLLTV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 25453427   129 VLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLFK 185
Cdd:pfam03188  81 ILYALQWVGGFVTFLFPGLSKRIRPLLLPLHVFFGLVIFVLAIVTALLGLLEKLIFQ 137
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
 51-178 5.74e-40

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: 134.28  E-value: 5.74e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427     51 VHPLCMVIGMIFLQGDALLVYR-VFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVFV 129
Cdd:smart00665   1 LHPVLMILGFGFLMGEAILVARpLTRFLSKPTWFLLHVVLQILALVLGVIGLLAIFISHNESGIANFYSLHSWLGLAAFV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 25453427    130 LYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGL 178
Cdd:smart00665  81 LAGLQWLSGFLRPLPPGLPSKYRSYLNPYHRFVGLAAFILAIVTIFLGL 129
PLN02680 PLN02680
carbon-monoxide oxygenase
 6-224 7.08e-39

carbon-monoxide oxygenase


Pssm-ID: 215365  Cd Length: 232  Bit Score: 134.93  E-value: 7.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427    6 ASVPAALPYYVAFSQLLGLTVVAVTGAWLGLYRGGIAWES---SLQFNVHPLCMVIGMIFLQGDALLVYRVFRrEAKRTT 82
Cdd:PLN02680   1 MAVPVIRFPIFMLVRLLGVIVAALVLTWTVHYRGGLALSSdnkDLIFNVHPVLMVIGLVLLNGEAMLAYKTVP-GTKNLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427   83 KILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFF 162
Cdd:PLN02680  80 KLVHLTLQFLAFCLSLIGVWAALKFHNEKGIDNFYSLHSWLGLACLFLFSLQWAAGFVTFWYPGGSRNSRASLLPWHVFF 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453427  163 GATIFLFSVGTALLGLKEALLF----KLGSKYSTfepEGVLANVLGLLLVCF-GVVVLYILAQADWK 224
Cdd:PLN02680 160 GIYIYALAVATATTGILEKATFlqsnKVISRYST---EAMLVNSLGILIVVLgGFVILAIVTPLNGK 223
 
Name Accession Description Interval E-value
Cyt_b561_CYB561 cd08763
Vertebrate cytochrome b(561), CYB561 gene product; Cytochrome b(561), as found in vertebrates, ...
 43-184 4.96e-77

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: 229.32  E-value: 4.96e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  43 WESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSW 122
Cdd:cd08763   1 WSGPLQFNVHPLCMVLGLVFLCGEALLVYRVFRNETKRSTKILHGLLHIMALVISLVGLVAVFDYHQANGYPDMYSLHSW 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453427 123 CGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLF 184
Cdd:cd08763  81 CGILTFVLYFLQWLIGFSFFLFPGASFTLRSQYKPLHEFFGRALFLSSVGTSLLGLTEKLLF 142
Cyt_b561_CG1275_like cd08764
Non-vertebrate eumetazoan cytochrome b(561); Cytochrome b(561), as found in non-vertebrate ...
 27-234 2.50e-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: 2.50e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  27 VAVTGAWLGLYRGGIAW-ESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVF 105
Cdd:cd08764   1 VVLVGIWLGKFRGGFSWtGPGLQFNWHPLLMVLGLIFLYGNSILVYRVFRNTRKKRLKLLHAVLHLLAFILAVIGLKAVF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427 106 DYH--KKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALL 183
Cdd:cd08764  81 DSHnlAKPPIPNMYSLHSWLGLTAVILFSLQWVGGFVSFLFPGLPETLRAAYLPLHVFFGLFIFVLAVATALLGITEKAF 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 25453427 184 FKLGsKYSTFEPEGVLANVLGLLLVCFGVVVLYILAQADWKRPSQAEEQAL 234
Cdd:cd08764 161 FSLN-KYSNLPAEGVLGNFIGIVLVIFGGLVVYLVTEPDYKRIELPEEEEL 210
Cytochrom_B561 pfam03188
Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport ...
 51-185 4.95e-49

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: 157.77  E-value: 4.95e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427    51 VHPLCMVIGMIFLQGDALLVYRV--FRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVF 128
Cdd:pfam03188   1 WHPVLMVIGFIFLMGEAILVYRVnsTRRLSKKTKKLLHWILQALALILAVIGLVAVFKFHNLSGIPHFYSLHSWLGLLTV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 25453427   129 VLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLFK 185
Cdd:pfam03188  81 ILYALQWVGGFVTFLFPGLSKRIRPLLLPLHVFFGLVIFVLAIVTALLGLLEKLIFQ 137
Cyt_b561 cd08554
Eukaryotic cytochrome b(561); Cytochrome b(561) is a family of endosomal or secretory ...
 48-178 7.86e-47

