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Conserved domains on  [gi|1933122339|gb|QPD01012|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Gomphocerus armeniacus]

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
 1-180 1.89e-119

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 336.80  E-value: 1.89e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00154   22 FFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00154  102 HQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQ 181

                         170       180
                  ....*....|....*....|
gi 1933122339 161 GTFTINRPGLFFGQCSEICG 180
Cdd:MTH00154  182 LNFLINRPGLFFGQCSEICG 201
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-180 1.89e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 336.80  E-value: 1.89e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00154   22 FFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00154  102 HQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQ 181

                         170       180
                  ....*....|....*....|
gi 1933122339 161 GTFTINRPGLFFGQCSEICG 180
Cdd:MTH00154  182 LNFLINRPGLFFGQCSEICG 201
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-180 7.51e-73

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: 215.51  E-value: 7.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|....*..
gi 1933122339 154 TPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICG 109
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-180 2.29e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 201.10  E-value: 2.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 153
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*..
gi 1933122339 154 TPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICG 107
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
36-180 2.19e-36

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 126.10  E-value: 2.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  36 HGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfvdvefdtymtPESDLEidgfrll 115
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA------- 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933122339 116 dVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:COG1622   135 -TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCG 198
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 7-180 1.01e-30

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: 110.55  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   7 MVVLLLITVIVGYSLSYTLM-----IKLTNRNMLHGH-LIETIWTTLPAI--TLIFIALPSLRLLYLLDDSVDAMiTIKT 78
Cdd:TIGR02866  17 LAVSTLISLLVAALLAYVVWkfrrkGDEEKPSQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLYLERPIPKDAL-KVKV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  79 IGRQWYWSYEYSDFvdvefdtymtpesdleidGFRlldVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRL 158
Cdd:TIGR02866  96 TGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQT 154

                         170       180
                  ....*....|....*....|..
gi 1933122339 159 NQGTFTINRPGLFFGQCSEICG 180
Cdd:TIGR02866 155 NALWFNADEPGVYYGFCAELCG 176
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-180 1.89e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 336.80  E-value: 1.89e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00154   22 FFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00154  102 HQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQ 181

                         170       180
                  ....*....|....*....|
gi 1933122339 161 GTFTINRPGLFFGQCSEICG 180
Cdd:MTH00154  182 LNFLINRPGLFFGQCSEICG 201
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-180 1.43e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 263.72  E-value: 1.43e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00140   22 FFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00140  102 HQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQ 181

                         170       180
                  ....*....|....*....|
gi 1933122339 161 GTFTINRPGLFFGQCSEICG 180
Cdd:MTH00140  182 LSFEPKRPGVFYGQCSEICG 201
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-180 1.71e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 263.70  E-value: 1.71e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00117   22 FFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00117  102 HQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQ 181

                         170       180
                  ....*....|....*....|
gi 1933122339 161 GTFTINRPGLFFGQCSEICG 180
Cdd:MTH00117  182 TSFITTRPGVFYGQCSEICG 201
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-180 2.63e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 253.10  E-value: 2.63e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00139   22 FFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00139  102 HQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQ 181

                         170       180
                  ....*....|....*....|
gi 1933122339 161 GTFTINRPGLFFGQCSEICG 180
Cdd:MTH00139  182 VGFFINRPGVFYGQCSEICG 201
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-180 7.13e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 246.92  E-value: 7.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00038   22 YFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00038  102 HQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQ 181

                         170       180
                  ....*....|....*....|
gi 1933122339 161 GTFTINRPGLFFGQCSEICG 180
Cdd:MTH00038  182 TTFFISRTGLFYGQCSEICG 201
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-180 2.51e-83

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 245.54  E-value: 2.51e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   2 FHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGR 81
Cdd:MTH00008   23 FHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  82 QWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQG 161
Cdd:MTH00008  103 QWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQI 182

                         170
                  ....*....|....*....
gi 1933122339 162 TFTINRPGLFFGQCSEICG 180
Cdd:MTH00008  183 GFTITRPGVFYGQCSEICG 201
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-180 1.32e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 243.35  E-value: 1.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00168   22 LFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00168  102 HQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQ 181

                         170       180
                  ....*....|....*....|
gi 1933122339 161 GTFTINRPGLFFGQCSEICG 180
Cdd:MTH00168  182 LAFLSSRPGSFYGQCSEICG 201
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-180 3.55e-79

