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Conserved domains on  [gi|847145490|gb|AKN21899|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Trebouxia asymmetrica]

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
 1-107 9.87e-58

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: 177.33  E-value: 9.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQSDnegllFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00154  63 IIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIE-----FDSYMIPTNELENNGFRLLD 137

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00154 138 VDNRLVLPMNTQIRILITAADVIHSWT 164
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-107 9.87e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 177.33  E-value: 9.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQSDnegllFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00154  63 IIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIE-----FDSYMIPTNELENNGFRLLD 137

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00154 138 VDNRLVLPMNTQIRILITAADVIHSWT 164
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 31-107 3.42e-49

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: 152.34  E-value: 3.42e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 847145490  31 PAVTIKAIGHQWYWSYEYSDYNqsdneGLLFDSYMIPEDELELGQLRLLDVDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFN-----DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWA 72
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
34-107 8.32e-42

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 133.30  E-value: 8.32e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847145490   34 TIKAIGHQWYWSYEYSDYnqsdnEGLLFDSYMIPEDELELGQLRLLDVDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDF-----GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWA 70
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-106 1.32e-24

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 92.58  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQsdnegllfdsymipedelelgqlrllD 80
Cdd:COG1622   81 IVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI--------------------------A 134

                         90       100
                 ....*....|....*....|....*.
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSW 106
Cdd:COG1622  135 TVNELVLPVGRPVRFLLTSADVIHSF 160
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-106 2.31e-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: 70.49  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490    1 IAWTVTPSLILVLIAIPSF-ALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYnqsdnegllfdsymipedelelgqlrLL 79
Cdd:TIGR02866  58 YVWTVIPLIIVVGLFAATAkGLLYLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GF 111

                          90       100
                  ....*....|....*....|....*..
gi 847145490   80 DVDNRVVVPVNTHIRMIITSADVLHSW 106
Cdd:TIGR02866 112 TTVNELVLPAGTPVELQVTSKDVIHSF 138
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-107 9.87e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 177.33  E-value: 9.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQSDnegllFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00154  63 IIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIE-----FDSYMIPTNELENNGFRLLD 137

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00154 138 VDNRLVLPMNTQIRILITAADVIHSWT 164
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-107 9.41e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 172.41  E-value: 9.41e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQsdnegLLFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00117  63 LIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD-----LSFDSYMIPTQDLPNGHFRLLE 137

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00117 138 VDHRMVIPMESPIRILITAEDVLHSWA 164
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-107 4.59e-53

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 166.08  E-value: 4.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYnqsDNEGLLFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00023  72 IVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLE 148

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00023 149 VDNRLVVPINTHVRILVTGADVLHSFA 175
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-107 9.82e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 164.38  E-value: 9.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQSDnegllFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00168  63 FVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLE-----FDSYMVPTQDLSPGQFRLLE 137

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00168 138 VDNRLVLPMDSKIRVLVTSADVLHSWT 164
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-107 3.36e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 163.19  E-value: 3.36e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNqsdneGLLFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00140  63 TIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFS-----VIEFDSYMVPENELELGDFRLLE 137

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00140 138 VDNRLVLPYSVDTRVLVTSADVIHSWT 164
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 3-107 3.50e-52

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 163.35  E-value: 3.50e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   3 WTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYnqsdnEGLLFDSYMIPEDELELGQLRLLDVD 82
Cdd:MTH00098  65 WTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVD 139

                         90       100
                 ....*....|....*....|....*
gi 847145490  83 NRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00098 140 NRVVLPMEMPIRMLISSEDVLHSWA 164
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 3-107 6.91e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 162.56  E-value: 6.91e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   3 WTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQSDnegllFDSYMIPEDELELGQLRLLDVD 82
Cdd:MTH00038  65 WTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLE-----FDSYMVPTSDLSTGLPRLLEVD 139

                         90       100
                 ....*....|....*....|....*
gi 847145490  83 NRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00038 140 NRLVLPYQTPIRVLVSSADVLHSWA 164
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 2-107 7.76e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 159.88  E-value: 7.76e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   2 AWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYnqsdnEGLLFDSYMIPEDELELGQLRLLDV 81
Cdd:MTH00139  64 IWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDF-----KNLSFDSYMIPTEDLSSGEFRLLEV 138

