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Conserved domains on  [gi|386800936|ref|YP_006303585|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Aspergillus nidulans FGSC A4]

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
 18-247 1.49e-108

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 312.53  E-value: 1.49e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  18 WG-IFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNfvaKKSpiaHKYMNHGTLIELIWTITPAFILILIA 96
Cdd:MTH00154   4 WSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFN---KFT---NRFLLEGQEIEIIWTILPAIILIFIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  97 FPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRF 176
Cdd:MTH00154  78 LPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386800936 177 VISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:MTH00154 153 LITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 18-247 1.49e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 312.53  E-value: 1.49e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  18 WG-IFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNfvaKKSpiaHKYMNHGTLIELIWTITPAFILILIA 96
Cdd:MTH00154   4 WSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFN---KFT---NRFLLEGQEIEIIWTILPAIILIFIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  97 FPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRF 176
Cdd:MTH00154  78 LPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386800936 177 VISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:MTH00154 153 LITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
114-238 2.41e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.92  E-value: 2.41e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  114 LVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRFVISAADVIHSYACPSLG 193
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 386800936  194 IKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSV 238
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 112-246 6.15e-80

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: 236.31  E-value: 6.15e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 112 PSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRFVISAADVIHSYACPS 191
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386800936 192 LGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLW 246
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-250 1.42e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 180.41  E-value: 1.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  10 ILMDAPTPWGIFFQDSASPQMEGIEELHNnIMFYLAIILFTVTW-MMITIIRNFVAKKSPIAHKYMNHGTLIELIWTITP 88
Cdd:COG1622    9 LLLALLLSGQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLVFgLLLYFAIRYRRRKGDADPAQFHHNTKLEIVWTVIP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  89 AFILILIAFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDftnednefiefdsyivpesdleEGQfrmlEVDNRVII 168
Cdd:COG1622   88 IIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD----------------------QGI----ATVNELVL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 169 PELTHTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWLR 248
Cdd:COG1622  142 PVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLA 221


                 ..
gi 386800936 249 EQ 250
Cdd:COG1622  222 EQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 26-247 1.31e-38

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: 133.27  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936   26 ASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNFVAKKSPIAHKYMNHGTLIELIWTITPAFILI-LIAFPSFKLLY 104
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  105 LMDEVMDPSLVVYAEGHQWYWSYQYPDFTnednefiefdsyivpesdleegqfrmLEVDNRVIIPELTHTRFVISAADVI 184
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPESG--------------------------FTTVNELVLPAGTPVELQVTSKDVI 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386800936  185 HSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:TIGR02866 136 HSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 18-247 1.49e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 312.53  E-value: 1.49e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  18 WG-IFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNfvaKKSpiaHKYMNHGTLIELIWTITPAFILILIA 96
Cdd:MTH00154   4 WSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFN---KFT---NRFLLEGQEIEIIWTILPAIILIFIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  97 FPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRF 176
Cdd:MTH00154  78 LPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386800936 177 VISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:MTH00154 153 LITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 13-247 5.11e-104

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 301.67  E-value: 5.11e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  13 DAPTPWGIFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNfvakKSpiAHKYMNHGTLIELIWTITPAFIL 92
Cdd:MTH00023   9 DIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNG----KF--YDRFLVDGTFLEIVWTIIPAVIL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  93 ILIAFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNEDnefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELT 172
Cdd:MTH00023  83 VFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGET---LEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINT 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386800936 173 HTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:MTH00023 160 HVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 12-252 1.16e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 292.84  E-value: 1.16e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  12 MDAPTPWGIFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMmitIIRNFVAKKSpiaHKYMNHGTLIELIWTITPAFI 91
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWL---IIRALTTKYY---HKYLFEGTLIEIIWTLIPAAI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  92 LILIAFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFtneDNEFIEFDSYIVPESDLEEGQFRMLEVDNRVIIPEL 171
Cdd:MTH00051  75 LIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDY---GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 172 THTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWLREQM 251
Cdd:MTH00051 152 TQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231