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 235.00  E-value: 3.55e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00098   22 HFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQ 160
Cdd:MTH00098  102 HQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQ 181

                         170       180
                  ....*....|....*....|
gi 1933122339 161 GTFTINRPGLFFGQCSEICG 180
Cdd:MTH00098  182 TTLMSTRPGLYYGQCSEICG 201
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-180 1.25e-75

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 226.56  E-value: 1.25e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00023   31 FFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDFVD--VEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRL 158
Cdd:MTH00023  111 HQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRL 190

                         170       180
                  ....*....|....*....|..
gi 1933122339 159 NQGTFTINRPGLFFGQCSEICG 180
Cdd:MTH00023  191 NQTGFFIKRPGVFYGQCSEICG 212
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 2-180 3.09e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 225.04  E-value: 3.09e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   2 FHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGR 81
Cdd:MTH00076   23 FHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  82 QWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQG 161
Cdd:MTH00076  103 QWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQT 182

                         170
                  ....*....|....*....
gi 1933122339 162 TFTINRPGLFFGQCSEICG 180
Cdd:MTH00076  183 SFIASRPGVYYGQCSEICG 201
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-180 3.41e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 224.98  E-value: 3.41e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   2 FHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGR 81
Cdd:MTH00129   23 FHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  82 QWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQG 161
Cdd:MTH00129  103 QWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQT 182

                         170
                  ....*....|....*....
gi 1933122339 162 TFTINRPGLFFGQCSEICG 180
Cdd:MTH00129  183 AFIASRPGVFYGQCSEICG 201
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-180 4.53e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 224.76  E-value: 4.53e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   2 FHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGR 81
Cdd:MTH00185   23 FHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGH 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  82 QWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQG 161
Cdd:MTH00185  103 QWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQA 182

                         170
                  ....*....|....*....
gi 1933122339 162 TFTINRPGLFFGQCSEICG 180
Cdd:MTH00185  183 TFIISRPGLYYGQCSEICG 201
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-180 4.01e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 220.04  E-value: 4.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLTNRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIG 80
Cdd:MTH00051   24 FFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  81 RQWYWSYEYSDF--VDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRL 158
Cdd:MTH00051  104 HQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRL 183

                         170       180
                  ....*....|....*....|..
gi 1933122339 159 NQGTFTINRPGLFFGQCSEICG 180
Cdd:MTH00051  184 NQTSFFIKRPGVFYGQCSEICG 205
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 74-180 7.51e-73

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: 215.51  E-value: 7.51e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|....*..
gi 1933122339 154 TPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEICG 109
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-180 2.29e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 201.10  E-value: 2.29e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 153
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*..
gi 1933122339 154 TPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICG 107
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-180 1.67e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 175.98  E-value: 1.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   2 FHDHtmvVLLLITVIVGYSLSYTLMIKLTNR------NMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSV-DAMI 74
Cdd:MTH00027   51 LHDQ---ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  75 TIKTIGRQWYWSYEYSDF--VDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKID 152
Cdd:MTH00027  128 TIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMD 207

                         170       180
                  ....*....|....*....|....*...
gi 1933122339 153 ATPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:MTH00027  208 AVPGRINETGFLIKRPGIFYGQCSEICG 235
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-180 1.90e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 164.41  E-value: 1.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLMIKLT---NRNMLHGHLIETIWTTLPAITLIFIALPSLRLLYLLD-DSVDAMITI 76
Cdd:MTH00080   21 WFHNFNCSLLFGEFVLAFVVFLFLYLISNNfyfKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  77 KTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPG 156
Cdd:MTH00080  101 KVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSG 180

                         170       180
                  ....*....|....*....|....
gi 1933122339 157 RLNQGTFTINRPGLFFGQCSEICG 180
Cdd:MTH00080  181 ILSTLCYSFPMPGVFYGQCSEICG 204
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
36-180 2.19e-36

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 126.10  E-value: 2.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  36 HGHLIETIWTTLPAITLIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfvdvefdtymtPESDLEidgfrll 115
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA------- 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1933122339 116 dVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:COG1622   135 -TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCG 198
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 7-180 1.01e-30

