NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|75811811|gb|ABA28347|]
View 

cytochrome c oxidase subunit II (mitochondrion) [Taterillus emini]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475897)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 2.65e-157

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 434.53  E-value: 2.65e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSL 226
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 2.65e-157

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 434.53  E-value: 2.65e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSL 226
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 8.77e-92

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: 265.20  E-value: 8.77e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  93 PVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKT 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 75811811 173 DAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 4.92e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.70  E-value: 4.92e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    95 LTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 75811811   175 IPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 1.98e-40

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 138.04  E-value: 1.98e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   6 QLGLQDASSPIMEELMNFHDHTLMIVFLISSLVlylISLML-------------TTKLIHTSTMdaqeVETVWTILPAII 72
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPIII 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  73 LILIALPSLRILYMMDEINNPVLTVKTMGHQWYWSYEYtdfedlsfdsymiptnelkPGElrQLEVDNRMVLPMELPIRM 152
Cdd:COG1622  91 VIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------------PDQ--GIATVNELVLPVGRPVRF 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811 153 LISSEDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:COG1622 150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.92e-36

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: 126.73  E-value: 1.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    12 ASSPIMEELMNFHDHTLMIVFLISSLVLYLISLML------TTKLIHTSTMDAQEVETVWTIL-PAIILILIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIpLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    85 YMMDEINNPVLTVKTMGHQWYWSYEYTDFedlsfdsymiptnelkpgelrQLEVDNRMVLPMELPIRMLISSEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 75811811   165 VPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 2.65e-157

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 434.53  E-value: 2.65e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSL 226
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.01e-146

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 407.76  E-value: 1.01e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSLT 227
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-227 3.09e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 368.72  E-value: 3.09e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSLT 227
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-226 3.46e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 363.65  E-value: 3.46e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSL 226
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-226 9.84e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 344.95  E-value: 9.84e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSL 226
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 1.13e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 334.49  E-value: 1.13e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSL 226
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 3.24e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 323.09  E-value: 3.24e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLS 225
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-222 6.75e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 322.42  E-value: 6.75e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 7.06e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 312.26  E-value: 7.06e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSL 226
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 2.35e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 305.87  E-value: 2.35e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75811811  161 HSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-227 4.60e-103

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 297.54  E-value: 4.60e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLY-LISLMLTtKLIHTSTMDAQEVETVWTILPAIILILIALP 79
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYaMTSLMFN-KLSNRYILEAQQIETIWTILPALILLFLAFP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   80 SLRILYMMDEINNPVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDV 159
Cdd:MTH00008  80 SLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75811811  160 LHSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSLT 227
Cdd:MTH00008 160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-227 2.17e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 275.86  E-value: 2.17e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    4 PLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPSLRI 83
Cdd:MTH00023  13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   84 LYMMDEINNPVLTVKTMGHQWYWSYEYTDFED--LSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVLH 161
Cdd:MTH00023  93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75811811  162 SWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSLT 227
Cdd:MTH00023 173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-227 7.64e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 272.04  E-value: 7.64e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    4 PLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPSLRI 83
Cdd:MTH00051   6 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   84 LYMMDEINNPVLTVKTMGHQWYWSYEYTDF--EDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVLH 161
Cdd:MTH00051  86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75811811  162 SWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSLT 227
Cdd:MTH00051 166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQS 231
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 8.77e-92

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: 265.20  E-value: 8.77e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  93 PVLTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKT 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 75811811 173 DAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 4.92e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.70  E-value: 4.92e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    95 LTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 75811811   175 IPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 1.25e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 216.43  E-value: 1.25e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    4 PLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHT---STMDAQEVETVWTILPAIILILIALPS 80
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   81 LRILYMMDE-INNPVLTVKTMGHQWYWSYEYTDF--EDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSE 157
Cdd:MTH00027 112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75811811  158 DVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 17-226 2.03e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 199.47  E-value: 2.03e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   17 MEELMNFHDHTLMIVFLISSLVLYLISLMLTTKLIHTSTMDAQEVETVWTILPAIILILIALPSLRILYMMDEIN-NPVL 95
Cdd:MTH00080  19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   96 TVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAI 175
Cdd:MTH00080  99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 75811811  176 PGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENWSLSL 226
Cdd:MTH00080 179 SGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLL 229
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-214 6.69e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 139.57  E-value: 6.69e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  117 SFDSYMIPTNELKPGELRQLEVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQC 196
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90
                 ....*....|....*...
gi 75811811  197 SEICGSNHSFMPIVLEMI 214
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEAV 147
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 1.98e-40

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 138.04  E-value: 1.98e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   6 QLGLQDASSPIMEELMNFHDHTLMIVFLISSLVlylISLML-------------TTKLIHTSTMdaqeVETVWTILPAII 72
Cdd:COG1622  18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPIII 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  73 LILIALPSLRILYMMDEINNPVLTVKTMGHQWYWSYEYtdfedlsfdsymiptnelkPGElrQLEVDNRMVLPMELPIRM 152
Cdd:COG1622  91 VIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------------PDQ--GIATVNELVLPVGRPVRF 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811 153 LISSEDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:COG1622 150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 96-214 1.18e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 135.08  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811   96 TVKTMGHQWYWSYEYTDfeDLSFDSYMIPTNELkpgelrqleVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAI 175
Cdd:MTH00047  83 TIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAI 151

