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Conserved domains on  [gi|587572851|gb|AHK06454|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Mollitrichosiphum luchuanum]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-216 6.91e-116

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 329.48  E-value: 6.91e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   1 MTWFKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  81 HLLYLMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIH 158
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 587572851 159 SWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNF 219
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-216 6.91e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 329.48  E-value: 6.91e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   1 MTWFKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  81 HLLYLMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIH 158
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 587572851 159 SWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNF 219
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-216 1.04e-74

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 221.68  E-value: 1.04e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  92 PIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKM 169
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIpeDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 587572851 170 DAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDF 127
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-211 6.39e-70

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 209.19  E-value: 6.39e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   94 MTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDA 171
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIptEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 587572851  172 IPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESI 211
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-209 2.88e-36

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 126.87  E-value: 2.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   6 FSFQNSNSPLMEQLIFFHDhTIFIIMMIMFTITY-MMIFIM------KNKFINIKIKENQLIEFIWTIIPPIILIFIALP 78
Cdd:COG1622   19 LSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLVFgLLLYFAiryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  79 SLHLLYLMDEIKSPIMTIKIFGHQWFWSYEYSDfsniefesymidnfknENfrlIEVDNKTIIPFKFNIRLLISSEDVIH 158
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD----------------QG---IATVNELVLPVGRPVRFLLTSADVIH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 587572851 159 SWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIE 209
Cdd:COG1622  159 SFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 82-209 7.83e-32

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: 114.79  E-value: 7.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   82 LLYLMDEIKSPIMTIKIFGHQWFWSYEYSDFsniefesymidnfknenfrLIEVDNKTIIPFKFNIRLLISSEDVIHSWT 161
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 587572851  162 IPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIE 209
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-216 6.91e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 329.48  E-value: 6.91e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   1 MTWFKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSL 80
Cdd:MTH00154   2 ATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  81 HLLYLMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIH 158
Cdd:MTH00154  82 RLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIH 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 587572851 159 SWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00154 162 SWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNF 219
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-213 1.59e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 290.69  E-value: 1.59e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   1 MTWFKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSL 80
Cdd:MTH00140   2 SYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  81 HLLYLMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMID--NFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIH 158
Cdd:MTH00140  82 RLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPenELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIH 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 587572851 159 SWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINL 213
Cdd:MTH00140 162 SWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPL 216
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 6-216 3.06e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 284.88  E-value: 3.06e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   6 FSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLHLLYL 85
Cdd:MTH00117   7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  86 MDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIP 163
Cdd:MTH00117  87 MDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIptQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 587572851 164 SLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00117 167 SLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHF 219
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 2-216 8.18e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 283.53  E-value: 8.18e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   2 TWFKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLH 81
Cdd:MTH00139   3 YWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  82 LLYLMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHS 159
Cdd:MTH00139  83 LLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIptEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHS 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 587572851 160 WTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00139 163 WTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFF 219
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-216 5.33e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 273.78  E-value: 5.33e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   1 MTWFKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSL 80
Cdd:MTH00168   2 ATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  81 HLLYLMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIH 158
Cdd:MTH00168  82 RLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVptQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLH 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 587572851 159 SWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00168 162 SWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETF 219
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-216 1.39e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 263.10  E-value: 1.39e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   2 TWFKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLH 81
Cdd:MTH00038   3 TWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  82 LLYLMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHS 159
Cdd:MTH00038  83 LLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVptSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHS 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 587572851 160 WTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00038 163 WAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTF 219
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 3-216 7.24e-89

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 260.94  E-value: 7.24e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   3 WFKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLHL 82
Cdd:MTH00008   4 WGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  83 LYLMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSW 160
Cdd:MTH00008  84 LYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLptSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 587572851 161 TIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00008 164 TVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSF 219
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 4-216 3.25e-86

