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Conserved domains on  [gi|400116839|gb|AFP67375|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Saccharomyces cerevisiae x Saccharomyces bayanus]

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
 2-195 1.17e-88

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 259.38  E-value: 1.17e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   2 IMFYLFVILGLVSWMLYTIVrtysNNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00154  27 TMMILIMITILVGYMMISLL----FNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  82 QWYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00154 103 QWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 400116839 162 RLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00154 178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVI 211
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 2-195 1.17e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 259.38  E-value: 1.17e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   2 IMFYLFVILGLVSWMLYTIVrtysNNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00154  27 TMMILIMITILVGYMMISLL----FNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  82 QWYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00154 103 QWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 400116839 162 RLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00154 178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVI 211
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-195 1.14e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 225.37  E-value: 1.14e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   74 MTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLG 153
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 400116839  154 IKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVI 117
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 72-195 1.69e-75

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: 222.83  E-value: 1.69e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  72 PAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPS 151
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 400116839 152 LGIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVV 119
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-195 8.31e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 171.16  E-value: 8.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   1 NIMFYLFVILGLVSW--MLYTIVR-TYSNNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIK 77
Cdd:COG1622   37 WVSLIIMLVIFVLVFglLLYFAIRyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  78 AIGYQWYWKYEYsdfindsgetvefesyvipddlLEEGQLrlldTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVD 157
Cdd:COG1622  117 VTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 400116839 158 ATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:COG1622  171 AIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKV 208
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-195 4.75e-38

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: 129.81  E-value: 4.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839    2 IMFYLFVILGLVSW--MLYTIV--RTYSNNPIAyKYIKHGQTIEVIWTIFPAV-VLLIIAFPSFILLYLCDEVISPAMTI 76
Cdd:TIGR02866  15 FVLAVSTLISLLVAalLAYVVWkfRRKGDEEKP-SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLLYLERPIPKDALKV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   77 KAIGYQWYWKYEYSDFindsgetvefesyvipddlleegqlrLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKV 156
Cdd:TIGR02866  94 KVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKI 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 400116839  157 DATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:TIGR02866 148 DAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKV 186
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 2-195 1.17e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 259.38  E-value: 1.17e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   2 IMFYLFVILGLVSWMLYTIVrtysNNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00154  27 TMMILIMITILVGYMMISLL----FNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  82 QWYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00154 103 QWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 400116839 162 RLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00154 178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVI 211
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-195 6.90e-82

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 243.12  E-value: 6.90e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   2 IMFYLFVILGLVSWMLYTIVrtysNNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00023  36 IMFLLIIIITVVLWLIVEAL----NGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGH 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  82 QWYWKYEYSDFindSGETVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00023 112 QWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPG 188

                        170       180       190
                 ....*....|....*....|....*....|....
gi 400116839 162 RLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00023 189 RLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVI 222
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 3-193 1.85e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 236.37  E-value: 1.85e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   3 MFYLFVILGLVSWMLYTIVRtysnNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQ 82
Cdd:MTH00140  28 MVVLVLIFSFVMYMLVLLLF----NKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  83 WYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGR 162
Cdd:MTH00140 104 WYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGR 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 400116839 163 LNQVSALIQREGVFYGNCSELCGTGHANMPI 193
Cdd:MTH00140 179 LNQLSFEPKRPGVFYGQCSEICGANHSFMPI 209
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 3-195 2.55e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 236.03  E-value: 2.55e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   3 MFYLFVILGLVSWMLYTIvrtySNNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQ 82
Cdd:MTH00168  28 LLILVLILTLVLYSLLVL----VTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  83 WYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGR 162
Cdd:MTH00168 104 WYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGR 178

                        170       180       190
                 ....*....|....*....|....*....|...
gi 400116839 163 LNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00168 179 LNQLAFLSSRPGSFYGQCSEICGANHSFMPIVV 211
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-195 1.14e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 225.37  E-value: 1.14e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   74 MTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLG 153
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 400116839  154 IKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVI 117
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-195 2.04e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 228.90  E-value: 2.04e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   2 IMFYLFVILGLVSWMlytIVRTYSNNpIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00051  29 IMFILTIIITTVLWL---IIRALTTK-YYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  82 QWYWKYEYSDFindSGETVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00051 105 QWYWSYEYSDY---GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPG 181

                        170       180       190
                 ....*....|....*....|....*....|....
gi 400116839 162 RLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00051 182 RLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVI 215
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 72-195 1.69e-75

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: 222.83  E-value: 1.69e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  72 PAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPS 151
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 400116839 152 LGIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVV 119
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 38-193 1.58e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 221.33  E-value: 1.58e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  38 QTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFindsgETVEFESYVIPDDLLEEGQL 117
Cdd:MTH00117  59 QEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDY-----KDLSFDSYMIPTQDLPNGHF 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 400116839 118 RLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPI 193
Cdd:MTH00117 134 RLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPI 209
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 3-195 4.99e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 219.97  E-value: 4.99e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   3 MFYLFVILGLVSWMLYTIVrtysNNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQ 82
Cdd:MTH00139  28 MVILIMILSFVGYISLSLM----SNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  83 WYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGR 162
Cdd:MTH00139 104 WYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGR 178

