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Conserved domains on  [gi|2067839381|gb|QXP00564|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Gryllidae gen. 2 sp. 2 JD-2021b]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 999987)

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

CATH:  1.10.287.90
EC:  7.1.1.9
Gene Ontology:  GO:0004129|GO:0005507
PubMed:  6307356|8083153
TCDB:  3.D.4.6.2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl33359
cytochrome c oxidase subunit II; Provisional
 1-111 2.13e-61

cytochrome c oxidase subunit II; Provisional


The actual alignment was detected with superfamily member MTH00154:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 186.57  E-value: 2.13e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMI--QPENLNSFRLLDV 78
Cdd:MTH00154   60 EIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIptNELENNGFRLLDV 138

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2067839381  79 DNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00154  139 DNRLVLPMNTQIRILITAADVIHSWTVPSLGVK 171
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-111 2.13e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 186.57  E-value: 2.13e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMI--QPENLNSFRLLDV 78
Cdd:MTH00154   60 EIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIptNELENNGFRLLDV 138

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2067839381  79 DNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00154  139 DNRLVLPMNTQIRILITAADVIHSWTVPSLGVK 171
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 34-111 2.89e-45

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: 142.71  E-value: 2.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381  34 PMITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLN--SFRLLDVDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEkgQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
36-111 4.05e-39

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 126.76  E-value: 4.05e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067839381  36 ITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLN--SFRLLDVDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEegQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIK 77
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-111 4.28e-20

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 81.03  E-value: 4.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqiefdsymiqpenlnsfrllDVDNR 81
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI--------------------ATVNE 138

                          90       100       110
                  ....*....|....*....|....*....|
gi 2067839381  82 TTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:COG1622   139 LVLPVGRPVRFLLTSADVIHSFWVPALGGK 168
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-111 9.55e-16

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: 68.95  E-value: 9.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEP-MITLKTIGHQWYWSYEYMDFknqiefdsymiqpenlnsfrLLDVDN 80
Cdd:TIGR02866  56 LEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVTGYQWWWDFEYPES--------------------GFTTVN 115

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2067839381  81 RTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:TIGR02866 116 ELVLPAGTPVELQVTSKDVIHSFWVPELGGK 146
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-111 2.13e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 186.57  E-value: 2.13e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMI--QPENLNSFRLLDV 78
Cdd:MTH00154   60 EIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIptNELENNGFRLLDV 138

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2067839381  79 DNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00154  139 DNRLVLPMNTQIRILITAADVIHSWTVPSLGVK 171
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-111 2.19e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 163.93  E-value: 2.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLN--SFRLLDV 78
Cdd:MTH00117   60 EVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD-LSFDSYMIPTQDLPngHFRLLEV 138

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2067839381  79 DNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00117  139 DHRMVIPMESPIRILITAEDVLHSWAVPSLGVK 171
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-111 3.01e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 156.03  E-value: 3.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLNS--FRLLDV 78
Cdd:MTH00139   60 EVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSgeFRLLEV 138

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2067839381  79 DNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00139  139 DNRLVLPYKSNIRALITAADVLHSWTVPSLGVK 171
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 2-111 3.57e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 155.87  E-value: 3.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLNS--FRLLDVD 79
Cdd:MTH00140   61 LETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELgdFRLLEVD 139

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2067839381  80 NRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00140  140 NRLVLPYSVDTRVLVTSADVIHSWTVPSLGVK 171
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-111 3.87e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 155.52  E-value: 3.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFkNQIEFDSYMIQPENLN--SFRLLDV 78
Cdd:MTH00168   60 MIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDY-NDLEFDSYMVPTQDLSpgQFRLLEV 138

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2067839381  79 DNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00168  139 DNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLK 171
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-111 5.74e-47

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 150.39  E-value: 5.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLN--SFRLLDVD 79
Cdd:MTH00008   61 IETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-LEFDSYMLPTSDLSpgQFRLLEVD 139

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2067839381  80 NRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00008  140 NRAVLPMQTEIRVLVTAADVIHSWTVPSLGVK 171
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-111 3.59e-46

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 148.36  E-value: 3.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNQ-IEFDSYMIQPENLNS--FRLLD 77
Cdd:MTH00023   69 FLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGEtLEFDSYMVPTSDLNSgdFRLLE 148

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2067839381  78 VDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00023  149 VDNRLVVPINTHVRILVTGADVLHSFAVPSLGLK 182
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 2-111 3.75e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 148.31  E-value: 3.75e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFkNQIEFDSYMIQPENLNS--FRLLDVD 79
Cdd:MTH00038   61 LETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-NDLEFDSYMVPTSDLSTglPRLLEVD 139

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2067839381  80 NRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00038  140 NRLVLPYQTPIRVLVSSADVLHSWAVPSLGVK 171
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 34-111 2.89e-45

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: 142.71  E-value: 2.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381  34 PMITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLN--SFRLLDVDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEkgQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-111 4.73e-43

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 140.24  E-value: 4.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLN--SFRLLDVD 79
Cdd:MTH00098   61 VETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKpgELRLLEVD 139

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2067839381  80 NRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00098  140 NRVVLPMEMPIRMLISSEDVLHSWAVPSLGLK 171
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-111 6.51e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 139.92  E-value: 6.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDF-KNQIEFDSYMIQPENLNS--FRLLD 77
Cdd:MTH00051   62 LIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgTDTIEFDSYMIPTSDLNSgdLRLLE 141

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2067839381  78 VDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00051  142 VDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVK 175
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-111 1.64e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 136.38  E-value: 1.64e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENL--NSFRLLDVD 79
Cdd:MTH00129   61 IEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLtpGQFRLLEAD 139