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: 152.05  E-value: 7.86e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  48 QFNVHPLCMVIGMIFLQGDALLVYRVFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILV 127
Cdd:cd08554   1 EFNWHPLLMVIGFVFLMGEALLVYRVFRLLTKRALKLLHAILHLLAFVLGLVGLLAVFLFHNAGGIANLYSLHSWLGLAT 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 25453427 128 FVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGL 178
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 ...
 49-184 8.99e-44

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: 8.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  49 FNVHPLCMVIGMIFLQGDALLVYRVFRREaKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVF 128
Cdd:cd08766   8 FNVHPVLMVIGFIFLAGEAILAYKTVPGS-REVQKAVHLTLHLVALVLGIVGIYAAFKFHNEVGIPNLYSLHSWLGIGTI 86

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 25453427 129 VLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLF 184
Cdd:cd08766  87 SLFGLQWLFGFVTFWFPGASRNTRAALLPWHVFLGLAIYYLAIATAETGLLEKLTF 142
Cyt_b561_CYBASC3 cd08762
Vertebrate cytochrome b(561), CYBASC3 gene product; Cytochrome b ascorbate-dependent 3, as ...
 17-186 6.73e-42

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: 141.16  E-value: 6.73e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  17 AFSQLLGLTVVAVTGAWLGLYRGGIAWE-SSLQFNVHPLCMVIGMIFLQGDALLVYRVFRR--EAKRTTKILHGLLHVFA 93
Cdd:cd08762   2 LLLGILGIACVVLVVHWNQMWRGGFAWDgSSKNFNWHPVLMVTGMVVLYGNAALVYRIPLTwgGPKLPWKLLHAGLLLLA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  94 FIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGT 173
Cdd:cd08762  82 FILTVIGLCAVFNFHNVHHTANLYSLHSWVGICTVALFTCQWVMGFTSFLLPWAPMWLRALVKPIHVFFGAMILVLSIAS 161

                       170
                ....*....|...
gi 25453427 174 ALLGLKEALLFKL 186
Cdd:cd08762 162 CISGINEKLFFSL 174
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
 51-178 5.74e-40

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: 134.28  E-value: 5.74e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427     51 VHPLCMVIGMIFLQGDALLVYR-VFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVFV 129
Cdd:smart00665   1 LHPVLMILGFGFLMGEAILVARpLTRFLSKPTWFLLHVVLQILALVLGVIGLLAIFISHNESGIANFYSLHSWLGLAAFV 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 25453427    130 LYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGL 178
Cdd:smart00665  81 LAGLQWLSGFLRPLPPGLPSKYRSYLNPYHRFVGLAAFILAIVTIFLGL 129
PLN02680 PLN02680
carbon-monoxide oxygenase
 6-224 7.08e-39

carbon-monoxide oxygenase


Pssm-ID: 215365  Cd Length: 232  Bit Score: 134.93  E-value: 7.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427    6 ASVPAALPYYVAFSQLLGLTVVAVTGAWLGLYRGGIAWES---SLQFNVHPLCMVIGMIFLQGDALLVYRVFRrEAKRTT 82
Cdd:PLN02680   1 MAVPVIRFPIFMLVRLLGVIVAALVLTWTVHYRGGLALSSdnkDLIFNVHPVLMVIGLVLLNGEAMLAYKTVP-GTKNLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427   83 KILHGLLHVFAFIIALVGLVAVFDYHKKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFF 162
Cdd:PLN02680  80 KLVHLTLQFLAFCLSLIGVWAALKFHNEKGIDNFYSLHSWLGLACLFLFSLQWAAGFVTFWYPGGSRNSRASLLPWHVFF 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453427  163 GATIFLFSVGTALLGLKEALLF----KLGSKYSTfepEGVLANVLGLLLVCF-GVVVLYILAQADWK 224
Cdd:PLN02680 160 GIYIYALAVATATTGILEKATFlqsnKVISRYST---EAMLVNSLGILIVVLgGFVILAIVTPLNGK 223
PLN02810 PLN02810
carbon-monoxide oxygenase
 27-221 1.09e-38

