DOMON domain-containing protein [Caenorhabditis elegans]
Protein Classification
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 ... |
718-931 | 7.68e-46 | ||||
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: 163.28 E-value: 7.68e-46
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| DOMON_SDR_2_like | cd09628 | DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ... |
193-367 | 2.24e-35 | ||||
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. : Pssm-ID: 187686 Cd Length: 169 Bit Score: 132.17 E-value: 2.24e-35
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
398-555 | 7.25e-25 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). : Pssm-ID: 214768 Cd Length: 148 Bit Score: 101.35 E-value: 7.25e-25
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
605-752 | 5.43e-24 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). : Pssm-ID: 214768 Cd Length: 148 Bit Score: 99.03 E-value: 5.43e-24
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
65-192 | 1.95e-20 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). : Pssm-ID: 214768 Cd Length: 148 Bit Score: 88.63 E-value: 1.95e-20
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| 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 ... |
718-931 | 7.68e-46 | ||||
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: 163.28 E-value: 7.68e-46
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| B561 | smart00665 | Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ... |
768-899 | 2.62e-36 | ||||
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: 2.62e-36
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| DOMON_SDR_2_like | cd09628 | DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ... |
193-367 | 2.24e-35 | ||||
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187686 Cd Length: 169 Bit Score: 132.17 E-value: 2.24e-35
|
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
398-555 | 7.25e-25 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). Pssm-ID: 214768 Cd Length: 148 Bit Score: 101.35 E-value: 7.25e-25
|
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
605-752 | 5.43e-24 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). Pssm-ID: 214768 Cd Length: 148 Bit Score: 99.03 E-value: 5.43e-24
|
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
217-365 | 2.58e-23 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). Pssm-ID: 214768 Cd Length: 148 Bit Score: 97.11 E-value: 2.58e-23
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| DOMON_SDR_2_like | cd09628 | DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ... |
376-544 | 5.48e-22 | ||||
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187686 Cd Length: 169 Bit Score: 94.03 E-value: 5.48e-22
|
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| DOMON_SDR_2_like | cd09628 | DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ... |
584-747 | 8.47e-22 | ||||
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187686 Cd Length: 169 Bit Score: 93.26 E-value: 8.47e-22
|
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
65-192 | 1.95e-20 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). Pssm-ID: 214768 Cd Length: 148 Bit Score: 88.63 E-value: 1.95e-20
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| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
401-524 | 7.02e-20 | ||||
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families. Pssm-ID: 460893 [Multi-domain] Cd Length: 116 Bit Score: 85.87 E-value: 7.02e-20
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| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
223-347 | 1.80e-18 | ||||
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families. Pssm-ID: 460893 [Multi-domain] Cd Length: 116 Bit Score: 82.02 E-value: 1.80e-18
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| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
605-726 | 3.41e-17 | ||||
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families. Pssm-ID: 460893 [Multi-domain] Cd Length: 116 Bit Score: 78.56 E-value: 3.41e-17
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| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
58-163 | 1.63e-16 | ||||
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families. Pssm-ID: 460893 [Multi-domain] Cd Length: 116 Bit Score: 76.63 E-value: 1.63e-16
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| DOMON_SDR_2_like | cd09628 | DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ... |
67-182 | 5.68e-11 | ||||
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187686 Cd Length: 169 Bit Score: 62.06 E-value: 5.68e-11
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| Cytochrom_B561 | pfam03188 | Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport ... |
768-897 | 2.38e-06 | ||||
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: 47.99 E-value: 2.38e-06
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| ProP | COG0477 | MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and ... |
747-932 | 1.16e-04 | ||||
MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and metabolism, Amino acid transport and metabolism, Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 440245 [Multi-domain] Cd Length: 295 Bit Score: 45.19 E-value: 1.16e-04
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| 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 ... |
718-931 | 7.68e-46 | ||||
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: 163.28 E-value: 7.68e-46
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| B561 | smart00665 | Cytochrome b-561 / ferric reductase transmembrane domain; Cytochrome b-561 recycles ascorbate ... |
768-899 | 2.62e-36 | ||||
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: 2.62e-36
|
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| DOMON_SDR_2_like | cd09628 | DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ... |
193-367 | 2.24e-35 | ||||
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187686 Cd Length: 169 Bit Score: 132.17 E-value: 2.24e-35
|
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
398-555 | 7.25e-25 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). Pssm-ID: 214768 Cd Length: 148 Bit Score: 101.35 E-value: 7.25e-25
|
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
