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Conserved domains on  [gi|296940227|ref|YP_003667898|]
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cytochrome c oxidase subunit II (mitochondrion) [Brookesia decaryi]

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
 1-227 4.26e-153

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 423.94  E-value: 4.26e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   1 MVEPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  81 MRTLFLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 4.26e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 423.94  E-value: 4.26e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   1 MVEPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  81 MRTLFLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 8.88e-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: 255.19  E-value: 8.88e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  93 PQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 296940227 173 DAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 3.26e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 225.37  E-value: 3.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   96 SIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDAV 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 296940227  176 PGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 3.05e-57

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 181.18  E-value: 3.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   6 QLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIAT-----TMKTYHTALTDANH-LEFLWTLLPVMILLFLATP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrRKGDADPAQFHHNTkLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  80 SMRTLFLLEDQENPQVSIKALGHQWYWSYEYSDyENILfdsymiqdpdlekgsprlleTDNRMIFPMQTPTRLLISAEDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 160 LHSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKM 226
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 3.88e-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: 146.76  E-value: 3.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   12 AASPMMEELLFFHDYSMLMMILIGTTVIiALIIATTMKtYHTALTDAN--------HLEFLWTLLPVMILLFLATPS-MR 82
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVA-ALLAYVVWK-FRRKGDEEKpsqihgnrRLEYVWTVIPLIIVVGLFAATaKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   83 TLFLLEDQENPQVSIKALGHQWYWSYEYSDYenilfdsymiqdpdlekgsprLLETDNRMIFPMQTPTRLLISAEDVLHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296940227  163 WTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWL 223
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 4.26e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 423.94  E-value: 4.26e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   1 MVEPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  81 MRTLFLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKML 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 6-227 2.87e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 336.03  E-value: 2.87e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   6 QLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLF 85
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  86 LLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTL 165
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296940227 166 PTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKML 227
Cdd:MTH00154 166 PSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.15e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 326.55  E-value: 1.15e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   1 MVEPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  81 MRTLFLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLD 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 6.43e-109

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 312.42  E-value: 6.43e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   1 MVEPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  81 MRTLFLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKML 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 6-226 1.55e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 311.49  E-value: 1.55e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   6 QLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMK-TYHTALTDANhLEFLWTLLPVMILLFLATPSMRTL 84
Cdd:MTH00140   6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKfSCRTILEAQK-LETIWTIVPALILVFLALPSLRLL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  85 FLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWT 164
Cdd:MTH00140  85 YLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWT 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296940227 165 LPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKM 226
Cdd:MTH00140 165 VPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 9.03e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 307.03  E-value: 9.03e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   1 MVEPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  81 MRTLFLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKML 227
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 2.06e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 303.55  E-value: 2.06e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   1 MVEPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  81 MRTLFLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKML 227
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 4.93e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 297.57  E-value: 4.93e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   1 MVEPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  81 MRTLFLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKML 227
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-227 2.09e-101

