NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1418578916|ref|YP_009487502|]
View 

cytochrome c oxidase subunit II (mitochondrion) [Lytechinus variegatus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 8.73e-174

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 476.50  E-value: 8.73e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYLEE 229
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
 
Name Accession Description Interval E-value
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 8.73e-174

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 476.50  E-value: 8.73e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYLEE 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 2.88e-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: 274.06  E-value: 2.88e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  93 PFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKM 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1418578916 173 DAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.59e-84

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 245.78  E-value: 3.59e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  95 LTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1418578916 175 VPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-225 1.31e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 192.35  E-value: 1.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFyGLasLLVS---------SSTNRFFLEGQELETIWTVIPAL 71
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVF-GL--LLYFairyrrrkgDADPAQFHHNTKLEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  72 ILIFIALPSLQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLefdsymvptsdislsdarlleVDNRLILPMQNPIR 151
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418578916 152 VLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQ 225
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-224 2.00e-45

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: 150.22  E-value: 2.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  12 ASSPLMEELTYFHDYALIVLTLITILVFYGLASLLV---SSSTNR---FFLEGQELETIWTVIPALILI-FIALPSLQLL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrRKGDEEkpsQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  85 YLMDEVNDPFLTIKAIGHQWYWSYEYTDYndlefdsymvptsdislsdarLLEVDNRLILPMQNPIRVLVSSADVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916 165 VPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVA 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-229 8.73e-174

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 476.50  E-value: 8.73e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYLEE 229
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 5.16e-155

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 428.86  E-value: 5.16e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYL 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-222 2.43e-143

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 399.29  E-value: 2.43e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENW 222
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 3.54e-142

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 396.27  E-value: 3.54e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQ 225
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-223 5.81e-133

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 373.12  E-value: 5.81e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWL 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-229 2.37e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 369.43  E-value: 2.37e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYLEE 229
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 6.49e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 367.89  E-value: 6.49e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQY 226
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-222 4.24e-130

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 365.97  E-value: 4.24e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-229 1.60e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 349.57  E-value: 1.60e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYLEE 229
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEE 229
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-228 2.33e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 344.07  E-value: 2.33e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYLE 228
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-228 3.09e-120

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 341.07  E-value: 3.09e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  81 LQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418578916 161 HSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYLE 228
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-223 8.82e-115

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 327.86  E-value: 8.82e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   6 QFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPSLQLLY 85
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  86 LMDEVNDPFLTIKAIGHQWYWSYEYTDYND--LEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVLHSW 163
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916 164 AVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-229 4.87e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 325.58  E-value: 4.87e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   6 QFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFFLEGQELETIWTVIPALILIFIALPSLQLLY 85
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  86 LMDEVNDPFLTIKAIGHQWYWSYEYTDY--NDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVLHSW 163
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418578916 164 AVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYLEE 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 2.88e-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: 274.06  E-value: 2.88e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  93 PFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKM 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1418578916 173 DAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-225 4.36e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 258.42  E-value: 4.36e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   6 QFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLVSSSTNRFF---LEGQELETIWTVIPALILIFIALPSLQ 82
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  83 LLYLMDE-VNDPFLTIKAIGHQWYWSYEYTDYND--LEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADV 159
Cdd:MTH00027  114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEknIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1418578916 160 LHSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQ 225
Cdd:MTH00027  194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.59e-84

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 245.78  E-value: 3.59e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  95 LTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1418578916 175 VPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 20-228 7.45e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 228.74  E-value: 7.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  20 LTYFHDYALIVLTLITILVFYgLASLLVSSSTNRFF----LEGQELETIWTVIPALILIFIALPSLQLLYLMDEVN-DPF 94
Cdd:MTH00080   19 MDWFHNFNCSLLFGEFVLAFV-VFLFLYLISNNFYFkskkIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  95 LTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:MTH00080   98 LTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDA 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1418578916 175 VPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQYLE 228
Cdd:MTH00080  178 MSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-225 1.31e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 192.35  E-value: 1.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFyGLasLLVS---------SSTNRFFLEGQELETIWTVIPAL 71
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVF-GL--LLYFairyrrrkgDADPAQFHHNTKLEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  72 ILIFIALPSLQLLYLMDEVNDPFLTIKAIGHQWYWSYEYTDYNDLefdsymvptsdislsdarlleVDNRLILPMQNPIR 151
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1418578916 152 VLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVAQ 225
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 26-214 2.21e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 170.14  E-value: 2.21e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  26 YALIVLTLITILVFYGLA-SLLVSSSTNRFFLEGQELETIWTVIPALILIFiaLPSLQLLYLM-DEVNDPFLTIKAIGHQ 103
Cdd:MTH00047   13 YILALCVFIPCWVYIMLCwQVVSGNGSVNFGSENQVLELLWTVVPTLLVLV--LCFLNLNFITsDLDCFSSETIKVIGHQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916 104 WYWSYEYTdyNDLEFDSYMvpTSDISLsdarlleVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTT 183
Cdd:MTH00047   91 WYWSYEYS--FGGSYDSFM--TDDIFG-------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLF 159

