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Conserved domains on  [gi|223542283|gb|EEF43825|]
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conserved hypothetical protein [Ricinus communis]

Protein Classification

cytochrome b561 domain-containing protein( domain architecture ID 10171754)

cytochrome b561 domain-containing protein is an integral membrane protein that binds two heme groups non-covalently and may function as a monodehydroascorbate reductase

Gene Ontology:  GO:0140575|GO:0016491|GO:0046872|GO:0020037
PubMed:  16169296

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cyt_b561_FRRS1_like cd08760
Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in ...
 48-236 1.29e-37

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: 130.93  E-value: 1.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223542283  48 NDSFPHGTENGAGTTNLGSWKGKSGSHHRHHFRNAHGILNIIGWGALLPTGVIVARYFKKVPLKceeWYNLHTLCQTSGY 127
Cdd:cd08760    4 SYSLDLASGTSSSGGSPFLLPNGSSVGSSDTLIKAHGVLMAIAWGILMPIGALLARYFLLGDPV---WFYLHAGLQLLAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223542283 128 IVGAVGWGVGLWLGNSSKQHTLKTHRILGIIIFTSATVQMLALCLQPKKDDDYRRYWEIYHQILGYALIAIIIANIFQGV 207
Cdd:cd08760   81 LLAIAGFVLGIVLVQGGGGSLNNAHAILGIIVLALAILQPLLGLLRPHPGSKKRSIWNWAHRWLGRAALILAIVNIFLGL 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 223542283 208 HNQA--HPEKWKWIYVGILVILGGVSLALEI 236
Cdd:cd08760  161 DLAGagTPKAWKIAYGVVVAVLALVYLILEI 191
 
Name Accession Description Interval E-value
Cyt_b561_FRRS1_like cd08760
Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in ...
 48-236 1.29e-37

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: 130.93  E-value: 1.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223542283  48 NDSFPHGTENGAGTTNLGSWKGKSGSHHRHHFRNAHGILNIIGWGALLPTGVIVARYFKKVPLKceeWYNLHTLCQTSGY 127
Cdd:cd08760    4 SYSLDLASGTSSSGGSPFLLPNGSSVGSSDTLIKAHGVLMAIAWGILMPIGALLARYFLLGDPV---WFYLHAGLQLLAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223542283 128 IVGAVGWGVGLWLGNSSKQHTLKTHRILGIIIFTSATVQMLALCLQPKKDDDYRRYWEIYHQILGYALIAIIIANIFQGV 207
Cdd:cd08760   81 LLAIAGFVLGIVLVQGGGGSLNNAHAILGIIVLALAILQPLLGLLRPHPGSKKRSIWNWAHRWLGRAALILAIVNIFLGL 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 223542283 208 HNQA--HPEKWKWIYVGILVILGGVSLALEI 236
Cdd:cd08760  161 DLAGagTPKAWKIAYGVVVAVLALVYLILEI 191
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
 83-193 3.87e-20

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: 83.43  E-value: 3.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223542283    83 HGILNIIGWGALLPTGVIVARYfKKVPLKCEEWYNLHTLCQTSGYIVGAVGWGVGLWLGNSSK-QHTLKTHRILGIIIFT 161
Cdd:smart00665   2 HPVLMILGFGFLMGEAILVARP-LTRFLSKPTWFLLHVVLQILALVLGVIGLLAIFISHNESGiANFYSLHSWLGLAAFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 223542283   162 SATVQMLA---LCLQPKKDDDYRRYWEIYHQILGY 193
Cdd:smart00665  81 LAGLQWLSgflRPLPPGLPSKYRSYLNPYHRFVGL 115
 
Name Accession Description Interval E-value
Cyt_b561_FRRS1_like cd08760
Eukaryotic cytochrome b(561), including the FRRS1 gene product; Cytochrome b(561), as found in ...
 48-236 1.29e-37

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: 130.93  E-value: 1.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223542283  48 NDSFPHGTENGAGTTNLGSWKGKSGSHHRHHFRNAHGILNIIGWGALLPTGVIVARYFKKVPLKceeWYNLHTLCQTSGY 127
Cdd:cd08760    4 SYSLDLASGTSSSGGSPFLLPNGSSVGSSDTLIKAHGVLMAIAWGILMPIGALLARYFLLGDPV---WFYLHAGLQLLAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223542283 128 IVGAVGWGVGLWLGNSSKQHTLKTHRILGIIIFTSATVQMLALCLQPKKDDDYRRYWEIYHQILGYALIAIIIANIFQGV 207
Cdd:cd08760   81 LLAIAGFVLGIVLVQGGGGSLNNAHAILGIIVLALAILQPLLGLLRPHPGSKKRSIWNWAHRWLGRAALILAIVNIFLGL 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 223542283 208 HNQA--HPEKWKWIYVGILVILGGVSLALEI 236
Cdd:cd08760  161 DLAGagTPKAWKIAYGVVVAVLALVYLILEI 191
B561 smart00665
Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ...
 83-193 3.87e-20

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: 83.43  E-value: 3.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 223542283    83 HGILNIIGWGALLPTGVIVARYfKKVPLKCEEWYNLHTLCQTSGYIVGAVGWGVGLWLGNSSK-QHTLKTHRILGIIIFT 161
Cdd:smart00665   2 HPVLMILGFGFLMGEAILVARP-LTRFLSKPTWFLLHVVLQILALVLGVIGLLAIFISHNESGiANFYSLHSWLGLAAFV 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 223542283   162 SATVQMLA---LCLQPKKDDDYRRYWEIYHQILGY 193
Cdd:smart00665  81 LAGLQWLSgflRPLPPGLPSKYRSYLNPYHRFVGL 115
 
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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