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Conserved domains on  [gi|52782796|sp|Q9XLW8|]
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RecName: Full=Cytochrome c oxidase subunit 2; AltName: Full=Cytochrome c oxidase polypeptide II; Flags: Precursor

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
 24-249 7.48e-104

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 300.59  E-value: 7.48e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   24 YFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFIL 103
Cdd:MTH00154   8 SFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLL----FNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  104 LYLCDEVISPAMTIKAIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAAD 183
Cdd:MTH00154  84 LYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAAD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52782796  184 VIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLN 249
Cdd:MTH00154 159 VIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 24-249 7.48e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 300.59  E-value: 7.48e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   24 YFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFIL 103
Cdd:MTH00154   8 SFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLL----FNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  104 LYLCDEVISPAMTIKAIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAAD 183
Cdd:MTH00154  84 LYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAAD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52782796  184 VIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLN 249
Cdd:MTH00154 159 VIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 113-247 8.63e-83

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: 243.25  E-value: 8.63e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 113 PAMTIKAIGLQWYWKYEYSDFinesgETVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPS 192
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDF-----NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 52782796 193 LGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEW 247
Cdd:cd13912  76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
115-239 7.27e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 233.07  E-value: 7.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   115 MTIKAIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPSLG 194
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 52782796   195 IKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAV 239
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
21-251 6.06e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 191.58  E-value: 6.06e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  21 YGVYFQDSATPNQEGILELHdNIMFYLLVILGLVSWLL---FTITRTYSKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIA 97
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLF-WVSLIIMLVIFVLVFGLllyFAIRYRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  98 FPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDfinesgetvefesyvipEDLLEDGQLrlldtdtsvVVPVDTHIRF 177
Cdd:COG1622  96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-----------------QGIATVNEL---------VLPVGRPVRF 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52782796 178 VVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLNEQ 251
Cdd:COG1622 150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 29-249 2.64e-42

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: 142.90  E-value: 2.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796    29 ATPNQEGILELHDNIMFYLLVILGLVSWLLFTIT---RTYSKNPIAyKYIKHGQTIEIIWTIFPAV-VLLIIAFPSFILL 104
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfRRKGDEEKP-SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   105 YLCDEVISPAMTIKAIGLQWYWKYEYSDFinesgetvefesyvipedlledgqlrLLDTDTSVVVPVDTHIRFVVTAADV 184
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52782796   185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLN 249
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 24-249 7.48e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 300.59  E-value: 7.48e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   24 YFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFIL 103
Cdd:MTH00154   8 SFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLL----FNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  104 LYLCDEVISPAMTIKAIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAAD 183
Cdd:MTH00154  84 LYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAAD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52782796  184 VIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLN 249
Cdd:MTH00154 159 VIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 10-248 8.10e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 288.19  E-value: 8.10e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   10 NMIIMNDVPTPYGVYFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITrtysKNPIAYKYIKHGQTIEIIWTIFP 89
Cdd:MTH00023   3 NNFFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL----NGKFYDRFLVDGTFLEIVWTIIP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   90 AVVLLIIAFPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFineSGETVEFESYVIPEDLLEDGQLRLLDTDTSVVV 169
Cdd:MTH00023  79 AVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52782796  170 PVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWL 248
Cdd:MTH00023 156 PINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 23-249 5.22e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 277.98  E-value: 5.22e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   23 VYFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFI 102
Cdd:MTH00140   7 LGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLL----FNKFSCRTILEAQKLETIWTIVPALILVFLALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  103 LLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAA 182
Cdd:MTH00140  83 LLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52782796  183 DVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLN 249
Cdd:MTH00140 158 DVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 15-251 2.56e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 273.97  E-value: 2.56e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   15 NDVPTPYGVYFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFT--ITRTYsknpiaYKYIKHGQTIEIIWTIFPAVV 92
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRalTTKYY------HKYLFEGTLIEIIWTLIPAAI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   93 LLIIAFPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFineSGETVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVD 172
Cdd:MTH00051  75 LIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDY---GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52782796  173 THIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLNEQ 251
Cdd:MTH00051 152 TQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 19-250 6.73e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 267.62  E-value: 6.73e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   19 TPYGVYFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTItrtySKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAF 98
Cdd:MTH00168   3 TYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVL----VTSKYTNRFLLDSQMIEFVWTIIPAFILISLAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   99 PSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFV 178
Cdd:MTH00168  79 PSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52782796  179 VTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLNE 250
Cdd:MTH00168 154 VTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 25-250 2.01e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 256.18  E-value: 2.01e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFILL 104
Cdd:MTH00139   9 FQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLM----SNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  105 YLCDEVISPAMTIKAIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAADV 184
Cdd:MTH00139  85 YLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52782796  185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLNE 250
Cdd:MTH00139 160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 25-249 5.93e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 252.53  E-value: 5.93e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTI--TRTYSKNpiaykyIKHGQTIEIIWTIFPAVVLLIIAFPSFI 102
Cdd:MTH00117   9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMltTKLTHTN------TVDAQEVELIWTILPAIVLILLALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  103 LLYLCDEVISPAMTIKAIGLQWYWKYEYSDFinesgETVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAA 182
Cdd:MTH00117  83 ILYLMDEINNPHLTIKAIGHQWYWSYEYTDY-----KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAE 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52782796  183 DVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLN 249
Cdd:MTH00117 158 DVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 113-247 8.63e-83

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: 243.25  E-value: 8.63e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 113 PAMTIKAIGLQWYWKYEYSDFinesgETVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPS 192
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDF-----NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 52782796 193 LGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEW 247
Cdd:cd13912  76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 23-248 2.07e-82

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 246.31  E-value: 2.07e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   23 VYFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITRtyskNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFI 102
Cdd:MTH00008   7 LMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMF----NKLSNRYILEAQQIETIWTILPALILLFLAFPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  103 LLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAA 182
Cdd:MTH00008  83 LLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52782796  183 DVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWL 248
Cdd:MTH00008 158 DVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 19-250 2.83e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 243.46  E-value: 2.83e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   19 TPYGVYFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITRTYSKNpiayKYIKHGQTIEIIWTIFPAVVLLIIAF 98
Cdd:MTH00038   3 TWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTN----RFFLEGQELETIWTIVPAFILIFIAL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   99 PSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFinesgETVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFV 178
Cdd:MTH00038  79 PSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-----NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVL 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52782796  179 VTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLNE 250
Cdd:MTH00038 154 VSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 25-247 4.89e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 240.00  E-value: 4.89e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   25 FQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITRTYSKNpiayKYIKHGQTIEIIWTIFPAVVLLIIAFPSFILL 104
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTN----KYILDSQEIEIIWTVLPAVILILIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  105 YLCDEVISPAMTIKAIGLQWYWKYEYSDFinesgETVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAADV 184
Cdd:MTH00129  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52782796  185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEW 247
Cdd:MTH00129 160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 18-251 4.67e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 237.75  E-value: 4.67e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   18 PTPYGvyFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTI--TRTYSKNPIaykyikHGQTIEIIWTIFPAVVLLI 95
Cdd:MTH00076   4 PSQLG--FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMmtTKLTNTNTM------DAQEIEMVWTIMPAIILIV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   96 IAFPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINESgetveFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHI 175
Cdd:MTH00076  76 IALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLS-----FDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52782796  176 RFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLNEQ 251
Cdd:MTH00076 151 RMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 25-247 6.85e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 237.48  E-value: 6.85e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   25 FQDSATPNQEGILELHDnimfYLLVILGLVSWLLFTITRTYSKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFILL 104
Cdd:MTH00185   9 LQDAASPVMEELIHFHD----HTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  105 YLCDEVISPAMTIKAIGLQWYWKYEYSDFinesgETVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAADV 184
Cdd:MTH00185  85 YLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52782796  185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEW 247
Cdd:MTH00185 160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
115-239 7.27e-79

