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Conserved domains on  [gi|92013945|emb|CAI79385|]
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cytochrome c oxidase, subunit II, partial (mitochondrion) [Saccharomyces sp. CBS 8614]

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 9.77e-92

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 267.46  E-value: 9.77e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    2 IMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTN----RFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   82 QWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00154 103 QWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 92013945  162 RLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00154 178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVI 211
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 2-195 9.77e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 267.46  E-value: 9.77e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    2 IMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTN----RFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   82 QWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00154 103 QWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 92013945  162 RLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00154 178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVI 211
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-195 2.23e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.60  E-value: 2.23e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    74 MTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLG 153
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 92013945   154 IKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 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 6.33e-78

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: 228.99  E-value: 6.33e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  72 PAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPS 151
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 92013945 152 LGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:cd13912  76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVV 119
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-195 2.18e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.71  E-value: 2.18e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   1 NIMFYLLVILGLVSW--MLYTIVM-TYSKNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIK 77
Cdd:COG1622  37 WVSLIIMLVIFVLVFglLLYFAIRyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVE 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  78 AIGYQWYWKYEYsdfindsgetvefesyvipdelLEEGQLrlldTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVD 157
Cdd:COG1622 117 VTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 92013945 158 ATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:COG1622 171 AIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKV 208
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-195 1.88e-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: 130.96  E-value: 1.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945     2 IMFYLLVILGLVSWMLYTIVM----TYSKNPIAyKYIKHGQTIEVIWTIFPAV-VLLIIAFPSFILLYLCDEVISPAMTI 76
Cdd:TIGR02866  15 FVLAVSTLISLLVAALLAYVVwkfrRKGDEEKP-SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLLYLERPIPKDALKV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    77 KAIGYQWYWKYEYSDFindsgetvefesyvipdelleegqlrLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKV 156
Cdd:TIGR02866  94 KVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKI 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 92013945   157 DATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:TIGR02866 148 DAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKV 186
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 2-195 9.77e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 267.46  E-value: 9.77e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    2 IMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00154  27 TMMILIMITILVGYMMISLLFNKFTN----RFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   82 QWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00154 103 QWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 92013945  162 RLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00154 178 RLNQLNFLINRPGLFFGQCSEICGANHSFMPIVI 211
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-195 2.09e-83

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 246.97  E-value: 2.09e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    2 IMFYLLVILGLVSWMLYTIVmtysKNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00023  36 IMFLLIIIITVVLWLIVEAL----NGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGH 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   82 QWYWKYEYSDFindSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00023 112 QWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPG 188

                        170       180       190
                 ....*....|....*....|....*....|....
gi 92013945  162 RLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00023 189 RLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVI 222
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 3-193 3.13e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 243.31  E-value: 3.13e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    3 MFYLLVILGLVSWMLYTIVMtyskNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQ 82
Cdd:MTH00140  28 MVVLVLIFSFVMYMLVLLLF----NKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   83 WYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGR 162
Cdd:MTH00140 104 WYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGR 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 92013945  163 LNQVSALIQREGVFYGQCSELCGTGHANMPI 193
Cdd:MTH00140 179 LNQLSFEPKRPGVFYGQCSEICGANHSFMPI 209
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 3-195 6.09e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 237.57  E-value: 6.09e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    3 MFYLLVILGLVSWMLYTIvmtySKNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQ 82
Cdd:MTH00168  28 LLILVLILTLVLYSLLVL----VTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   83 WYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGR 162
Cdd:MTH00168 104 WYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGR 178

                        170       180       190
                 ....*....|....*....|....*....|...
gi 92013945  163 LNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00168 179 LNQLAFLSSRPGSFYGQCSEICGANHSFMPIVV 211
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-195 2.23e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 229.60  E-value: 2.23e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    74 MTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLG 153
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 92013945   154 IKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 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 6.33e-78

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: 228.99  E-value: 6.33e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  72 PAMTIKAIGYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPS 151
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 92013945 152 LGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:cd13912  76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVV 119
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-195 2.77e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 231.21  E-value: 2.77e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    2 IMFYLLVILGLVSWMLYTIVMTysKNPiaYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00051  29 IMFILTIIITTVLWLIIRALTT--KYY--HKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   82 QWYWKYEYSDFindSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00051 105 QWYWSYEYSDY---GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPG 181

                        170       180       190
                 ....*....|....*....|....*....|....
gi 92013945  162 RLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00051 182 RLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVI 215
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 6-193 3.07e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 225.56  E-value: 3.07e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    6 LLVILGLVSWMLYTI-VMTYSKnpIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQWY 84
Cdd:MTH00117  28 LMVALLISSLVLYLLtLMLTTK--LTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   85 WKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLN 164
Cdd:MTH00117 106 WSYEYTDY-----KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLN 180

