knickkopf [Drosophila melanogaster]
Protein Classification
cytochrome and DOMON domain-containing protein( domain architecture ID 11274691)
cytochrome and DOMON domain-containing protein may bind heme and participate in electron transport reactions
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| DM13 | smart00686 | Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ... |
166-272 | 4.06e-47 | ||||
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9; : Pssm-ID: 128929 Cd Length: 108 Bit Score: 161.76 E-value: 4.06e-47
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| DM13 | smart00686 | Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ... |
51-156 | 1.52e-45 | ||||
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9; : Pssm-ID: 128929 Cd Length: 108 Bit Score: 157.52 E-value: 1.52e-45
|
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| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
292-454 | 1.48e-30 | ||||
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: 117.14 E-value: 1.48e-30
|
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| Name | Accession | Description | Interval | E-value | ||||
| DM13 | smart00686 | Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ... |
166-272 | 4.06e-47 | ||||
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9; Pssm-ID: 128929 Cd Length: 108 Bit Score: 161.76 E-value: 4.06e-47
|
||||||||
| DM13 | smart00686 | Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ... |
51-156 | 1.52e-45 | ||||
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9; Pssm-ID: 128929 Cd Length: 108 Bit Score: 157.52 E-value: 1.52e-45
|
||||||||
| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
292-454 | 1.48e-30 | ||||
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: 117.14 E-value: 1.48e-30
|
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| DM13 | pfam10517 | Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ... |
48-149 | 4.56e-28 | ||||
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme. Pssm-ID: 463130 Cd Length: 105 Bit Score: 108.49 E-value: 4.56e-28
|
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| DOMON_DOH | cd09631 | DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ... |
290-442 | 2.11e-25 | ||||
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: 102.20 E-value: 2.11e-25
|
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| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
295-425 | 3.40e-24 | ||||
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: 97.82 E-value: 3.40e-24
|
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| DM13 | pfam10517 | Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ... |
163-265 | 4.27e-24 | ||||
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme. Pssm-ID: 463130 Cd Length: 105 Bit Score: 97.32 E-value: 4.27e-24
|
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| Name | Accession | Description | Interval | E-value | ||||
| DM13 | smart00686 | Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ... |
166-272 | 4.06e-47 | ||||
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9; Pssm-ID: 128929 Cd Length: 108 Bit Score: 161.76 E-value: 4.06e-47
|
||||||||
| DM13 | smart00686 | Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis ... |
51-156 | 1.52e-45 | ||||
Domain present in fly proteins (CG14681, CG12492, CG6217), worm H06A10.1 and Arabidopsis thaliana MBG8.9; Pssm-ID: 128929 Cd Length: 108 Bit Score: 157.52 E-value: 1.52e-45
|
||||||||
| DoH | smart00664 | Possible catecholamine-binding domain present in a variety of eukaryotic proteins; A ... |
292-454 | 1.48e-30 | ||||
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: 117.14 E-value: 1.48e-30
|
||||||||
| DM13 | pfam10517 | Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ... |
48-149 | 4.56e-28 | ||||
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme. Pssm-ID: 463130 Cd Length: 105 Bit Score: 108.49 E-value: 4.56e-28
|
||||||||
| DOMON_DOH | cd09631 | DOMON-like domain of copper-dependent monooxygenases and related proteins; This diverse family ... |
290-442 | 2.11e-25 | ||||
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: 102.20 E-value: 2.11e-25
|
||||||||
| DOMON | pfam03351 | DOMON domain; The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 ... |
295-425 | 3.40e-24 | ||||
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: 97.82 E-value: 3.40e-24
|
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| DM13 | pfam10517 | Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system ... |
163-265 | 4.27e-24 | ||||
Electron transfer DM13; The DM13 domain is a component of a novel electron-transfer system potentially involved in oxidative modification of animal cell-surface proteins. It contains a nearly absolutely conserved cysteine, which could be involved in a redox reaction, either as a naked thiol group or through binding a prosthetic group like heme. Pssm-ID: 463130 Cd Length: 105 Bit Score: 97.32 E-value: 4.27e-24
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| Blast search parameters | ||||
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