NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|37731373|gb|AAN75252|]
View 

cytochrome oxidase subunit II, partial (mitochondrion) [Melanoplus spretus]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 2-126 9.09e-81

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 236.65  E-value: 9.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00154  68 LPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMN 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00154 148 TQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLF 192
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 2-126 9.09e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 236.65  E-value: 9.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00154  68 LPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMN 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00154 148 TQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLF 192
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 29-126 1.40e-64

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 192.01  E-value: 1.40e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373  29 ITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:cd13912   3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                        90
                ....*....|....*...
gi 37731373 109 TPGRLNQGTFTMNRPGLF 126
Cdd:cd13912  83 VPGRLNQTSFFIERPGVY 100
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
29-126 7.97e-59

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 177.22  E-value: 7.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    29 ITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*...
gi 37731373   109 TPGRLNQGTFTMNRPGLF 126
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVF 98
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-126 8.92e-25

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 93.74  E-value: 8.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373   1 ALPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDfENIEfdtymtpendleingfrlldVDNRTILPM 80
Cdd:COG1622  85 VIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPV 143

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 37731373  81 NTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:COG1622 144 GRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 29-126 3.63e-23

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: 88.98  E-value: 3.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    29 ITIKTIGRQWYWSYEYSDFeniefdtymtpendleinGFRlldVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:TIGR02866  91 LKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDA 149

                          90
                  ....*....|....*...
gi 37731373   109 TPGRLNQGTFTMNRPGLF 126
Cdd:TIGR02866 150 IPGQTNALWFNADEPGVY 167
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 2-126 9.09e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 236.65  E-value: 9.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00154  68 LPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMN 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00154 148 TQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLF 192
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-126 2.37e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 197.44  E-value: 2.37e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    1 ALPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPM 80
Cdd:MTH00117  67 ILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPM 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 37731373   81 NTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00117 147 ESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVF 192
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 29-126 1.40e-64

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 192.01  E-value: 1.40e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373  29 ITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:cd13912   3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                        90
                ....*....|....*...
gi 37731373 109 TPGRLNQGTFTMNRPGLF 126
Cdd:cd13912  83 VPGRLNQTSFFIERPGVY 100
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 2-126 6.59e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 186.30  E-value: 6.59e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00140  68 VPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYS 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00140 148 VDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVF 192
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 2-126 4.56e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 181.45  E-value: 4.56e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00139  68 LPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYK 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00139 148 SNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVF 192
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
29-126 7.97e-59

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 177.22  E-value: 7.97e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    29 ITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*...
gi 37731373   109 TPGRLNQGTFTMNRPGLF 126
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVF 98
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 3-126 1.48e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 177.97  E-value: 1.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    3 PAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMNT 82
Cdd:MTH00038  69 PAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQT 148

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 37731373   83 EVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00038 149 PIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLF 192
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 2-126 1.38e-56

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 175.43  E-value: 1.38e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00008  68 LPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQ 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00008 148 TEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVF 192
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-126 2.00e-56

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 174.91  E-value: 2.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00098  68 LPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPME 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00098 148 MPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLY 192
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 2-126 5.41e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 173.63  E-value: 5.41e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00168  68 IPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMD 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00168 148 SKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSF 192
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-126 1.90e-55

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 172.38  E-value: 1.90e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00185  68 LPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPME 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00185 148 SPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLY 192
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-126 1.95e-54

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 170.32  E-value: 1.95e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDF--ENIEFDTYMTPENDLEINGFRLLDVDNRTILP 79
Cdd:MTH00023  77 IPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVP 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 37731373   80 MNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00023 157 INTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVF 203
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-126 2.77e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 169.51  E-value: 2.77e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00129  68 LPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVE 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00129 148 SPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVF 192
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 2-126 1.59e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 167.65  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMN 81
Cdd:MTH00076  68 MPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPME 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 37731373   82 TEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00076 148 SPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVY 192
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-126 4.11e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 166.49  E-value: 4.11e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDF--ENIEFDTYMTPENDLEINGFRLLDVDNRTILP 79
Cdd:MTH00051  70 IPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVP 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 37731373   80 MNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00051 150 IQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVF 196
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 29-126 1.52e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 137.06  E-value: 1.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373   29 ITIKTIGRQWYWSYEYSDFENIEFDTYMTPENDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDA 177

                         90
                 ....*....|....*...
gi 37731373  109 TPGRLNQGTFTMNRPGLF 126
Cdd:MTH00080 178 MSGILSTLCYSFPMPGVF 195
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-126 4.53e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 136.69  E-value: 4.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    2 LPAITLIFIALPSLRLLYLLDDSV-DALITIKTIGRQWYWSYEYSDF--ENIEFDTYMTPENDLEINGFRLLDVDNRTIL 78
Cdd:MTH00027  99 IPAFILILIAFPSLRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLIL 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 37731373   79 PMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:MTH00027 179 PVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIF 226
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 30-126 6.17e-27

