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Conserved domains on  [gi|226463936|ref|YP_002727991|]
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cytochrome c oxidase subunit II (mitochondrion) [Chamaeleo dilepis]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475905)

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 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 3.68e-155

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 429.33  E-value: 3.68e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  81 MRTLFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 3.68e-155

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 429.33  E-value: 3.68e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  81 MRTLFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 6.61e-88

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: 255.57  E-value: 6.61e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  93 PHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226463936 173 DAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 8.97e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 226.91  E-value: 8.97e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   96 TIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAV 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226463936  176 PGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 1.57e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 189.65  E-value: 1.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   6 QLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIAS-----TMKTYHTALTDANH-LEFLWTLLPVMILLFLATP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrRKGDADPAQFHHNTkLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  80 SMRTLFLLENQENPHTTIKAVGHQWYWSYEYSDyENILfdsymiqdqdlengsprlleTDNRMVFPMQTPTRLLISAEDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463936 160 LHSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 1.09e-44

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: 147.91  E-value: 1.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   12 AASPVMEELLFFHDYSMLMMLLIGTTVIiALIIASTMKtYHTALTDAN--------HLEFLWTLLPVMILLFLATPS-MR 82
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVA-ALLAYVVWK-FRRKGDEEKpsqihgnrRLEYVWTVIPLIIVVGLFAATaKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   83 TLFLLENQENPHTTIKAVGHQWYWSYEYSDYenilfdsymiqdqdlengsprLLETDNRMVFPMQTPTRLLISAEDVLHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226463936  163 WTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 3.68e-155

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 429.33  E-value: 3.68e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  81 MRTLFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 6-227 1.49e-119

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 339.11  E-value: 1.49e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   6 QLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLF 85
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  86 LLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTL 165
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226463936 166 PALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKMI 227
Cdd:MTH00154 166 PSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 3.06e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 333.10  E-value: 3.06e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  81 MRTLFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLD 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 5.53e-110

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 315.12  E-value: 5.53e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  81 MRTLFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKMI 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 1.82e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 313.96  E-value: 1.82e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  81 MRTLFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKMI 227
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 6-226 4.90e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 309.95  E-value: 4.90e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   6 QLSLHDAASPVMEELLFFHDYSMlmMLLIGTTVIIALIIASTMKTYHTALT--DANHLEFLWTLLPVMILLFLATPSMRT 83
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAM--VVLVLIFSFVMYMLVLLLFNKFSCRTilEAQKLETIWTIVPALILVFLALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  84 LFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSW 163
Cdd:MTH00140  84 LYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSW 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226463936 164 TLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00140 164 TVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 1.15e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 304.32  E-value: 1.15e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  81 MRTLFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKMI 227
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 6.46e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 302.19  E-value: 6.46e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  81 MRTLFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKMI 227
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 2.87e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 298.23  E-value: 2.87e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  81 MRTLFLLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 6-223 1.67e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 293.55  E-value: 1.67e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   6 QLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLF 85
Cdd:MTH00139   6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  86 LLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTL 165
Cdd:MTH00139  86 LMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTV 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 226463936 166 PALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:MTH00139 166 PSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 3-223 9.33e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 284.34  E-value: 9.33e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   3 EPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMR 82
Cdd:MTH00023  12 EPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  83 TLFLLENQENPHTTIKAVGHQWYWSYEYSDY--ENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00023  92 LLYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVL 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:MTH00023 172 HSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 3-223 1.69e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 283.60  E-value: 1.69e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   3 EPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMR 82
Cdd:MTH00051   5 EPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  83 TLFLLENQENPHTTIKAVGHQWYWSYEYSDY--ENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVL 160
Cdd:MTH00051  85 LLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226463936 161 HSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:MTH00051 165 HSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 6-225 7.51e-96

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 279.43  E-value: 7.51e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   6 QLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLF 85
Cdd:MTH00008   6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  86 LLENQENPHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTL 165
Cdd:MTH00008  86 LMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936 166 PALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDK 225
Cdd:MTH00008 166 PSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 6.61e-88

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: 255.57  E-value: 6.61e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  93 PHTTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 226463936 173 DAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 8.97e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 226.91  E-value: 8.97e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   96 TIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAV 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 226463936  176 PGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 3-225 1.33e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 226.45  E-value: 1.33e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   3 EPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTV---IIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATP 79
Cdd:MTH00027  31 EPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVlwlIIRILLGNNYYSYYWNKLDGSLIEVIWTLIPAFILILIAFP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  80 SMRTLFLL-ENQENPHTTIKAVGHQWYWSYEYSDY--ENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISA 156
Cdd:MTH00027 111 SLRLLYIMdECGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITA 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226463936 157 EDVLHSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDK 225
Cdd:MTH00027 191 ADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 20-223 1.55e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 204.86  E-value: 1.55e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  20 LLFFHDYSMLMMLL---IGTTVIIALIIASTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLFLLE--NQENpH 94
Cdd:MTH00080  19 MDWFHNFNCSLLFGefvLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlmNLDS-N 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  95 TTIKAVGHQWYWSYEYSDYENILFDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDA 174
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDA 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 226463936 175 VPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:MTH00080 178 MSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 1.57e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 189.65  E-value: 1.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   6 QLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIAS-----TMKTYHTALTDANH-LEFLWTLLPVMILLFLATP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrRKGDADPAQFHHNTkLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  80 SMRTLFLLENQENPHTTIKAVGHQWYWSYEYSDyENILfdsymiqdqdlengsprlleTDNRMVFPMQTPTRLLISAEDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226463936 160 LHSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWLDKM 226
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-214 4.39e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 151.65  E-value: 4.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  57 DANHLEFLWTLLPVMILLFLAtpSMRTLFLLENQE-NPHTTIKAVGHQWYWSYEYSDyeNILFDSYMIQDQDLengsprl 135
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLC--FLNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG------- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226463936 136 leTDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESV 214
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 1.09e-44

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: 147.91  E-value: 1.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   12 AASPVMEELLFFHDYSMLMMLLIGTTVIiALIIASTMKtYHTALTDAN--------HLEFLWTLLPVMILLFLATPS-MR 82
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVA-ALLAYVVWK-FRRKGDEEKpsqihgnrRLEYVWTVIPLIIVVGLFAATaKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936   83 TLFLLENQENPHTTIKAVGHQWYWSYEYSDYenilfdsymiqdqdlengsprLLETDNRMVFPMQTPTRLLISAEDVLHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226463936  163 WTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-218 8.46e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 129.17  E-value: 8.46e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936 118 FDSYMIQDQDLENGSPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 226463936 198 EICGANHSFMPISTESV-PTKY 218
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVsPEAY 152
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 96-207 1.08e-28

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: 103.85  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  96 TIKAVGHQWYWSYEYSDYEnilfdsymiqdqdlengsPRLLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAV 175
Cdd:cd04213    3 TIEVTGHQWWWEFRYPDEP------------------GRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64

                         90       100       110
                 ....*....|....*....|....*....|..
gi 226463936 176 PGRLNQLIISTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd04213   65 PGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 96-208 8.48e-27

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: 98.91  E-value: 8.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  96 TIKAVGHQWYWSYEYSDyenilfdsymiqdqdlengsprlLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAV 175
Cdd:cd13842    2 TVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58

                         90       100       110
                 ....*....|....*....|....*....|...
gi 226463936 176 PGRLNQLIISTMRPGIFYGQCSEICGANHSFMP 208
Cdd:cd13842   59 PGYTSELWFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-223 1.44e-21

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: 85.54  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  95 TTIKAVGHQWYWSYEYSDyENIlfdsymiqdqdlengsprllETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDA 174
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPE-ANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 226463936 175 VPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 1.68e-21

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: 85.38  E-value: 1.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  96 TIKAVGHQWYWSYEYSDYenilfDSYMIQDQDLENGSprlletdnrMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAV 175
Cdd:cd13919    3 VVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPE---------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68

                         90       100       110
                 ....*....|....*....|....*....|..
gi 226463936 176 PGRLNQLIISTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13919   69 PGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 2.40e-21

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: 84.60  E-value: 2.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  96 TIKAVGHQWYWSYEYSdyenilfdsymiqdqdleNGsprlLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAV 175
Cdd:cd13915    3 EIQVTGRQWMWEFTYP------------------NG----KREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                         90       100       110
                 ....*....|....*....|....*....|..
gi 226463936 176 PGRLNQLIISTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13915   61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 70-223 1.11e-20

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 84.43  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  70 VMILLFLATPSMrTLFL----LENQENPhTTIKAVGHQWYWSYEYSdyenilfdsymiqdqdleNGsprlLETDNRMVFP 145
Cdd:cd13918    6 IVISLIVWTYGM-LLYVedppDEADEDA-LEVEVEGFQFGWQFEYP------------------NG----VTTGNTLRVP 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226463936 146 MQTPTRLLISAEDVLHSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKYFEKWL 223
Cdd:cd13918   62 ADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-82 5.29e-14

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: 65.05  E-value: 5.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936    1 MVEPIQLSLHDAASPVMEELLFFHDYSMLMMLLIGTTVIIALIIASTMKTY------HTALTDANHLEFLWTLLPVMILL 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRrknpitARYTTHGQTIEIIWTIIPAVILI 80


                  ....*...
gi 226463936   75 FLATPSMR 82
Cdd:pfam02790  81 LIALPSFK 88
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 29-225 1.19e-08

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 54.03  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  29 LMMLLIGTTVIIALIIA------STMKTYHTALTDANHLE-FLWTLlPVMILLFLATPSMRTLFLLE------NQENPhT 95
Cdd:PRK10525  50 LMLIVVIPAILMAVGFAwkyrasNKDAKYSPNWSHSNKVEaVVWTV-PILIIIFLAVLTWKTTHALEpskplaHDEKP-I 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  96 TIKAVGHQWYWSYEYSdyenilfdsymiqdqdlENGsprlLETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAV 175
Cdd:PRK10525 128 TIEVVSMDWKWFFIYP-----------------EQG----IATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAM 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 226463936 176 PGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESVPTKY-FEKWLDK 225
Cdd:PRK10525 187 AGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAeFDQWVAK 237
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 96-214 5.94e-06

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: 43.69  E-value: 5.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  96 TIKAVGHQWYWSYEYSDYeNIlfdsymiqdqdlengsprllETDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAV 175
Cdd:cd04212    2 EIQVVSLDWKWLFIYPEQ-GI--------------------ATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAM 60

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 226463936 176 PGRLNQLIISTMRPGIFYGQCSEICGANHSFMPISTESV 214
Cdd:cd04212   61 AGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 138-207 6.99e-05

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: 40.63  E-value: 6.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936 138 TDNRMVFPMQTPTRLLISAEDVLHSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13913   23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 2.84e-04

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 38.90  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226463936  95 TTIKAVGHQWYWSyeysdyenilfdsyMIQDQdlengsprlletdnrmvFPMQTPTRLLISAEDVLHSWTL--PALGV-- 170
Cdd:cd13916    1 QVVAVTGHQWYWE--------------LSRTE-----------------IPAGKPVEFRVTSADVNHGFGIydPDMRLla 49

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 226463936 171 KIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13916   50 QTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-207 1.43e-03

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 36.58  E-value: 1.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 226463936 151 RLLISAEDVLHSWTLPALGVKIDAVPGRLNQLIISTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13917   25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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