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Conserved domains on  [gi|1100877015|gb|APB87837|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Sitophilus oryzae]

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
 1-183 1.20e-99

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 286.72  E-value: 1.20e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00154   15 PLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00154   95 ITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00154  175 VPGRLNQLNFLINRPGLFFGQCS 197
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-183 1.20e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 286.72  E-value: 1.20e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00154   15 PLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00154   95 ITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00154  175 VPGRLNQLNFLINRPGLFFGQCS 197
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 79-183 1.77e-67

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: 202.03  E-value: 1.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  79 PSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKI 158
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100
                  ....*....|....*....|....*
gi 1100877015 159 DSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCS 105
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
81-183 1.58e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 178.76  E-value: 1.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCS 103
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
68-183 1.25e-25

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 98.36  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  68 RLLYILDEINNPSITIKIIGHQWYWSYEYSDYkNIEFDSYM-IPTkelnsfnfrllevdNRTpfpyktqIRLLVTSADVI 146
Cdd:COG1622   100 RVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-GIATVNELvLPV--------------GRP-------VRFLLTSADVI 157

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1100877015 147 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:COG1622   158 HSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCA 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 69-182 1.17e-23

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: 92.44  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  69 LLYILDEINNPSITIKIIGHQWYWSYEYSDYkniefdsymiptkelnsfnfrLLEVDNRTPFPYKTQIRLLVTSADVIHS 148
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1100877015 149 WTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQC 182
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFC 171
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-183 1.20e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 286.72  E-value: 1.20e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00154   15 PLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00154   95 ITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00154  175 VPGRLNQLNFLINRPGLFFGQCS 197
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-183 5.68e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 247.16  E-value: 5.68e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00140   15 PLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00140   95 LTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00140  175 IPGRLNQLSFEPKRPGVFYGQCS 197
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-183 2.52e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 240.59  E-value: 2.52e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00117   15 PIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00117   95 LTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00117  175 VPGRLNQTSFITTRPGVFYGQCS 197
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-183 1.44e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 238.46  E-value: 1.44e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00139   15 PLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00139   95 LTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00139  175 VPGRLNQVGFFINRPGVFYGQCS 197
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-183 1.42e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 231.13  E-value: 1.42e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00038   15 PLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00038   95 LTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00038  175 VPGRLNQTTFFISRTGLFYGQCS 197
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-183 2.98e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 230.25  E-value: 2.98e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00168   15 PVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00168   95 LTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00168  175 VPGRLNQLAFLSSRPGSFYGQCS 197
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-183 1.55e-75

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 225.89  E-value: 1.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00008   15 PVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00008   95 ITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00008  175 VPGRLNQIGFTITRPGVFYGQCS 197
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-183 8.69e-74

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 221.52  E-value: 8.69e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00098   15 PIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00098   95 LTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00098  175 IPGRLNQTTLMSTRPGLYYGQCS 197
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-183 6.85e-72

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 216.93  E-value: 6.85e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00023   24 PVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYK--NIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKI 158
Cdd:MTH00023  104 LTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKI 183

                         170       180
                  ....*....|....*....|....*
gi 1100877015 159 DSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00023  184 DAVPGRLNQTGFFIKRPGVFYGQCS 208
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-183 1.76e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 215.73  E-value: 1.76e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00129   15 PVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00129   95 LTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00129  175 VPGRLNQTAFIASRPGVFYGQCS 197
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-183 5.54e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 209.36  E-value: 5.54e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00185   15 PVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00185   95 LTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00185  175 VPGRLNQATFIISRPGLYYGQCS 197
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-183 2.39e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 207.71  E-value: 2.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00076   15 PIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:MTH00076   95 LTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDA 174

                         170       180
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00076  175 IPGRLNQTSFIASRPGVYYGQCS 197
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 79-183 1.77e-67

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: 202.03  E-value: 1.77e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  79 PSITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKI 158
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100
                  ....*....|....*....|....*
gi 1100877015 159 DSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCS 105
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-183 9.46e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 203.86  E-value: 9.46e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS 80
Cdd:MTH00051   17 PVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDY--KNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKI 158
Cdd:MTH00051   97 LTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKI 176

                         170       180
                  ....*....|....*....|....*
gi 1100877015 159 DSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00051  177 DAVPGRLNQTSFFIKRPGVFYGQCS 201
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
81-183 1.58e-58

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 178.76  E-value: 1.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCS 103
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-183 1.33e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 166.35  E-value: 1.33e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFL---LEGQLIETIWTILPAIILILIALPSLRLLYILDE-I 76
Cdd:MTH00027   43 PVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  77 NNPSITIKIIGHQWYWSYEYSDY--KNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSM 154
Cdd:MTH00027  123 FSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSL 202

