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Conserved domains on  [gi|2018442087|gb|QTG58683|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Neduba ambagiosa x Neduba carinata]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-117 3.91e-86

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 249.75  E-value: 3.91e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   1 DFSTpYEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPG 80
Cdd:MTH00154  112 DFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPG 190

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2018442087  81 IFFGQCSEICGANHSFMPIVIESVNTKTFIKWINSML 117
Cdd:MTH00154  191 LFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-117 3.91e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 249.75  E-value: 3.91e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   1 DFSTpYEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPG 80
Cdd:MTH00154  112 DFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPG 190

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2018442087  81 IFFGQCSEICGANHSFMPIVIESVNTKTFIKWINSML 117
Cdd:MTH00154  191 LFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 1-112 3.23e-74

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.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 216.28  E-value: 3.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   1 DFSTpYEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPG 80
Cdd:cd13912    20 DFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPG 98

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2018442087  81 IFFGQCSEICGANHSFMPIVIESVNTKTFIKW 112
Cdd:cd13912    99 VYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
7-104 3.13e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 193.01  E-value: 3.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   7 EFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQC 86
Cdd:pfam00116  23 EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQC 102

                          90
                  ....*....|....*...
gi 2018442087  87 SEICGANHSFMPIVIESV 104
Cdd:pfam00116 103 SEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
27-120 2.42e-34

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 118.39  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087  27 DVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFMPIVIESVNT 106
Cdd:COG1622   134 ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213

                          90
                  ....*....|....
gi 2018442087 107 KTFIKWINSMLQAS 120
Cdd:COG1622   214 EEFDAWLAEQKASA 227
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 28-114 8.82e-29

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]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 103.23  E-value: 8.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087  28 VDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTK 107
Cdd:TIGR02866 113 TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKE 192


                  ....*..
gi 2018442087 108 TFIKWIN 114
Cdd:TIGR02866 193 EFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-117 3.91e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 249.75  E-value: 3.91e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   1 DFSTpYEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPG 80
Cdd:MTH00154  112 DFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPG 190

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2018442087  81 IFFGQCSEICGANHSFMPIVIESVNTKTFIKWINSML 117
Cdd:MTH00154  191 LFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 1-112 3.23e-74

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.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 216.28  E-value: 3.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   1 DFSTpYEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPG 80
Cdd:cd13912    20 DFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPG 98

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2018442087  81 IFFGQCSEICGANHSFMPIVIESVNTKTFIKW 112
Cdd:cd13912    99 VYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 6-116 4.31e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 211.72  E-value: 4.31e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   6 YEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQ 85
Cdd:MTH00140  116 IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQ 195

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2018442087  86 CSEICGANHSFMPIVIESVNTKTFIKWINSM 116
Cdd:MTH00140  196 CSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 7-117 1.78e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 210.16  E-value: 1.78e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   7 EFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQC 86
Cdd:MTH00117  117 SFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQC 196

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2018442087  87 SEICGANHSFMPIVIESVNTKTFIKWINSML 117
Cdd:MTH00117  197 SEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 7-116 6.15e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 201.10  E-value: 6.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   7 EFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQC 86
Cdd:MTH00139  117 SFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQC 196

                          90       100       110
                  ....*....|....*....|....*....|
gi 2018442087  87 SEICGANHSFMPIVIESVNTKTFIKWINSM 116
Cdd:MTH00139  197 SEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 6-115 2.04e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 199.82  E-value: 2.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   6 YEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQ 85
Cdd:MTH00168  116 LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQ 195

                          90       100       110
                  ....*....|....*....|....*....|
gi 2018442087  86 CSEICGANHSFMPIVIESVNTKTFIKWINS 115
Cdd:MTH00168  196 CSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-115 1.25e-65

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 198.16  E-value: 1.25e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   1 DFSTpYEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPG 80
Cdd:MTH00008  112 DFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPG 190

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2018442087  81 IFFGQCSEICGANHSFMPIVIESVNTKTFIKWINS 115
Cdd:MTH00008  191 VFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
7-104 3.13e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 193.01  E-value: 3.13e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   7 EFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQC 86
Cdd:pfam00116  23 EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQC 102

                          90
                  ....*....|....*...
gi 2018442087  87 SEICGANHSFMPIVIESV 104
Cdd:pfam00116 103 SEICGINHSFMPIVIEAV 120
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 7-119 1.88e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 192.61  E-value: 1.88e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   7 EFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQC 86
Cdd:MTH00038  117 EFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQC 196

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2018442087  87 SEICGANHSFMPIVIESVNTKTFIKWINSMLQA 119
Cdd:MTH00038  197 SEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-116 2.14e-62

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 190.35  E-value: 2.14e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   7 EFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQC 86
Cdd:MTH00023  128 EFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQC 207

                          90       100       110
                  ....*....|....*....|....*....|
gi 2018442087  87 SEICGANHSFMPIVIESVNTKTFIKWINSM 116
Cdd:MTH00023  208 SEICGANHSFMPIVIEAVSLDKYINWLLSL 237
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 4-118 7.79e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 188.38  E-value: 7.79e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   4 TPYE---FDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPG 80
Cdd:MTH00129  111 TDYEdlgFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPG 190

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2018442087  81 IFFGQCSEICGANHSFMPIVIESVNTKTFIKWINSMLQ 118
Cdd:MTH00129  191 VFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 4-117 2.90e-61

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 186.85  E-value: 2.90e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   4 TPYE---FDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPG 80
Cdd:MTH00098  111 TDYEdlsFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPG 190

