NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1036436316|gb|ANK35838|]
View 

cytochrome oxidase subunit II, partial (mitochondrion) [Microcebus lehilahytsara]

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
 1-213 1.38e-159

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 439.92  E-value: 1.38e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLEL 213
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLEL 213
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-213 1.38e-159

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 439.92  E-value: 1.38e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLEL 213
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLEL 213
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-212 2.28e-84

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: 245.94  E-value: 2.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  93 PSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1036436316 173 DAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVE 120
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.22e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 228.45  E-value: 1.22e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  95 LTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1036436316 175 IPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLEL 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-212 6.22e-52

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 166.93  E-value: 6.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   6 QLGFQDAASPIMEELmyfhDHTLMIVFLISSLV-LYIISLML-------------TTELTHTSTMdaqeVETVWTILPAV 71
Cdd:COG1622    18 QLSLPDPAGPIAEEI----DDLFWVSLIIMLVIfVLVFGLLLyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  72 ILILIALPSLRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLcfdsymtppleldpgelrlleVDNRVVLPTEMSIR 151
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036436316 152 MLISSEDVLHSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-212 1.03e-41

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: 139.82  E-value: 1.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  12 AASPIMEELMYFHDHTLMIVFLISSLVLYIISLML------TTELTHTSTMDAQEVETVWTILPAVILI-LIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  85 YMMDEITTPSLTLKTMGHQWYWSYEYTDYeslcfdsymtppleldpgelrLLEVDNRVVLPTEMSIRMLISSEDVLHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1036436316 165 VPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-213 1.38e-159

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 439.92  E-value: 1.38e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLEL 213
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLEL 213
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-212 1.16e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 414.70  E-value: 1.16e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-212 8.37e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 377.20  E-value: 8.37e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVE 212
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-212 3.35e-132

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 370.58  E-value: 3.35e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-212 3.97e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 362.61  E-value: 3.97e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-212 3.61e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 353.04  E-value: 3.61e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVE 212
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-212 1.81e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 340.80  E-value: 1.81e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-212 1.14e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 333.98  E-value: 1.14e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIE 212
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-212 4.10e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 329.98  E-value: 4.10e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-212 2.01e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 323.21  E-value: 2.01e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-212 1.68e-106

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 305.63  E-value: 1.68e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1036436316 161 HSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLE 212
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-212 2.43e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 293.19  E-value: 2.43e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   4 PAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRI 83
Cdd:MTH00023   13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  84 LYMMDEITTPSLTLKTMGHQWYWSYEYTDYES--LCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLH 161
Cdd:MTH00023   93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1036436316 162 SWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00023  173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIE 223
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-212 6.06e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 286.68  E-value: 6.06e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   4 PAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRI 83
Cdd:MTH00051    6 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  84 LYMMDEITTPSLTLKTMGHQWYWSYEYTDY--ESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLH 161
Cdd:MTH00051   86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1036436316 162 SWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00051  166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIE 216
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-212 2.28e-84

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: 245.94  E-value: 2.28e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  93 PSLTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1036436316 173 DAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVE 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-212 3.82e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 242.62  E-value: 3.82e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   4 PAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTTELTHT---STMDAQEVETVWTILPAVILILIALPS 80
Cdd:MTH00027   32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  81 LRILYMMDE-ITTPSLTLKTMGHQWYWSYEYTDY--ESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSE 157
Cdd:MTH00027  112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1036436316 158 DVLHSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00027  192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVE 246
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 1.22e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 228.45  E-value: 1.22e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  95 LTLKTMGHQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1036436316 175 IPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLEL 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEA 119
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-213 2.97e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 218.73  E-value: 2.97e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  23 FHDHTLMIVFLISSLVLYIISLMLTTELTHTSTMDAQEVETVWTILPAVILILIALPSLRILYMMDEITTPS-LTLKTMG 101
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLDSnLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316 102 HQWYWSYEYTDYESLCFDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTDAIPGRLNQ 181
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1036436316 182 ATLMTSRPGIYYGQCSEICGANHSFMPIVLEL 213
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEV 216
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-212 6.22e-52

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 166.93  E-value: 6.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   6 QLGFQDAASPIMEELmyfhDHTLMIVFLISSLV-LYIISLML-------------TTELTHTSTMdaqeVETVWTILPAV 71
Cdd:COG1622    18 QLSLPDPAGPIAEEI----DDLFWVSLIIMLVIfVLVFGLLLyfairyrrrkgdaDPAQFHHNTK----LEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  72 ILILIALPSLRILYMMDEITTPSLTLKTMGHQWYWSYEYTDYESLcfdsymtppleldpgelrlleVDNRVVLPTEMSIR 151
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1036436316 152 MLISSEDVLHSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-212 7.89e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 140.09  E-value: 7.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  57 DAQEVETVWTILPAVI-LILIALPSLRILYMMDeiTTPSLTLKTMGHQWYWSYEYTDyeSLCFDSYMTPPLELdpgelrl 135
Cdd:MTH00047   45 ENQVLELLWTVVPTLLvLVLCFLNLNFITSDLD--CFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG------- 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1036436316 136 leVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:MTH00047  114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-212 1.03e-41

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: 139.82  E-value: 1.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  12 AASPIMEELMYFHDHTLMIVFLISSLVLYIISLML------TTELTHTSTMDAQEVETVWTILPAVILI-LIALPSLRIL 84
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrkGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  85 YMMDEITTPSLTLKTMGHQWYWSYEYTDYeslcfdsymtppleldpgelrLLEVDNRVVLPTEMSIRMLISSEDVLHSWT 164
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1036436316 165 VPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-212 6.28e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 131.48  E-value: 6.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316 118 FDSYMTPPLELDPGELRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*
gi 1036436316 198 EICGANHSFMPIVLE 212
Cdd:PTZ00047  131 EMCGTLHGFMPIVVE 145
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.09e-30

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 108.15  E-value: 1.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  95 LTLKTMGHQWYWSYEYTDyeslcfdsymtppleldpgelrlLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTDA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1036436316 175 IPGRLNQATLMTSRPGIYYGQCSEICGANHSFMPIVLE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.30e-29

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: 105.49  E-value: 1.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316   1 MAYPAQLGFQDAASPIMEELMYFHDHTLMIVFLISSLVLYIISLMLTT------ELTHTSTMDAQEVETVWTILPAVILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1036436316  75 LIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-207 7.32e-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: 103.85  E-value: 7.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  94 SLTLKTMGHQWYWSYEYTDYESlcfdsymtppleldpgelRLLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTD 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPG------------------RGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1036436316 174 AIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 207
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 5.55e-22

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 86.16  E-value: 5.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  95 LTLKTMGHQWYWSYEYTDYeslcfDSYMTPPLELDPGELRLlEVDNRVvlptemsiRMLISSEDVLHSWTVPALGVKTDA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL-PVGRPV--------LFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1036436316 175 IPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-207 1.24e-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: 79.98  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  94 SLTLKTMGHQWYWSYEYtdyeslcfdsymtppleldPGELRlleVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTD 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1036436316 174 AIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 207
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-207 9.99e-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: 78.65  E-value: 9.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316  67 ILPAVILI-LIALPSLRILYMMDEITTP---SLTLKTMGHQWYWSYEYTD-YESLcfdsymtppleldpgelrllevdNR 141
Cdd:cd13918     1 GLSAIIVIsLIVWTYGMLLYVEDPPDEAdedALEVEVEGFQFGWQFEYPNgVTTG-----------------------NT 57

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036436316 142 VVLPTEMSIRMLISSEDVLHSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 207
Cdd:cd13918    58 LRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-207 4.15e-18

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: 76.29  E-value: 4.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316 101 GHQWYWSYEYTDYEslcfdsymtppleldpgelrlLEVDNRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTDAIPGRLN 180
Cdd:cd13914     7 AYQWGWEFSYPEAN---------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                          90       100
                  ....*....|....*....|....*....
gi 1036436316 181 qaTLMTS--RPGIYYGQCSEICGANHSFM 207
Cdd:cd13914    66 --TIKTEatEEGEYQLYCAEYCGAGHSQM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 4.67e-08

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: 49.11  E-value: 4.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036436316 140 NRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 207
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 130-212 5.11e-08

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: 49.54  E-value: 5.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316 130 PGELRLLEVDNRVVLPTEMSIRMLISSE-DVLHSWTVPALGVKTDAI---------------PGRLNQATLMTSRPGIYY 193
Cdd:cd00920    13 TYNGVLLFGPPVLVVPVGDTVRVQFVNKlGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYW 92

                          90
                  ....*....|....*....
gi 1036436316 194 GQCSEICGaNHSFMPIVLE 212
Cdd:cd00920    93 FYCTIPGH-NHAGMVGTIN 110
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 140-207 1.40e-05

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 42.54  E-value: 1.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036436316 140 NRVVLPTEMSIRMLISSEDVLHSWTVPALGVKTDAIPGRLNQATLMTSRPGIYYGQCSEICGANHSFM 207
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-207 4.48e-04

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 38.13  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036436316 101 GHQWYWsyeytdyeslcfdsymtpplELDPGELRLLE-VDNRVvlptemsirmliSSEDVLHSWTV--PALGV--KTDAI 175
Cdd:cd13916     7 GHQWYW--------------------ELSRTEIPAGKpVEFRV------------TSADVNHGFGIydPDMRLlaQTQAM 54

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1036436316 176 PGRLNQATLMTSRPGIYYGQCSEICGANHSFM 207
Cdd:cd13916    55 PGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
 
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