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Conserved domains on  [gi|1933122345|gb|QPD01015|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Stenobothrus eurasius]

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
 1-185 7.12e-118

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 332.95  E-value: 7.12e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00154   16 LMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00154   96 TLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00154  176 PGRLNQLNFLINRPGLFFGQCSEIC 200
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-185 7.12e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 332.95  E-value: 7.12e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00154   16 LMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00154   96 TLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00154  176 PGRLNQLNFLINRPGLFFGQCSEIC 200
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 80-185 2.23e-70

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: 209.35  E-value: 2.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  80 ITIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEIC 108
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
80-185 2.35e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 196.48  E-value: 2.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  80 ITIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEIC 106
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-185 1.65e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 123.79  E-value: 1.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   2 MEQLSFFHDHTMIVLLLITVIVgysLSYMLVINLMNR---------NMLHGHLIETIWTALPAITLIFIALPSLRLLYLL 72
Cdd:COG1622    29 AEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHAL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  73 DDSVDAMITIKTIGRQWYWSYEYsdfvdvefdtymlPESDLKTDsfrlldvdNRTILPMNTEVRILTSASDVLHSWAVPA 152
Cdd:COG1622   106 DDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIATV--------NELVLPVGRPVRFLLTSADVIHSFWVPA 164

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1933122345 153 IGIKIDATPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:COG1622   165 LGGKQDAIPGRVTELWFTADKPGTYRGQCAELC 197
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-185 1.09e-29

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: 108.24  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLvinLMNRN--------MLHGH-LIETIWTALPAI--TLIFIALPSLRLL 69
Cdd:TIGR02866   5 IAQQIAFLFLFVLAVSTLISLLVAALLAYVV---WKFRRkgdeekpsQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  70 YLLDDSVDAMiTIKTIGRQWYWSYEYsdfvdvefdtymlPESDLKTDsfrlldvdNRTILPMNTEVRILTSASDVLHSWA 149
Cdd:TIGR02866  82 LERPIPKDAL-KVKVTGYQWWWDFEY-------------PESGFTTV--------NELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1933122345 150 VPAIGIKIDATPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELC 175
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-185 7.12e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 332.95  E-value: 7.12e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00154   16 LMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00154   96 TLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00154  176 PGRLNQLNFLINRPGLFFGQCSEIC 200
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-185 1.62e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 264.08  E-value: 1.62e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00117   16 IMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00117   96 TIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00117  176 PGRLNQTSFITTRPGVFYGQCSEIC 200
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-185 3.46e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 255.41  E-value: 3.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00139   16 LMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00139   96 TFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00139  176 PGRLNQVGFFINRPGVFYGQCSEIC 200
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-185 6.89e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 252.17  E-value: 6.89e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00140   16 LMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00140   96 TVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAI 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00140  176 PGRLNQLSFEPKRPGVFYGQCSEIC 200
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-185 1.35e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 251.54  E-value: 1.35e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00038   16 LMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00038   96 TIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00038  176 PGRLNQTTFFISRTGLFYGQCSEIC 200
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-185 3.49e-84

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 247.85  E-value: 3.49e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00008   16 VMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00008   96 TLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00008  176 PGRLNQIGFTITRPGVFYGQCSEIC 200
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-185 6.56e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 239.50  E-value: 6.56e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00168   16 VMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00168   96 TIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00168  176 PGRLNQLAFLSSRPGSFYGQCSEIC 200
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-185 8.22e-80

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 236.92  E-value: 8.22e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00098   16 IMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00098   96 TVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAI 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00098  176 PGRLNQTTLMSTRPGLYYGQCSEIC 200
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-185 3.73e-75

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 225.40  E-value: 3.73e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   2 MEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMIT 81
Cdd:MTH00023   26 MEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  82 IKTIGRQWYWSYEYSDFVD--VEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:MTH00023  106 IKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDA 185

                         170       180
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00023  186 VPGRLNQTGFFIKRPGVFYGQCSEIC 211
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-185 8.27e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 224.27  E-value: 8.27e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00076   16 IMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00076   96 TVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAI 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00076  176 PGRLNQTSFIASRPGVYYGQCSEIC 200
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-185 3.35e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 222.67  E-value: 3.35e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00129   16 VMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00129   96 TIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00129  176 PGRLNQTAFIASRPGVFYGQCSEIC 200
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-185 6.18e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 222.07  E-value: 6.18e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMI 80
Cdd:MTH00185   16 VMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00185   96 TIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAV 175

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00185  176 PGRLNQATFIISRPGLYYGQCSEIC 200
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-185 2.41e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 218.11  E-value: 2.41e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   2 MEQLSFFHDHTMIVLLLITVIVGYSLSYMLVINLMNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDDSVDAMIT 81
Cdd:MTH00051   19 MEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  82 IKTIGRQWYWSYEYSDF--VDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:MTH00051   99 IKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDA 178

                         170       180
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00051  179 VPGRLNQTSFFIKRPGVFYGQCSEIC 204
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 80-185 2.23e-70

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: 209.35  E-value: 2.23e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  80 ITIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEIC 108
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
80-185 2.35e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 196.48  E-value: 2.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  80 ITIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEIC 106
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-185 6.72e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 174.83  E-value: 6.72e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHtmiVLLLITVIVGYSLSYMLVINLMNR------NMLHGHLIETIWTALPAITLIFIALPSLRLLYLLDD 74
Cdd:MTH00027   44 VMEEIIMLHDQ---ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDE 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  75 SV-DAMITIKTIGRQWYWSYEYSDF--VDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVP 151
Cdd:MTH00027  121 CGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVP 200