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 233.07  E-value: 7.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   115 MTIKAIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPSLG 194
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 52782796   195 IKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAV 239
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 18-247 5.89e-76

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 229.60  E-value: 5.89e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   18 PTPYGVYFQDSATPNQEGILELHDnimfYLLVILGLVSWLLFTITRTYSKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIA 97
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHD----HTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   98 FPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFinesgETVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRF 177
Cdd:MTH00098  78 LPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRM 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  178 VVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEW 247
Cdd:MTH00098 153 LISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-251 7.97e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 222.98  E-value: 7.97e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796    1 MLTFLSNLNNMIIMNDVPTPYGVYFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITrtYSKNPIAYKYIK-HGQ 79
Cdd:MTH00027  13 EGGALYPMNVASMIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRIL--LGNNYYSYYWNKlDGS 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   80 TIEIIWTIFPAVVLLIIAFPSFILLYLCDE-VISPAMTIKAIGLQWYWKYEYSDFineSGETVEFESYVIPEDLLEDGQL 158
Cdd:MTH00027  91 LIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDY---GEKNIEFDSYMIPTADLEFGDL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  159 RLLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEA 238
Cdd:MTH00027 168 RLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVES 247

                        250
                 ....*....|...
gi 52782796  239 VSLPSFLEWLNEQ 251
Cdd:MTH00027 248 VSLSKYIDWIGRE 260
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
21-251 6.06e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 191.58  E-value: 6.06e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  21 YGVYFQDSATPNQEGILELHdNIMFYLLVILGLVSWLL---FTITRTYSKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIA 97
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLF-WVSLIIMLVIFVLVFGLllyFAIRYRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  98 FPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDfinesgetvefesyvipEDLLEDGQLrlldtdtsvVVPVDTHIRF 177
Cdd:COG1622  96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-----------------QGIATVNEL---------VLPVGRPVRF 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52782796 178 VVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLNEQ 251
Cdd:COG1622 150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 41-248 2.95e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 187.14  E-value: 2.95e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   41 DNIMFYLLVILGLVSWLLFTITRTYSknpiaYKYIK-HGQTIEIIWTIFPAVVLLIIAFPSFILLYLCDEV-ISPAMTIK 118
Cdd:MTH00080  27 CSLLFGEFVLAFVVFLFLYLISNNFY-----FKSKKiEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  119 AIGLQWYWKYEYSDFINesgetVEFESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPSLGIKVD 198
Cdd:MTH00080 102 VTGHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 52782796  199 ATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWL 248
Cdd:MTH00080 177 AMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 143-240 1.10e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 145.35  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  143 FESYVIPEDLLEDGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCS 222
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*...
gi 52782796  223 ELCGTAHSAMPIKIEAVS 240
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVS 148
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 29-249 2.64e-42

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: 142.90  E-value: 2.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796    29 ATPNQEGILELHDNIMFYLLVILGLVSWLLFTIT---RTYSKNPIAyKYIKHGQTIEIIWTIFPAV-VLLIIAFPSFILL 104
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfRRKGDEEKP-SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   105 YLCDEVISPAMTIKAIGLQWYWKYEYSDFinesgetvefesyvipedlledgqlrLLDTDTSVVVPVDTHIRFVVTAADV 184
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52782796   185 IHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWLN 249
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 79-239 7.33e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 131.23  E-value: 7.33e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796   79 QTIEIIWTIFPAVVLLIIAFpsFILLYL-CDEVISPAMTIKAIGLQWYWKYEYSDFInesgetvEFESYVIPEDLLEDGQ 157
Cdd:MTH00047  47 QVLELLWTVVPTLLVLVLCF--LNLNFItSDLDCFSSETIKVIGHQWYWSYEYSFGG-------SYDSFMTDDIFGVDKP 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  158 LRLLdtdtsvvvpVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIE 237
Cdd:MTH00047 118 LRLV---------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188


                 ..
gi 52782796  238 AV 239
Cdd:MTH00047 189 VV 190
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 17-103 2.61e-37