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1418578916 184 FFAARTGLFYGQCSEICGANHSFMPIVIESV 214
Cdd:MTH00047  160 FCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-224 2.00e-45

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: 150.22  E-value: 2.00e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  12 ASSPLMEELTYFHDYALIVLTLITILVFYGLASLLV---SSSTNR---FFLEGQELETIWTVIPALILI-FIALPSLQLL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrRKGDEEkpsQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  85 YLMDEVNDPFLTIKAIGHQWYWSYEYTDYndlefdsymvptsdislsdarLLEVDNRLILPMQNPIRVLVSSADVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916 165 VPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVA 224
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-229 5.82e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 137.26  E-value: 5.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916 118 FDSYMVPTSDISLSDARLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1418578916 198 EICGANHSFMPIVIESVPFNTFENWVAQYLEE 229
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAYAAHAKKYYKD 162
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 4.70e-31

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: 109.73  E-value: 4.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916   1 MATWAQFGLQDASSPLMEELTYFHDYALIVLTLITILVFYGLASLLV------SSSTNRFFLEGQELETIWTVIPALILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1418578916  75 FIALPSLQL 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 5.14e-31

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: 109.69  E-value: 5.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  95 LTIKAIGHQWYWSYEYTDyndlefdsymvptsdislsdarlLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1418578916 175 VPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 1.04e-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: 109.25  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  95 LTIKAIGHQWYWSYEYTDyndlefdsymvptsdislSDARLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1418578916 175 VPGRLNQTTFFAARTGLFYGQCSEICGANHSFM 207
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 8.90e-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: 93.86  E-value: 8.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  95 LTIKAIGHQWYWSYEYtdyndlefdsymvPTSDISLSDARLLEVdNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1418578916 175 VPGRLNQTTFFAARTGLFYGQCSEICGANHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 8.09e-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: 91.15  E-value: 8.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  95 LTIKAIGHQWYWSYEYTDYNdlefdsymvptsdislsdarllEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYPNGK----------------------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1418578916 175 VPGRLNQTTFFAARTGLFYGQCSEICGANHSFM 207
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 68-223 1.34e-22

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 89.44  E-value: 1.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  68 IPALILI-FIALPSLQLLYLMD---EVNDPFLTIKAIGHQWYWSYEYTdyNDLEFDSYMVptsdislsdarllevdnrli 143
Cdd:cd13918     2 LSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTLR-------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916 144 LPMQNPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 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 2.71e-20

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 82.46  E-value: 2.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  96 TIKAIGHQWYWSYEYTDYNdlefdsymVPTSdislsdarllevdNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDAV 175
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEAN--------VTTS-------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1418578916 176 PGRLNQTTFFAARTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 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 ...
 148-207 8.77e-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: 46.02  E-value: 8.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418578916 148 NPIRV--------LVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFM 207
Cdd:cd13913    25 NEIEVpagatvtfYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 95-207 1.24e-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: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  95 LTIKAIGHQWYWSYEYTDYNdlefdsymvptsdislsdarlLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDA 174
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQG---------------------IATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYA 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1418578916 175 VPGRLNQTTFFAARTGLFYGQCSEICGANHSFM 207
Cdd:cd04212    60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 97-212 8.98e-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: 40.68  E-value: 8.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916  97 IKAIGHQWYWSYEYTDYndlefdsymvptsdislsdarLLEVDNRLILPMQNPIRV-LVSSADVLHSWAVPSLGVKMDA- 174
Cdd:cd00920     1 ITVTASDWGWSFTYNGV---------------------LLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAm 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1418578916 175 --------------VPGRLNQTTFFAARTGLFYGQCSEICGaNHSFMPIVIE 212
Cdd:cd00920    60 agganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 158-207 5.12e-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: 37.98  E-value: 5.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1418578916 158 DVLHSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHSFM 207
Cdd:cd04223    38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 126-207 8.55e-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: 34.65  E-value: 8.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418578916 126 SDISLsDARLLEVDNRLILPMQNPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFAARTGLFYGQCSEICGANHS 205
Cdd:cd13917     1 GDVYL-VARAWQWRPVLVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHH 79


                  ..
gi 1418578916 206 FM 207
Cdd:cd13917    80 TM 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH