NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2018442201|gb|QTG58740|]
View 

cytochrome oxidase subunit II, partial (mitochondrion) [Neduba convexa]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-161 3.66e-111

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 315.23  E-value: 3.66e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTPhEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00154   66 TILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00154  145 PMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224


                  .
gi 2018442201 161 S 161
Cdd:MTH00154  225 N 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-161 3.66e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 315.23  E-value: 3.66e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTPhEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00154   66 TILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00154  145 PMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224


                  .
gi 2018442201 161 S 161
Cdd:MTH00154  225 N 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 28-158 2.05e-90

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: 259.04  E-value: 2.05e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  28 PIITIKTVGHQWYWSYEYTDFSTpHEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVK 107
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2018442201 108 VDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKW 158
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
30-150 4.05e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 230.37  E-value: 4.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWSYEYTDFSTPhEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 109
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2018442201 110 ATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESV 150
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-166 1.27e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 141.50  E-value: 1.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDfstphefdsymipynemnEDGfrllDVDNRTIL 80
Cdd:COG1622    84 TVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------------QGI----ATVNELVL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:COG1622   142 PVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLA 221


                  ....*.
gi 2018442201 161 SALQAS 166
Cdd:COG1622   222 EQKASA 227
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-160 6.14e-34

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: 118.25  E-value: 6.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDP-IITIKTVGHQWYWSYEYTdfstphefdsymipynemnEDGFRlldVDNRTI 79
Cdd:TIGR02866  61 TVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVTGYQWWWDFEYP-------------------ESGFT---TVNELV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  80 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWI 159
Cdd:TIGR02866 119 LPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198


                  .
gi 2018442201 160 S 160
Cdd:TIGR02866 199 E 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-161 3.66e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 315.23  E-value: 3.66e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTPhEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00154   66 TILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00154  145 PMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224


                  .
gi 2018442201 161 S 161
Cdd:MTH00154  225 N 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-161 6.66e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 269.09  E-value: 6.66e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTPhEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00117   66 TILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDL-SFDSYMIPTQDLPNGHFRLLEVDHRMVI 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00117  145 PMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224


                  .
gi 2018442201 161 S 161
Cdd:MTH00117  225 L 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 28-158 2.05e-90

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: 259.04  E-value: 2.05e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  28 PIITIKTVGHQWYWSYEYTDFSTpHEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVK 107
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2018442201 108 VDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKW 158
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-161 3.15e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 262.18  E-value: 3.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTpHEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00140   66 TIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00140  145 PYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224


                  .
gi 2018442201 161 S 161
Cdd:MTH00140  225 L 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-162 5.58e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 259.26  E-value: 5.58e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTpHEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00139   66 TVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00139  145 PYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWIL 224


                  ..
gi 2018442201 161 SA 162
Cdd:MTH00139  225 EK 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-161 3.82e-87

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 254.78  E-value: 3.82e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTPhEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00008   66 TILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNL-EFDSYMLPTSDLSPGQFRLLEVDNRAVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00008  145 PMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224


                  .
gi 2018442201 161 S 161
Cdd:MTH00008  225 S 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-161 7.01e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 253.75  E-value: 7.01e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTpHEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00168   66 TIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00168  145 PMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224


                  .
gi 2018442201 161 S 161
Cdd:MTH00168  225 S 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-161 5.03e-85

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 249.67  E-value: 5.03e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTPH-EFDSYMIPYNEMNEDGFRLLDVDNRTI 79
Cdd:MTH00023   75 TIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETlEFDSYMVPTSDLNSGDFRLLEVDNRLV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  80 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWI 159
Cdd:MTH00023  155 VPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234


                  ..
gi 2018442201 160 SS 161
Cdd:MTH00023  235 LS 236
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-165 4.20e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 246.92  E-value: 4.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTPhEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00038   66 TIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDL-EFDSYMVPTSDLSTGLPRLLEVDNRLVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00038  145 PYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224