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2018442087  81 IFFGQCSEICGANHSFMPIVIESVNTKTFIKWINSML 117
Cdd:MTH00098  191 LYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-118 3.25e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 186.91  E-value: 3.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   7 EFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQC 86
Cdd:MTH00051  121 EFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQC 200

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2018442087  87 SEICGANHSFMPIVIESVNTKTFIKWINSMLQ 118
Cdd:MTH00051  201 SEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 8-117 6.02e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 181.13  E-value: 6.02e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   8 FDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCS 87
Cdd:MTH00076  118 FDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCS 197

                          90       100       110
                  ....*....|....*....|....*....|
gi 2018442087  88 EICGANHSFMPIVIESVNTKTFIKWINSML 117
Cdd:MTH00076  198 EICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 7-120 2.56e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 179.70  E-value: 2.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   7 EFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQC 86
Cdd:MTH00185  117 EFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQC 196

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2018442087  87 SEICGANHSFMPIVIESVNTKTFIKWINSMLQAS 120
Cdd:MTH00185  197 SEICGANHSFMPIVVEAVPLEHFENWSSLMLEEA 230
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-113 3.67e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 162.50  E-value: 3.67e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   6 YEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQ 85
Cdd:MTH00027  150 IEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQ 229

                          90       100
                  ....*....|....*....|....*...
gi 2018442087  86 CSEICGANHSFMPIVIESVNTKTFIKWI 113
Cdd:MTH00027  230 CSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-117 1.66e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 147.08  E-value: 1.66e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   7 EFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQC 86
Cdd:MTH00080  120 EFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQC 199

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2018442087  87 SEICGANHSFMPIVIESVNTKTFIKWINSML 117
Cdd:MTH00080  200 SEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 6-109 8.71e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.03  E-value: 8.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   6 YEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQ 85
Cdd:PTZ00047   49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128

                          90       100
                  ....*....|....*....|....
gi 2018442087  86 CSEICGANHSFMPIVIESVNTKTF 109
Cdd:PTZ00047  129 CSEMCGTLHGFMPIVVEAVSPEAY 152
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
27-120 2.42e-34

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 118.39  E-value: 2.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087  27 DVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFMPIVIESVNT 106
Cdd:COG1622   134 ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213

                          90
                  ....*....|....
gi 2018442087 107 KTFIKWINSMLQAS 120
Cdd:COG1622   214 EEFDAWLAEQKASA 227
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-104 3.80e-30

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 106.58  E-value: 3.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   1 DFSTPYEFDSYMipynemNEDGFrllDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPG 80
Cdd:MTH00047   96 EYSFGGSYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHG 166

                          90       100
                  ....*....|....*....|....
gi 2018442087  81 IFFGQCSEICGANHSFMPIVIESV 104
Cdd:MTH00047  167 VFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 28-114 8.82e-29

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]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 103.23  E-value: 8.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087  28 VDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTK 107
Cdd:TIGR02866 113 TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKE 192


                  ....*..
gi 2018442087 108 TFIKWIN 114
Cdd:TIGR02866 193 EFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 28-102 1.14e-23

Cupredoxin domain of Heme-copper oxidase subunit II; 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.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 86.97  E-value: 1.14e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018442087  28 VDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFMPIVIE 102
Cdd:cd13842    21 TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 30-97 1.37e-20

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.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 79.59  E-value: 1.37e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018442087  30 NRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFM 97
Cdd:cd04213    29 NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 6-113 7.16e-19

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.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 75.14  E-value: 7.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087   6 YEFDsymipYNEMNEDGFrlldvdNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQ 85
Cdd:cd13914    12 WEFS-----YPEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLY 80

                          90       100
                  ....*....|....*....|....*...
gi 2018442087  86 CSEICGANHSFMPIVIESVNTKTFIKWI 113
Cdd:cd13914    81 CAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 29-97 7.85e-19

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.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 74.97  E-value: 7.85e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018442087  29 DNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFM 97
Cdd:cd13915    24 INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 34-97 2.90e-17

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.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 71.13  E-value: 2.90e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018442087  34 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFM 97
Cdd:cd13919    37 LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 30-112 1.29e-16

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.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 70.56  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087  30 NRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTF 109
Cdd:cd13918    56 NTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEF 135


                  ...
gi 2018442087 110 IKW 112
Cdd:cd13918   136 EAW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 34-97 5.08e-08

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 47.18  E-value: 5.08e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018442087  34 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFM 97
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 30-97 4.31e-07

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 44.85  E-value: 4.31e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018442087  30 NRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFM 97
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 10-102 1.63e-04

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.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 38.37  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442087  10 SYMIPYNEMNEDGFrlldVDNRTILPMNTQIRMLIT-AADVLHSWTVPALGVKVDA---------------TPGRLNQTK 73
Cdd:cd00920     7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVT 82

                          90       100
                  ....*....|....*....|....*....
gi 2018442087  74 FFVNRPGIFFGQCSEICGaNHSFMPIVIE 102
Cdd:cd00920    83 FTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 31-97 8.03e-04

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.


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 35.82  E-value: 8.03e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018442087  31 RTILPMNTQIRMLITAADVLHSWTV--PALGV--KVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFM 97
Cdd:cd13916    16 RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 37-97 2.67e-03

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.


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 34.65  E-value: 2.67e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018442087  37 NTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFM 97
Cdd:cd13917    21 GKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 48-97 4.50e-03

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 34.13  E-value: 4.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2018442087  48 DVLHSWTVPALGVKVDATPGRLNQTKFFVNRPGIFFGQCSEICGANHSFM 97
Cdd:cd04223    38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
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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