                 .
gi 386800936 252 E 252
Cdd:MTH00051 232 E 232
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 18-247 1.41e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 282.21  E-value: 1.41e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  18 WG-IFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNfvakksPIAHKYMNHGTLIELIWTITPAFILILIA 96
Cdd:MTH00140   4 WGqLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFN------KFSCRTILEAQKLETIWTIVPALILVFLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  97 FPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRF 176
Cdd:MTH00140  78 LPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386800936 177 VISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:MTH00140 153 LVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 16-247 9.78e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 272.24  E-value: 9.78e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  16 TPWGIFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMitiirnFVAKKSPIAHKYMNHGTLIELIWTITPAFILILI 95
Cdd:MTH00168   3 TYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSL------LVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  96 AFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTR 175
Cdd:MTH00168  77 ALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386800936 176 FVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:MTH00168 152 VLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 18-249 1.89e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 271.59  E-value: 1.89e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  18 WGIF-FQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNFVAKKSPIAhkymnhGTLIELIWTITPAFILILIA 96
Cdd:MTH00139   4 WGQLgFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLE------SQEVETIWTVLPAFILLFLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  97 FPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRF 176
Cdd:MTH00139  78 LPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386800936 177 VISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWLRE 249
Cdd:MTH00139 153 LITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 22-247 1.28e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 266.78  E-value: 1.28e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  22 FQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIrnfvakKSPIAHKYMNHGTLIELIWTITPAFILILIAFPSFK 101
Cdd:MTH00117   9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLML------TTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 102 LLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRFVISAA 181
Cdd:MTH00117  83 ILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD-----LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAE 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386800936 182 DVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:MTH00117 158 DVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWS 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 16-252 6.96e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 255.01  E-value: 6.96e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  16 TPWGIFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNfvakkSPiAHKYMNHGTLIELIWTITPAFILILI 95
Cdd:MTH00038   3 TWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFS-----SP-TNRFFLEGQELETIWTIVPAFILIFI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  96 AFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTR 175
Cdd:MTH00038  77 ALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYND-----LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIR 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386800936 176 FVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWLREQME 252
Cdd:MTH00038 152 VLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 18-247 1.84e-84

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 251.31  E-value: 1.84e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  18 WG-IFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNfvakksPIAHKYMNHGTLIELIWTITPAFILILIA 96
Cdd:MTH00008   4 WGqLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFN------KLSNRYILEAQQIETIWTILPALILLFLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  97 FPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRF 176
Cdd:MTH00008  78 FPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386800936 177 VISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:MTH00008 153 LVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 12-252 2.82e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 248.54  E-value: 2.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  12 MDAPTPWGifFQDSASPQMEGIEELHNNIMFYLAII----LFTVTWMMITiirnfvakkspiahKYMNHGTL----IELI 83
Cdd:MTH00076   1 MAHPSQLG--FQDAASPIMEELLHFHDHALMAVFLIstlvLYIITIMMTT--------------KLTNTNTMdaqeIEMV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  84 WTITPAFILILIAFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVD 163
Cdd:MTH00076  65 WTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-----LSFDSYMIPTQDLTPGQFRLLEVD 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 164 NRVIIPELTHTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDF 243
Cdd:MTH00076 140 NRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNF 219


                 ....*....
gi 386800936 244 LLWLREQME 252
Cdd:MTH00076 220 LNWSSSMLE 228
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 12-246 1.97e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 243.85  E-value: 1.97e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  12 MDAPTPWGifFQDSASPQMEGIEELHNNIMfylaIILFTVTWMMITIIRNFVAKKspIAHKYMNHGTLIELIWTITPAFI 91
Cdd:MTH00129   1 MAHPSQLG--FQDAASPVMEELLHFHDHAL----MIVFLISTLVLYIIVAMVSTK--LTNKYILDSQEIEIIWTVLPAVI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  92 LILIAFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPEL 171
Cdd:MTH00129  73 LILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED-----LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVE 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386800936 172 THTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLW 246
Cdd:MTH00129 148 SPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 15-246 1.58e-80

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 241.55  E-value: 1.58e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  15 PTPWGIFFQDSASPQMEGIEELHNNIMfylaIILFTVTWMMITIIRNFVAKKspIAHKYMNHGTLIELIWTITPAFILIL 94
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHDHTL----MIVFLISSLVLYIISLMLTTK--LTHTSTMDAQEVETIWTILPAIILIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  95 IAFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFtnednEFIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHT 174
Cdd:MTH00098  76 IALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386800936 175 RFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLW 246
Cdd:MTH00098 151 RMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
114-238 2.41e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.92  E-value: 2.41e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  114 LVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRFVISAADVIHSYACPSLG 193
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 386800936  194 IKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSV 238
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 112-246 6.15e-80