605-752 | 5.43e-24 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). Pssm-ID: 214768 Cd Length: 148 Bit Score: 99.03 E-value: 5.43e-24
|
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
217-365 | 2.58e-23 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). Pssm-ID: 214768 Cd Length: 148 Bit Score: 97.11 E-value: 2.58e-23
|
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| DOMON_SDR_2_like | cd09628 | DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ... |
376-544 | 5.48e-22 | ||||
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187686 Cd Length: 169 Bit Score: 94.03 E-value: 5.48e-22
|
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| DOMON_SDR_2_like | cd09628 | DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ... |
584-747 | 8.47e-22 | ||||
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187686 Cd Length: 169 Bit Score: 93.26 E-value: 8.47e-22
|
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
65-192 | 1.95e-20 | ||||
Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press). Pssm-ID: 214768 Cd Length: 148 Bit Score: 88.63 E-value: 1.95e-20
|
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| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
401-524 | 7.02e-20 | ||||
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families. Pssm-ID: 460893 [Multi-domain] Cd Length: 116 Bit Score: 85.87 E-value: 7.02e-20
|
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| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
223-347 | 1.80e-18 | ||||
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families. Pssm-ID: 460893 [Multi-domain] Cd Length: 116 Bit Score: 82.02 E-value: 1.80e-18
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| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
605-726 | 3.41e-17 | ||||
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families. Pssm-ID: 460893 [Multi-domain] Cd Length: 116 Bit Score: 78.56 E-value: 3.41e-17
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| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
58-163 | 1.63e-16 | ||||
DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families. Pssm-ID: 460893 [Multi-domain] Cd Length: 116 Bit Score: 76.63 E-value: 1.63e-16
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| Cyt_b561_CYB561D2_like | cd08761 | Eukaryotic cytochrome b(561), including the CYB561D2 gene product; Cytochrome b(561), as found ... |
762-927 | 1.08e-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: 67.70 E-value: 1.08e-12
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| Cyt_b561 | cd08554 | Eukaryotic cytochrome b(561); Cytochrome b(561) is a family of endosomal or secretory ... |
768-897 | 2.92e-11 | ||||
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: 61.92 E-value: 2.92e-11
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| DOMON_SDR_2_like | cd09628 | DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related ... |
67-182 | 5.68e-11 | ||||
DOMON domain of stromal cell-derived receptor 2 (ferric chelate reductase 1) and related proteins; Stromal cell-derived receptor 2 (or ferric chelate reductase 1) reduces Fe(3+) to Fe(2+) ahead of iron transport from the endosome to the cytoplasm. This transmembrane protein is a member of the cytochrome b561 family and contains a DOMON domain which may bind to heme or another ligand. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187686 Cd Length: 169 Bit Score: 62.06 E-value: 5.68e-11
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| Cytochrom_B561 | pfam03188 | Eukaryotic cytochrome b561; Cytochrome b561 is a secretory vesicle-specific electron transport ... |
768-897 | 2.38e-06 | ||||
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: 47.99 E-value: 2.38e-06
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| DOMON_DOH | cd09631 | DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ... |
396-545 | 3.60e-05 | ||||
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family characterizes DOMON domains found in dopamine beta-hydroxylase (DBH), monooxygenase X (MOX), and various other proteins, some of which contain DOMON domains exclusively; the family is not restricted to eukaryotes. DBH is a membrane-bound enzyme that converts dopamine to L-norepinephrine, and plays a central role in the metabolism of catecholamine neurotransmitters. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187689 Cd Length: 138 Bit Score: 44.80 E-value: 3.60e-05
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| ProP | COG0477 | MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and ... |
747-932 | 1.16e-04 | ||||
MFS family permease, includes anhydromuropeptide permease AmpG [Carbohydrate transport and metabolism, Amino acid transport and metabolism, Inorganic ion transport and metabolism, General function prediction only]; Pssm-ID: 440245 [Multi-domain] Cd Length: 295 Bit Score: 45.19 E-value: 1.16e-04
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| DOMON_DOH | cd09631 | DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ... |
605-743 | 2.25e-03 | ||||
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family characterizes DOMON domains found in dopamine beta-hydroxylase (DBH), monooxygenase X (MOX), and various other proteins, some of which contain DOMON domains exclusively; the family is not restricted to eukaryotes. DBH is a membrane-bound enzyme that converts dopamine to L-norepinephrine, and plays a central role in the metabolism of catecholamine neurotransmitters. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187689 Cd Length: 138 Bit Score: 39.41 E-value: 2.25e-03
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| DOMON_DOH | cd09631 | DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ... |
212-266 | 6.68e-03 | ||||
DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family characterizes DOMON domains found in dopamine beta-hydroxylase (DBH), monooxygenase X (MOX), and various other proteins, some of which contain DOMON domains exclusively; the family is not restricted to eukaryotes. DBH is a membrane-bound enzyme that converts dopamine to L-norepinephrine, and plays a central role in the metabolism of catecholamine neurotransmitters. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases. Pssm-ID: 187689 Cd Length: 138 Bit Score: 38.25 E-value: 6.68e-03
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