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Conserved domains on  [gi|1933122337|gb|QPD01011|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Gomphocerus sibiricus]

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
 1-178 5.19e-114

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 322.93  E-value: 5.19e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00154   18 EQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00154   98 KTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00154  178 RLNQLNFLINRPGLFFGQ 195
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-178 5.19e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 322.93  E-value: 5.19e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00154   18 EQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00154   98 KTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00154  178 RLNQLNFLINRPGLFFGQ 195
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 78-178 1.17e-65

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: 197.02  E-value: 1.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  78 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 157
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|.
gi 1933122337 158 TPGRLNQGTFTINRPGLFFGQ 178
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
78-178 1.05e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.15  E-value: 1.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  78 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 157
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 1933122337 158 TPGRLNQGTFTINRPGLFFGQ 178
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-178 1.28e-30

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 111.07  E-value: 1.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGyslsyTLMI-----------KLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYL 69
Cdd:COG1622    30 EEIDDLFWVSLIIMLVIFVLVF-----GLLLyfairyrrrkgDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  70 LDDSVDAMITIKTIGRQWYWSYEYsdfvdvefdtymtPESDLEidgfrlldVDNRTILPMNTEVRILTSASDVLHSWAVP 149
Cdd:COG1622   105 LDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIHSFWVP 163

                         170       180
                  ....*....|....*....|....*....
gi 1933122337 150 ALGIKIDATPGRLNQGTFTINRPGLFFGQ 178
Cdd:COG1622   164 ALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-178 6.53e-27

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: 100.53  E-value: 6.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLM-----IKLTNRNMLHGN-LIETIWTTLPAI--TLIFIALPSLRLLYLLDD 72
Cdd:TIGR02866   7 QQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkGDEEKPSQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLYLERPI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  73 SVDAMiTIKTIGRQWYWSYEYSDFvdvefdtymtpesdleidGFRlldVDNRTILPMNTEVRILTSASDVLHSWAVPALG 152
Cdd:TIGR02866  87 PKDAL-KVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELG 144

                         170       180
                  ....*....|....*....|....*.
gi 1933122337 153 IKIDATPGRLNQGTFTINRPGLFFGQ 178
Cdd:TIGR02866 145 GKIDAIPGQTNALWFNADEPGVYYGF 170
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-178 5.19e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 322.93  E-value: 5.19e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00154   18 EQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00154   98 KTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00154  178 RLNQLNFLINRPGLFFGQ 195
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-178 9.00e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 249.06  E-value: 9.00e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00117   18 EELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00117   98 KAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00117  178 RLNQTSFITTRPGVFYGQ 195
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-178 1.08e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 248.70  E-value: 1.08e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00140   18 EELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00140   98 KAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00140  178 RLNQLSFEPKRPGVFYGQ 195
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-178 5.44e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 239.23  E-value: 5.44e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00139   18 EQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00139   98 KAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00139  178 RLNQVGFFINRPGVFYGQ 195
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-178 2.43e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 232.67  E-value: 2.43e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00038   18 EELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00038   98 KAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00038  178 RLNQTTFFISRTGLFYGQ 195
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-178 2.97e-77

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 230.13  E-value: 2.97e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   2 QLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIK 81
Cdd:MTH00008   19 QLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLK 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  82 TIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGR 161
Cdd:MTH00008   99 TIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGR 178

                         170
                  ....*....|....*..
gi 1933122337 162 LNQGTFTINRPGLFFGQ 178
Cdd:MTH00008  179 LNQIGFTITRPGVFYGQ 195
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-178 2.12e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 227.56  E-value: 2.12e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00168   18 EELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00168   98 KAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00168  178 RLNQLAFLSSRPGSFYGQ 195
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-178 1.57e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 220.36  E-value: 1.57e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00098   18 EELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00098   98 KTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00098  178 RLNQTTLMSTRPGLYYGQ 195
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-178 1.20e-70

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 213.84  E-value: 1.20e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00023   27 EEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVD--VEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDAT 158
Cdd:MTH00023  107 KAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAV 186

                         170       180
                  ....*....|....*....|
gi 1933122337 159 PGRLNQGTFTINRPGLFFGQ 178
Cdd:MTH00023  187 PGRLNQTGFFIKRPGVFYGQ 206
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-178 7.00e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 211.28  E-value: 7.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00185   18 EELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00185   98 KAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00185  178 RLNQATFIISRPGLYYGQ 195
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-178 1.39e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 210.73  E-value: 1.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00129   18 EELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00129   98 KAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00129  178 RLNQTAFIASRPGVFYGQ 195
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-178 1.47e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 210.41  E-value: 1.47e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00076   18 EELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 160
Cdd:MTH00076   98 KAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPG 177

                         170
                  ....*....|....*...
gi 1933122337 161 RLNQGTFTINRPGLFFGQ 178
Cdd:MTH00076  178 RLNQTSFIASRPGVYYGQ 195
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-178 1.02e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 206.17  E-value: 1.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITI 80
Cdd:MTH00051   20 EEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  81 KTIGRQWYWSYEYSDF--VDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDAT 158
Cdd:MTH00051  100 KAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAV 179

                         170       180
                  ....*....|....*....|
gi 1933122337 159 PGRLNQGTFTINRPGLFFGQ 178
Cdd:MTH00051  180 PGRLNQTSFFIKRPGVFYGQ 199
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 78-178 1.17e-65

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: 197.02  E-value: 1.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  78 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 157
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|.
gi 1933122337 158 TPGRLNQGTFTINRPGLFFGQ 178
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
78-178 1.05e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 184.15  E-value: 1.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  78 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 157
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 1933122337 158 TPGRLNQGTFTINRPGLFFGQ 178
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-178 7.71e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 164.04  E-value: 7.71e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHtmvVLLLITVIVGYSLSYTLMIKLTNR------NMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLDDSV 74
Cdd:MTH00027   46 EEIIMLHDQ---ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECG 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  75 -DAMITIKTIGRQWYWSYEYSDF--VDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAL 151
Cdd:MTH00027  123 fSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSL 202

                         170       180
                  ....*....|....*....|....*..
gi 1933122337 152 GIKIDATPGRLNQGTFTINRPGLFFGQ 178
Cdd:MTH00027  203 AVKMDAVPGRINETGFLIKRPGIFYGQ 229
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-178 1.17e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 149.78  E-value: 1.17e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   3 LSFFHDHTMVVLLLITVIVGYSLSYTLMIKLT---NRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYLLD-DSVDAMI 78
Cdd:MTH00080   19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNfyfKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  79 TIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDAT 158
Cdd:MTH00080   99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                         170       180
                  ....*....|....*....|
gi 1933122337 159 PGRLNQGTFTINRPGLFFGQ 178
Cdd:MTH00080  179 SGILSTLCYSFPMPGVFYGQ 198
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-178 1.28e-30

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 111.07  E-value: 1.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGyslsyTLMI-----------KLTNRNMLHGNLIETIWTTLPAITLIFIALPSLRLLYL 69
Cdd:COG1622    30 EEIDDLFWVSLIIMLVIFVLVF-----GLLLyfairyrrrkgDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  70 LDDSVDAMITIKTIGRQWYWSYEYsdfvdvefdtymtPESDLEidgfrlldVDNRTILPMNTEVRILTSASDVLHSWAVP 149
Cdd:COG1622   105 LDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIHSFWVP 163

                         170       180
                  ....*....|....*....|....*....
gi 1933122337 150 ALGIKIDATPGRLNQGTFTINRPGLFFGQ 178
Cdd:COG1622   164 ALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-178 6.53e-27