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 98.49  E-value: 6.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373   30 TIKTIGRQWYWSYEYSDfeNIEFDTYMTpenDLeINGfrlldVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDAT 109
Cdd:MTH00047  83 TIKVIGHQWYWSYEYSF--GGSYDSFMT---DD-IFG-----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAI 151

                         90
                 ....*....|....*..
gi 37731373  110 PGRLNQGTFTMNRPGLF 126
Cdd:MTH00047 152 PGRINHLFFCPDRHGVF 168
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-126 8.92e-25

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 93.74  E-value: 8.92e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373   1 ALPAITLIFIALPSLRLLYLLDDSVDALITIKTIGRQWYWSYEYSDfENIEfdtymtpendleingfrlldVDNRTILPM 80
Cdd:COG1622  85 VIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPV 143

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 37731373  81 NTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:COG1622 144 GRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 29-126 3.63e-23

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: 88.98  E-value: 3.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373    29 ITIKTIGRQWYWSYEYSDFeniefdtymtpendleinGFRlldVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:TIGR02866  91 LKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDA 149

                          90
                  ....*....|....*...
gi 37731373   109 TPGRLNQGTFTMNRPGLF 126
Cdd:TIGR02866 150 IPGQTNALWFNADEPGVY 167
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 52-126 1.71e-20

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 81.02  E-value: 1.71e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37731373   52 FDTYMTPENDLEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVF 125
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 29-126 2.21e-17

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 71.17  E-value: 2.21e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373  29 ITIKTIGRQWYWSYEYSDfeniefdtymtpendleingfrlLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90
                ....*....|....*...
gi 37731373 109 TPGRLNQGTFTMNRPGLF 126
Cdd:cd13842  58 VPGYTSELWFVADKPGTY 75
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 29-126 2.69e-16

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: 68.42  E-value: 2.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373  29 ITIKTIGRQWYWSYEYsdfeniefdtymtPENDLEINGfrlLDVdnrtilPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:cd13915   2 LEIQVTGRQWMWEFTY-------------PNGKREINE---LHV------PVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90
                ....*....|....*...
gi 37731373 109 TPGRLNQGTFTMNRPGLF 126
Cdd:cd13915  60 VPGRYTYLWFEATKPGEY 77
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 29-126 5.55e-15

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: 65.33  E-value: 5.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373  29 ITIKTIGRQWYWSYEYSDFENIEFDTymtpENDLeingfrlldvdnrtILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                        90
                ....*....|....*...
gi 37731373 109 TPGRLNQGTFTMNRPGLF 126
Cdd:cd04213  64 IPGRTNRLWLQADEPGVY 81
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 29-126 1.54e-14

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: 64.20  E-value: 1.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373  29 ITIKTIGRQWYWSYEYsdfeniefdtymtPENDlEINGFRLLDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:cd13919   2 LVVEVTAQQWAWTFRY-------------PGGD-GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90
                ....*....|....*...
gi 37731373 109 TPGRLNQGTFTMNRPGLF 126
Cdd:cd13919  68 VPGRTTRLWFTPTREGEY 85
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 29-114 2.12e-11

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 56.26  E-value: 2.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373  29 ITIKTIGRQWYWSYEYSDfENIefdtymtpendleingfrllDVDNRTILPMNTEVRVLTSASDVLHSWAVPALGIKIDA 108
Cdd:cd13914   1 VEIEVEAYQWGWEFSYPE-ANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                ....*.
gi 37731373 109 TPGRLN 114
Cdd:cd13914  60 FPGQYN 65
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 22-124 2.95e-07

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: 46.29  E-value: 2.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37731373  22 DDSVDALITIKTIGRQWYWSYEYsdfeniefdtymtPENDLEINGFRLldvdnrtilPMNTEVRVLTSASDVLHSWAVPA 101
Cdd:cd13918  26 DEADEDALEVEVEGFQFGWQFEY-------------PNGVTTGNTLRV---------PADTPIALRVTSTDVFHTFGIPE 83

                        90       100
                ....*....|....*....|...
gi 37731373 102 LGIKIDATPGRLNQGTFTMNRPG 124
Cdd:cd13918  84 LRVKADAIPGEYTSTWFEADEPG 106
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 78-126 4.58e-04

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 36.78  E-value: 4.58e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 37731373  78 LPMNTEVRVLTSASDVLHSWAVPALGIKIDATPGRLNQGTFTMNRPGLF 126
Cdd:cd13913  29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEY 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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