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Conserved domains on  [gi|63025142|ref|YP_232807|]
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cytochrome c oxidase subunit II (mitochondrion) [Tethya actinia]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475883)

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 MTH00051
cytochrome c oxidase subunit II; Provisional
 10-243 2.58e-163

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 450.77  E-value: 2.58e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   10 KDVPEPWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAF 89
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   90 PSLKLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTG 169
Cdd:MTH00051  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63025142  170 ADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTESI 243
Cdd:MTH00051 161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 10-243 2.58e-163

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 450.77  E-value: 2.58e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   10 KDVPEPWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAF 89
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   90 PSLKLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTG 169
Cdd:MTH00051  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63025142  170 ADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTESI 243
Cdd:MTH00051 161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 104-235 2.60e-95

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: 274.83  E-value: 2.60e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 104 PALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSFALPSLSV 183
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 63025142 184 KIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNW 235
Cdd:cd13912  79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
106-227 3.20e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.15  E-value: 3.20e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   106 LTIKVVGHQWYWSYEYSDYGaeTIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKI 185
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG--DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 63025142   186 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 227
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
16-242 5.12e-63

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 196.59  E-value: 5.12e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  16 WQLGFQDAASPVMEEVIFFHDQIMFILIIIISIV----LWFIVRslmtkyYHK--------YLFEGTLIEIIWTLIPAGV 83
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfgllLYFAIR------YRRrkgdadpaQFHHNTKLEIVWTVIPIII 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  84 LVFIAFPSLKLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevDNRLVVPIQTQV 163
Cdd:COG1622  91 VIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPV 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63025142 164 RVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTES 242
Cdd:COG1622 148 RFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKAS 226
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 64-237 4.06e-46

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: 152.15  E-value: 4.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142    64 KYLFEGTLIEIIWTLIPAG-VLVFIAFPSLKLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYGAETiefdsymvptsdln 142
Cdd:TIGR02866  48 SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT-------------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   143 ngdlrllevDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPI 222
Cdd:TIGR02866 114 ---------VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLF 184

                         170
                  ....*....|....*
gi 63025142   223 VIEAVSLEKFVNWVA 237
Cdd:TIGR02866 185 KVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 10-243 2.58e-163

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 450.77  E-value: 2.58e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   10 KDVPEPWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAF 89
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   90 PSLKLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTG 169
Cdd:MTH00051  81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63025142  170 ADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTESI 243
Cdd:MTH00051 161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEEI 234
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-242 6.22e-149

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 414.53  E-value: 6.22e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142    7 ICFKDVPEPWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVF 86
Cdd:MTH00023   5 FFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   87 IAFPSLKLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVL 166
Cdd:MTH00023  85 IALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRIL 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025142  167 VTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTES 242
Cdd:MTH00023 165 VTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSND 240
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 17-236 1.22e-133

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 375.32  E-value: 1.22e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   17 QLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLKLLY 96
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   97 LMDEVIDPALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSF 176
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDF--KNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  177 ALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWV 236
Cdd:MTH00154 164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 13-240 7.87e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 365.78  E-value: 7.87e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   13 PEPWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSL 92
Cdd:MTH00117   2 ANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   93 KLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADV 172
Cdd:MTH00117  82 RILYLMDEINNPHLTIKAIGHQWYWSYEYTDY--KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63025142  173 LHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQT 240
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 17-236 5.80e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 343.46  E-value: 5.80e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   17 QLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLKLLY 96
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   97 LMDEVIDPALTIKVVGHQWYWSYEYSDYGaeTIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSF 176
Cdd:MTH00140  86 LLDETNNPLLTVKAIGHQWYWSYEYSDFS--VIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  177 ALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWV 236
Cdd:MTH00140 164 TVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 17-238 1.18e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 340.03  E-value: 1.18e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   17 QLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLKLLY 96
Cdd:MTH00168   6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   97 LMDEVIDPALTIKVVGHQWYWSYEYSDYGaeTIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSF 176
Cdd:MTH00168  86 LMDEIDKPDLTIKAVGHQWYWSYEYTDYN--DLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63025142  177 ALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVAT 238
Cdd:MTH00168 164 TLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 15-242 1.16e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 337.83  E-value: 1.16e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   15 PWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLKL 94
Cdd:MTH00038   4 WLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   95 LYLMDEVIDPALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLH 174
Cdd:MTH00038  84 LYLMDEVNNPFLTIKAIGHQWYWSYEYTDY--NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63025142  175 SFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTES 242
Cdd:MTH00038 162 SWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 15-242 1.28e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 332.45  E-value: 1.28e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   15 PWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLKL 94
Cdd:MTH00129   4 PSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   95 LYLMDEVIDPALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLH 174
Cdd:MTH00129  84 LYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63025142  175 SFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTES 242
Cdd:MTH00129 162 SWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 17-236 1.29e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 329.76  E-value: 1.29e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   17 QLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLKLLY 96
Cdd:MTH00139   6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   97 LMDEVIDPALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSF 176
Cdd:MTH00139  86 LMDEVSDPYLTFKAVGHQWYWSYEYSDF--KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  177 ALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWV 236
Cdd:MTH00139 164 TVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 13-238 6.93e-113