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 75811811  176 PGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMI 214
Cdd:MTH00047 152 PGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.92e-36

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: 126.73  E-value: 1.92e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    12 ASSPIMEELMNFHDHTLMIVFLISSLVLYLISLML------TTKLIHTSTMDAQEVETVWTIL-PAIILILIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIpLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811    85 YMMDEINNPVLTVKTMGHQWYWSYEYTDFedlsfdsymiptnelkpgelrQLEVDNRMVLPMELPIRMLISSEDVLHSWA 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 75811811   165 VPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.97e-32

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: 113.16  E-value: 1.97e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  95 LTVKTMGHQWYWSYEYTDfedlsfdsymiptnelkpgelrqLEVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 75811811 175 IPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLE 212
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 5.97e-29

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: 104.62  E-value: 5.97e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  95 LTVKTMGHQWYWSYEYTDfedlsfdsymiptnelkpGELRQLEVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPD------------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                        90       100       110
                ....*....|....*....|....*....|...
gi 75811811 175 IPGRLNQATVTSNRPGVFYGQCSEICGSNHSFM 207
Cdd:cd04213  64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.26e-24

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 93.47  E-value: 1.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  95 LTVKTMGHQWYWSYEYTDFEDLSFDSYMIPTNELkpgelrqlevdnrmVLPMELPIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 75811811 175 IPGRLNQATVTSNRPGVFYGQCSEICGSNHSFM 207
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-222 3.26e-23

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 90.98  E-value: 3.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  88 DEINNPVLTVKTMGHQWYWSYEYtdfedlsfdsymiptnelkPGELRQLevdNRMVLPMELPIRMLISSEDVLHSWAVPS 167
Cdd:cd13918  26 DEADEDALEVEVEGFQFGWQFEY-------------------PNGVTTG---NTLRVPADTPIALRVTSTDVFHTFGIPE 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 75811811 168 LGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:cd13918  84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 4.54e-23

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 89.23  E-value: 4.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  95 LTVKTMGHQWYWSYEYtdfedlsfdsymiptnelkPGELRQlevDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDA 174
Cdd:cd13915   2 LEIQVTGRQWMWEFTY-------------------PNGKRE---INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90       100       110
                ....*....|....*....|....*....|...
gi 75811811 175 IPGRLNQATVTSNRPGVFYGQCSEICGSNHSFM 207
Cdd:cd13915  60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 7.79e-19

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 78.60  E-value: 7.79e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  96 TVKTMGHQWYWSYEYTDFEdlsfdsymiptnelkpgelrqLEVDNRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAI 175
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEAN---------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 75811811 176 PGRLNQATVTSNRPGVFYGQCSEICGSNHSFMPIVLEMIPLKLFENW 222
Cdd:cd13914  61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-66 1.40e-17

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: 74.68  E-value: 1.40e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75811811     1 MAYPLQLGLQDASSPIMEELMNFHDHTLMIVFLISSLVLYLISLMLTT------KLIHTSTMDAQEVETVWT 66
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWT 72
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 1.32e-09

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: 53.73  E-value: 1.32e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75811811 140 NRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFM 207
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 1.35e-07

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: 48.15  E-value: 1.35e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  96 TVKTMGHQWYWSyeytdfedlsfdsymIPTNELKPGElrqlevdnrmvlpmelPIRMLISSEDVLHSWAV--PSLGL--K 171
Cdd:cd13916   2 VVAVTGHQWYWE---------------LSRTEIPAGK----------------PVEFRVTSADVNHGFGIydPDMRLlaQ 50

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 75811811 172 TDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFM 207
Cdd:cd13916  51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 6.70e-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: 43.31  E-value: 6.70e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75811811 140 NRMVLPMELPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFM 207
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 97-212 1.01e-05

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 43.37  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75811811  97 VKTMGHQWYWSYEYTDFEDLSFDSYmiptnELKPGELRQLEvdnrmvlpmelpirmLISSEDVLHSWAVPSLGLKTDAI- 175
Cdd:cd00920   1 ITVTASDWGWSFTYNGVLLFGPPVL-----VVPVGDTVRVQ---------------FVNKLGENHSVTIAGFGVPVVAMa 60

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 75811811 176 --------------PGRLNQATVTSNRPGVFYGQCSEIcGSNHSFMPIVLE 212
Cdd:cd00920  61 gganpglvntlvigPGESAEVTFTTDQAGVYWFYCTIP-GHNHAGMVGTIN 110
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-207 3.62e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 38.51  E-value: 3.62e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75811811 151 RMLISSEDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHSFM 207
Cdd:cd13917  25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 157-213 1.54e-03

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 36.83  E-value: 1.54e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 75811811 157 EDVLHSWAVPSLGLKTDAIPGRLNQATVTSNRPGVFYGQCSEICGSNHsfmpivLEM 213
Cdd:cd04223  37 EDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALH------LEM 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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