                         90       100
                 ....*....|....*....|....*.
gi 847145490  82 DNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00139 139 DNRLVLPYKSNIRALITAADVLHSWT 164
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 31-107 3.42e-49

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: 152.34  E-value: 3.42e-49
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 847145490  31 PAVTIKAIGHQWYWSYEYSDYNqsdneGLLFDSYMIPEDELELGQLRLLDVDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFN-----DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWA 72
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-107 8.12e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 154.94  E-value: 8.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNqsdNEGLLFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00051  65 IIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYG---TDTIEFDSYMIPTSDLNSGDLRLLE 141

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00051 142 VDNRLIVPIQTQVRVLVTAADVLHSFA 168
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 3-107 9.76e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 151.86  E-value: 9.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   3 WTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQsdnegLLFDSYMIPEDELELGQLRLLDVD 82
Cdd:MTH00076  65 WTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-----LSFDSYMIPTQDLTPGQFRLLEVD 139

                         90       100
                 ....*....|....*....|....*
gi 847145490  83 NRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00076 140 NRMVVPMESPIRMLITAEDVLHSWA 164
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-107 1.19e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 151.79  E-value: 1.19e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYnqsdnEGLLFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00129  63 IIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLE 137

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00129 138 ADHRMVVPVESPIRVLVSAEDVLHSWA 164
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-107 1.43e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 146.57  E-value: 1.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQsdnegLLFDSYMIPEDELELGQLRLLD 80
Cdd:MTH00185  63 IVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ-----LEFDSYMTPTQDLTPGQFRLLE 137

                         90       100
                 ....*....|....*....|....*..
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00185 138 TDHRMVVPMESPIRVLITAEDVLHSWT 164
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 3-107 6.98e-45

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 144.61  E-value: 6.98e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   3 WTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQSDnegllFDSYMIPEDELELGQLRLLDVD 82
Cdd:MTH00008  65 WTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLE-----FDSYMLPTSDLSPGQFRLLEVD 139

                         90       100
                 ....*....|....*....|....*
gi 847145490  83 NRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00008 140 NRAVLPMQTEIRVLVTAADVIHSWT 164
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
34-107 8.32e-42

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 133.30  E-value: 8.32e-42
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847145490   34 TIKAIGHQWYWSYEYSDYnqsdnEGLLFDSYMIPEDELELGQLRLLDVDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDF-----GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWA 70
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 3-107 1.05e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 131.67  E-value: 1.05e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   3 WTVTPSLILVLIAIPSFALLYSMDEV-VDPAVTIKAIGHQWYWSYEYSDYnqsdnEGLLFDSYMIPEDELELGQLRLLDV 81
Cdd:MTH00080  67 CSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTGHQWYWSYEFSDI-----PGLEFDSYMKSLDQLRLGEPRLLEV 141

                         90       100
                 ....*....|....*....|....*.
gi 847145490  82 DNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:MTH00080 142 DNRCVLPCDTNIRFCITSSDVIHSWA 167
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-106 4.80e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 125.52  E-value: 4.80e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPA-VTIKAIGHQWYWSYEYSDYNQSDNEgllFDSYMIPEDELELGQLRLL 79
Cdd:MTH00027  94 VIWTLIPAFILILIAFPSLRLLYIMDECGFSAnITIKVTGHQWYWSYSYEDYGEKNIE---FDSYMIPTADLEFGDLRLL 170

                         90       100
                 ....*....|....*....|....*..
gi 847145490  80 DVDNRVVVPVNTHIRMIITSADVLHSW 106
Cdd:MTH00027 171 EVDNRLILPVDTNVRVLITAADVLHSW 197
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-106 1.32e-24

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 92.58  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   1 IAWTVTPSLILVLIAIPSFALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYNQsdnegllfdsymipedelelgqlrllD 80
Cdd:COG1622   81 IVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI--------------------------A 134