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 323.21  E-value: 6.93e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   13 PEPWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSL 92
Cdd:MTH00098   2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   93 KLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADV 172
Cdd:MTH00098  82 RILYMMDEINNPSLTVKTMGHQWYWSYEYTDY--EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025142  173 LHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVAT 238
Cdd:MTH00098 160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSAS 225
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 14-242 4.33e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 316.06  E-value: 4.33e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   14 EPWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLK 93
Cdd:MTH00185   3 HPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   94 LLYLMDEVIDPALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVL 173
Cdd:MTH00185  83 ILYLMDEINDPHLTIKAMGHQWYWSYEYTDY--EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63025142  174 HSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTES 242
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 10-239 1.67e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 315.81  E-value: 1.67e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   10 KDVPEPWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLF---EGTLIEIIWTLIPAGVLVF 86
Cdd:MTH00027  27 KDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYWnklDGSLIEVIWTLIPAFILIL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   87 IAFPSLKLLYLMDE-VIDPALTIKVVGHQWYWSYEYSDYGAETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRV 165
Cdd:MTH00027 107 IAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRV 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63025142  166 LVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQ 239
Cdd:MTH00027 187 LITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRE 260
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 15-241 1.10e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 312.48  E-value: 1.10e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   15 PWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLKL 94
Cdd:MTH00076   4 PSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   95 LYLMDEVIDPALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLH 174
Cdd:MTH00076  84 LYLMDEINDPHLTVKAIGHQWYWSYEYTDY--EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLH 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63025142  175 SFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTE 241
Cdd:MTH00076 162 SWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 17-241 3.43e-108

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 311.02  E-value: 3.43e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   17 QLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLKLLY 96
Cdd:MTH00008   6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   97 LMDEVIDPALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSF 176
Cdd:MTH00008  86 LMDEVSNPSITLKTIGHQWYWSYEYSDF--SNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 63025142  177 ALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTE 241
Cdd:MTH00008 164 TVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 104-235 2.60e-95

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: 274.83  E-value: 2.60e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 104 PALTIKVVGHQWYWSYEYSDYgaETIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSFALPSLSV 183
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 63025142 184 KIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNW 235
Cdd:cd13912  79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
106-227 3.20e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 236.15  E-value: 3.20e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   106 LTIKVVGHQWYWSYEYSDYGaeTIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKI 185
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG--DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 63025142   186 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 227
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 49-235 8.46e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 226.43  E-value: 8.46e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   49 VLWFIVRSLMTKYYHKYLFEGTLIEIIWTLIPAGVLVFIAFPSLKLLYLMDEV-IDPALTIKVVGHQWYWSYEYSDYGAe 127
Cdd:MTH00080  40 VFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTGHQWYWSYEFSDIPG- 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  128 tIEFDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYG 207
Cdd:MTH00080 119 -LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYG 197

                        170       180
                 ....*....|....*....|....*...
gi 63025142  208 QCSEICGANHSFMPIVIEAVSLEKFVNW 235
Cdd:MTH00080 198 QCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
16-242 5.12e-63

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 196.59  E-value: 5.12e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  16 WQLGFQDAASPVMEEVIFFHDQIMFILIIIISIV----LWFIVRslmtkyYHK--------YLFEGTLIEIIWTLIPAGV 83
Cdd:COG1622  17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfgllLYFAIR------YRRrkgdadpaQFHHNTKLEIVWTVIPIII 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  84 LVFIAFPSLKLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevDNRLVVPIQTQV 163
Cdd:COG1622  91 VIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT-----------------------VNELVLPVGRPV 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63025142 164 RVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWVATQTES 242
Cdd:COG1622 148 RFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKAS 226
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 68-227 1.34e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 160.89  E-value: 1.34e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   68 EGTLIEIIWTLIPAGVLVFIAFpsLKLLYLM-DEVIDPALTIKVVGHQWYWSYEYSDYGaetiEFDSYMvptSDLNNGdl 146
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLCF--LNLNFITsDLDCFSSETIKVIGHQWYWSYEYSFGG----SYDSFM---TDDIFG-- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  147 rlleVDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEA 226
Cdd:MTH00047 114 ----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEV 189


                 .
gi 63025142  227 V 227
Cdd:MTH00047 190 V 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 64-237 4.06e-46

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: 152.15  E-value: 4.06e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142    64 KYLFEGTLIEIIWTLIPAG-VLVFIAFPSLKLLYLMDEVIDPALTIKVVGHQWYWSYEYSDYGAETiefdsymvptsdln 142
Cdd:TIGR02866  48 SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT-------------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   143 ngdlrllevDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPI 222
Cdd:TIGR02866 114 ---------VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLF 184

                         170
                  ....*....|....*
gi 63025142   223 VIEAVSLEKFVNWVA 237
Cdd:TIGR02866 185 KVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 131-232 9.04e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 150.36  E-value: 9.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  131 FDSYMVPTSDLNNGDLRLLEVDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCS 210
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 63025142  211 EICGANHSFMPIVIEAVSLEKF 232
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 105-220 2.29e-30

