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Conserved domains on  [gi|1933122365|gb|QPD01025|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Ramburiella bolivari]

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
 1-176 3.00e-111

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 316.00  E-value: 3.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00154   25 DHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00154  105 YWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00154  185 LINRPGLFFGQCSEIC 200
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-176 3.00e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 316.00  E-value: 3.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00154   25 DHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00154  105 YWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00154  185 LINRPGLFFGQCSEIC 200
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 71-176 2.16e-72

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: 213.97  E-value: 2.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  71 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 150
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|....*.
gi 1933122365 151 TPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEIC 108
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
71-176 4.66e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 200.33  E-value: 4.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  71 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 150
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*.
gi 1933122365 151 TPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEIC 106
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
33-176 4.63e-34

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 119.93  E-value: 4.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  33 HEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQWYWSYEYsdfvdvefdtymtPESDLEingfrll 112
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA------- 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933122365 113 dVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:COG1622   135 -TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELC 197
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 4-176 2.09e-28

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: 104.38  E-value: 2.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   4 MVVLLLITVIVGYSLSYMLM-----IN*TNRNMLHEH-LIETIWTALPAITLIFIALPSLRLLYLLDDSMDT-MITIKTI 76
Cdd:TIGR02866  17 LAVSTLISLLVAALLAYVVWkfrrkGDEEKPSQIHGNrRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  77 GRQWYWSYEYSDFvdvefdtymtpesdleinGFRlldVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLN 156
Cdd:TIGR02866  97 GYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTN 155

                         170       180
                  ....*....|....*....|
gi 1933122365 157 QGTFSINRPGLFFGQCSEIC 176
Cdd:TIGR02866 156 ALWFNADEPGVYYGFCAELC 175
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-176 3.00e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 316.00  E-value: 3.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00154   25 DHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00154  105 YWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00154  185 LINRPGLFFGQCSEIC 200
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-176 1.61e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 248.29  E-value: 1.61e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00117   25 DHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00117  105 YWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00117  185 ITTRPGVFYGQCSEIC 200
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-176 3.53e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 242.54  E-value: 3.53e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00140   25 DHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00140  105 YWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00140  185 EPKRPGVFYGQCSEIC 200
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-176 2.03e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 238.08  E-value: 2.03e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00139   25 DHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00139  105 YWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00139  185 FINRPGVFYGQCSEIC 200
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-176 6.54e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 236.91  E-value: 6.54e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00038   25 DYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00038  105 YWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00038  185 FISRTGLFYGQCSEIC 200
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-176 1.43e-78

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 233.21  E-value: 1.43e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00008   25 DHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00008  105 YWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00008  185 TITRPGVFYGQCSEIC 200
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-176 3.14e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 229.87  E-value: 3.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00168   25 DHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00168  105 YWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00168  185 LSSRPGSFYGQCSEIC 200
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-176 3.40e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 219.59  E-value: 3.40e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00098   25 DHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00098  105 YWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTL 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00098  185 MSTRPGLYYGQCSEIC 200
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 71-176 2.16e-72

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: 213.97  E-value: 2.16e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  71 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 150
Cdd:cd13912     3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                          90       100
                  ....*....|....*....|....*.
gi 1933122365 151 TPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:cd13912    83 VPGRLNQTSFFIERPGVYYGQCSEIC 108
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-176 2.90e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 214.75  E-value: 2.90e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00185   25 DHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00185  105 YWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00185  185 IISRPGLYYGQCSEIC 200
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-176 4.79e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 214.19  E-value: 4.79e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00129   25 DHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00129  105 YWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00129  185 IASRPGVFYGQCSEIC 200
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-176 6.24e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 211.56  E-value: 6.24e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00076   25 DHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQW 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTF 160
Cdd:MTH00076  105 YWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSF 184

                         170
                  ....*....|....*.
gi 1933122365 161 SINRPGLFFGQCSEIC 176
Cdd:MTH00076  185 IASRPGVYYGQCSEIC 200
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-176 2.02e-69

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 210.38  E-value: 2.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00023   34 DQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQW 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDFVD--VEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQG 158
Cdd:MTH00023  114 YWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQT 193

                         170
                  ....*....|....*...
gi 1933122365 159 TFSINRPGLFFGQCSEIC 176
Cdd:MTH00023  194 GFFIKRPGVFYGQCSEIC 211
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
71-176 4.66e-67

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 200.33  E-value: 4.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  71 ITIKTIGRQWYWSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 150
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*.
gi 1933122365 151 TPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEIC 106
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-176 7.13e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 203.86  E-value: 7.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLMIN*TNRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQW 80
Cdd:MTH00051   27 DQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQW 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  81 YWSYEYSDF--VDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQG 158
Cdd:MTH00051  107 YWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQT 186

                         170
                  ....*....|....*...
gi 1933122365 159 TFSINRPGLFFGQCSEIC 176
Cdd:MTH00051  187 SFFIKRPGVFYGQCSEIC 204
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-176 4.03e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 167.12  E-value: 4.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   6 VLLLITVIVGYSLSYMLMIN*TNR------NMLHEHLIETIWTALPAITLIFIALPSLRLLYLLDDS-MDTMITIKTIGR 78
Cdd:MTH00027   55 ILFILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECgFSANITIKVTGH 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  79 QWYWSYEYSDF--VDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLN 156
Cdd:MTH00027  135 QWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRIN 214