                         90       100
                 ....*....|....*....|....*.
gi 847145490  81 VDNRVVVPVNTHIRMIITSADVLHSW 106
Cdd:COG1622  135 TVNELVLPVGRPVRFLLTSADVIHSF 160
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-106 2.31e-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: 70.49  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490    1 IAWTVTPSLILVLIAIPSF-ALLYSMDEVVDPAVTIKAIGHQWYWSYEYSDYnqsdnegllfdsymipedelelgqlrLL 79
Cdd:TIGR02866  58 YVWTVIPLIIVVGLFAATAkGLLYLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GF 111

                          90       100
                  ....*....|....*....|....*..
gi 847145490   80 DVDNRVVVPVNTHIRMIITSADVLHSW 106
Cdd:TIGR02866 112 TTVNELVLPAGTPVELQVTSKDVIHSF 138
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 3-105 1.02e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 63.43  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   3 WTVTPSLI-LVLIAIPSFALLYSMDEVVdpAVTIKAIGHQWYWSYEYSDynqsdneGLLFDSYMIPEdelelgqlrLLDV 81
Cdd:MTH00047  53 WTVVPTLLvLVLCFLNLNFITSDLDCFS--SETIKVIGHQWYWSYEYSF-------GGSYDSFMTDD---------IFGV 114

                         90       100
                 ....*....|....*....|....
gi 847145490  82 DNRVVVPVNTHIRMIITSADVLHS 105
Cdd:MTH00047 115 DKPLRLVYGVPYHLLVTSSDVIHS 138
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 61-107 6.23e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 60.99  E-value: 6.23e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 847145490  61 FDSYMIPEDELELGQLRLLDVDNRVVVPVNTHIRMIITSADVLHSWA 107
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWS 97
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 32-105 4.47e-09

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 49.55  E-value: 4.47e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847145490  32 AVTIKAIGHQWYWSYEYSDYNQSDNEgllfdsymipedelelgqlrlldvdnrVVVPVNTHIRMIITSADVLHS 105
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGKREINE---------------------------LHVPVGKPVRLILTSKDVIHS 47
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 33-106 4.52e-08

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: 46.91  E-value: 4.52e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847145490  33 VTIKAIGHQWYWSYEYSDYNqsdnegllfdsymipedelelgqlrlldVDNRVVVPVNTHIRMIITSADVLHSW 106
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVR----------------------------TPNEIVVPAGTPVRFRVTSPDVIHGF 46
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 32-105 8.90e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 46.09  E-value: 8.90e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 847145490  32 AVTIKAIGHQWYWSYEYSDYNQSDNegllfdsymiPEDELELGQLRLldvdnrvvvPVNTHIRMIITSADVLHS 105
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGDGKLG----------TDDDVTSPELHL---------PVGRPVLFNLRSKDVIHS 55
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 32-107 1.57e-07

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: 45.69  E-value: 1.57e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 847145490  32 AVTIKAIGHQWYWSYEYSDYnqsdnegllfdsymiPEDELELGqlrlldvdNRVVVPVNTHIRMIITSADVLHS-WA 107
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDE---------------PGRGIVTA--------NELHIPVGRPVRLRLTSADVIHSfWV 54
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 8-105 6.22e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 36.66  E-value: 6.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 847145490   8 SLILV--LIAIPSFALLY---SMDEVVDPAVTIKAIGHQWYWSYEYSDYNQSDNEgllfdsymipedelelgqlrlldvd 82
Cdd:cd13918    3 SAIIVisLIVWTYGMLLYvedPPDEADEDALEVEVEGFQFGWQFEYPNGVTTGNT------------------------- 57

                         90       100
                 ....*....|....*....|...
gi 847145490  83 nrVVVPVNTHIRMIITSADVLHS 105
Cdd:cd13918   58 --LRVPADTPIALRVTSTDVFHT 78
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 33-105 7.25e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 35.85  E-value: 7.25e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 847145490  33 VTIKAIGHQWYWSYEYSDYNQSDNegllfdsymipedelelgqlrlldvdNRVVVPVNTHIRMIITSADVLHS 105
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEANVTTS--------------------------EQLVIPADRPVYFRITSRDVIHA 47
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-21 1.51e-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: 35.00  E-value: 1.51e-03
                          10        20
                  ....*....|....*....|.
gi 847145490    1 IAWTVTPSLILVLIAIPSFAL 21
Cdd:pfam02790  69 IIWTIIPAVILILIALPSFKL 89
 
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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