                         170       180
                  ....*....|....*....|....*....
gi 1100877015 155 GIKIDSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00027  203 AVKMDAVPGRINETGFLIKRPGIFYGQCS 231
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-183 4.40e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 148.62  E-value: 4.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015   3 MEHLTLFHDHTILILILITILVSQMLLSMLLNKLSHRFLLEGQLIETIWTILPAIILILIALPSLRLLYILDEINNPS-I 81
Cdd:MTH00080   19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLDSnL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  82 TIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDST 161
Cdd:MTH00080   99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                         170       180
                  ....*....|....*....|..
gi 1100877015 162 PGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00080  179 SGILSTLCYSFPMPGVFYGQCS 200
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 43-183 3.33e-31

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 111.58  E-value: 3.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  43 EGQLIETIWTILPAIILILIALPslRLLYILDEIN-NPSITIKIIGHQWYWSYEYSDykNIEFDSYMipTKELNSfnfrl 121
Cdd:MTH00047   45 ENQVLELLWTVVPTLLVLVLCFL--NLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFM--TDDIFG----- 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1100877015 122 leVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:MTH00047  114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCS 173
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 104-183 3.88e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 97.58  E-value: 3.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015 104 FDSYMIPTKELNSFNFRLLEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
68-183 1.25e-25

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 98.36  E-value: 1.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  68 RLLYILDEINNPSITIKIIGHQWYWSYEYSDYkNIEFDSYM-IPTkelnsfnfrllevdNRTpfpyktqIRLLVTSADVI 146
Cdd:COG1622   100 RVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-GIATVNELvLPV--------------GRP-------VRFLLTSADVI 157

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1100877015 147 HSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:COG1622   158 HSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCA 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 69-182 1.17e-23

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: 92.44  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  69 LLYILDEINNPSITIKIIGHQWYWSYEYSDYkniefdsymiptkelnsfnfrLLEVDNRTPFPYKTQIRLLVTSADVIHS 148
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1100877015 149 WTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQC 182
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFC 171
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 80-183 1.23e-17

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: 74.19  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  80 SITIKIIGHQWYWSYEYSDYKNIEFDS---YMIPTKElnsfnfrllevdnrtpfpyktQIRLLVTSADVIHSWTVPSMGI 156
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIVTaneLHIPVGR---------------------PVRLRLTSADVIHSFWVPSLAG 59

                          90       100
                  ....*....|....*....|....*..
gi 1100877015 157 KIDSTPGRLNQANLIANRSSIFFGQCS 183
Cdd:cd04213    60 KMDMIPGRTNRLWLQADEPGVYRGQCA 86
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 81-183 4.55e-15

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: 66.94  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYsdykniefdsymiptkeLNSFNFRLLEVDNRTPfpyktqIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:cd13842     1 LTVYVTGVQWSWTFIY-----------------PNVRTPNEIVVPAGTP------VRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICA 80
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 81-183 8.54e-12

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: 58.81  E-value: 8.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKELNsfnfrlLEVDNRtpfpyktqIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELH------LPVGRP--------VLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|...
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQCS 183
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCA 90
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 81-166 1.75e-10

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: 55.49  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKNIEFDSYMIPTKelnsfnfrllevdnrtpfpykTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTSEQLVIPAD---------------------RPVYFRITSRDVIHAFHVPELGLKQDA 59


                  ....*.
gi 1100877015 161 TPGRLN 166
Cdd:cd13914    60 FPGQYN 65
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-183 4.47e-10

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: 54.17  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  80 SITIKIIGHQWYWSYEYSDYKniefdsymiptkelnsfnfrllEVDNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKID 159
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGK----------------------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100
                  ....*....|....*....|....
gi 1100877015 160 STPGRLNQANLIANRSSIFFGQCS 183
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCT 82
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 69-182 8.71e-09

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: 51.69  E-value: 8.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  69 LLYILD---EINNPSITIKIIGHQWYWSYEYSDykNIEFDSYMIptkelnsfnfrllevdnrtpFPYKTQIRLLVTSADV 145
Cdd:cd13918    18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTLR--------------------VPADTPIALRVTSTDV 75

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1100877015 146 IHSWTVPSMGIKIDSTPGRLNQANLIANRSSIFFGQC 182
Cdd:cd13918    76 FHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKC 112
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-55 1.17e-05

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: 41.93  E-value: 1.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1100877015   1 PLMEHLTLFHDHTILILILITILVSQMLLSMLL------NKLSHRFLLEGQLIETIWTILP 55
Cdd:pfam02790  15 PLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIP 75
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 81-181 1.35e-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: 42.15  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1100877015  81 ITIKIIGHQWYWSYEYSDYKniefdsymIPTKelnsfnfrllevdNRTPFPYKTQIRLLVTSADVIHSWTVPSMGIKIDS 160
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQG--------IATV-------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYA 59

                          90       100
                  ....*....|....*....|.
gi 1100877015 161 TPGRLNQANLIANRSSIFFGQ 181
Cdd:cd04212    60 MAGMQTQLHLIADKPGTYQGL 80
 
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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