                  ....*
gi 2018442201 161 SALQA 165
Cdd:MTH00038  225 NFLEE 229
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-163 2.36e-81

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 240.01  E-value: 2.36e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTpHEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00098   66 TILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVL 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00098  145 PMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224


                  ...
gi 2018442201 161 SAL 163
Cdd:MTH00098  225 SML 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-161 3.91e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 239.68  E-value: 3.91e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTPH-EFDSYMIPYNEMNEDGFRLLDVDNRTI 79
Cdd:MTH00051   68 TLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTiEFDSYMIPTSDLNSGDLRLLEVDNRLI 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  80 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWI 159
Cdd:MTH00051  148 VPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227


                  ..
gi 2018442201 160 SS 161
Cdd:MTH00051  228 AT 229
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-164 6.55e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 238.85  E-value: 6.55e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTpHEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00129   66 TVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVV 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00129  145 PVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224


                  ....
gi 2018442201 161 SALQ 164
Cdd:MTH00129  225 LMLE 228
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
30-150 4.05e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 230.37  E-value: 4.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWSYEYTDFSTPhEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 109
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2018442201 110 ATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESV 150
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-163 5.73e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 233.90  E-value: 5.73e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTpHEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00076   66 TIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVV 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00076  145 PMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSS 224


                  ...
gi 2018442201 161 SAL 163
Cdd:MTH00076  225 SML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-166 1.05e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 230.93  E-value: 1.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDFSTpHEFDSYMIPYNEMNEDGFRLLDVDNRTIL 80
Cdd:MTH00185   66 TILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVV 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:MTH00185  145 PMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224


                  ....*.
gi 2018442201 161 SALQAS 166
Cdd:MTH00185  225 LMLEEA 230
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-159 3.64e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 194.86  E-value: 3.64e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDES-MDPIITIKTVGHQWYWSYEYTDFSTPH-EFDSYMIPYNEMNEDGFRLLDVDNRT 78
Cdd:MTH00027   97 TLIPAFILILIAFPSLRLLYIMDECgFSANITIKVTGHQWYWSYSYEDYGEKNiEFDSYMIPTADLEFGDLRLLEVDNRL 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  79 ILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKW 158
Cdd:MTH00027  177 ILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256


                  .
gi 2018442201 159 I 159
Cdd:MTH00027  257 I 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 30-159 2.12e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 179.05  E-value: 2.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWSYEYTDFSTPhEFDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 109
Cdd:MTH00080   98 LTVKVTGHQWYWSYEFSDIPGL-EFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMD 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2018442201 110 ATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWI 159
Cdd:MTH00080  177 AMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-166 1.27e-42

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 141.50  E-value: 1.27e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDPIITIKTVGHQWYWSYEYTDfstphefdsymipynemnEDGfrllDVDNRTIL 80
Cdd:COG1622    84 TVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------------QGI----ATVNELVL 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  81 PMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWIS 160
Cdd:COG1622   142 PVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLA 221


                  ....*.
gi 2018442201 161 SALQAS 166
Cdd:COG1622   222 EQKASA 227
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 31-150 7.30e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 138.55  E-value: 7.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  31 TIKTVGHQWYWSYEYTDFStphEFDSYMipynemNEDGFrllDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDA 110
Cdd:MTH00047   83 TIKVIGHQWYWSYEYSFGG---SYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDA 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2018442201 111 TPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESV 150
Cdd:MTH00047  151 IPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 54-155 1.02e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 134.56  E-value: 1.02e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  54 FDSYMIPYNEMNEDGFRLLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCS 133
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 2018442201 134 EICGANHSFMPIVIESVNTKTF 155
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-160 6.14e-34