                        170       180       190
                 ....*....|....*....|....*....|...
gi 400116839 163 LNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00139 179 LNQVGFFINRPGVFYGQCSEICGANHSFMPIVV 211
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 3-195 4.99e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 220.11  E-value: 4.99e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   3 MFYLFVILGLVSWMLYTI-VRTYSNnpiayKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00008  28 LLILTLVLTVVGYAMTSLmFNKLSN-----RYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  82 QWYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00008 103 QWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPG 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 400116839 162 RLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00008 178 RLNQIGFTITRPGVFYGQCSEICGANHSFMPIVL 211
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 6-195 5.69e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 212.27  E-value: 5.69e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   6 LFVILGLVSWMLYTIVRTYSNNpIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYW 85
Cdd:MTH00129  28 LMIVFLISTLVLYIIVAMVSTK-LTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  86 KYEYSDFindsgETVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQ 165
Cdd:MTH00129 107 SYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQ 181

                        170       180       190
                 ....*....|....*....|....*....|
gi 400116839 166 VSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00129 182 TAFIASRPGVFYGQCSEICGANHSFMPIVV 211
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-195 5.74e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 212.25  E-value: 5.74e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   2 IMFYLFVILGLVSWMLYTIVRTYSNNpiayKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00038  27 ALIILTLITILVFYGLASLLFSSPTN----RFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  82 QWYWKYEYSDFindsgETVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00038 103 QWYWSYEYTDY-----NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPG 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 400116839 162 RLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00038 178 RLNQTTFFISRTGLFYGQCSEICGANHSFMPIVI 211
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 6-193 7.32e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 212.05  E-value: 7.32e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   6 LFVILGLVSWMLYTIVRTYSNNpiayKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYW 85
Cdd:MTH00185  31 VFLISTLVLYIIVAMVTTKLTN----KYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  86 KYEYSDFindsgETVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQ 165
Cdd:MTH00185 107 SYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQ 181

                        170       180
                 ....*....|....*....|....*...
gi 400116839 166 VSALIQREGVFYGNCSELCGTGHANMPI 193
Cdd:MTH00185 182 ATFIISRPGLYYGQCSEICGANHSFMPI 209
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 38-193 5.38e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 204.63  E-value: 5.38e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  38 QTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFINDSgetveFESYVIPDDLLEEGQL 117
Cdd:MTH00076  59 QEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLS-----FDSYMIPTQDLTPGQF 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 400116839 118 RLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPI 193
Cdd:MTH00076 134 RLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPI 209
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-193 6.61e-67

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 204.57  E-value: 6.61e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   2 IMFYL-FVILGLVSWMLYTIVrTYSNNPIAykyikhgQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIG 80
Cdd:MTH00098  30 IVFLIsSLVLYIISLMLTTKL-THTSTMDA-------QEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  81 YQWYWKYEYSDFindsgETVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATP 160
Cdd:MTH00098 102 HQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIP 176

                        170       180       190
                 ....*....|....*....|....*....|...
gi 400116839 161 GRLNQVSALIQREGVFYGNCSELCGTGHANMPI 193
Cdd:MTH00098 177 GRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPI 209
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-195 1.31e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 184.46  E-value: 1.31e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   2 IMFYLFVILGLVSWMLYTIVrtYSNNPIAYKYIK-HGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDE-VISPAMTIKAI 79
Cdd:MTH00027  55 ILFILTIIVGVVLWLIIRIL--LGNNYYSYYWNKlDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANITIKVT 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  80 GYQWYWKYEYSDFindSGETVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDAT 159
Cdd:MTH00027 133 GHQWYWSYSYEDY---GEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAV 209

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 400116839 160 PGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00027 210 PGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVV 245
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 2-195 5.18e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 176.74  E-value: 5.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   2 IMFYLFVILGLVSWMLYTIVRTYSnnpiaYKYIK-HGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEV-ISPAMTIKAI 79
Cdd:MTH00080  29 LLFGEFVLAFVVFLFLYLISNNFY-----FKSKKiEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  80 GYQWYWKYEYSDFINdsgetVEFESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDAT 159
Cdd:MTH00080 104 GHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 400116839 160 PGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00080 179 SGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAV 214
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-195 8.31e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 171.16  E-value: 8.31e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   1 NIMFYLFVILGLVSW--MLYTIVR-TYSNNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIK 77
Cdd:COG1622   37 WVSLIIMLVIFVLVFglLLYFAIRyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  78 AIGYQWYWKYEYsdfindsgetvefesyvipddlLEEGQLrlldTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVD 157
Cdd:COG1622  117 VTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 400116839 158 ATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:COG1622  171 AIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKV 208
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 102-195 4.70e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 136.49  E-value: 4.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839 102 FESYVIPDDLLEEGQLRLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGNCS 181
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....
gi 400116839 182 ELCGTGHANMPIKI 195
Cdd:PTZ00047 131 EMCGTLHGFMPIVV 144
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-195 4.75e-38