                        170       180
                 ....*....|....*....|....*....
gi 92013945  165 QVSALIQREGVFYGQCSELCGTGHANMPI 193
Cdd:MTH00117 181 QTSFITTRPGVFYGQCSEICGANHSFMPI 209
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 3-195 2.10e-74

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 223.58  E-value: 2.10e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    3 MFYLLVILGLVSWMLYTIVMtyskNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQ 82
Cdd:MTH00008  28 LLILTLVLTVVGYAMTSLMF----NKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   83 WYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGR 162
Cdd:MTH00008 104 WYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGR 178

                        170       180       190
                 ....*....|....*....|....*....|...
gi 92013945  163 LNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00008 179 LNQIGFTITRPGVFYGQCSEICGANHSFMPIVL 211
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 3-195 3.36e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 223.06  E-value: 3.36e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    3 MFYLLVILGLVSWMLYTIVmtysKNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQ 82
Cdd:MTH00139  28 MVILIMILSFVGYISLSLM----SNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   83 WYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGR 162
Cdd:MTH00139 104 WYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGR 178

                        170       180       190
                 ....*....|....*....|....*....|...
gi 92013945  163 LNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00139 179 LNQVGFFINRPGVFYGQCSEICGANHSFMPIVV 211
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 5-195 2.92e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 218.04  E-value: 2.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    5 YLLVILGLVSWMLYTIVMTYSKNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQWY 84
Cdd:MTH00129  26 HALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWY 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   85 WKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLN 164
Cdd:MTH00129 106 WSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLN 180

                        170       180       190
                 ....*....|....*....|....*....|.
gi 92013945  165 QVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00129 181 QTAFIASRPGVFYGQCSEICGANHSFMPIVV 211
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-195 3.92e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 217.65  E-value: 3.92e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    2 IMFYLLVILGLVSWMLYTIVMTYSKNpiayKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGY 81
Cdd:MTH00038  27 ALIILTLITILVFYGLASLLFSSPTN----RFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   82 QWYWKYEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPG 161
Cdd:MTH00038 103 QWYWSYEYTDY-----NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPG 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 92013945  162 RLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00038 178 RLNQTTFFISRTGLFYGQCSEICGANHSFMPIVI 211
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 7-193 2.57e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 215.90  E-value: 2.57e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    7 LVILGLVSWMLYTIVMTYSKNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYWK 86
Cdd:MTH00185  28 LMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   87 YEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQV 166
Cdd:MTH00185 108 YEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQA 182

                        170       180
                 ....*....|....*....|....*..
gi 92013945  167 SALIQREGVFYGQCSELCGTGHANMPI 193
Cdd:MTH00185 183 TFIISRPGLYYGQCSEICGANHSFMPI 209
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 38-193 2.45e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 208.09  E-value: 2.45e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   38 QTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYWKYEYSDFINDSgetveFESYVIPDELLEEGQL 117
Cdd:MTH00076  59 QEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLS-----FDSYMIPTQDLTPGQF 133

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 92013945  118 RLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPI 193
Cdd:MTH00076 134 RLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPI 209
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 7-193 4.33e-68

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 207.26  E-value: 4.33e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    7 LVILGLVSWMLYTIVMTYSKNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGYQWYWK 86
Cdd:MTH00098  28 LMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   87 YEYSDFindsgETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQV 166
Cdd:MTH00098 108 YEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQT 182

                        170       180
                 ....*....|....*....|....*..
gi 92013945  167 SALIQREGVFYGQCSELCGTGHANMPI 193
Cdd:MTH00098 183 TLMSTRPGLYYGQCSEICGSNHSFMPI 209
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-195 2.93e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 186.38  E-value: 2.93e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    2 IMFYLLVILGLVSWMLYTIVMtySKNPIAYKYIK-HGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDE-VISPAMTIKAI 79
Cdd:MTH00027  55 ILFILTIIVGVVLWLIIRILL--GNNYYSYYWNKlDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANITIKVT 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   80 GYQWYWKYEYSDFindSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDAT 159
Cdd:MTH00027 133 GHQWYWSYSYEDY---GEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAV 209