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: 118.25  E-value: 6.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201   1 TILPAVTLIFIALPSLRLLYLLDESMDP-IITIKTVGHQWYWSYEYTdfstphefdsymipynemnEDGFRlldVDNRTI 79
Cdd:TIGR02866  61 TVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVTGYQWWWDFEYP-------------------ESGFT---TVNELV 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  80 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWI 159
Cdd:TIGR02866 119 LPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198


                  .
gi 2018442201 160 S 160
Cdd:TIGR02866 199 E 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 30-148 1.04e-28

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: 101.60  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWSYEYTDFSTPHEFdsymipynemnedgfrlldvdnrtILPMNTQIRMLITAADVLHSWTVPALGVKVD 109
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRTPNEI------------------------VVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2018442201 110 ATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIE 148
Cdd:cd13842    57 AVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 30-143 4.84e-24

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: 89.99  E-value: 4.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWSYEYTDfSTPHEFDSYmipyNEMnedgfrlldvdnrtILPMNTQIRMLITAADVLHSWTVPALGVKVD 109
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD-EPGRGIVTA----NEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2018442201 110 ATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFM 143
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 30-143 5.68e-21

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: 81.91  E-value: 5.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWSYEYTDfstphefdsymipynemnedGFRlldVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 109
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN--------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2018442201 110 ATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFM 143
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 30-143 1.03e-20

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: 81.53  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWSYEYTDFSTPHEFDSyMIPYNEMNedgfrlldvdnrtiLPMNTQIRMLITAADVLHSWTVPALGVKVD 109
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDD-DVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2018442201 110 ATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFM 143
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 30-159 8.54e-20

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: 79.37  E-value: 8.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWSYEYTDFStphefdsymipynemnedgfrlLDVDNRTILPMNTQIRMLITAADVLHSWTVPALGVKVD 109
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2018442201 110 ATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKWI 159
Cdd:cd13914    59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 23-158 6.34e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 72.87  E-value: 6.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  23 DESMDPIITIKTVGHQWYWSYEYTDFSTPHefdsymipyNEMnedgfrlldvdnrtILPMNTQIRMLITAADVLHSWTVP 102
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNGVTTG---------NTL--------------RVPADTPIALRVTSTDVFHTFGIP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2018442201 103 ALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPIVIESVNTKTFIKW 158
Cdd:cd13918    83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 80-143 6.27e-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: 47.95  E-value: 6.27e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018442201  80 LPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFM 143
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 76-143 9.45e-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: 9.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018442201  76 NRTILPMNTQIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFM 143
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 30-143 1.27e-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: 38.90  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWsyeytdfstphefdsymipynEMNedgfrlldvdnRTILPMNTQIRMLITAADVLHSWTV--PALGV- 106
Cdd:cd13916     1 QVVAVTGHQWYW---------------------ELS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLl 48

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2018442201 107 -KVDATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFM 143
Cdd:cd13916    49 aQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 56-148 8.81e-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: 37.21  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  56 SYMIPYNEMNEDGFrlldVDNRTILPMNTQIRMLIT-AADVLHSWTVPALGVKVDA---------------TPGRLNQTS 119
Cdd:cd00920     7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVT 82

                          90       100
                  ....*....|....*....|....*....
gi 2018442201 120 FFVNRPGIFFGQCSEICGaNHSFMPIVIE 148
Cdd:cd00920    83 FTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 30-166 9.97e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 35.55  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018442201  30 ITIKTVGHQWYWSYEYTDFSTPhefdsymipynEMNEDGFrlldvdnrtilPMNTQIRMLITAADVLHSWTVPALGVKVD 109
Cdd:PRK10525  127 ITIEVVSMDWKWFFIYPEQGIA-----------TVNEIAF-----------PANVPVYFKVTSNSVMNSFFIPRLGSQIY 184

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2018442201 110 ATPGRLNQTSFFVNRPGIFFGQCSEICGANHSFMPI-VIESVNTKTFIKWISSALQAS 166
Cdd:PRK10525  185 AMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFkAIATPDRAEFDQWVAKAKQSP 242
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH