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Conserved domains on  [gi|383281837|gb|AFH01102|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Pseudolasius similus]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-185 1.29e-100

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 289.42  E-value: 1.29e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   1 MNTW-TLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPS 79
Cdd:MTH00154   1 MATWsNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  80 IKILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180
                 ....*....|....*....|....*.
gi 383281837 160 HSWTVPSLGIKMDSTPGRLNQSLLLM 185
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLI 186
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-185 1.29e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 289.42  E-value: 1.29e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   1 MNTW-TLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPS 79
Cdd:MTH00154   1 MATWsNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  80 IKILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180
                 ....*....|....*....|....*.
gi 383281837 160 HSWTVPSLGIKMDSTPGRLNQSLLLM 185
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLI 186
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-181 5.85e-55

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: 5.85e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  94 ITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDS 173
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82


                 ....*...
gi 383281837 174 TPGRLNQS 181
Cdd:cd13912   83 VPGRLNQT 90
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-180 1.31e-49

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 156.42  E-value: 1.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   94 ITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDS 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80


                  ....*..
gi 383281837  174 TPGRLNQ 180
Cdd:pfam00116  81 VPGRLNQ 87
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-180 9.19e-29

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 106.45  E-value: 9.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   3 TWTLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMF-SMI-----NNKLINRFLLQGHTIELIWTITPMIILIFVA 76
Cdd:COG1622   16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLyFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  77 IPSIKILYLTDEMFTNKITIKSLGHQWYWSYEYSDfLNIEfdsymtptnqlnfndfrlldVDNRCILPFNYPIRILTSSM 156
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSA 154

                        170       180
                 ....*....|....*....|....
gi 383281837 157 DVIHSWTVPSLGIKMDSTPGRLNQ 180
Cdd:COG1622  155 DVIHSFWVPALGGKQDAIPGRVTE 178
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 60-179 1.72e-22

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: 89.36  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   60 IELIWTITPMIILIFVAIPSI-KILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLniefdsymtptnqlnfndfrlLDVD 138
Cdd:TIGR02866  56 LEYVWTVIPLIIVVGLFAATAkGLLYLERPIPKDALKVKVTGYQWWWDFEYPESG---------------------FTTV 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 383281837  139 NRCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDSTPGRLN 179
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTN 155
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-185 1.29e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 289.42  E-value: 1.29e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   1 MNTW-TLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPS 79
Cdd:MTH00154   1 MATWsNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  80 IKILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180
                 ....*....|....*....|....*.
gi 383281837 160 HSWTVPSLGIKMDSTPGRLNQSLLLM 185
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLI 186
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-183 4.28e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 245.23  E-value: 4.28e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   1 MNTW-TLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPS 79
Cdd:MTH00140   1 MSYWgQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  80 IKILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVI 159
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180
                 ....*....|....*....|....
gi 383281837 160 HSWTVPSLGIKMDSTPGRLNQSLL 183
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSF 184
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-180 6.70e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 242.30  E-value: 6.70e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   1 MNTWT-LTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPS 79
Cdd:MTH00038   1 MATWLqLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  80 IKILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVI 159
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180
                 ....*....|....*....|.
gi 383281837 160 HSWTVPSLGIKMDSTPGRLNQ 180
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQ 181
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-180 3.26e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 240.27  E-value: 3.26e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   1 MNTWT-LTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPS 79
Cdd:MTH00168   1 MATYSqLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  80 IKILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVI 159
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180
                 ....*....|....*....|.
gi 383281837 160 HSWTVPSLGIKMDSTPGRLNQ 180
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQ 181
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-185 3.76e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 227.68  E-value: 3.76e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   1 MNTW-TLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPS 79
Cdd:MTH00139   1 MAYWgQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  80 IKILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVI 159
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180
                 ....*....|....*....|....*.
gi 383281837 160 HSWTVPSLGIKMDSTPGRLNQSLLLM 185
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFI 186
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 6-183 6.07e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 227.10  E-value: 6.07e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   6 LTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPSIKILYL 85
Cdd:MTH00117   7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  86 TDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVP 165
Cdd:MTH00117  87 MDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVP 166

                        170
                 ....*....|....*...
gi 383281837 166 SLGIKMDSTPGRLNQSLL 183
Cdd:MTH00117 167 SLGVKTDAVPGRLNQTSF 184
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 6-181 1.01e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 218.99  E-value: 1.01e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   6 LTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPSIKILYL 85
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  86 TDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVP 165
Cdd:MTH00185  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVP 166

                        170
                 ....*....|....*.
gi 383281837 166 SLGIKMDSTPGRLNQS 181
Cdd:MTH00185 167 ALGVKMDAVPGRLNQA 182
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-180 1.39e-72