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 254.26  E-value: 3.25e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   4 FKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLHLL 83
Cdd:MTH00098   5 FQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  84 YLMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWT 161
Cdd:MTH00098  85 YMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIptSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 587572851 162 IPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00098 165 VPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 8-216 1.85e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 245.01  E-value: 1.85e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   8 FQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLHLLYLMD 87
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  88 EIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSL 165
Cdd:MTH00129  89 EINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIptQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 587572851 166 GIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00129 169 GVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 5-216 3.03e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 244.41  E-value: 3.03e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   5 KFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLHLLY 84
Cdd:MTH00185   6 QLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  85 LMDEIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTI 162
Cdd:MTH00185  86 LMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTptQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTV 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 587572851 163 PSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00185 166 PALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-216 1.32e-81

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 243.12  E-value: 1.32e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   4 FKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLHLL 83
Cdd:MTH00023  14 WQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  84 YLMDEIKSPIMTIKIFGHQWFWSYEYSDF--SNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHS 159
Cdd:MTH00023  94 YLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVptSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHS 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 587572851 160 WTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00023 174 FAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKY 230
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 8-216 1.13e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 237.75  E-value: 1.13e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   8 FQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLHLLYLMD 87
Cdd:MTH00076   9 FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  88 EIKSPIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSL 165
Cdd:MTH00076  89 EINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIptQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 587572851 166 GIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00076 169 GIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNF 219
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 8-216 4.36e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 233.90  E-value: 4.36e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   8 FQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPSLHLLYLMD 87
Cdd:MTH00051  11 FQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  88 EIKSPIMTIKIFGHQWFWSYEYSDF--SNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIP 163
Cdd:MTH00051  91 EVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIptSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 587572851 164 SLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00051 171 SLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKY 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-216 1.04e-74

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 221.68  E-value: 1.04e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  92 PIMTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKM 169
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIpeDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 587572851 170 DAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDF 127
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-211 6.39e-70

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 209.19  E-value: 6.39e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   94 MTIKIFGHQWFWSYEYSDFSNIEFESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDA 171
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIptEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 587572851  172 IPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESI 211
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-216 6.77e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 193.70  E-value: 6.77e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   4 FKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIM--KNKFINIKIK-ENQLIEFIWTIIPPIILIFIALPSL 80
Cdd:MTH00027  33 WQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILlgNNYYSYYWNKlDGSLIEVIWTLIPAFILILIAFPSL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  81 HLLYLMDE-IKSPIMTIKIFGHQWFWSYEYSDF--SNIEFESYMIDNFKNE--NFRLIEVDNKTIIPFKFNIRLLISSED 155
Cdd:MTH00027 113 RLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEfgDLRLLEVDNRLILPVDTNVRVLITAAD 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 587572851 156 VIHSWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00027 193 VLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKY 253
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 8-216 4.51e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 187.91  E-value: 4.51e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   8 FQNSNSPLMEQLIF--------FHDHTIFIIMMIMFTITYMMIFIMKNKFINIKIKENQLIEFIWTIIPPIILIFIALPS 79
Cdd:MTH00080   3 FQGYNLNFSNSLFSsymdwfhnFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  80 LHLLYLMDEIKSPI-MTIKIFGHQWFWSYEYSDFSNIEFESYM--IDNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDV 156
Cdd:MTH00080  83 LSLLYYYGLMNLDSnLTVKVTGHQWYWSYEFSDIPGLEFDSYMksLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDV 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851 157 IHSWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESINLIKF 216
Cdd:MTH00080 163 IHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNF 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 95-211 1.68e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 134.31  E-value: 1.68e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  95 TIKIFGHQWFWSYEYSDfsNIEFESYMIDNFKNenfrlieVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDAIPG 174
Cdd:MTH00047  83 TIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG-------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPG 153

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 587572851 175 RMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIESI 211
Cdd:MTH00047 154 RINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-209 2.88e-36

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 126.87  E-value: 2.88e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   6 FSFQNSNSPLMEQLIFFHDhTIFIIMMIMFTITY-MMIFIM------KNKFINIKIKENQLIEFIWTIIPPIILIFIALP 78
Cdd:COG1622   19 LSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLVFgLLLYFAiryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  79 SLHLLYLMDEIKSPIMTIKIFGHQWFWSYEYSDfsniefesymidnfknENfrlIEVDNKTIIPFKFNIRLLISSEDVIH 158
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD----------------QG---IATVNELVLPVGRPVRFLLTSADVIH 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 587572851 159 SWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIE 209
Cdd:COG1622  159 SFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-211 1.87e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 123.01  E-value: 1.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851 117 FESYMI--DNFKNENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCS 194
Cdd:PTZ00047  51 FQSNLVtdEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 587572851 195 EICGINHSFMPIQIESI 211
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 82-209 7.83e-32