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: 110.55  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   7 MVVLLLITVIVGYSLSYTLM-----IKLTNRNMLHGH-LIETIWTTLPAI--TLIFIALPSLRLLYLLDDSVDAMiTIKT 78
Cdd:TIGR02866  17 LAVSTLISLLVAALLAYVVWkfrrkGDEEKPSQIHGNrRLEYVWTVIPLIivVGLFAATAKGLLYLERPIPKDAL-KVKV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  79 IGRQWYWSYEYSDFvdvefdtymtpesdleidGFRlldVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRL 158
Cdd:TIGR02866  96 TGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQT 154

                         170       180
                  ....*....|....*....|..
gi 1933122339 159 NQGTFTINRPGLFFGQCSEICG 180
Cdd:TIGR02866 155 NALWFNADEPGVYYGFCAELCG 176
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 7-180 2.96e-30

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 109.27  E-value: 2.96e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339   7 MVVLLLITVIVGYSLSytlmIKLTNRNmlhgHLIETIWTTLPaiTLIFIALPSLRLLYLLDDSVDAMI-TIKTIGRQWYW 85
Cdd:MTH00047   24 WVYIMLCWQVVSGNGS----VNFGSEN----QVLELLWTVVP--TLLVLVLCFLNLNFITSDLDCFSSeTIKVIGHQWYW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  86 SYEYSDfvDVEFDTYMTPESDLeidgfrlldVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTI 165
Cdd:MTH00047   94 SYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162

                         170
                  ....*....|....*
gi 1933122339 166 NRPGLFFGQCSEICG 180
Cdd:MTH00047  163 DRHGVFVGYCSELCG 177
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 97-180 5.18e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 104.90  E-value: 5.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  97 FDTYMTPESDLEIDGFRLLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQCS 176
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130


                  ....
gi 1933122339 177 EICG 180
Cdd:PTZ00047  131 EMCG 134
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 74-180 5.09e-22

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: 85.04  E-value: 5.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWSYEYSDfvdvefdtymtpesdleidgfrlLDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|....*..
gi 1933122339 154 TPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCG 84
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 74-180 2.62e-21

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: 83.44  E-value: 2.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWSYEYSDFVDVEFDTymtpesdleidgfrlldvDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100
                  ....*....|....*....|....*..
gi 1933122339 154 TPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCG 90
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-180 6.65e-20

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: 79.99  E-value: 6.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEidgfrlldvdnrtiLPMNTEVRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|....*..
gi 1933122339 154 TPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCG 94
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-180 1.64e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 76.13  E-value: 1.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWSYEYSDfvdvefdtymtpesdleidGFRlldVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100
                  ....*....|....*....|....*..
gi 1933122339 154 TPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCG 86
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-180 4.74e-14

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 64.74  E-value: 4.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWSYEYsdfvdvefdtymtPESDLeidgfrllDVDNRTILPMNTEVRILTSASDVLHSWAVPALGIKIDA 153
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANV--------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100
                  ....*....|....*....|....*..
gi 1933122339 154 TPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYCG 86
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-56 1.74e-12

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: 60.04  E-value: 1.74e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1933122339   1 FFHDHTMVVLLLITVIVGYSLSYTLM------IKLTNRNMLHGHLIETIWTTLPAITLIFIA 56
Cdd:pfam02790  22 ELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-180 1.32e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 59.01  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  67 DDSVDAMITIKTIGRQWYWSYEYSDFVDvefdtymtpesdlEIDGFRLldvdnrtilPMNTEVRILTSASDVLHSWAVPA 146
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNGVT-------------TGNTLRV---------PADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1933122339 147 LGIKIDATPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCG 117
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 123-180 1.51e-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: 41.79  E-value: 1.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1933122339 123 LPMNTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCG 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 119-174 1.04e-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: 36.76  E-value: 1.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1933122339 119 NRTILPMNTEVRI-LTSASdVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQ 174
Cdd:cd04212    25 NELVIPVGRPVNFrLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-180 1.87e-03

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 36.21  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122339  74 ITIKTIGRQWYWsyeysdfvdvefdtymtpesdlEIDgfrlldvdnRTILPMNTEVRILTSASDVLHSWAV--PALGI-- 149
Cdd:cd13916     1 QVVAVTGHQWYW----------------------ELS---------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLla 49

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1933122339 150 KIDATPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13916    50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCG 80
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 126-180 6.22e-03

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 34.27  E-value: 6.22e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1933122339 126 NTEVRILTSASDVLHSWAVPALGIKIDATPGRLNQGTFTINRPGLFFGQCSEICG 180
Cdd:cd13917    21 GKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCG 75
 
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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