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Conserved domains on  [gi|342161315|gb|AEL16539|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Rhammatocerus pictus]

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
 1-121 2.33e-77

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 227.79  E-value: 2.33e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   1 TLIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVR 80
Cdd:MTH00154  72 ILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIR 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 342161315  81 VLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00154 152 ILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLF 192
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-121 2.33e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 227.79  E-value: 2.33e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   1 TLIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVR 80
Cdd:MTH00154  72 ILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIR 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 342161315  81 VLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00154 152 ILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLF 192
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 24-121 5.09e-64

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: 190.47  E-value: 5.09e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  24 ITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90
                 ....*....|....*...
gi 342161315 104 TPGRLNQGTFTMNRPGLF 121
Cdd:cd13912   83 VPGRLNQTSFFIERPGVY 100
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
24-121 2.11e-59

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 178.37  E-value: 2.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   24 ITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*...
gi 342161315  104 TPGRLNQGTFTMNRPGLF 121
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVF 98
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 24-121 5.18e-24

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: 90.90  E-value: 5.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   24 ITIKTIGRQWYWSYEYsdfvnvefdtymtpesdlENEGFRlldVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:TIGR02866  91 LKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDA 149

                          90
                  ....*....|....*...
gi 342161315  104 TPGRLNQGTFTMNRPGLF 121
Cdd:TIGR02866 150 IPGQTNALWFNADEPGVY 167
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-121 1.95e-22

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 87.58  E-value: 1.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfvnvefdtymtPESDLEnegfrlldVDNRTVLPMNTEVRV 81
Cdd:COG1622   91 VIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRF 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 342161315  82 LTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:COG1622  150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-121 2.33e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 227.79  E-value: 2.33e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   1 TLIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVR 80
Cdd:MTH00154  72 ILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIR 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 342161315  81 VLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00154 152 ILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLF 192
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 24-121 5.09e-64

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: 190.47  E-value: 5.09e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  24 ITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90
                 ....*....|....*...
gi 342161315 104 TPGRLNQGTFTMNRPGLF 121
Cdd:cd13912   83 VPGRLNQTSFFIERPGVY 100
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-121 3.18e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 189.35  E-value: 3.18e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   1 TLIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVR 80
Cdd:MTH00117  72 VLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIR 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 342161315  81 VLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00117 152 ILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVF 192
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
24-121 2.11e-59

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 178.37  E-value: 2.11e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   24 ITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*...
gi 342161315  104 TPGRLNQGTFTMNRPGLF 121
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVF 98
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 2-121 7.82e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 175.51  E-value: 7.82e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRV 81
Cdd:MTH00140  73 LVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRV 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 342161315  82 LTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00140 153 LVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVF 192
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-121 8.88e-56

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 173.12  E-value: 8.88e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   1 TLIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVR 80
Cdd:MTH00008  72 ILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIR 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 342161315  81 VLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00008 152 VLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVF 192
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-121 4.02e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 171.42  E-value: 4.02e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRV 81
Cdd:MTH00038  73 LIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRV 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 342161315  82 LTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00038 153 LVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLF 192
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 2-121 7.81e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 170.67  E-value: 7.81e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRV 81
Cdd:MTH00139  73 LLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRA 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 342161315  82 LTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00139 153 LITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVF 192
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 17-121 2.62e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 169.01  E-value: 2.62e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  17 DDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRVLTSASDVLHSWAVPA 96
Cdd:MTH00168  88 DEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPS 167

                         90       100
                 ....*....|....*....|....*
gi 342161315  97 LGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00168 168 LGLKMDAVPGRLNQLAFLSSRPGSF 192
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-121 2.70e-52

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 164.54  E-value: 2.70e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFV--NVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEV 79
Cdd:MTH00023  82 LVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHV 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 342161315  80 RVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00023 162 RILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVF 203
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-121 2.71e-52

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 164.12  E-value: 2.71e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRV 81
Cdd:MTH00098  73 LILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRM 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 342161315  82 LTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00098 153 LISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLY 192
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-121 1.41e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 162.64  E-value: 1.41e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDF--VNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEV 79
Cdd:MTH00051  75 LIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQV 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 342161315  80 RVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00051 155 RVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVF 196
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-121 2.57e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 161.98  E-value: 2.57e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRV 81
Cdd:MTH00185  73 LIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRV 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 342161315  82 LTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00185 153 LITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLY 192
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 2-121 3.88e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 158.79  E-value: 3.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRV 81
Cdd:MTH00076  73 LIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRM 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 342161315  82 LTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00076 153 LITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVY 192
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-121 4.21e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 158.72  E-value: 4.21e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRV 81
Cdd:MTH00129  73 LILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRV 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 342161315  82 LTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00129 153 LVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVF 192
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 21-121 4.18e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 135.91  E-value: 4.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  21 DAMITIKTIGRQWYWSYEYSDFVNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIK 100
Cdd:MTH00080  95 DSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIK 174