                         170       180
                  ....*....|....*....|
gi 1933122365 157 QGTFSINRPGLFFGQCSEIC 176
Cdd:MTH00027  215 ETGFLIKRPGIFYGQCSEIC 234
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-176 1.05e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 162.49  E-value: 1.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   6 VLLLITVIVGYSLSYMLMIN*T---NRNMLHEHLIETIWTALPAITLIFIALPSLRLLYLLD-DSMDTMITIKTIGRQWY 81
Cdd:MTH00080   29 LLFGEFVLAFVVFLFLYLISNNfyfKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTGHQWY 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  82 WSYEYSDFVDVEFDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFS 161
Cdd:MTH00080  109 WSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYS 188

                         170
                  ....*....|....*
gi 1933122365 162 INRPGLFFGQCSEIC 176
Cdd:MTH00080  189 FPMPGVFYGQCSEIC 203
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
33-176 4.63e-34

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 119.93  E-value: 4.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  33 HEHLIETIWTALPAITLIFIALPSLRLLYLLDDSMDTMITIKTIGRQWYWSYEYsdfvdvefdtymtPESDLEingfrll 112
Cdd:COG1622    75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA------- 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1933122365 113 dVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:COG1622   135 -TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELC 197
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 4-176 1.86e-29

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 106.96  E-value: 1.86e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   4 MVVLLLITVIVGYSLSymlmIN*TNRNmlheHLIETIWTALPA-ITLIFIALPSLRLLYLLDDSMDTmiTIKTIGRQWYW 82
Cdd:MTH00047   24 WVYIMLCWQVVSGNGS----VNFGSEN----QVLELLWTVVPTlLVLVLCFLNLNFITSDLDCFSSE--TIKVIGHQWYW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  83 SYEYSDfvDVEFDTYMTpesDLeINGfrlldVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFSI 162
Cdd:MTH00047   94 SYEYSF--GGSYDSFMT---DD-IFG-----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162

                         170
                  ....*....|....
gi 1933122365 163 NRPGLFFGQCSEIC 176
Cdd:MTH00047  163 DRHGVFVGYCSELC 176
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 4-176 2.09e-28

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: 104.38  E-value: 2.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365   4 MVVLLLITVIVGYSLSYMLM-----IN*TNRNMLHEH-LIETIWTALPAITLIFIALPSLRLLYLLDDSMDT-MITIKTI 76
Cdd:TIGR02866  17 LAVSTLISLLVAALLAYVVWkfrrkGDEEKPSQIHGNrRLEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  77 GRQWYWSYEYSDFvdvefdtymtpesdleinGFRlldVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLN 156
Cdd:TIGR02866  97 GYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTN 155

                         170       180
                  ....*....|....*....|
gi 1933122365 157 QGTFSINRPGLFFGQCSEIC 176
Cdd:TIGR02866 156 ALWFNADEPGVYYGFCAELC 175
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 94-176 4.26e-28

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 102.59  E-value: 4.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  94 FDTYMTPESDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCS 173
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130


                  ...
gi 1933122365 174 EIC 176
Cdd:PTZ00047  131 EMC 133
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 71-176 4.66e-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: 80.03  E-value: 4.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  71 ITIKTIGRQWYWSYEYSDfvdvefdtymtpesdleingfrlLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 150
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|....*.
gi 1933122365 151 TPGRLNQGTFSINRPGLFFGQCSEIC 176
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), ...
 71-176 1.02e-19

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: 79.20  E-value: 1.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  71 ITIKTIGRQWYWSYEYSDFVDVEFDTymtpesdleingfrlldvDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 150
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT------------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100
                  ....*....|....*....|....*.
gi 1933122365 151 TPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFC 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-176 5.26e-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: 74.98  E-value: 5.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  71 ITIKTIGRQWYWSYEYsdfvdvefdtymtPESDlEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 150
Cdd:cd13919     2 LVVEVTAQQWAWTFRY-------------PGGD-GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|....*.
gi 1933122365 151 TPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELC 93
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-176 1.57e-17

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: 73.43  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  71 ITIKTIGRQWYWSYEYSdfvdvefdtymtpesdleiNGFRlldVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 150
Cdd:cd13915     2 LEIQVTGRQWMWEFTYP-------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100
                  ....*....|....*....|....*.
gi 1933122365 151 TPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYC 85
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 71-176 1.08e-12

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 61.27  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  71 ITIKTIGRQWYWSYEYsdfvdvefdtymtPESDLeingfrllDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 150
Cdd:cd13914     1 VEIEVEAYQWGWEFSY-------------PEANV--------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                          90       100
                  ....*....|....*....|....*.
gi 1933122365 151 TPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:cd13914    60 FPGQYNTIKTEATEEGEYQLYCAEYC 85
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-53 6.62e-10

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: 53.10  E-value: 6.62e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1933122365   1 DHTMVVLLLITVIVGYSLSYMLM------IN*TNRNMLHEHLIETIWTALPAITLIFIA 53
Cdd:pfam02790  25 DYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-176 6.78e-10

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 54.38  E-value: 6.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1933122365  64 DDSMDTMITIKTIGRQWYWSYEYSDFVDvefdtymtpesdlEINGFRLldvdnrtilPMNTEVRVLTSASDVLHSWAVPA 143
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNGVT-------------TGNTLRV---------PADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1933122365 144 LGIKIDATPGRLNQGTFSINRPGLFFGQCSEIC 176
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 ...
 120-176 4.16e-03

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 35.24  E-value: 4.16e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1933122365 120 LPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQCSEIC 176
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYC 85
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 116-171 7.38e-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: 34.45  E-value: 7.38e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1933122365 116 NRTILPMNTEVR-VLTSASdVLHSWAVPALGIKIDATPGRLNQGTFSINRPGLFFGQ 171
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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