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 218.57  E-value: 1.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   1 MNTW-TLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPS 79
Cdd:MTH00008   1 MPHWgQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  80 IKILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVI 159
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180
                 ....*....|....*....|.
gi 383281837 160 HSWTVPSLGIKMDSTPGRLNQ 180
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQ 181
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 3-181 1.56e-72

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 218.85  E-value: 1.56e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   3 TWTLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPSIKI 82
Cdd:MTH00023  13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  83 LYLTDEMFTNKITIKSLGHQWYWSYEYSDFL--NIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIH 160
Cdd:MTH00023  93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                        170       180
                 ....*....|....*....|.
gi 383281837 161 SWTVPSLGIKMDSTPGRLNQS 181
Cdd:MTH00023 173 SFAVPSLGLKIDAVPGRLNQT 193
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 6-181 1.80e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 215.73  E-value: 1.80e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   6 LTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPSIKILYL 85
Cdd:MTH00129   7 LGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  86 TDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVP 165
Cdd:MTH00129  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVP 166

                        170
                 ....*....|....*.
gi 383281837 166 SLGIKMDSTPGRLNQS 181
Cdd:MTH00129 167 ALGVKMDAVPGRLNQT 182
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 6-184 3.59e-71

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 214.97  E-value: 3.59e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   6 LTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPSIKILYL 85
Cdd:MTH00098   7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  86 TDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVP 165
Cdd:MTH00098  87 MDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVP 166

                        170
                 ....*....|....*....
gi 383281837 166 SLGIKMDSTPGRLNQSLLL 184
Cdd:MTH00098 167 SLGLKTDAIPGRLNQTTLM 185
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 6-184 3.51e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 202.32  E-value: 3.51e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   6 LTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPSIKILYL 85
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  86 TDEMFTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVP 165
Cdd:MTH00076  87 MDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVP 166

                        170
                 ....*....|....*....
gi 383281837 166 SLGIKMDSTPGRLNQSLLL 184
Cdd:MTH00076 167 SLGIKTDAIPGRLNQTSFI 185
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-185 7.54e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 201.55  E-value: 7.54e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   4 WTLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPSIKIL 83
Cdd:MTH00051   7 WQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  84 YLTDEMFTNKITIKSLGHQWYWSYEYSDF--LNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHS 161
Cdd:MTH00051  87 YLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHS 166

                        170       180
                 ....*....|....*....|....
gi 383281837 162 WTVPSLGIKMDSTPGRLNQSLLLM 185
Cdd:MTH00051 167 FAVPSLSVKIDAVPGRLNQTSFFI 190
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-181 5.85e-55

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: 5.85e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  94 ITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDS 173
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82


                 ....*...
gi 383281837 174 TPGRLNQS 181
Cdd:cd13912   83 VPGRLNQT 90
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-185 3.18e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 167.89  E-value: 3.18e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   4 WTLTLQNSNSPMYDMMIFFHDFTMMILTFIT-LLIFFIMFSMINNKLINRFL--LQGHTIELIWTITPMIILIFVAIPSI 80
Cdd:MTH00027  33 WQLGFQDAGSPVMEEIIMLHDQILFILTIIVgVVLWLIIRILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  81 KILYLTDE-MFTNKITIKSLGHQWYWSYEYSDF--LNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMD 157
Cdd:MTH00027 113 RLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAAD 192

                        170       180
                 ....*....|....*....|....*...
gi 383281837 158 VIHSWTVPSLGIKMDSTPGRLNQSLLLM 185
Cdd:MTH00027 193 VLHSWTVPSLAVKMDAVPGRINETGFLI 220
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 8-179 6.99e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 163.26  E-value: 6.99e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   8 LQNSNSPMYDMMIFFHDFTMMIL---TFITLLIFFIMFSMINNKLINRFLLQGHTIELIWTITPMIILIFVAIPSIKILY 84
Cdd:MTH00080   8 LNFSNSLFSSYMDWFHNFNCSLLfgeFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  85 LTDEM-FTNKITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWT 163
Cdd:MTH00080  88 YYGLMnLDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWA 167

                        170
                 ....*....|....*.
gi 383281837 164 VPSLGIKMDSTPGRLN 179
Cdd:MTH00080 168 LPSLSIKMDAMSGILS 183
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-180 1.31e-49

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 156.42  E-value: 1.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   94 ITIKSLGHQWYWSYEYSDFLNIEFDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDS 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80


                  ....*..
gi 383281837  174 TPGRLNQ 180
Cdd:pfam00116  81 VPGRLNQ 87
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-180 9.19e-29