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: 114.79  E-value: 7.83e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851   82 LLYLMDEIKSPIMTIKIFGHQWFWSYEYSDFsniefesymidnfknenfrLIEVDNKTIIPFKFNIRLLISSEDVIHSWT 161
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 587572851  162 IPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIE 209
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-204 1.22e-26

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: 98.08  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  94 MTIKIFGHQWFWSYEYSDfsniefesymidnfknENFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDAIP 173
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPD----------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIP 65

                         90       100       110
                 ....*....|....*....|....*....|.
gi 587572851 174 GRMNQINLFLNRPGLFFGQCSEICGINHSFM 204
Cdd:cd04213   66 GRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-209 7.41e-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: 93.51  E-value: 7.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  94 MTIKIFGHQWFWSYEYSDfsniefesymidnfknenfrlIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDAIP 173
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN---------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVP 59

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 587572851 174 GRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIE 209
Cdd:cd13842   60 GYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-204 3.67e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 89.24  E-value: 3.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  94 MTIKIFGHQWFWSYEYSDfSNIEFesymidnfkneNFRLIEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDAIP 173
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPG-GDGKL-----------GTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVP 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 587572851 174 GRMNQINLFLNRPGLFFGQCSEICGINHSFM 204
Cdd:cd13919   70 GRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-204 3.18e-19

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 78.82  E-value: 3.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  94 MTIKIFGHQWFWSYEYsdfsniefesymidnfKNENfrliEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDAIP 173
Cdd:cd13915    2 LEIQVTGRQWMWEFTY----------------PNGK----REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVP 61

                         90       100       110
                 ....*....|....*....|....*....|.
gi 587572851 174 GRMNQINLFLNRPGLFFGQCSEICGINHSFM 204
Cdd:cd13915   62 GRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-204 1.69e-17

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 74.75  E-value: 1.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  95 TIKIFGHQWFWSYEYSDFSNIEFESymidnfknenfrlievdnkTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDAIPG 174
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTSEQ-------------------LVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPG 62

                         90       100       110
                 ....*....|....*....|....*....|
gi 587572851 175 RMNQINLFLNRPGLFFGQCSEICGINHSFM 204
Cdd:cd13914   63 QYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 82-204 1.08e-14

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: 68.25  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851  82 LLYLMD---EIKSPIMTIKIFGHQWFWSYEYSdfsniefesymidnfkNEnfrlIEVDNKTIIPFKFNIRLLISSEDVIH 158
Cdd:cd13918   18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYP----------------NG----VTTGNTLRVPADTPIALRVTSTDVFH 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 587572851 159 SWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFM 204
Cdd:cd13918   78 TFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 2-82 2.30e-08

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: 50.02  E-value: 2.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587572851    2 TWFKFSFQNSNSPLMEQLIFFHDHTIFIIMMIMFTITYMMIFIM------KNKFINIKIKENQLIEFIWTIIPPIILIFI 75
Cdd:pfam02790   3 TPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILILI 82


                  ....*..
gi 587572851   76 ALPSLHL 82
Cdd:pfam02790  83 ALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 151-204 9.56e-08

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 48.33  E-value: 9.56e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 587572851 151 ISSEDVIHSWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFM 204
Cdd:cd13913   39 VTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 133-204 1.41e-05

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: 42.54  E-value: 1.41e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 587572851 133 IEVDNKTIIPFKFNIRLLISSEDVIHSWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFM 204
Cdd:cd04212   21 IATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 148-204 4.74e-05

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: 40.82  E-value: 4.74e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 587572851 148 RLLISSEDVIHSWTIPSLGIKMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFM 204
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-209 4.22e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 35.44  E-value: 4.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 587572851 151 ISSEDVIHSWTI--PSLGI--KMDAIPGRMNQINLFLNRPGLFFGQCSEICGINHSFMPIQIE 209
Cdd:cd13916   29 VTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFT 91
 
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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