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Conserved domains on  [gi|1896069663|gb|QNJ46987|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Propsednura eyrei]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl33359
cytochrome c oxidase subunit II; Provisional
 1-91 4.20e-62

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: 187.73  E-value: 4.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00154  180 NQLNFLINRPG 190
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-91 4.20e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 187.73  E-value: 4.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00154  180 NQLNFLINRPG 190
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 1-91 1.42e-56

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: 170.44  E-value: 1.42e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:cd13912     8 IGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRL 87

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:cd13912    88 NQTSFFIERPG 98
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
1-91 1.73e-51

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 157.19  E-value: 1.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:pfam00116   6 IGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRL 85

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:pfam00116  86 NQTSFSIDREG 96
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-91 1.63e-19

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: 78.19  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFkniefdtymlnendleknsfrLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:TIGR02866  96 TGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQT 154

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:TIGR02866 155 NALWFNADEPG 165
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-91 2.21e-19

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 78.33  E-value: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYsdfkniefdtymLNENdleknsfrlIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:COG1622   118 TGYQWKWLFRY------------PDQG---------IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRV 176

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:COG1622   177 TELWFTADKPG 187
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-91 4.20e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 187.73  E-value: 4.20e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00154  100 IGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00154  180 NQLNFLINRPG 190
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 1-91 1.42e-56

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: 170.44  E-value: 1.42e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:cd13912     8 IGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRL 87

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:cd13912    88 NQTSFFIERPG 98
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-91 5.03e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 169.71  E-value: 5.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00117  100 IGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00117  180 NQTSFITTRPG 190
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
1-91 1.73e-51

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 157.19  E-value: 1.73e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:pfam00116   6 IGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRL 85

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:pfam00116  86 NQTSFSIDREG 96
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-91 7.41e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 158.95  E-value: 7.41e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00140  100 IGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00140  180 NQLSFEPKRPG 190
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-91 4.00e-48

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 152.18  E-value: 4.00e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00139  100 VGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00139  180 NQVGFFINRPG 190
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-91 1.11e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 150.90  E-value: 1.11e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00168  100 VGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00168  180 NQLAFLSSRPG 190
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-91 1.27e-46

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 148.47  E-value: 1.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00008  100 IGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00008  180 NQIGFTITRPG 190
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-91 9.85e-45

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 143.71  E-value: 9.85e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00098  100 MGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00098  180 NQTTLMSTRPG 190
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-91 1.24e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 143.30  E-value: 1.24e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00038  100 IGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00038  180 NQTTFFISRTG 190
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-91 5.98e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 141.77  E-value: 5.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00129  100 MGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00129  180 NQTAFIASRPG 190
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-91 6.17e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 141.46  E-value: 6.17e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00076  100 IGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00076  180 NQTSFIASRPG 190
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-91 1.31e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 140.79  E-value: 1.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00185  100 MGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRL 179

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00185  180 NQATFIISRPG 190
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-91 6.08e-43

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 139.50  E-value: 6.08e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFK--NIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPG 78
Cdd:MTH00023  109 IGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPG 188

                          90
                  ....*....|...
gi 1896069663  79 RLNQGTMMVNRPG 91
Cdd:MTH00023  189 RLNQTGFFIKRPG 201
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-91 6.64e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 134.14  E-value: 6.64e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDF--KNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPG 78
Cdd:MTH00051  102 IGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPG 181

                          90
                  ....*....|...
gi 1896069663  79 RLNQGTMMVNRPG 91
Cdd:MTH00051  182 RLNQTSFFIKRPG 194
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-91 7.42e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 123.58  E-value: 7.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00080  103 TGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGIL 182

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:MTH00080  183 STLCYSFPMPG 193
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-91 2.45e-34

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 117.82  E-value: 2.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   2 GRQWYWSYEYSDF--KNIEFDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGR 79
Cdd:MTH00027  133 GHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGR 212

                          90
                  ....*....|..
gi 1896069663  80 LNQGTMMVNRPG 91
Cdd:MTH00027  213 INETGFLIKRPG 224
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 1-82 2.73e-21

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 82.69  E-value: 2.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDfkNIEFDTYMLNENDLEKNSFRLIdvdnrtiipINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:MTH00047   87 IGHQWYWSYEYSF--GGSYDSFMTDDIFGVDKPLRLV---------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRI 155


                  ..
gi 1896069663  81 NQ 82
Cdd:MTH00047  156 NH 157
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 19-91 7.84e-20

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 77.94  E-value: 7.84e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896069663  19 FDTYMLNENDLEKNSFRLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRLNQGTMMVNRPG 91
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREG 123
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-91 1.63e-19

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: 78.19  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFkniefdtymlnendleknsfrLIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:TIGR02866  96 TGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQT 154

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:TIGR02866 155 NALWFNADEPG 165
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-91 2.21e-19

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 78.33  E-value: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYsdfkniefdtymLNENdleknsfrlIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:COG1622   118 TGYQWKWLFRY------------PDQG---------IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRV 176

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:COG1622   177 TELWFTADKPG 187
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 1-91 3.67e-15

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: 64.24  E-value: 3.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663  1 IGRQWYWSYEYSDfkniefdtymlnendleknsfrlIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:cd13842    6 TGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYT 62

                         90
                 ....*....|.
gi 1896069663 81 NQGTMMVNRPG 91
Cdd:cd13842   63 SELWFVADKPG 73
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 1-91 5.91e-13

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: 58.79  E-value: 5.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYSDFKNIEFDTymlnENDLeknsfrlidvdnrtIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:cd04213     7 TGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRT 68

                          90
                  ....*....|.
gi 1896069663  81 NQGTMMVNRPG 91
Cdd:cd04213    69 NRLWLQADEPG 79
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 1-91 5.52e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 53.79  E-value: 5.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663  1 IGRQWYWSYEYSDFKNIefdtymlnendleknsfrlidvDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:cd13915    7 TGRQWMWEFTYPNGKRE----------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                         90
                 ....*....|.
gi 1896069663 81 NQGTMMVNRPG 91
Cdd:cd13915   65 TYLWFEATKPG 75
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 2-81 1.02e-10

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 53.18  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   2 GRQWYWSYEYSDfkniefdtymlnENdleknsfrlIDVDNRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRLN 81
Cdd:cd13914     7 AYQWGWEFSYPE------------AN---------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 1-82 2.41e-10

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 52.26  E-value: 2.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069663   1 IGRQWYWSYEYsdfknIEFDTYMLNENDLEKNSFRLidvdnrtiiPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRL 80
Cdd:cd13919     7 TAQQWAWTFRY-----PGGDGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRT 72


                  ..
gi 1896069663  81 NQ 82
Cdd:cd13919    73 TR 74
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 41-91 2.00e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 40.13  E-value: 2.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1896069663  41 NRTIIPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRLNQGTMMVNRPG 91
Cdd:cd13918    56 NTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPG 106
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 41-91 2.63e-04

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 36.37  E-value: 2.63e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 1896069663 41 NRTIIPINSEIRI-LTSASdVLHSWTLPSLGIKIDAMPGRLNQGTMMVNRPG 91
Cdd:cd04212   25 NELVIPVGRPVNFrLTSDS-VMNSFFIPQLGGQIYAMAGMQTQLHLIADKPG 75
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 45-91 8.93e-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: 35.24  E-value: 8.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 1896069663 45 IPINSEIRILTSASDVLHSWTLPSLGIKIDAMPGRLNQGTMMVNRPG 91
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPG 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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