carbon-monoxide oxygenase


Pssm-ID: 178406  Cd Length: 231  Bit Score: 134.56  E-value: 1.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427   27 VAVTGA-----WLGLYRGGIAWES---SLQFNVHPLCMVIGMIFLQGDALLVYRVFRREaKRTTKILHGLLHVFAFIIAL 98
Cdd:PLN02810  17 LAVIGAimvlvWSIYYRGGLAWEAtnkNLIFNLHPVLMLIGLIIIGGEAIMSYKSLPLK-KEVKKLIHLVLHAIALILGI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427   99 VGLVAVFDYHKKKGYADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGL 178
Cdd:PLN02810  96 FGICAAFKNHNESGIANLYSLHSWLGIGIISLYGIQWIYGFIVFFFPGGSTNLRSGSLPWHVLFGLFVYILAVGNAALGF 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 25453427  179 KEALLFKLGSKYSTFEPEGVLANVLGLLLVCFGV-VVLYILAQA 221
Cdd:PLN02810 176 LEKLTFLESGGLDKYGSEALLVNFTAIITILYGAfVVLTALAQS 219
Cyt_b561_CYBRD1 cd08765
Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate ...
 40-188 5.13e-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: 125.01  E-value: 5.13e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  40 GIAWE-SSLQFNVHPLCMVIGMIFLQGDALLVYRV--FRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYADL 116
Cdd:cd08765   2 GLGWDgGAAEFNWHPVLMVIGFIFIQGIAIIVYRLpwTWKCSKLLMKLIHAGLHILAFILAIISVVAVFVFHNAKNIPNM 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25453427 117 YSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLKEALLFKLGS 188
Cdd:cd08765  82 YSLHSWVGLAAVILYPLQLVLGISVYLLPVAPVRLRAALMPLHVYSGLFIFGTVIATALMGITEKLIFSLKS 153
PLN02351 PLN02351
cytochromes b561 family protein
 5-242 7.25e-22

cytochromes b561 family protein


Pssm-ID: 215201  Cd Length: 242  Bit Score: 90.74  E-value: 7.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427    5 SASVPAALPYYVAFSQLLGLTVVAVTGAWLGLYRGGIAWESSLQFNV-----HPLCMVIGMIFLQGDALLVYRvFRREAK 79
Cdd:PLN02351   2 ATVDSSSLLPLLLFARLSGLVVAVLVLYWALFFKSSFLPQSTSQEDLvyavlHPLLMVIGFILISGEAILVHR-WLPGSR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427   80 RTTKILHGLLHVFAFIIALVGLVAVFdyHKKKG-YADLYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLRSRYRPQ 158
Cdd:PLN02351  81 KTKKSVHLWLQGLALASGVFGIWTKF--HGQDGiVANFYSLHSWMGLICVSLFGAQWLTGFMSFWHRGEMRTTRTTVLPW 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  159 HIFFGATIFLFSVGTALLGLKEALLFKLGSK-YSTFEPEGVLANVLGLLLVCFGVVVlyILAQADWKRPSQAEEQALSMD 237
Cdd:PLN02351 159 HVFLGLYTYGLAVATAETGLLEKLTFLQTKRnVSKHGSESMVVNGLGLGLALLSGIV--ILAAVLPKYQSHSSKLVYSSQ 236


                 ....*
gi 25453427  238 FKTLT 242
Cdd:PLN02351 237 DKCLS 241
Cyt_b561_CYB561D2_like cd08761
Eukaryotic cytochrome b(561), including the CYB561D2 gene product; Cytochrome b(561), as found ...
 39-180 2.36e-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: 63.46  E-value: 2.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  39 GGIAWESSLQFNVHPLCMVIGMIFLQGDALLVYR---VFRREAKRTTKILHGLLHVFAFIIALVGLVAVFDYHKKKGYAD 115
Cdd:cd08761  11 LYIARPGTSLFSWHPLLMSLGFLLLMTEALLLLQptsSLTKLARKTKVRLHWILQLLALLCILAGLVAIYYNKERNGKPH 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25453427 116 LYSLHSWCGILVFVLYFVQWLVGFSFFLFPGASFSLR--SRYRPQHIFFGATIFLFSVGTALLGLKE 180
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 ...
 27-179 1.26e-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: 56.20  E-value: 1.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25453427  27 VAVTGAWLGLYRGGIAWESSLQFNVHPLCMVIGMIFLQGDALLVYRVFRReAKRTTKILHGLLHVFAFIIALVGLVAVFd 106
Cdd:cd08760  14 SSSGGSPFLLPNGSSVGSSDTLIKAHGVLMAIAWGILMPIGALLARYFLL-GDPVWFYLHAGLQLLAVLLAIAGFVLGI- 91

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25453427 107 YHKKKGYADLYSLHSWCGILVFVLYFVQWLVGfsfFLFPGASFSLRSRYRPQHIFFGATIFLFSVGTALLGLK 179
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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