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 293.22  E-value: 2.09e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   1 MVEPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  81 MRTLFLLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKML 227
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 6-223 1.32e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 291.24  E-value: 1.32e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   6 QLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLF 85
Cdd:MTH00139   6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  86 LLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTL 165
Cdd:MTH00139  86 LMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTV 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 296940227 166 PTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWL 223
Cdd:MTH00139 166 PSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 3-223 5.86e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 284.75  E-value: 5.86e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   3 EPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMR 82
Cdd:MTH00051   5 EPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  83 TLFLLEDQENPQVSIKALGHQWYWSYEYSDY--ENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00051  85 LLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWL 223
Cdd:MTH00051 165 HSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 3-223 3.01e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 283.18  E-value: 3.01e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   3 EPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMR 82
Cdd:MTH00023  12 EPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  83 TLFLLEDQENPQVSIKALGHQWYWSYEYSDY--ENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVL 160
Cdd:MTH00023  92 LLYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVL 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296940227 161 HSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWL 223
Cdd:MTH00023 172 HSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 6-225 1.33e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 278.66  E-value: 1.33e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   6 QLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLF 85
Cdd:MTH00008   6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  86 LLEDQENPQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTL 165
Cdd:MTH00008  86 LMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227 166 PTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDK 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 8.88e-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: 255.19  E-value: 8.88e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  93 PQVSIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKI 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 296940227 173 DAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKW 222
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-214 3.26e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 225.37  E-value: 3.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   96 SIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDAV 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 296940227  176 PGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAV 214
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 3-225 1.68e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 226.45  E-value: 1.68e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   3 EPIQLALHDAASPMMEELLFFHDYSMLMMILIGTTV---IIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATP 79
Cdd:MTH00027  31 EPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVlwlIIRILLGNNYYSYYWNKLDGSLIEVIWTLIPAFILILIAFP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  80 SMRTLFLLEDQE-NPQVSIKALGHQWYWSYEYSDY--ENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISA 156
Cdd:MTH00027 111 SLRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITA 190

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296940227 157 EDVLHSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDK 225
Cdd:MTH00027 191 ADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGR 259
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 20-223 1.83e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 202.16  E-value: 1.83e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  20 LLFFHDYS---MLMMILIGTTVIIALIIATTMKTYHTALTDANHLEFLWTLLPVMILLFLATPSMRTLFLLE-DQENPQV 95
Cdd:MTH00080  19 MDWFHNFNcslLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  96 SIKALGHQWYWSYEYSDYENILFDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDAV 175
Cdd:MTH00080  99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 296940227 176 PGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWL 223
Cdd:MTH00080 179 SGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 3.05e-57

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 181.18  E-value: 3.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   6 QLALHDAASPMMEELLFFHDYSMLMMILIGTTVIIALIIAT-----TMKTYHTALTDANH-LEFLWTLLPVMILLFLATP 79
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAiryrrRKGDADPAQFHHNTkLEIVWTVIPIIIVIVLAVP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  80 SMRTLFLLEDQENPQVSIKALGHQWYWSYEYSDyENILfdsymiqdpdlekgsprlleTDNRMIFPMQTPTRLLISAEDV 159
Cdd:COG1622   98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA--------------------TVNELVLPVGRPVRFLLTSADV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 160 LHSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWLDKM 226
Cdd:COG1622  157 IHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-214 1.26e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 152.80  E-value: 1.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  57 DANHLEFLWTLLPVMILLFLAtpSMRTLFLLEDQE-NPQVSIKALGHQWYWSYEYSDyeNILFDSYMIQDPDLekgsprl 135
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLC--FLNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG------- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296940227 136 leTDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAV 214
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 3.88e-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: 146.76  E-value: 3.88e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   12 AASPMMEELLFFHDYSMLMMILIGTTVIiALIIATTMKtYHTALTDAN--------HLEFLWTLLPVMILLFLATPS-MR 82
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVA-ALLAYVVWK-FRRKGDEEKpsqihgnrRLEYVWTVIPLIIVVGLFAATaKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227   83 TLFLLEDQENPQVSIKALGHQWYWSYEYSDYenilfdsymiqdpdlekgsprLLETDNRMIFPMQTPTRLLISAEDVLHS 162
Cdd:TIGR02866  79 LLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296940227  163 WTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWL 223
Cdd:TIGR02866 138 FWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-222 6.18e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 129.55  E-value: 6.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227 118 FDSYMIQDPDLEKGSPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|....*....
gi 296940227 198 EICGANHSFMPIATEAV-PTK---HFEKW 222
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVsPEAyaaHAKKY 159
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 1.23e-27

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: 101.16  E-value: 1.23e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  95 VSIKALGHQWYWSYEYSDYEnilfdsymiqdpdlekgsPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDA 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEP------------------GRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                         90       100       110
                 ....*....|....*....|....*....|...
gi 296940227 175 VPGRLNQLILSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd04213   64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-208 5.44e-26