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1933122345 152 AIGIKIDATPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00027  201 SLAVKMDAVPGRINETGFLIKRPGIFYGQCSEIC 234
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 5-185 9.14e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 157.86  E-value: 9.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   5 LSFFHDHTMIVLLLITVIVGYSLSYMLVINL---MNRNMLHGHLIETIWTALPAITLIFIALPSLRLLYLLD-DSVDAMI 80
Cdd:MTH00080   19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNnfyFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  81 TIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDAT 160
Cdd:MTH00080   99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                         170       180
                  ....*....|....*....|....*
gi 1933122345 161 PGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:MTH00080  179 SGILSTLCYSFPMPGVFYGQCSEIC 203
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-185 1.65e-35

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 123.79  E-value: 1.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   2 MEQLSFFHDHTMIVLLLITVIVgysLSYMLVINLMNR---------NMLHGHLIETIWTALPAITLIFIALPSLRLLYLL 72
Cdd:COG1622    29 AEEIDDLFWVSLIIMLVIFVLV---FGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHAL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  73 DDSVDAMITIKTIGRQWYWSYEYsdfvdvefdtymlPESDLKTDsfrlldvdNRTILPMNTEVRILTSASDVLHSWAVPA 152
Cdd:COG1622   106 DDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIATV--------NELVLPVGRPVRFLLTSADVIHSFWVPA 164

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1933122345 153 IGIKIDATPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:COG1622   165 LGGKQDAIPGRVTELWFTADKPGTYRGQCAELC 197
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-185 1.09e-29

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: 108.24  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLvinLMNRN--------MLHGH-LIETIWTALPAI--TLIFIALPSLRLL 69
Cdd:TIGR02866   5 IAQQIAFLFLFVLAVSTLISLLVAALLAYVV---WKFRRkgdeekpsQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  70 YLLDDSVDAMiTIKTIGRQWYWSYEYsdfvdvefdtymlPESDLKTDsfrlldvdNRTILPMNTEVRILTSASDVLHSWA 149
Cdd:TIGR02866  82 LERPIPKDAL-KVKVTGYQWWWDFEY-------------PESGFTTV--------NELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1933122345 150 VPAIGIKIDATPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELC 175
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 103-185 1.42e-28

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 104.13  E-value: 1.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345 103 FDTYMLPESDLKTDSFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDATPGRLNQGTFTINRPGLFFGQCS 182
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130


                  ...
gi 1933122345 183 EIC 185
Cdd:PTZ00047  131 EMC 133
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 13-185 4.35e-28

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 103.88  E-value: 4.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  13 MIVLLLITVIVGYSL-SYMLVINLMNRNmlhgHLIETIWTALPaiTLIFIALPSLRLLYLLDDSVDAMI-TIKTIGRQWY 90
Cdd:MTH00047   19 VFIPCWVYIMLCWQVvSGNGSVNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWY 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  91 WSYEYSDfvDVEFDTYMLPESDLktdsfrlldVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDATPGRLNQGTFT 170
Cdd:MTH00047   93 WSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFC 161

                         170
                  ....*....|....*
gi 1933122345 171 INRPGLFFGQCSEIC 185
Cdd:MTH00047  162 PDRHGVFVGYCSELC 176
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 80-185 1.64e-20

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: 81.19  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  80 ITIKTIGRQWYWSYEYSDfvdvefdtymlpesdlktdsfrlLDVDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYC 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 80-185 9.41e-20

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: 79.59  E-value: 9.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  80 ITIKTIGRQWYWSYEYSDFVDVEFDTymlpesdlktdsfrlldvDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFC 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-185 2.05e-18

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: 76.14  E-value: 2.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  80 ITIKTIGRQWYWSYEYSDFVDVEFDTYMLPESDLKtdsfrlldvdnrtiLPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELC 93
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-185 1.83e-16

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: 70.74  E-value: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  80 ITIKTIGRQWYWSYEYSDfvdvefdtymlpesDLKTdsfrlldvDNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN--------------GKRE--------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYC 85
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-62 2.98e-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: 65.05  E-value: 2.98e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1933122345   1 LMEQLSFFHDHTMIVLLLITVIVGYSLSYMLV------INLMNRNMLHGHLIETIWTALPAITLIFIA 62
Cdd:pfam02790  16 LMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-185 3.45e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 62.81  E-value: 3.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  80 ITIKTIGRQWYWSYEYsdfvdvefdtymlPESDLKTDsfrlldvdNRTILPMNTEVRILTSASDVLHSWAVPAIGIKIDA 159
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANVTTS--------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100
                  ....*....|....*....|....*.
gi 1933122345 160 TPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYC 85
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-185 1.11e-09

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 54.00  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122345  73 DDSVDAMITIKTIGRQWYWSYEYSdfVDVEFDTYMlpesdlktdsfrlldvdnrtILPMNTEVRILTSASDVLHSWAVPA 152
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1933122345 153 IGIKIDATPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELC 116
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 129-185 8.95e-05

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: 39.86  E-value: 8.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1933122345 129 LPMNTEVRILTSASDVLHSWAVPAIGIKIDATPGRLNQGTFTINRPGLFFGQCSEIC 185
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYC 85
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 141-186 3.56e-03

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 35.29  E-value: 3.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1933122345 141 ASDVLHSWAVPAIGIKIDATPGRLNQGTFTINRPGLFFGQCSEICS 186
Cdd:cd04223    36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCS 81
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 125-180 4.26e-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: 35.22  E-value: 4.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1933122345 125 NRTILPMNTEVRI-LTSASdVLHSWAVPAIGIKIDATPGRLNQGTFTINRPGLFFGQ 180
Cdd:cd04212    25 NELVIPVGRPVNFrLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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