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 92013945  160 PGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 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 92013945    2 IMFYLLVILGLVSWMLYTIVMTYSknpiaYKYIK-HGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEV-ISPAMTIKAI 79
Cdd:MTH00080  29 LLFGEFVLAFVVFLFLYLISNNFY-----FKSKKiEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   80 GYQWYWKYEYSDFINdsgetVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDAT 159
Cdd:MTH00080 104 GHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 92013945  160 PGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:MTH00080 179 SGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAV 214
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-195 2.18e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.71  E-value: 2.18e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   1 NIMFYLLVILGLVSW--MLYTIVM-TYSKNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIK 77
Cdd:COG1622  37 WVSLIIMLVIFVLVFglLLYFAIRyRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVE 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  78 AIGYQWYWKYEYsdfindsgetvefesyvipdelLEEGQLrlldTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVD 157
Cdd:COG1622 117 VTGYQWKWLFRY----------------------PDQGIA----TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 92013945 158 ATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:COG1622 171 AIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKV 208
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 102-195 6.16e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 141.11  E-value: 6.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  102 FESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCS 181
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....
gi 92013945  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 1.88e-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: 130.96  E-value: 1.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945     2 IMFYLLVILGLVSWMLYTIVM----TYSKNPIAyKYIKHGQTIEVIWTIFPAV-VLLIIAFPSFILLYLCDEVISPAMTI 76
Cdd:TIGR02866  15 FVLAVSTLISLLVAALLAYVVwkfrRKGDEEKP-SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLLYLERPIPKDALKV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945    77 KAIGYQWYWKYEYSDFindsgetvefesyvipdelleegqlrLLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKV 156
Cdd:TIGR02866  94 KVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKI 147

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 92013945   157 DATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:TIGR02866 148 DAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKV 186
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 38-195 6.21e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 126.99  E-value: 6.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945   38 QTIEVIWTIFPAVVLLIIAFpsFILLYL-CDEVISPAMTIKAIGYQWYWKYEYSDFIndsgetvEFESYVIPDELLEEGQ 116
Cdd:MTH00047  47 QVLELLWTVVPTLLVLVLCF--LNLNFItSDLDCFSSETIKVIGHQWYWSYEYSFGG-------SYDSFMTDDIFGVDKP 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 92013945  117 LRLLdtdtsmvvpVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 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 1.23e-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: 105.39  E-value: 1.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  73 AMTIKAIGYQWYWKYEYSDfinDSGETVEfesyvipdelleegqlrlldTDTSMVVPVDTHIRFVVTAADVIHDFAIPSL 152
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPD---EPGRGIV--------------------TANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 92013945 153 GIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 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 1.46e-27

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: 100.02  E-value: 1.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  73 AMTIKAIGYQWYWKYEYSDfindSGETVEFESYVIPDELleegqlrlldtdtsmVVPVDTHIRFVVTAADVIHDFAIPSL 152
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPG----GDGKLGTDDDVTSPEL---------------HLPVGRPVLFNLRSKDVIHSFWVPEF 61

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 92013945 153 GIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANM 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 9.70e-25

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: 92.36  E-value: 9.70e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  74 MTIKAIGYQWYWKYEYSDfindsgetvefesyvipdelleegqlrlLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLG 153
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 92013945 154 IKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 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 7.69e-24

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: 90.38  E-value: 7.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  73 AMTIKAIGYQWYWKYEYSdfiNDSGETVEfesyvipdelleegqlrlldtdtsMVVPVDTHIRFVVTAADVIHDFAIPSL 152
Cdd:cd13915   1 ALEIQVTGRQWMWEFTYP---NGKREINE------------------------LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 92013945 153 GIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 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 8.31e-24

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: 90.08  E-value: 8.31e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92013945     1 NIMFYLLVILGLVSWMLYTIVMTY--SKNPIAYKYIKHGQTIEVIWTIFPAVVLLIIAFPSFIL 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 3.18e-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: 86.31  E-value: 3.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  75 TIKAIGYQWYWKYEYsdfiNDSGetvefesyvipdelleegqlrlLDTDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGI 154
Cdd:cd13914   2 EIEVEAYQWGWEFSY----PEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 92013945 155 KVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANM 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 2.12e-19

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 80.19  E-value: 2.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  50 VVLLIIAFPSFILLYLCD---EVISPAMTIKAIGYQWYWKYEYSDFINDSGEtvefesyvipdelleegqlrlldtdtsM 126
Cdd:cd13918   6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTGNT---------------------------L 58

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 92013945 127 VVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANM 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 2.02e-14

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: 65.67  E-value: 2.02e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 92013945 122 TDTSMVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 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 1.92e-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: 1.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 92013945  75 TIKAIGYQWYWKyeysdfindsgetvefesyvipdelleegqlrlLDTDTsmvVPVDTHIRFVVTAADVIHDFAI--PSL 152
Cdd:cd13916   2 VVAVTGHQWYWE---------------------------------LSRTE---IPAGKPVEFRVTSADVNHGFGIydPDM 45

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 92013945 153 GI--KVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANM 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 5.61e-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: 46.00  E-value: 5.61e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 92013945 126 MVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANM 191
Cdd:cd04212  27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 135-195 4.84e-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: 35.04  E-value: 4.84e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 92013945 135 RFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTGHANMPIKI 195
Cdd:cd13917  25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRI 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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