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: 236.31  E-value: 6.15e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 112 PSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRFVISAADVIHSYACPS 191
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386800936 192 LGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLW 246
Cdd:cd13912   76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 10-247 1.52e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 235.30  E-value: 1.52e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  10 ILMDAPTPWGIFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNfvakkSPIAHKYMNH--GTLIELIWTIT 87
Cdd:MTH00027  25 MIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLG-----NNYYSYYWNKldGSLIEVIWTLI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  88 PAFILILIAFPSFKLLYLMDE-VMDPSLVVYAEGHQWYWSYQYPDFTNEDnefIEFDSYIVPESDLEEGQFRMLEVDNRV 166
Cdd:MTH00027 100 PAFILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKN---IEFDSYMIPTADLEFGDLRLLEVDNRL 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 167 IIPELTHTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLW 246
Cdd:MTH00027 177 ILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256


                 .
gi 386800936 247 L 247
Cdd:MTH00027 257 I 257
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 22-252 2.26e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 230.93  E-value: 2.26e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  22 FQDSASPQMEGIEELHNNIMfylaIILFTVTWMMITIIRNFVAKKspIAHKYMNHGTLIELIWTITPAFILILIAFPSFK 101
Cdd:MTH00185   9 LQDAASPVMEELIHFHDHTL----MIVFLISTLVLYIIVAMVTTK--LTNKYILDSQEIEIVWTILPAIILIMIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 102 LLYLMDEVMDPSLVVYAEGHQWYWSYQYPDFtnednEFIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRFVISAA 181
Cdd:MTH00185  83 ILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAE 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386800936 182 DVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWLREQME 252
Cdd:MTH00185 158 DVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 18-247 3.90e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 194.84  E-value: 3.90e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  18 WGIFFQDSASPQ-MEGIEELHNNIMFYLAIILFTVTWMMITIIRNFVAKKSpiahkyMNHGTLIELIWTITPAFILILIA 96
Cdd:MTH00080   6 YNLNFSNSLFSSyMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSK------KIEYQFGELLCSVFPVLILLMQM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  97 FPSFKLLYLMdEVM--DPSLVVYAEGHQWYWSYQYPDFTNednefIEFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHT 174
Cdd:MTH00080  80 VPSLSLLYYY-GLMnlDSNLTVKVTGHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNI 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386800936 175 RFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:MTH00080 154 RFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
10-250 1.42e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 180.41  E-value: 1.42e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  10 ILMDAPTPWGIFFQDSASPQMEGIEELHNnIMFYLAIILFTVTW-MMITIIRNFVAKKSPIAHKYMNHGTLIELIWTITP 88
Cdd:COG1622    9 LLLALLLSGQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLVFgLLLYFAIRYRRRKGDADPAQFHHNTKLEIVWTVIP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  89 AFILILIAFPSFKLLYLMDEVMDPSLVVYAEGHQWYWSYQYPDftnednefiefdsyivpesdleEGQfrmlEVDNRVII 168
Cdd:COG1622   88 IIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD----------------------QGI----ATVNELVL 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 169 PELTHTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWLR 248
Cdd:COG1622  142 PVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLA 221


                 ..
gi 386800936 249 EQ 250
Cdd:COG1622  222 EQ 223
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 14-102 8.28e-41

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: 135.54  E-value: 8.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936   14 APTPWGIFFQDSASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNFVAKKSPIAHKYMNHGTLIELIWTITPAFILI 93
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 386800936   94 LIAFPSFKL 102
Cdd:pfam02790  81 LIALPSFKL 89
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 127-239 2.34e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 136.87  E-value: 2.34e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 127 YQYPDFTNEDNEFI----EFDSYIVPESDLEEGQFRMLEVDNRVIIPELTHTRFVISAADVIHSYACPSLGIKADAYPGR 202
Cdd:PTZ00047  32 YPIPQKYLEDPDLIpkyySFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGR 111

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 386800936 203 LNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVS 239
Cdd:PTZ00047 112 LHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVS 148
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 26-247 1.31e-38

