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Conserved domains on  [gi|1806608662|gb|QHW12253|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Chorthippus fallax strelkovi]

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
 1-184 4.78e-119

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 336.03  E-value: 4.78e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00154   12 SASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00154   92 NPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00154  172 VDAVPGRLNQLNFLINRPGLFFGQ 195
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-184 4.78e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 336.03  E-value: 4.78e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00154   12 SASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00154   92 NPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00154  172 VDAVPGRLNQLNFLINRPGLFFGQ 195
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 84-184 5.82e-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: 195.48  E-value: 5.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  84 ITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDA 163
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|.
gi 1806608662 164 TPGRLNQGTFTINRPGLFFGQ 184
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
84-184 7.84e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 182.22  E-value: 7.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  84 ITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDA 163
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 1806608662 164 TPGRLNQGTFTINRPGLFFGQ 184
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-184 3.83e-33

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 117.62  E-value: 3.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   2 ASPLMEQLSFFHDHTMVVLLLITVIVGyslsyTLMI-----------KLTNRNMLHGHLIETIWTALPAITLIFIALPSL 70
Cdd:COG1622    25 AGPIAEEIDDLFWVSLIIMLVIFVLVF-----GLLLyfairyrrrkgDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  71 RLLYLLDDSVDAMITIKTIGQQWYWSYEYsdfvdvefdtymtPESDLEidsfrlldVDNRTILPMNTEVRILTSASDVLH 150
Cdd:COG1622   100 RVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIH 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1806608662 151 SWAVPALGVKIDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:COG1622   159 SFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-184 1.45e-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: 102.46  E-value: 1.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   2 ASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLM-----IKLTNRNMLHGH-LIETIWTALPAI--TLIFIALPSLRLL 73
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkGDEEKPSQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  74 YLLDDSVDAMiTIKTIGQQWYWSYEYSDFvdvefdtymtpesdleidsfrLLDVDNRTILPMNTEVRILTSASDVLHSWA 153
Cdd:TIGR02866  82 LERPIPKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1806608662 154 VPALGVKIDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGF 170
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-184 4.78e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 336.03  E-value: 4.78e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00154   12 SASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00154   92 NPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00154  172 VDAVPGRLNQLNFLINRPGLFFGQ 195
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 2-184 4.79e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 260.23  E-value: 4.79e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   2 ASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVD 81
Cdd:MTH00117   13 SSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  82 AMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKI 161
Cdd:MTH00117   93 PHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKT 172

                         170       180
                  ....*....|....*....|...
gi 1806608662 162 DATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00117  173 DAVPGRLNQTSFITTRPGVFYGQ 195
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-184 3.32e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 255.63  E-value: 3.32e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00140   12 PASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00140   92 NPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00140  172 VDAIPGRLNQLSFEPKRPGVFYGQ 195
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-184 1.02e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 251.56  E-value: 1.02e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00139   12 SASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00139   92 DPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00139  172 IDAVPGRLNQVGFFINRPGVFYGQ 195
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-184 7.85e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 244.61  E-value: 7.85e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00038   12 ASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00038   92 NPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00038  172 MDAVPGRLNQTTFFISRTGLFYGQ 195
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-184 2.29e-80

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 238.22  E-value: 2.29e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00008   12 AASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00008   92 NPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00008  172 VDAVPGRLNQIGFTITRPGVFYGQ 195
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-184 2.56e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 232.95  E-value: 2.56e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00168   12 AASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEID 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00168   92 KPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00168  172 MDAVPGRLNQLAFLSSRPGSFYGQ 195
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-184 1.63e-76

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 228.45  E-value: 1.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00098   12 ATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEIN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00098   92 NPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00098  172 TDAIPGRLNQTTLMSTRPGLYYGQ 195
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-184 1.65e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 221.16  E-value: 1.65e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00023   21 AADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVD--VEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALG 158
Cdd:MTH00023  101 SPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLG 180