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2067839381  80 NRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00129  140 HRMVVPVESPIRVLVSAEDVLHSWAVPALGVK 171
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 2-111 2.11e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 136.06  E-value: 2.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLN--SFRLLDVD 79
Cdd:MTH00076   61 IEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTpgQFRLLEVD 139

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2067839381  80 NRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00076  140 NRMVVPMESPIRMLITAEDVLHSWAVPSLGIK 171
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-111 4.00e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 135.40  E-value: 4.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFkNQIEFDSYMIQPENLNS--FRLLDVD 79
Cdd:MTH00185   61 IEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-EQLEFDSYMTPTQDLTPgqFRLLETD 139

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2067839381  80 NRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00185  140 HRMVVPMESPIRVLITAEDVLHSWTVPALGVK 171
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
36-111 4.05e-39

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 126.76  E-value: 4.05e-39
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067839381  36 ITLKTIGHQWYWSYEYMDFKNqIEFDSYMIQPENLN--SFRLLDVDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEegQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIK 77
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-111 3.95e-32

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 112.41  E-value: 3.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLD-ESMEPMITLKTIGHQWYWSYEYMDFKNqIEFDSYM--IQPENLNSFRLLD 77
Cdd:MTH00080   62 FGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPG-LEFDSYMksLDQLRLGEPRLLE 140

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2067839381  78 VDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00080  141 VDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIK 174
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-111 2.55e-31

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 111.27  E-value: 2.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   1 MIEIIWTILPAIILIFIALPSLRLLYLLDES-MEPMITLKTIGHQWYWSYEYMDF-KNQIEFDSYMIQPENLN--SFRLL 76
Cdd:MTH00027   91 LIEVIWTLIPAFILILIAFPSLRLLYIMDECgFSANITIKVTGHQWYWSYSYEDYgEKNIEFDSYMIPTADLEfgDLRLL 170

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2067839381  77 DVDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00027  171 EVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVK 205
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-111 4.28e-20

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 81.03  E-value: 4.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEPMITLKTIGHQWYWSYEYMDFKNqiefdsymiqpenlnsfrllDVDNR 81
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI--------------------ATVNE 138

                          90       100       110
                  ....*....|....*....|....*....|
gi 2067839381  82 TTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:COG1622   139 LVLPVGRPVRFLLTSADVIHSFWVPALGGK 168
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 2-111 2.39e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 78.46  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLlDESMEPMITLKTIGHQWYWSYEYmdfKNQIEFDSYMIQPENLnsfrlldVDNR 81
Cdd:MTH00047   49 LELLWTVVPTLLVLVLCFLNLNFITS-DLDCFSSETIKVIGHQWYWSYEY---SFGGSYDSFMTDDIFG-------VDKP 117

                          90       100       110
                  ....*....|....*....|....*....|
gi 2067839381  82 TTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:MTH00047  118 LRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-111 9.55e-16

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: 68.95  E-value: 9.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381   2 IEIIWTILPAIILIFIALPSLRLLYLLDESMEP-MITLKTIGHQWYWSYEYMDFknqiefdsymiqpenlnsfrLLDVDN 80
Cdd:TIGR02866  56 LEYVWTVIPLIIVVGLFAATAKGLLYLERPIPKdALKVKVTGYQWWWDFEYPES--------------------GFTTVN 115

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2067839381  81 RTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:TIGR02866 116 ELVLPAGTPVELQVTSKDVIHSFWVPELGGK 146
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 60-111 1.00e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 68.31  E-value: 1.00e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2067839381  60 FDSYMIQPENLNS--FRLLDVDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:PTZ00047   51 FQSNLVTDEDLKPgmLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIK 104
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 36-111 5.34e-09

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: 49.22  E-value: 5.34e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2067839381  36 ITLKTIGHQWYWSYEYMDfknqiefdsymiqpenlnsfrlLDVDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVK 54
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 36-111 1.19e-05

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: 40.68  E-value: 1.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2067839381  36 ITLKTIGHQWYWSYEYMDfknqiefdsymIQPENLNSfrlldvDNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD-----------EPGRGIVT------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGK 60
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 36-111 4.54e-05

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: 39.16  E-value: 4.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067839381  36 ITLKTIGHQWYWSYEYmdfknqiefdsymiqPENLNSFRLLDVDNRTTL--PMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:cd13919     2 LVVEVTAQQWAWTFRY---------------PGGDGKLGTDDDVTSPELhlPVGRPVLFNLRSKDVIHSFWVPEFRVK 64
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 36-111 3.01e-04

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: 36.84  E-value: 3.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2067839381  36 ITLKTIGHQWYWSYEYMDFKNQIefdsymiqpenlnsfrlldvdNRTTLPMNTQIRTLVTAADVIHSWTIPSLGMK 111
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPNGKREI---------------------NELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 2-18 2.46e-03

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: 34.23  E-value: 2.46e-03
                          10
                  ....*....|....*..
gi 2067839381   2 IEIIWTILPAIILIFIA 18
Cdd:pfam02790  67 IEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 29-111 3.00e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 34.74  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067839381  29 DESMEPMITLKTIGHQWYWSYEYmdfKNQIEFDSYMIQPEnlnsfrlldvdnrttlpmNTQIRTLVTAADVIHSWTIPSL 108
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEY---PNGVTTGNTLRVPA------------------DTPIALRVTSTDVFHTFGIPEL 84


                  ...
gi 2067839381 109 GMK 111
Cdd:cd13918    85 RVK 87
 
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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