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Conserved domains on  [gi|821317068|ref|YP_009138161|]
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cytochrome c oxidase subunit II (mitochondrion) [Sterechinus neumayeri]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475878)

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 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 4.70e-177

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 484.59  E-value: 4.70e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYLEE 229
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
 
Name Accession Description Interval E-value
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 4.70e-177

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 484.59  E-value: 4.70e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYLEE 229
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 6.64e-96

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: 275.60  E-value: 6.64e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  93 PFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKM 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 821317068 173 DAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 7.85e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 250.02  E-value: 7.85e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   95 LTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 821317068  175 VPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-225 8.57e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 190.42  E-value: 8.57e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFyglvSLLI-------SSNTN---RFFLEGQELETIWTVVPA 70
Cdd:COG1622   13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVF----GLLLyfairyrRRKGDadpAQFHHNTKLEIVWTVIPI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  71 FILIFIALPSLQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLefdsymvptsdvsfgnprlleVDNRLILPMQNPI 150
Cdd:COG1622   89 IIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPV 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821317068 151 RVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQ 225
Cdd:COG1622  148 RFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-224 4.14e-43

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: 144.06  E-value: 4.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   12 ASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLI-----SSNTN-RFFLEGQELETIWTVVPAFILI-FIALPSLQLL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkGDEEKpSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   85 YLMDEVNDPFLTIKAIGHQWYWSYEYTDYndlefdsymvptsdvsfgnprLLEVDNRLILPMQNPIRVLVSSADVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  165 VPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVA 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 4.70e-177

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 484.59  E-value: 4.70e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYLEE 229
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 2.56e-156

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 432.33  E-value: 2.56e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYL 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-222 1.62e-146

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 407.38  E-value: 1.62e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENW 222
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENW 222
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 1.14e-140

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 392.42  E-value: 1.14e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQ 225
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-223 2.45e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 376.59  E-value: 2.45e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWV 223
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-229 9.35e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 375.21  E-value: 9.35e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYLEE 229
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-222 1.14e-131

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 369.82  E-value: 1.14e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENW 222
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 1.51e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 369.43  E-value: 1.51e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQY 226
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-229 1.86e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 356.89  E-value: 1.86e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYLEE 229
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 1.49e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 349.46  E-value: 1.49e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYLE 228
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-228 2.96e-120

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 341.07  E-value: 2.96e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 821317068 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYLE 228
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-223 1.54e-114

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 327.09  E-value: 1.54e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   6 QFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPSLQLLY 85
Cdd:MTH00023  15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  86 LMDEVNDPFLTIKAIGHQWYWSYEYTDYND--LEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVLHSW 163
Cdd:MTH00023  95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068 164 AVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWV 223
Cdd:MTH00023 175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-229 1.83e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 324.04  E-value: 1.83e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   6 QFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFFLEGQELETIWTVVPAFILIFIALPSLQLLY 85
Cdd:MTH00051   8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  86 LMDEVNDPFLTIKAIGHQWYWSYEYTDY--NDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVLHSW 163
Cdd:MTH00051  88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 821317068 164 AVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYLEE 229
Cdd:MTH00051 168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 6.64e-96

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: 275.60  E-value: 6.64e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  93 PFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKM 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 821317068 173 DAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-225 5.01e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 265.74  E-value: 5.01e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   6 QFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLISSNTNRFF---LEGQELETIWTVVPAFILIFIALPSLQ 82
Cdd:MTH00027  34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  83 LLYLMDE-VNDPFLTIKAIGHQWYWSYEYTDYND--LEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADV 159
Cdd:MTH00027 114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEknIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 821317068 160 LHSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQ 225
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 7.85e-86

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 250.02  E-value: 7.85e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   95 LTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 821317068  175 VPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 20-228 9.08e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 231.05  E-value: 9.08e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  20 LTYFHDYALIVLTLITILVFYGLVSLLISSNTNRF---FLEGQELETIWTVVPAFILIFIALPSLQLLYLMDEVN-DPFL 95
Cdd:MTH00080  19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFkskKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  96 TIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDAV 175
Cdd:MTH00080  99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 821317068 176 PGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQYLE 228
Cdd:MTH00080 179 SGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-225 8.57e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 190.42  E-value: 8.57e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFyglvSLLI-------SSNTN---RFFLEGQELETIWTVVPA 70
Cdd:COG1622   13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVF----GLLLyfairyrRRKGDadpAQFHHNTKLEIVWTVIPI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  71 FILIFIALPSLQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLefdsymvptsdvsfgnprlleVDNRLILPMQNPI 150
Cdd:COG1622   89 IIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPV 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821317068 151 RVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVAQ 225
Cdd:COG1622  148 RFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 26-218 3.23e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 167.05  E-value: 3.23e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  26 YALIVLTLITILVFYGLVSLLISSNTNRFFL-EGQELETIWTVVPAFILIFiaLPSLQLLYLM-DEVNDPFLTIKAIGHQ 103
Cdd:MTH00047  13 YILALCVFIPCWVYIMLCWQVVSGNGSVNFGsENQVLELLWTVVPTLLVLV--LCFLNLNFITsDLDCFSSETIKVIGHQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068 104 WYWSYEYTDynDLEFDSYMvptSDVSFGnprlleVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTT 183
Cdd:MTH00047  91 WYWSYEYSF--GGSYDSFM---TDDIFG------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLF 159

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 821317068 184 FFAARAGLFYGQCSEICGANHSFMPIVVESVPFNN 218
Cdd:MTH00047 160 FCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVDS 194
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-224 4.14e-43

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: 144.06  E-value: 4.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   12 ASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLI-----SSNTN-RFFLEGQELETIWTVVPAFILI-FIALPSLQLL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkGDEEKpSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068   85 YLMDEVNDPFLTIKAIGHQWYWSYEYTDYndlefdsymvptsdvsfgnprLLEVDNRLILPMQNPIRVLVSSADVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  165 VPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWVA 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-214 2.73e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.41  E-value: 2.73e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068 118 FDSYMVPTSDVSFGNPRLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 821317068 198 EICGANHSFMPIVVESV 214
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 2.69e-32

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: 112.81  E-value: 2.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068    1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLVSLLI------SSNTNRFFLEGQELETIWTVVPAFILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 821317068   75 FIALPSLQL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 2.08e-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: 2.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  95 LTIKAIGHQWYWSYEYTDYNdlefdsymvptsdvsfgnPRLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEP------------------GRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 821317068 175 VPGRLNQTTFFAARAGLFYGQCSEICGANHSFM 207
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 4.16e-30

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: 107.38  E-value: 4.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  95 LTIKAIGHQWYWSYEYTDyndlefdsymvptsdvsfgnprlLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 821317068 175 VPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVE 212
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-212 3.58e-25

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 95.01  E-value: 3.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  95 LTIKAIGHQWYWSYEYtdyndlefdsymvPTSDVSFGNPRLLEVdNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 821317068 175 VPGRLNQTTFFAARAGLFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13919   68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-211 1.42e-23

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 90.38  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  95 LTIKAIGHQWYWSYEYtdyndlefdsymvptsdvsfgnPRLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTY----------------------PNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 821317068 175 VPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVV 211
Cdd:cd13915   60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-223 6.76e-23

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 90.21  E-value: 6.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  68 VPAFILI-FIALPSLQLLYLMD---EVNDPFLTIKAIGHQWYWSYEYtdyndlefdsymvptsdvsfgnPRLLEVDNRLI 143
Cdd:cd13918    2 LSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY----------------------PNGVTTGNTLR 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068 144 LPMQNPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWV 223
Cdd:cd13918   60 VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-223 3.68e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 79.37  E-value: 3.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  96 TIKAIGHQWYWSYEYTDYNdlefdsymVPTSdvsfgnprllevdNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDAV 175
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEAN--------VTTS-------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 821317068 176 PGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESVPFNNFENWV 223
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 148-212 3.29e-07

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: 47.18  E-value: 3.29e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 821317068 148 NPIRV--------LVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13913   25 NEIEVpagatvtfYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 95-214 1.34e-05

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: 42.54  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068  95 LTIKAIGHQWYWSYEYTDYNdlefdsymvptsdvsfgnprlLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQG---------------------IATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 821317068 175 VPGRLNQTTFFAARAGLFYGQCSEICGANHSFMPIVVESV 214
Cdd:cd04212   60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 128-212 6.69e-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: 41.06  E-value: 6.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 821317068 128 VSFGNPRLLEVDNRLILPMQNPIRV-LVSSADVLHSWAVPSLGVKMDA---------------VPGRLNQTTFFAARAGL 191
Cdd:cd00920   11 SFTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGV 90

                         90       100
                 ....*....|....*....|.
gi 821317068 192 FYGQCSEICGaNHSFMPIVVE 212
Cdd:cd00920   91 YWFYCTIPGH-NHAGMVGTIN 110
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 158-207 2.22e-04

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: 39.14  E-value: 2.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 821317068 158 DVLHSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFM 207
Cdd:cd04223   38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 158-207 7.07e-03

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 37.26  E-value: 7.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 821317068 158 DVLHSWAVPSLGVKMDAVPGRLNQTTFFAARAGLFYGQCSEICGANHSFM 207
Cdd:PRK02888 577 DLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEM 626
 
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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