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: 100.53  E-value: 6.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLM-----IKLTNRNMLHGN-LIETIWTTLPAI--TLIFIALPSLRLLYLLDD 72
Cdd:TIGR02866   7 QQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkGDEEKPSQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLYLERPI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  73 SVDAMiTIKTIGRQWYWSYEYSDFvdvefdtymtpesdleidGFRlldVDNRTILPMNTEVRILTSASDVLHSWAVPALG 152
Cdd:TIGR02866  87 PKDAL-KVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELG 144

                         170       180
                  ....*....|....*....|....*.
gi 1933122337 153 IKIDATPGRLNQGTFTINRPGLFFGQ 178
Cdd:TIGR02866 145 GKIDAIPGQTNALWFNADEPGVYYGF 170
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 11-177 1.83e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 99.26  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  11 MVVLLLITVIVGYSLSytlmIKLTNRNmlhgNLIETIWTTLPaiTLIFIALPSLRLLYLLDDSVDAMI-TIKTIGRQWYW 89
Cdd:MTH00047   24 WVYIMLCWQVVSGNGS----VNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  90 SYEYSDfvDVEFDTYMTPESDLeidgfrlldVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTI 169
Cdd:MTH00047   94 SYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162


                  ....*...
gi 1933122337 170 NRPGLFFG 177
Cdd:MTH00047  163 DRHGVFVG 170
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 101-178 4.74e-23

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 89.49  E-value: 4.74e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933122337 101 FDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQ 178
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 78-178 5.35e-17

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: 71.94  E-value: 5.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  78 ITIKTIGRQWYWSYEYSDfvdvefdtymtpesdleidgfrlLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 157
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|.
gi 1933122337 158 TPGRLNQGTFTINRPGLFFGQ 178
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTII 78
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 78-178 4.95e-16

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: 69.57  E-value: 4.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  78 ITIKTIGRQWYWSYEYSDFVDVEFDTymtpesdleidgfrlldvDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 157
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100
                  ....*....|....*....|.
gi 1933122337 158 TPGRLNQGTFTINRPGLFFGQ 178
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQ 84
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 78-175 1.46e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 65.73  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  78 ITIKTIGRQWYWSYEYSDfvdvefdtymtpesdleidGFRlldVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 157
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90
                  ....*....|....*...
gi 1933122337 158 TPGRLNQGTFTINRPGLF 175
Cdd:cd13915    60 VPGRYTYLWFEATKPGEY 77
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 78-178 2.06e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 65.74  E-value: 2.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  78 ITIKTIGRQWYWSYEYsdfvdvefdtymtPESDlEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 157
Cdd:cd13919     2 LVVEVTAQQWAWTFRY-------------PGGD-GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|.
gi 1933122337 158 TPGRLNQGTFTINRPGLFFGQ 178
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVR 88
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-60 5.07e-14

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: 64.28  E-value: 5.07e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1933122337   1 EQLSFFHDHTMVVLLLITVIVGYSLSYTLM------IKLTNRNMLHGNLIETIWTTLPAITLIFIA 60
Cdd:pfam02790  18 EGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 78-163 7.45e-11

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: 56.26  E-value: 7.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  78 ITIKTIGRQWYWSYEYsdfvdvefdtymtPESDLeidgfrllDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 157
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANV--------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                  ....*.
gi 1933122337 158 TPGRLN 163
Cdd:cd13914    60 FPGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-173 2.05e-07

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: 47.84  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122337  71 DDSVDAMITIKTIGRQWYWSYEYSDFVDvefdtymtpesdlEIDGFRLldvdnrtilPMNTEVRILTSASDVLHSWAVPA 150
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNGVT-------------TGNTLRV---------PADTPIALRVTSTDVFHTFGIPE 83

                          90       100
                  ....*....|....*....|...
gi 1933122337 151 LGIKIDATPGRLNQGTFTINRPG 173
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPG 106
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 123-178 1.37e-03

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: 36.37  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1933122337 123 NRTILPMNTEVRI-LTSASdVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQ 178
Cdd:cd04212    25 NELVIPVGRPVNFrLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 127-175 2.97e-03

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: 35.62  E-value: 2.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1933122337 127 LPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLF 175
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEY 77
 
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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