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: 126.29  E-value: 2.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796    17 VPTPYGVYFQDSATPNQEGILELHDNIMFYLLVILGLVSWLLFTITRTY--SKNPIAYKYIKHGQTIEIIWTIFPAVVLL 94
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFnrRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 52782796    95 IIAFPSFIL 103
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 114-239 1.16e-27

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: 101.93  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 114 AMTIKAIGLQWYWKYEYsdfinesgetvefesyvipedllEDGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPSL 193
Cdd:cd04213   1 ALTIEVTGHQWWWEFRY-----------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 52782796 194 GIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAV 239
Cdd:cd04213  58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-232 7.48e-25

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: 94.63  E-value: 7.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 114 AMTIKAIGLQWYWKYEYSDfinesgetvefesyvipedllEDGQLRLLDTDTS--VVVPVDTHIRFVVTAADVIHDFAIP 191
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPG---------------------GDGKLGTDDDVTSpeLHLPVGRPVLFNLRSKDVIHSFWVP 59

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 52782796 192 SLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAM 232
Cdd:cd13919  60 EFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 115-237 5.76e-24

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: 91.97  E-value: 5.76e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 115 MTIKAIGLQWYWKYEYSDfinesgetvefesyvipedlledgqlrlLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPSLG 194
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 52782796 195 IKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIE 237
Cdd:cd13842  53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-238 4.55e-23

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: 90.00  E-value: 4.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 114 AMTIKAIGLQWYWKYEYsdfinesgetvefesyviPEDLLEDGQLrlldtdtsvVVPVDTHIRFVVTAADVIHDFAIPSL 193
Cdd:cd13915   1 ALEIQVTGRQWMWEFTY------------------PNGKREINEL---------HVPVGKPVRLILTSKDVIHSFYVPAF 53

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 52782796 194 GIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEA 238
Cdd:cd13915  54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-248 2.36e-22

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: 88.23  E-value: 2.36e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 116 TIKAIGLQWYWKYEYsdfiNESGetvefesyvipedlledgqlrlLDTDTSVVVPVDTHIRFVVTAADVIHDFAIPSLGI 195
Cdd:cd13914   2 EIEVEAYQWGWEFSY----PEAN----------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 52782796 196 KVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEWL 248
Cdd:cd13914  56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 91-248 4.71e-20

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: 83.27  E-value: 4.71e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796  91 VVLLIIAFPSFILLYLCD---EVISPAMTIKAIGLQWYWKYEYSDFINESGEtvefesyvipedlledgqlrlldtdtsV 167
Cdd:cd13918   6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTGNT---------------------------L 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 168 VVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAVSLPSFLEW 247
Cdd:cd13918  59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138


                .
gi 52782796 248 L 248
Cdd:cd13918 139 Y 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 163-239 8.59e-14

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: 65.28  E-value: 8.59e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52782796 163 TDTSVVVPVDTHIRFVVTAADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAV 239
Cdd:cd13913  23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 161-239 2.83e-08

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 50.07  E-value: 2.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 161 LDTDTsvvVPVDTHIRFVVTAADVIHDFAI--PSLGI--KVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKI 236
Cdd:cd13916  14 LSRTE---IPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEF 90


                ...
gi 52782796 237 EAV 239
Cdd:cd13916  91 TVV 93
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 115-239 8.43e-07

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: 46.00  E-value: 8.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52782796 115 MTIKAIGLQWYWKYEYSDF----INEsgetvefesyvipedlledgqlrlldtdtsVVVPVDTHIRFVVTAADVIHDFAI 190
Cdd:cd04212   1 LEIQVVSLDWKWLFIYPEQgiatVNE------------------------------LVIPVGRPVNFRLTSDSVMNSFFI 50

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 52782796 191 PSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAMPIKIEAV 239
Cdd:cd04212  51 PQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 174-232 7.99e-03

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 34.90  E-value: 7.99e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52782796 174 HIRFVVT----AADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGQCSELCGTAHSAM 232
Cdd:cd04223  25 EVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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