                         170       180
                  ....*....|....*....|....*.
gi 1806608662 159 VKIDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00023  181 LKIDAVPGRLNQTGFFIKRPGVFYGQ 206
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-184 3.82e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 220.04  E-value: 3.82e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00076   12 AASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEIN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00076   92 DPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00076  172 TDAIPGRLNQTSFIASRPGVYYGQ 195
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-184 5.36e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 219.59  E-value: 5.36e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00129   12 AASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEIN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00129   92 DPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00129  172 MDAVPGRLNQTAFIASRPGVFYGQ 195
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-184 2.50e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 217.83  E-value: 2.50e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00185   12 AASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEIN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVK 160
Cdd:MTH00185   92 DPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVK 171

                         170       180
                  ....*....|....*....|....
gi 1806608662 161 IDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00185  172 MDAVPGRLNQATFIISRPGLYYGQ 195
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-184 9.02e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 213.87  E-value: 9.02e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSV 80
Cdd:MTH00051   14 AASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  81 DAMITIKTIGQQWYWSYEYSDF--VDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALG 158
Cdd:MTH00051   94 DPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLS 173

                         170       180
                  ....*....|....*....|....*.
gi 1806608662 159 VKIDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00051  174 VKIDAVPGRLNQTSFFIKRPGVFYGQ 199
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 84-184 5.82e-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: 195.48  E-value: 5.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  84 ITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDA 163
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|.
gi 1806608662 164 TPGRLNQGTFTINRPGLFFGQ 184
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQ 103
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
84-184 7.84e-60

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 182.22  E-value: 7.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  84 ITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDA 163
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|.
gi 1806608662 164 TPGRLNQGTFTINRPGLFFGQ 184
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQ 101
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-184 5.59e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 172.13  E-value: 5.59e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   1 SASPLMEQLSFFHDHtmvVLLLITVIVGYSLSYTLMIKLTNR------NMLHGHLIETIWTALPAITLIFIALPSLRLLY 74
Cdd:MTH00027   40 AGSPVMEEIIMLHDQ---ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  75 LLDDSV-DAMITIKTIGQQWYWSYEYSDF--VDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHS 151
Cdd:MTH00027  117 IMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHS 196

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1806608662 152 WAVPALGVKIDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00027  197 WTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQ 229
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 9-184 3.55e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 148.62  E-value: 3.55e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   9 LSFFHDHTMVVLLLITVIVGYSLSYTLMIKLT---NRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLD-DSVDAMI 84
Cdd:MTH00080   19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNfyfKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  85 TIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDAT 164
Cdd:MTH00080   99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                         170       180
                  ....*....|....*....|
gi 1806608662 165 PGRLNQGTFTINRPGLFFGQ 184
Cdd:MTH00080  179 SGILSTLCYSFPMPGVFYGQ 198
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-184 3.83e-33

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 117.62  E-value: 3.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   2 ASPLMEQLSFFHDHTMVVLLLITVIVGyslsyTLMI-----------KLTNRNMLHGHLIETIWTALPAITLIFIALPSL 70
Cdd:COG1622    25 AGPIAEEIDDLFWVSLIIMLVIFVLVF-----GLLLyfairyrrrkgDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  71 RLLYLLDDSVDAMITIKTIGQQWYWSYEYsdfvdvefdtymtPESDLEidsfrlldVDNRTILPMNTEVRILTSASDVLH 150
Cdd:COG1622   100 RVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRFLLTSADVIH 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1806608662 151 SWAVPALGVKIDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:COG1622   159 SFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-184 1.45e-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: 102.46  E-value: 1.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662   2 ASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLM-----IKLTNRNMLHGH-LIETIWTALPAI--TLIFIALPSLRLL 73
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkGDEEKPSQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  74 YLLDDSVDAMiTIKTIGQQWYWSYEYSDFvdvefdtymtpesdleidsfrLLDVDNRTILPMNTEVRILTSASDVLHSWA 153
Cdd:TIGR02866  82 LERPIPKDAL-KVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1806608662 154 VPALGVKIDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGF 170
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-183 2.61e-24