                         90       100
                 ....*....|....*....|.
gi 342161315 101 IDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00080 175 MDAMSGILSTLCYSFPMPGVF 195
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-121 1.56e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 130.15  E-value: 1.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSV-DAMITIKTIGRQWYWSYEYSDF--VNVEFDTYMTPESDLENEGFRLLDVDNRTVLPMNTE 78
Cdd:MTH00027 104 LILIAFPSLRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTN 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 342161315  79 VRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:MTH00027 184 VRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIF 226
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 25-121 2.89e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 96.56  E-value: 2.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  25 TIKTIGRQWYWSYEYSDfvNVEFDTYMTPESDLenegfrlldVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDAT 104
Cdd:MTH00047  83 TIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAI 151

                         90
                 ....*....|....*..
gi 342161315 105 PGRLNQGTFTMNRPGLF 121
Cdd:MTH00047 152 PGRINHLFFCPDRHGVF 168
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 24-121 5.18e-24

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: 90.90  E-value: 5.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   24 ITIKTIGRQWYWSYEYsdfvnvefdtymtpesdlENEGFRlldVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:TIGR02866  91 LKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDA 149

                          90
                  ....*....|....*...
gi 342161315  104 TPGRLNQGTFTMNRPGLF 121
Cdd:TIGR02866 150 IPGQTNALWFNADEPGVY 167
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-121 1.95e-22

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 87.58  E-value: 1.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315   2 LIFIALPSLRLLYLLDDSVDAMITIKTIGRQWYWSYEYsdfvnvefdtymtPESDLEnegfrlldVDNRTVLPMNTEVRV 81
Cdd:COG1622   91 VIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGIA--------TVNELVLPVGRPVRF 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 342161315  82 LTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:COG1622  150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 47-121 1.33e-20

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 81.40  E-value: 1.33e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 342161315  47 FDTYMTPESDLENEGFRLLDVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVF 125
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 24-121 3.07e-17

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 70.79  E-value: 3.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  24 ITIKTIGRQWYWSYEYSDfvnvefdtymtpesdlenegfrlLDVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90
                 ....*....|....*...
gi 342161315 104 TPGRLNQGTFTMNRPGLF 121
Cdd:cd13842   58 VPGYTSELWFVADKPGTY 75
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 24-121 1.63e-15

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 66.50  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  24 ITIKTIGRQWYWSYEYSDfvnvefdtymtpesdleneGFRlldVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:cd13915    2 LEIQVTGRQWMWEFTYPN-------------------GKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90
                 ....*....|....*...
gi 342161315 104 TPGRLNQGTFTMNRPGLF 121
Cdd:cd13915   60 VPGRYTYLWFEATKPGEY 77
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 24-121 2.62e-15

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 66.12  E-value: 2.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  24 ITIKTIGRQWYWSYEYsdfvnvefdtymtPESDlENEGFRLLDVDNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:cd13919    2 LVVEVTAQQWAWTFRY-------------PGGD-GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90
                 ....*....|....*...
gi 342161315 104 TPGRLNQGTFTMNRPGLF 121
Cdd:cd13919   68 VPGRTTRLWFTPTREGEY 85
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 24-121 1.74e-14

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: 63.79  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  24 ITIKTIGRQWYWSYEYSDfvnvefdtymTPESDLENEgfrlldvdNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPD----------EPGRGIVTA--------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90
                 ....*....|....*...
gi 342161315 104 TPGRLNQGTFTMNRPGLF 121
Cdd:cd04213   64 IPGRTNRLWLQADEPGVY 81
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 24-109 1.63e-11

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 56.26  E-value: 1.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  24 ITIKTIGRQWYWSYEYsdfvnvefdtymtPESDLENEgfrlldvdNRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDA 103
Cdd:cd13914    1 VEIEVEAYQWGWEFSY-------------PEANVTTS--------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                 ....*.
gi 342161315 104 TPGRLN 109
Cdd:cd13914   60 FPGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 17-119 9.23e-08

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 47.45  E-value: 9.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 342161315  17 DDSVDAMITIKTIGRQWYWSYEYSdfvnvefdtymtpesdleNEGFRLldvdNRTVLPMNTEVRVLTSASDVLHSWAVPA 96
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYP------------------NGVTTG----NTLRVPADTPIALRVTSTDVFHTFGIPE 83

                         90       100
                 ....*....|....*....|...
gi 342161315  97 LGIKIDATPGRLNQGTFTMNRPG 119
Cdd:cd13918   84 LRVKADAIPGEYTSTWFEADEPG 106
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 69-121 4.49e-04

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 36.78  E-value: 4.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 342161315  69 NRTVLPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEY 77
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 69-121 4.27e-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: 34.06  E-value: 4.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 342161315  69 NRTVLPMNTEVR-VLTSASdVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 121
Cdd:cd04212   25 NELVIPVGRPVNfRLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTY 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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