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: 96.60  E-value: 5.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  95 VSIKALGHQWYWSYEYSDyenilfdsymiqdpdlekgsprlLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDA 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                         90       100       110
                 ....*....|....*....|....*....|....
gi 296940227 175 VPGRLNQLILSTMRPGIFYGQCSEICGANHSFMP 208
Cdd:cd13842   58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-223 4.00e-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: 84.38  E-value: 4.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  95 VSIKALGHQWYWSYEYSDyENIlfdsymiqdpdlekgsprllETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDA 174
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPE-ANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDA 59

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 296940227 175 VPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWL 223
Cdd:cd13914   60 FPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 70-223 1.33e-19

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 81.35  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  70 VMILLFLATPSMrTLFL----LEDQENPqVSIKALGHQWYWSYEYsdyenilfdsymiqdpdlekgsPRLLETDNRMIFP 145
Cdd:cd13918    6 IVISLIVWTYGM-LLYVedppDEADEDA-LEVEVEGFQFGWQFEY----------------------PNGVTTGNTLRVP 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296940227 146 MQTPTRLLISAEDVLHSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKHFEKWL 223
Cdd:cd13918   62 ADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-207 5.41e-19

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 78.84  E-value: 5.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  97 IKALGHQWYWSYEYSDYenilfDSYMIQDPDLEKGSPRLletdnrmifPMQTPTRLLISAEDVLHSWTLPTLGVKIDAVP 176
Cdd:cd13919    4 VEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVP 69

                         90       100       110
                 ....*....|....*....|....*....|.
gi 296940227 177 GRLNQLILSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13919   70 GRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-207 6.76e-19

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 78.44  E-value: 6.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  97 IKALGHQWYWSYEYsdyenilfdsymiqdpdlekgsPRLLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDAVP 176
Cdd:cd13915    4 IQVTGRQWMWEFTY----------------------PNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVP 61

                         90       100       110
                 ....*....|....*....|....*....|.
gi 296940227 177 GRLNQLILSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13915   62 GRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-82 7.09e-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: 64.66  E-value: 7.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227    1 MVEPIQLALHDAASPMMEELLFFHDYsmLMMILIGTTVIIALIIATTMKTY--------HTALTDANHLEFLWTLLPVMI 72
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDY--IMFILTLILILVLYILVTCLIRFnrrknpitARYTTHGQTIEIIWTIIPAVI 78

                          90
                  ....*....|
gi 296940227   73 LLFLATPSMR 82
Cdd:pfam02790  79 LILIALPSFK 88
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 29-225 6.84e-10

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 57.89  E-value: 6.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  29 LMMILIGTTVIIALIIA------TTMKTYHTALTDANHLE-FLWTLlPVMILLFLATPSMRTLFLLE-----DQENPQVS 96
Cdd:PRK10525  50 LMLIVVIPAILMAVGFAwkyrasNKDAKYSPNWSHSNKVEaVVWTV-PILIIIFLAVLTWKTTHALEpskplAHDEKPIT 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296940227  97 IKALGHQWYWSYEYsdyenilfdsymiqdPDLEkgsprlLETDNRMIFPMQTPTRLLISAEDVLHSWTLPTLGVKIDAVP 176
Cdd:PRK10525 129 IEVVSMDWKWFFIY---------------PEQG------IATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMA 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 296940227 177 GRLNQLILSTMRPGIFYGQCSEICGANHSFMPIATEAVPTKH-FEKWLDK 225
Cdd:PRK10525 188 GMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAeFDQWVAK 237
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 154-207 8.54e-04

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: 37.55  E-value: 8.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 296940227 154 ISAEDVLHSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFM 207
Cdd:cd13913   39 VTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-207 1.59e-03

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 36.58  E-value: 1.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296940227 151 RLLISAEDVLHSWTLPTLGVKIDAVPGRLNQLILSTMRPGIFYGQCSEICGANHSFM 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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