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 93.87  E-value: 2.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  17 MVVLLLITVIVGYSLSytlmIKLTNRNmlhgHLIETIWTALPaiTLIFIALPSLRLLYLLDDSVDAMI-TIKTIGQQWYW 95
Cdd:MTH00047   24 WVYIMLCWQVVSGNGS----VNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  96 SYEYSDfvDVEFDTYMTPESDLeidsfrlldVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDATPGRLNQGTFTI 175
Cdd:MTH00047   94 SYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162


                  ....*...
gi 1806608662 176 NRPGLFFG 183
Cdd:MTH00047  163 DRHGVFVG 170
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 107-184 1.77e-22

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 88.34  E-value: 1.77e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1806608662 107 FDTYMTPESDLEIDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDATPGRLNQGTFTINRPGLFFGQ 184
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-66 9.67e-18

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: 73.91  E-value: 9.67e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1806608662   1 SASPLMEQLSFFHDHTMVVLLLITVIVGYSLSYTLM------IKLTNRNMLHGHLIETIWTALPAITLIFIA 66
Cdd:pfam02790  12 AASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 84-184 4.10e-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: 72.33  E-value: 4.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  84 ITIKTIGQQWYWSYEYSDfvdvefdtymtpesdleidsfrlLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDA 163
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|.
gi 1806608662 164 TPGRLNQGTFTINRPGLFFGQ 184
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), ...
 84-184 8.78e-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: 69.19  E-value: 8.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  84 ITIKTIGQQWYWSYEYSDFVDVEFDTymtpesdleidsfrlldvDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDA 163
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100
                  ....*....|....*....|.
gi 1806608662 164 TPGRLNQGTFTINRPGLFFGQ 184
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQ 84
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-184 3.69e-15

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: 67.67  E-value: 3.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  84 ITIKTIGQQWYWSYEYSDFVDVEFDTYMTPESDLEidsfrlldvdnrtiLPMNTEVRILTSASDVLHSWAVPALGVKIDA 163
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|.
gi 1806608662 164 TPGRLNQGTFTINRPGLFFGQ 184
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVR 88
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-181 1.21e-13

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: 63.42  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  84 ITIKTIGQQWYWSYEYsdfvdvefdtymtPESDLEIdsfrlldvdNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDA 163
Cdd:cd13915     2 LEIQVTGRQWMWEFTY-------------PNGKREI---------NELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90
                  ....*....|....*...
gi 1806608662 164 TPGRLNQGTFTINRPGLF 181
Cdd:cd13915    60 VPGRYTYLWFEATKPGEY 77
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-169 1.03e-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: 58.57  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  84 ITIKTIGQQWYWSYEYsdfvdvefdtymtPESDLeidsfrllDVDNRTILPMNTEVRILTSASDVLHSWAVPALGVKIDA 163
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANV--------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                  ....*.
gi 1806608662 164 TPGRLN 169
Cdd:cd13914    60 FPGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 77-179 2.23e-08

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 50.53  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1806608662  77 DDSVDAMITIKTIGQQWYWSYEYSDFVDvefdtymtpesdlEIDSFRLldvdnrtilPMNTEVRILTSASDVLHSWAVPA 156
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNGVT-------------TGNTLRV---------PADTPIALRVTSTDVFHTFGIPE 83

                          90       100
                  ....*....|....*....|...
gi 1806608662 157 LGVKIDATPGRLNQGTFTINRPG 179
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPG 106
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 129-184 1.34e-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: 1.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1806608662 129 NRTILPMNTEVRI-LTSASdVLHSWAVPALGVKIDATPGRLNQGTFTINRPGLFFGQ 184
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 ...
 133-181 1.99e-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: 36.01  E-value: 1.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1806608662 133 LPMNTEVRILTSASDVLHSWAVPALGVKIDATPGRLNQGTFTINRPGLF 181
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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