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cytochrome oxidase subunit III, partial (mitochondrion) [Prolemur simus]
List of domain hits
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Name | Accession | Description | Interval | E-value | ||
Heme_Cu_Oxidase_III_like super family | cl00211 | Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in ... |
1-17 | 7.17e-07 | ||
Heme-copper oxidase subunit III. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which couple the reduction of molecular oxygen to water to, proton pumping across the membrane. The heme-copper oxidase superfamily is diverse in terms of electron donors, subunit composition, and heme types. This superfamily includes cytochrome c and ubiquinol oxidases. Bacterial oxidases typically contain 3 or 4 subunits in contrast to the 13 subunit bovine cytochrome c oxidase (CcO). Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunits I, II and III of ubiquinol oxidase are homologous to the corresponding subunits in CcO. This group additionally contains proteins which are fusions between subunits I and III, such as Sulfolobus acidocaldarius SoxM, a subunit of the SoxM terminal oxidase complex. It also includes NorE which has been speculated to be a subunit of nitric oxide reductase. Some archaebacterial cytochrome oxidases lack subunit III. Although not required for catalytic activity, subunit III is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The actual alignment was detected with superfamily member MTH00118: Pssm-ID: 444752 Cd Length: 261 Bit Score: 41.09 E-value: 7.17e-07
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Name | Accession | Description | Interval | E-value | ||
COX3 | MTH00118 | cytochrome c oxidase subunit III; Provisional |
1-17 | 7.17e-07 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 177179 Cd Length: 261 Bit Score: 41.09 E-value: 7.17e-07
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COX3 | pfam00510 | Cytochrome c oxidase subunit III; |
1-17 | 8.80e-05 | ||
Cytochrome c oxidase subunit III; Pssm-ID: 395410 Cd Length: 258 Bit Score: 35.46 E-value: 8.80e-05
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Cyt_c_Oxidase_III | cd01665 | Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-15 | 1.75e-03 | ||
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme. Pssm-ID: 238834 Cd Length: 243 Bit Score: 31.72 E-value: 1.75e-03
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Name | Accession | Description | Interval | E-value | ||
COX3 | MTH00118 | cytochrome c oxidase subunit III; Provisional |
1-17 | 7.17e-07 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 177179 Cd Length: 261 Bit Score: 41.09 E-value: 7.17e-07
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COX3 | MTH00099 | cytochrome c oxidase subunit III; Validated |
1-17 | 6.03e-06 | ||
cytochrome c oxidase subunit III; Validated Pssm-ID: 177161 Cd Length: 261 Bit Score: 38.55 E-value: 6.03e-06
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COX3 | MTH00130 | cytochrome c oxidase subunit III; Provisional |
1-17 | 1.04e-05 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 177188 Cd Length: 261 Bit Score: 37.82 E-value: 1.04e-05
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COX3 | MTH00075 | cytochrome c oxidase subunit III; Provisional |
1-17 | 1.11e-05 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 177146 Cd Length: 261 Bit Score: 37.80 E-value: 1.11e-05
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COX3 | MTH00189 | cytochrome c oxidase subunit III; Provisional |
1-17 | 3.61e-05 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 177238 Cd Length: 260 Bit Score: 36.49 E-value: 3.61e-05
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COX3 | pfam00510 | Cytochrome c oxidase subunit III; |
1-17 | 8.80e-05 | ||
Cytochrome c oxidase subunit III; Pssm-ID: 395410 Cd Length: 258 Bit Score: 35.46 E-value: 8.80e-05
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COX3 | MTH00039 | cytochrome c oxidase subunit III; Validated |
1-17 | 1.79e-04 | ||
cytochrome c oxidase subunit III; Validated Pssm-ID: 177114 Cd Length: 260 Bit Score: 34.32 E-value: 1.79e-04
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COX3 | MTH00219 | cytochrome c oxidase subunit III; Provisional |
1-17 | 2.19e-04 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 214464 Cd Length: 262 Bit Score: 34.38 E-value: 2.19e-04
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COX3 | MTH00028 | cytochrome c oxidase subunit III; Provisional |
1-17 | 3.80e-04 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 214406 Cd Length: 297 Bit Score: 33.50 E-value: 3.80e-04
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COX3 | MTH00141 | cytochrome c oxidase subunit III; Provisional |
1-17 | 4.18e-04 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 177199 Cd Length: 259 Bit Score: 33.33 E-value: 4.18e-04
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COX3 | MTH00024 | cytochrome c oxidase subunit III; Validated |
1-17 | 8.32e-04 | ||
cytochrome c oxidase subunit III; Validated Pssm-ID: 214403 Cd Length: 261 Bit Score: 32.42 E-value: 8.32e-04
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Cyt_c_Oxidase_III | cd01665 | Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-15 | 1.75e-03 | ||
Cytochrome c oxidase subunit III. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. CcO catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, is believed to play a role in assembly of the multimer complex. Rhodobacter CcO subunit III stabilizes the integrity of the binuclear center in subunit I. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit III contains bound phospholipids in several crystal structures and is proposed to contain a "lipid pool." These phospholipids are believed to intrinsic constituents similar to cofactors of the enzyme. Pssm-ID: 238834 Cd Length: 243 Bit Score: 31.72 E-value: 1.75e-03
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COX3 | MTH00009 | cytochrome c oxidase subunit III; Validated |
1-17 | 3.44e-03 | ||
cytochrome c oxidase subunit III; Validated Pssm-ID: 177101 Cd Length: 259 Bit Score: 30.96 E-value: 3.44e-03
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COX3 | MTH00052 | cytochrome c oxidase subunit III; Provisional |
1-17 | 5.51e-03 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 164623 Cd Length: 262 Bit Score: 30.15 E-value: 5.51e-03
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COX3 | MTH00155 | cytochrome c oxidase subunit III; Provisional |
1-13 | 5.69e-03 | ||
cytochrome c oxidase subunit III; Provisional Pssm-ID: 214439 Cd Length: 255 Bit Score: 30.15 E-value: 5.69e-03
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