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: 129.81  E-value: 4.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839    2 IMFYLFVILGLVSW--MLYTIV--RTYSNNPIAyKYIKHGQTIEVIWTIFPAV-VLLIIAFPSFILLYLCDEVISPAMTI 76
Cdd:TIGR02866  15 FVLAVSTLISLLVAalLAYVVWkfRRKGDEEKP-SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLLYLERPIPKDALKV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839   77 KAIGYQWYWKYEYSDFindsgetvefesyvipddlleegqlrLLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKV 156
Cdd:TIGR02866  94 KVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKI 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 400116839  157 DATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:TIGR02866 148 DAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKV 186
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 38-195 1.15e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 126.22  E-value: 1.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  38 QTIEVIWTIFPAVVLLIIAFpsFILLYL-CDEVISPAMTIKAIGYQWYWKYEYSDFIndsgetvEFESYVIPDDLLEEGQ 116
Cdd:MTH00047  47 QVLELLWTVVPTLLVLVLCF--LNLNFItSDLDCFSSETIKVIGHQWYWSYEYSFGG-------SYDSFMTDDIFGVDKP 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 400116839 117 LRLLdtdtsivvpVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:MTH00047 118 LRLV---------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVI 187
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 73-195 3.64e-29

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: 104.24  E-value: 3.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  73 AMTIKAIGYQWYWKYEYSDfinDSGETVEfesyvipddlleegqlrlldTDTSIVVPVDTHIRFVVTAADVIHDFAIPSL 152
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD---EPGRGIV--------------------TANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 400116839 153 GIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:cd04213   58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKV 100
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-191 6.74e-26

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: 95.79  E-value: 6.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  73 AMTIKAIGYQWYWKYEYSDfindSGETVEFESYVIPDDLleegqlrlldtdtsiVVPVDTHIRFVVTAADVIHDFAIPSL 152
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPG----GDGKLGTDDDVTSPEL---------------HLPVGRPVLFNLRSKDVIHSFWVPEF 61

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 400116839 153 GIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANM 191
Cdd:cd13919   62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 74-195 2.53e-24

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: 91.59  E-value: 2.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  74 MTIKAIGYQWYWKYEYSDfindsgetvefesyvipddlleegqlrlLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLG 153
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 400116839 154 IKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:cd13842   53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKV 94
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-195 1.94e-23

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: 89.23  E-value: 1.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  73 AMTIKAIGYQWYWKYEYSdfiNDSGETVEfesyvipddlleegqlrlldtdtsIVVPVDTHIRFVVTAADVIHDFAIPSL 152
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYP---NGKREINE------------------------LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 400116839 153 GIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:cd13915   54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-62 4.14e-23

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 88.16  E-value: 4.14e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 400116839    1 NIMFYLFVILGLVSWMLYTIVRTY--SNNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFIL 62
Cdd:pfam02790  26 YIMFILTLILILVLYILVTCLIRFnrRKNPITARYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-191 5.50e-22

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: 85.92  E-value: 5.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  75 TIKAIGYQWYWKYEYsdfiNDSGetvefesyvipddlleegqlrlLDTDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGI 154
Cdd:cd13914    2 EIEVEAYQWGWEFSY----PEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 400116839 155 KVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANM 191
Cdd:cd13914   56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 50-191 1.48e-18

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: 77.88  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  50 VVLLIIAFPSFILLYLCD---EVISPAMTIKAIGYQWYWKYEYSDFINDSGEtvefesyvipddlleegqlrlldtdtsI 126
Cdd:cd13918    6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTGNT---------------------------L 58

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 400116839 127 VVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANM 191
Cdd:cd13918   59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 122-195 8.29e-15

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: 66.82  E-value: 8.29e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 400116839 122 TDTSIVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:cd13913   23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKI 96
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-191 1.90e-08

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: 49.69  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839  75 TIKAIGYQWYWKyeysdfindsgetvefesyvipddlleegqlrlLDTDTsivVPVDTHIRFVVTAADVIHDFAI--PSL 152
Cdd:cd13916    2 VVAVTGHQWYWE---------------------------------LSRTE---IPAGKPVEFRVTSADVNHGFGIydPDM 45

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 400116839 153 GI--KVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANM 191
Cdd:cd13916   46 RLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 126-191 7.94e-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: 45.62  E-value: 7.94e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 400116839 126 IVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANM 191
Cdd:cd04212   27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 126-195 3.32e-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: 35.42  E-value: 3.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 400116839 126 IVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGNCSELCGTGHANMPIKI 195
Cdd:cd13917   16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRI 85
 
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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