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: 108.48  E-value: 2.29e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 105 ALTIKVVGHQWYWSYEYSDYGAETIEfdsymvpTSdlnngdlrllevdNRLVVPIQTQVRVLVTGADVLHSFALPSLSVK 184
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPDEPGRGIV-------TA-------------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGK 60

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 63025142 185 IDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 220
Cdd:cd04213  61 MDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 106-225 2.35e-29

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: 105.84  E-value: 2.35e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 106 LTIKVVGHQWYWSYEYSDygaetiefdsymvptsdlnngdlrlLEVDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKI 185
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKV 55

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 63025142 186 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIE 225
Cdd:cd13842  56 DAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-236 9.61e-26

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: 97.91  E-value: 9.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  83 VLVFIAFPSLKLLYLMD---EVIDPALTIKVVGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevdNRLVVPI 159
Cdd:cd13918   7 VISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG------------------------NTLRVPA 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 63025142 160 QTQVRVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWV 236
Cdd:cd13918  63 DTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 105-220 1.27e-24

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: 93.46  E-value: 1.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 105 ALTIKVVGHQWYWSYEYSdygaetiefdsymvptsdlnNGDlrllEVDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVK 184
Cdd:cd13915   1 ALEIQVTGRQWMWEFTYP--------------------NGK----REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 63025142 185 IDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 220
Cdd:cd13915  57 QDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 12-94 2.53e-24

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: 92.78  E-value: 2.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142    12 VPEPWQLGFQDAASPVMEEVIFFHDQIMFILIIIISIVLWFIVRSLMTKYY------HKYLFEGTLIEIIWTLIPAGVLV 85
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 63025142    86 FIAFPSLKL 94
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 105-220 3.27e-24

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: 92.70  E-value: 3.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 105 ALTIKVVGHQWYWSYEYSDYGAETIEFDSYMVPTsdlnngdlrllevdnrLVVPIQTQVRVLVTGADVLHSFALPSLSVK 184
Cdd:cd13919   1 ALVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPE----------------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVK 64

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 63025142 185 IDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 220
Cdd:cd13919  65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 107-236 9.60e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 81.30  E-value: 9.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 107 TIKVVGHQWYWSYEYSDYGAETiefdsymvptsdlnngdlrllevDNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKID 186
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEANVTT-----------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 63025142 187 AVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLEKFVNWV 236
Cdd:cd13914  59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 153-220 1.81e-10

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: 56.04  E-value: 1.81e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63025142 153 NRLVVPIQTQVRVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 220
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 106-227 2.67e-09

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: 52.94  E-value: 2.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 106 LTIKVVGHQWYWSYEYSDYGAETIefdsymvptsdlnngdlrllevdNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKI 185
Cdd:cd04212   1 LEIQVVSLDWKWLFIYPEQGIATV-----------------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQI 57

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 63025142 186 DAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEAV 227
Cdd:cd04212  58 YAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 107-220 2.32e-06

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: 44.68  E-value: 2.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 107 TIKVVGHQWYWSYEYSDYGA-ETIEFDsymvptsdlnngdlrllevdnrlvvpiqtqvrvlVTGADVLHSFALPS----L 181
Cdd:cd13916   2 VVAVTGHQWYWELSRTEIPAgKPVEFR----------------------------------VTSADVNHGFGIYDpdmrL 47

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 63025142 182 SVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 220
Cdd:cd13916  48 LAQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 108-225 4.04e-05

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 41.83  E-value: 4.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142 108 IKVVGHQWYWSYEYsdygaetiefdsymvptsdlnngDLRLLEVDNRLVVPIQTQVRV-LVTGADVLHSFALPSLSVKID 186
Cdd:cd00920   1 ITVTASDWGWSFTY-----------------------NGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVV 57

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 63025142 187 A---------------VPGRLNQTSFFIKRPGVFYGQCSEICGaNHSFMPIVIE 225
Cdd:cd00920  58 AmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 74-242 4.50e-04

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 40.55  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142   74 IIWTlIPAGVLVFIAFPSLKLLYLMDE----VID-PALTIKVVGHQWYWSYEYSDYGAETIefdsymvptsdlnngdlrl 148
Cdd:PRK10525  91 VVWT-VPILIIIFLAVLTWKTTHALEPskplAHDeKPITIEVVSMDWKWFFIYPEQGIATV------------------- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025142  149 levdNRLVVPIQTQVRVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPI-VIEAV 227
Cdd:PRK10525 151 ----NEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFkAIATP 226

                        170
                 ....*....|....*
gi 63025142  228 SLEKFVNWVATQTES 242
Cdd:PRK10525 227 DRAEFDQWVAKAKQS 241
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 171-220 3.09e-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: 36.06  E-value: 3.09e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 63025142 171 DVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 220
Cdd:cd04223  38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 155-220 3.59e-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: 35.81  E-value: 3.59e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025142 155 LVVPIQTQVRVLVTGADVLHSFALPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFM 220
Cdd:cd13917  16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
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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