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: 133.27  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936   26 ASPQMEGIEELHNNIMFYLAIILFTVTWMMITIIRNFVAKKSPIAHKYMNHGTLIELIWTITPAFILI-LIAFPSFKLLY 104
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  105 LMDEVMDPSLVVYAEGHQWYWSYQYPDFTnednefiefdsyivpesdleegqfrmLEVDNRVIIPELTHTRFVISAADVI 184
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPESG--------------------------FTTVNELVLPAGTPVELQVTSKDVI 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386800936  185 HSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:TIGR02866 136 HSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 36-238 1.07e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 120.44  E-value: 1.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  36 LHNNIMFY-LAIILFTVTWMMITIIRNFVAKKSPIAHkyMNHGTLIELIWTITPAFI-LILIAFP-SFKLLYLMDEVMDP 112
Cdd:MTH00047   6 LYYDIVCYiLALCVFIPCWVYIMLCWQVVSGNGSVNF--GSENQVLELLWTVVPTLLvLVLCFLNlNFITSDLDCFSSET 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 113 SLVVyaeGHQWYWSYQYPDFtnednefIEFDSYIVPESDLeegqfrmleVDNRVIIPELTHTRFVISAADVIHSYACPSL 192
Cdd:MTH00047  84 IKVI---GHQWYWSYEYSFG-------GSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDL 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 386800936 193 GIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSV 238
Cdd:MTH00047 145 NLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 114-232 4.40e-23

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: 89.66  E-value: 4.40e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 114 LVVYAEGHQWYWSYQYPDftnednefiefdsyivpesdleegqfrmLEVDNRVIIPELTHTRFVISAADVIHSYACPSLG 193
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 386800936 194 IKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMP 232
Cdd:cd13842   53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 113-231 4.82e-20

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: 81.90  E-value: 4.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 113 SLVVYAEGHQWYWSYQYPDftnednefiefdsyivpesdleeGQFRMLEVDNRVIIPELTHTRFVISAADVIHSYACPSL 192
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPD-----------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 386800936 193 GIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSM 231
Cdd:cd04213   58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 113-231 6.95e-19

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: 78.82  E-value: 6.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 113 SLVVYAEGHQWYWSYQYPDFTNEDNEfiefdsyivpesdleegqfrmlevdnrVIIPELTHTRFVISAADVIHSYACPSL 192
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGKREINE---------------------------LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 386800936 193 GIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSM 231
Cdd:cd13915   54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-231 8.59e-19

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: 78.84  E-value: 8.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 114 LVVYAEGHQWYWSYQYPDftnEDNEFIEFDSYIVPEsdLEegqfrmLEVDNRViipelthtRFVISAADVIHSYACPSLG 193
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPG---GDGKLGTDDDVTSPE--LH------LPVGRPV--------LFNLRSKDVIHSFWVPEFR 62

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 386800936 194 IKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSM 231
Cdd:cd13919   63 VKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-247 1.01e-17

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: 76.29  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 115 VVYAEGHQWYWSYQYPDFTNEDNefiefdsyivpesdleegqfrmlevdNRVIIPELTHTRFVISAADVIHSYACPSLGI 194
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTS--------------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 386800936 195 KADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFLLWL 247
Cdd:cd13914   56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 89-247 3.13e-16

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 73.26  E-value: 3.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936  89 AFILI-LIAFPSFKLLYLMD---EVMDPSLVVYAEGHQWYWSYQYPDFTNEDNEfiefdsyivpesdleegqfrmlevdn 164
Cdd:cd13918    4 AIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTGNT-------------------------- 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 165 rVIIPELTHTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSMPIAIQSVSIKDFL 244
Cdd:cd13918   58 -LRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFE 136


                 ...
gi 386800936 245 LWL 247
Cdd:cd13918  137 AWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 164-231 7.53e-08

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: 49.11  E-value: 7.53e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386800936 164 NRVIIPELTHTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSM 231
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-231 1.09e-03

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: 37.36  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386800936 115 VVYAEGHQWYWsyqypdftnednefiEFDSYIVPESDLEEgqfrmlevdnrviipelthtrFVISAADVIHSYAC--PSL 192
Cdd:cd13916    2 VVAVTGHQWYW---------------ELSRTEIPAGKPVE---------------------FRVTSADVNHGFGIydPDM 45

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 386800936 193 GIKAD--AYPGRLNQASVYINRPGTFFGQCSEICGILHSSM 231
Cdd:cd13916   46 RLLAQtqAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 175-231 2.33e-03

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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 36.20  E-value: 2.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 386800936 175 RFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSM 231
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 164-231 8.21e-03

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: 34.83  E-value: 8.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386800936 164 NRVIIPELTHTRFVISAADVIHSYACPSLGIKADAYPGRLNQASVYINRPGTFFGQCSEICGILHSSM 231
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
 
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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