Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 62857218   1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISW 48
Cdd:cd13912  83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130

C-terminal domain of Cytochrome c Oxidase subunit II; 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. It 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 62857218   1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISW 48
Cdd:cd13912  83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130

Cytochrome C oxidase subunit II, periplasmic domain;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 62857218     1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAV 40
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 62857218     1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWIS 50
Cdd:TIGR02866 150 IPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199

C-terminal domain of Cytochrome c Oxidase subunit II; 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. It 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. 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 II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 62857218   1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISW 48
Cdd:cd13912  83 VPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130

cytochrome c oxidase subunit II; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62857218    1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWISNKLNE 55
Cdd:MTH00038 175 VPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229

cytochrome c oxidase subunit II; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62857218    1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWISN 51
Cdd:MTH00140 175 IPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225

cytochrome c oxidase subunit II; Validated

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 62857218    1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWISNKLNE 55
Cdd:MTH00023 186 VPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240

cytochrome c oxidase subunit II; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62857218    1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWISN 51
Cdd:MTH00168 175 VPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225

cytochrome c oxidase subunit II; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 62857218    1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWISNK 52
Cdd:MTH00139 175 VPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226

cytochrome c oxidase subunit II; Validated

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 62857218    1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWISN 51
Cdd:MTH00008 175 VPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225

cytochrome c oxidase subunit II; Validated

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 62857218    1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWIS 50
Cdd:MTH00098 175 IPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224

cytochrome c oxidase subunit II; Provisional

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 62857218    1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNY 45
Cdd:PTZ00047 108 IPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPEAY 152

cytochrome c oxidase subunit II; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 62857218    1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWISNKLN 54
Cdd:MTH00080 178 MSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 62857218     1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISWIS 50
Cdd:TIGR02866 150 IPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 62857218   1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAV 40
Cdd:cd04213  64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 62857218   1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEAVNLSNYISW 48
Cdd:cd13918  91 IPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.

                       10        20        30
               ....*....|....*....|....*....|....*....
gi 62857218  1 VPGRLNQTSLFIKREGIYYGQCSEICGINHGFMPIVVEA 39
Cdd:cd13915 60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98