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 106.45  E-value: 9.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   3 TWTLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMF-SMI-----NNKLINRFLLQGHTIELIWTITPMIILIFVA 76
Cdd:COG1622   16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLyFAIryrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  77 IPSIKILYLTDEMFTNKITIKSLGHQWYWSYEYSDfLNIEfdsymtptnqlnfndfrlldVDNRCILPFNYPIRILTSSM 156
Cdd:COG1622   96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSA 154

                        170       180
                 ....*....|....*....|....
gi 383281837 157 DVIHSWTVPSLGIKMDSTPGRLNQ 180
Cdd:COG1622  155 DVIHSFWVPALGGKQDAIPGRVTE 178
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 31-185 8.46e-28

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 103.11  E-value: 8.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  31 TFITLLIFFIM-FSMINNKLINRFLLQGHTIELIWTITP-MIILIFVAIpsiKILYLTDEM-FTNKITIKSLGHQWYWSY 107
Cdd:MTH00047  19 VFIPCWVYIMLcWQVVSGNGSVNFGSENQVLELLWTVVPtLLVLVLCFL---NLNFITSDLdCFSSETIKVIGHQWYWSY 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 383281837 108 EYSDflNIEFDSYMTptnQLNFNdfrlldVDNRCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDSTPGRLNQSLLLM 185
Cdd:MTH00047  96 EYSF--GGSYDSFMT---DDIFG------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 60-179 1.72e-22

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: 89.36  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837   60 IELIWTITPMIILIFVAIPSI-KILYLTDEMFTNKITIKSLGHQWYWSYEYSDFLniefdsymtptnqlnfndfrlLDVD 138
Cdd:TIGR02866  56 LEYVWTVIPLIIVVGLFAATAkGLLYLERPIPKDALKVKVTGYQWWWDFEYPESG---------------------FTTV 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 383281837  139 NRCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDSTPGRLN 179
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTN 155
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 4-82 1.42e-16

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: 70.82  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837    4 WTLTLQNSNSPMYDMMIFFHDFTMMILTFITLLIFFIMFSMI------NNKLINRFLLQGHTIELIWTITPMIILIFVAI 77
Cdd:pfam02790   5 WGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILILIAL 84


                  ....*
gi 383281837   78 PSIKI 82
Cdd:pfam02790  85 PSFKL 89
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-178 6.08e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 68.69  E-value: 6.08e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 383281837 117 FDSYMTPTNQLNFNDFRLLDVDNRCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDSTPGRL 178
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRL 112
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-179 1.59e-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: 63.41  E-value: 1.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  94 ITIKSLGHQWYWSYEYSDFLNIEFdsymTPTNQLnfndfrlldvdnrcILPFNYPIRILTSSMDVIHSWTVPSLGIKMDS 173
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGI----VTANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63


                 ....*.
gi 383281837 174 TPGRLN 179
Cdd:cd04213   64 IPGRTN 69
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-180 4.27e-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: 56.87  E-value: 4.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  94 ITIKSLGHQWYWSYEYsdflniefdsymtPTNQLNFNDfrlLDVdnrcilPFNYPIRILTSSMDVIHSWTVPSLGIKMDS 173
Cdd:cd13915    2 LEIQVTGRQWMWEFTY-------------PNGKREINE---LHV------PVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59


                 ....*..
gi 383281837 174 TPGRLNQ 180
Cdd:cd13915   60 VPGRYTY 66
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-180 1.82e-10

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: 54.99  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  94 ITIKSLGHQWYWSYEYSDflniefdsymtptnqlnfndfrlLDVDNRCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDS 173
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57


                 ....*..
gi 383281837 174 TPGRLNQ 180
Cdd:cd13842   58 VPGYTSE 64
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-179 2.30e-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: 55.11  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  94 ITIKSLGHQWYWSYEYSDflniefdSYMTPTNQLnfndfrlldvdnrcILPFNYPIRILTSSMDVIHSWTVPSLGIKMDS 173
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPE-------ANVTTSEQL--------------VIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59


                 ....*.
gi 383281837 174 TPGRLN 179
Cdd:cd13914   60 FPGQYN 65
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-180 9.88e-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: 53.41  E-value: 9.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383281837  94 ITIKSLGHQWYWSYEYSDflniefdsymtPTNQLNFNDFRLLDVdnrCILPFNYPIRILTSSMDVIHSWTVPSLGIKMDS 173
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPG-----------GDGKLGTDDDVTSPE---LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67


                 ....*..
gi 383281837 174 TPGRLNQ 180
Cdd:cd13919   68 VPGRTTR 74
 
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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